enzyme_display_name: Dihydrofolate reductase type 2

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 7; buffer MTA; cofactor NADPH

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row wt R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.

raw_value_unit_evidence: Table 1 wt R67 DHFR row: kcat 1.3 s^-1; Km(DHF) 5.8 uM; Km(NADPH) 3.0 uM.

row_label: wt R67 DHFR

enzyme: Dihydrofolate reductase type 2


organism: Escherichia coli

substrate_name: NADPH

source_db: uniprot

verification_status: verified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row wt R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(NADPH) for NADPH.

normalized_value_unit_evidence: Km(NADPH) 0.003 mM.

data_origin: experimental

substrate: NADPH

status: verified

source: uniprot


substrate_name: NADP+

source_db: oed

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature C58Y to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADP+

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'C58Y', substrate column 'NADP'; column 'Km (uM)' = 233 +/- 21; column 'Vmax (umol min^-1 mg^-1)' = 2.7 +/- 0.1; column 'kcat (min^-1)' = 167 +/- 4; column 'kcat/Km (min^-1 uM^-1)' = 0.7.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row C58Y, substrate NADP: Km = 233 +/- 21 uM; kcat = 167 +/- 4 min^-1; printed kcat/Km = 0.7 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row C58Y, substrate column value NADP

table_label: Table 3: Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD (Biochemistry 2015, 54(22):3504-3513)

substrate: NADP+

status: corrected

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature K54S to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'K54S', substrate column 'NADP'; column 'Km (uM)' = 143 +/- 5; column 'Vmax (umol min^-1 mg^-1)' = 12 +/- 0.1; column 'kcat (min^-1)' = 736 +/- 5; column 'kcat/Km (min^-1 uM^-1)' = 5.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row K54S, substrate NADP: Km = 143 +/- 5 uM; kcat = 736 +/- 5 min^-1; printed kcat/Km = 5 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row K54S, substrate column value NADP


column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'WT', substrate column 'NADP'; column 'Km (uM)' = 187 +/- 33; column 'Vmax (umol min^-1 mg^-1)' = 16 +/- 1; column 'kcat (min^-1)' = 1025 +/- 50; column 'kcat/Km (min^-1 uM^-1)' = 5.5.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row WT, substrate NADP: Km = 187 +/- 33 uM; kcat = 1025 +/- 50 min^-1; printed kcat/Km = 5.5 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row WT, substrate column value NADP


column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'C58Y', substrate column '5,10-CH2-THF'; column 'Km (uM)' = 302 +/- 36; column 'Vmax (umol min^-1 mg^-1)' = 2.5 +/- 0.1; column 'kcat (min^-1)' = 155 +/- 5; column 'kcat/Km (min^-1 uM^-1)' = 0.5.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row C58Y, substrate 5,10-CH2-THF: Km = 302 +/- 36 uM; kcat = 155 +/- 5 min^-1; printed kcat/Km = 0.5 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row C58Y, substrate column value 5,10-CH2-THF


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature D121A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'D121A', substrate column '5,10-CH2-THF'; column 'Km (uM)' = 104 +/- 17; column 'Vmax (umol min^-1 mg^-1)' = 0.012; column 'kcat (min^-1)' = 0.7; column 'kcat/Km (min^-1 uM^-1)' = 0.007.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row D121A, substrate 5,10-CH2-THF: Km = 104 +/- 17 uM; kcat = 0.7 min^-1; printed kcat/Km = 0.007 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row D121A, substrate column value 5,10-CH2-THF


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24186 and applied mutation signature G122D to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'G122D', substrate column '5,10-CH2-THF'; column 'Km (uM)' = 68 +/- 5; column 'Vmax (umol min^-1 mg^-1)' = 0.056; column 'kcat (min^-1)' = 3.5; column 'kcat/Km (min^-1 uM^-1)' = 0.05.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row G122D, substrate 5,10-CH2-THF: Km = 68 +/- 5 uM; kcat = 3.5 min^-1; printed kcat/Km = 0.05 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row G122D, substrate column value 5,10-CH2-THF


column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'K54S', substrate column '5,10-CH2-THF'; column 'Km (uM)' = 205 +/- 12; column 'Vmax (umol min^-1 mg^-1)' = 14 +/- 0.2; column 'kcat (min^-1)' = 860 +/- 15; column 'kcat/Km (min^-1 uM^-1)' = 4.2.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row K54S, substrate 5,10-CH2-THF: Km = 205 +/- 12 uM; kcat = 860 +/- 15 min^-1; printed kcat/Km = 4.2 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row K54S, substrate column value 5,10-CH2-THF


column_label: Table 3 (Kinetic Properties of the Dehydrogenase and Cyclohydrolase of FolD), Dehydrogenase section, enzyme row 'WT', substrate column '5,10-CH2-THF'; column 'Km (uM)' = 279 +/- 39; column 'Vmax (umol min^-1 mg^-1)' = 19 +/- 1; column 'kcat (min^-1)' = 1195 +/- 65; column 'kcat/Km (min^-1 uM^-1)' = 4.2.

raw_value_unit_evidence: Table 3, Dehydrogenase section, enzyme row WT, substrate 5,10-CH2-THF: Km = 279 +/- 39 uM; kcat = 1195 +/- 65 min^-1; printed kcat/Km = 4.2 min^-1 uM^-1.

row_label: Table 3, Dehydrogenase section, enzyme row WT, substrate column value 5,10-CH2-THF


enzyme_display_name: pyrroline-5-carboxylate reductase

organism: Homo sapiens

substrate_name: NAD+

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P32322 and applied mutation signature E221A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

column_label: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper). Measurement identity: E221A mutant human P5CR, varied cofactor NAD+ at 1 mM fixed thioproline. Printed Km statement: the affinity of the E221A mutant for NAD+ (apparent KM = 0.235(±0.032) mM). Printed Kcat statement: Kcat = 13 s−1, fixed 1 mM NADP+. No efficiency statement is printed for this measurement.

normalized_value_unit_evidence: Km: printed value 0.235 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.235 mM. kcat: printed value 13 s−1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 13.0 s^(-1). kcat/Km: no efficiency cell is printed in this paper, so the exported ratio is the full-precision quotient of the two printed cells above, 13.0 / 0.235 = 55.319148936170215 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper); E221A mutant human P5CR, varied cofactor NAD+ at 1 mM fixed thioproline; printed Km cell: the affinity of the E221A mutant for NAD+ (apparent KM = 0.235(±0.032) mM); printed kcat cell: Kcat = 13 s−1, fixed 1 mM NADP+; the paper prints no catalytic-efficiency cell anywhere in its text.

enzyme: pyrroline-5-carboxylate reductase

substrate: NAD+


column_label: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper). Measurement identity: wild-type recombinant human P5CR, varied cofactor NAD+ at 1 mM fixed thioproline. Printed Km statement: The affinity of P5CR for NAD+ (apparent KM = 0.151(±0.023) mM). Printed Kcat statement: Kcat = 55 s−1, fixed 1 mM NADP+. No efficiency statement is printed for this measurement.

normalized_value_unit_evidence: Km: printed value 0.151 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.151 mM. kcat: printed value 55 s−1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 55.0 s^(-1). kcat/Km: no efficiency cell is printed in this paper, so the exported ratio is the full-precision quotient of the two printed cells above, 55.0 / 0.151 = 364.2384105960265 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper); wild-type recombinant human P5CR, varied cofactor NAD+ at 1 mM fixed thioproline; printed Km cell: The affinity of P5CR for NAD+ (apparent KM = 0.151(±0.023) mM); printed kcat cell: Kcat = 55 s−1, fixed 1 mM NADP+; the paper prints no catalytic-efficiency cell anywhere in its text.


column_label: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper). Measurement identity: E221A mutant human P5CR, varied cofactor NADP+ at 1 mM fixed thioproline. Printed Km statement: was only twofold higher than for NADP + (apparent KM = 0.480(±0.021) mM). Printed Kcat statement: Kcat = 13 s−1, fixed 1 mM NADP+. No efficiency statement is printed for this measurement.

normalized_value_unit_evidence: Km: printed value 0.480 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.48 mM. kcat: printed value 13 s−1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 13.0 s^(-1). kcat/Km: no efficiency cell is printed in this paper, so the exported ratio is the full-precision quotient of the two printed cells above, 13.0 / 0.48 = 27.083333333333336 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper); E221A mutant human P5CR, varied cofactor NADP+ at 1 mM fixed thioproline; printed Km cell: was only twofold higher than for NADP + (apparent KM = 0.480(±0.021) mM); printed kcat cell: Kcat = 13 s−1, fixed 1 mM NADP+; the paper prints no catalytic-efficiency cell anywhere in its text.


column_label: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper). Measurement identity: wild-type recombinant human P5CR, varied cofactor NADP+ at 1 mM fixed thioproline. Printed Km statement: is 20-fold higher than for NADP+ (apparent KM = 3.06(±0.042) mM). Printed Kcat statement: Kcat = 55 s−1, fixed 1 mM NADP+. No efficiency statement is printed for this measurement.

normalized_value_unit_evidence: Km: printed value 3.06 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 3.06 mM. kcat: printed value 55 s−1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 55.0 s^(-1). kcat/Km: no efficiency cell is printed in this paper, so the exported ratio is the full-precision quotient of the two printed cells above, 55.0 / 3.06 = 17.973856209150327 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper); wild-type recombinant human P5CR, varied cofactor NADP+ at 1 mM fixed thioproline; printed Km cell: is 20-fold higher than for NADP+ (apparent KM = 3.06(±0.042) mM); printed kcat cell: Kcat = 55 s−1, fixed 1 mM NADP+; the paper prints no catalytic-efficiency cell anywhere in its text.


substrate_name: Thioproline

column_label: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper). Measurement identity: E221A mutant human P5CR, varied substrate thioproline at 1 mM fixed NADP+. Printed Km statement: (KM = 0.73(±0.023) mM; Kcat = 13 s−1, fixed 1 mM NADP+). Printed Kcat statement: Kcat = 13 s−1, fixed 1 mM NADP+. No efficiency statement is printed for this measurement.

normalized_value_unit_evidence: Km: printed value 0.73 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.73 mM. kcat: printed value 13 s−1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 13.0 s^(-1). kcat/Km: no efficiency cell is printed in this paper, so the exported ratio is the full-precision quotient of the two printed cells above, 13.0 / 0.73 = 17.808219178082194 s^-1 mM^-1, which is the exported value.

raw_value_unit_evidence: Mutagenesis subsection of Results, J. Mol. Biol. 2006, 359, pages 1372-1373 (running prose, no kinetics table in this paper); E221A mutant human P5CR, varied substrate thioproline at 1 mM fixed NADP+; printed Km cell: (KM = 0.73(±0.023) mM; Kcat = 13 s−1, fixed 1 mM NADP+); printed kcat cell: Kcat = 13 s−1, fixed 1 mM NADP+; the paper prints no catalytic-efficiency cell anywhere in its text.

substrate: Thioproline


column_label: PMID 16730026 Results and Discussion, Mutagenesis prose, journal page 1372: wild-type P5CR, fixed 1 mM NADP+; thioproline Km=1.26 +/- 0.032 mM and kcat=55 s^-1 in the same sentence and assay series.

normalized_value_unit_evidence: Km normalized_value=1.26 normalized_unit=mM; kcat normalized_value=55 normalized_unit=s^-1; same-prose-pair kcat/Km normalized_value=43.65079365079365 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Wild-type P5CR with fixed 1 mM NADP+: thioproline Km 1.26 +/- 0.032 mM; kcat 55 s^-1; same-pair ratio 55/1.26.

row_label: wild-type P5CR / thioproline / fixed 1 mM NADP+


organism: Azospirillum brasilense

assay_conditions_summary: pH 6.5; 303.15 K; buffer 10 mM Pyr2C or Pip2C in 50 mM potassium phosphate; cofactor NADH

column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row AbLhpI / Pyr2C / NADH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 0.837 ± 0.080 mM | kcat 36900 ± 2400 min^-1 | kcat/Km 44100 ± 1400 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=615.0 normalized_unit=s^-1; Km normalized_value=0.837 normalized_unit=mM; kcat/Km normalized_value=734.7670250896058 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=36900 ± 2400 raw_unit=min^-1; Km raw_value=0.837 ± 0.080 raw_unit=mM; kcat/Km raw_value=44100 ± 1400 raw_unit=min^-1*mM^-1

row_label: AbLhpI / Pyr2C / NADH


column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row AbLhpI / Pyr4SH2C / NADPH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 0.491 ± 0.063 mM | kcat 621 ± 58 min^-1 | kcat/Km 1270 ± 45 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.35 normalized_unit=s^-1; Km normalized_value=0.491 normalized_unit=mM; kcat/Km normalized_value=21.079429735234214 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=621 ± 58 raw_unit=min^-1; Km raw_value=0.491 ± 0.063 raw_unit=mM; kcat/Km raw_value=1270 ± 45 raw_unit=min^-1*mM^-1

row_label: AbLhpI / Pyr4SH2C / NADPH


assay_conditions_summary: pH 6.5; 303.15 K; buffer 10 mM Pyr2C or Pip2C in 50 mM potassium phosphate; cofactor NADPH

table_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction


substrate_name: L-Pipecolate

assay_conditions_summary: pH 10.5; 303.15 K; cofactor NAD+

column_label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction; row AbLhpI / L-Pipecolate / NAD+; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 14.8 ± 2.1 mM | kcat 222 ± 24 min^-1 | kcat/Km 15.0 ± 0.5 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=3.7 normalized_unit=s^-1; Km normalized_value=14.8 normalized_unit=mM; kcat/Km normalized_value=0.25 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=222 ± 24 raw_unit=min^-1; Km raw_value=14.8 ± 2.1 raw_unit=mM; kcat/Km raw_value=15.0 ± 0.5 raw_unit=min^-1*mM^-1

row_label: AbLhpI / L-Pipecolate / NAD+

substrate: L-Pipecolate


substrate_name: L-proline

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NAD+

column_label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction; row AbLhpI / L-Proline / NAD+; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 3.99 ± 0.18 mM | kcat 254 ± 3 min^-1 | kcat/Km 63.6 ± 2.1 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=4.233 normalized_unit=s^-1; Km normalized_value=3.99 normalized_unit=mM; kcat/Km normalized_value=1.0609022556390977 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=254 ± 3 raw_unit=min^-1; Km raw_value=3.99 ± 0.18 raw_unit=mM; kcat/Km raw_value=63.6 ± 2.1 raw_unit=min^-1*mM^-1

row_label: AbLhpI / L-Proline / NAD+

substrate: L-proline


enzyme_display_name: dihydrofolate reductase

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L22R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.65; 293.15 K; cofactor NADPH

enzyme: dihydrofolate reductase

status: unverified


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +3, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


substrate_name: dihydrofolate

substrate: dihydrofolate


enzyme_display_name: Ketimine reductase mu-crystallin

organism: Bos taurus

substrate_name: NADPH (at pH 5.5 and 37 degrees Celsius)

assay_conditions_summary: pH 5.5; cofactor NADPH

column_label: Table V (Apparent kinetic constants), row NADPH a, column Km (mM), value 0.015; footnote a says variable NAD(P)H, 1 mM delta1-piperidine 2-carboxylate, and pH 5.5; Materials and Methods says 37 C

raw_value_unit_evidence: Table V row NADPH a, column Km (mM) = 0.015

row_label: NADPH a

table_label: Table V

enzyme: Ketimine reductase mu-crystallin


substrate_name: NADH (at pH 5.5 and 37 degrees Celsius)

assay_conditions_summary: pH 5.5; cofactor NADH

column_label: Table V (Apparent kinetic constants), row NADH a, column Km (mM), value 0.26; footnote a says variable NAD(P)H, 1 mM delta1-piperidine 2-carboxylate, and pH 5.5; Materials and Methods says 37 C

raw_value_unit_evidence: Table V row NADH a, column Km (mM) = 0.26

row_label: NADH a

substrate: NADH (at pH 5.5 and 37 degrees Celsius)


substrate_name: delta(1)-piperideine-2-carboxylate (at pH 5.0 and 37 degrees Celsius)

assay_conditions_summary: pH 5; cofactor NADPH

column_label: Table V (Apparent kinetic constants), row delta1-Piperidine 2-carboxylate, column Km (mM), value 0.33; Table V note says pH 5.0; Materials and Methods says spectrophotometry at 340 nm and 37 C

raw_value_unit_evidence: Table V row delta1-Piperidine 2-carboxylate, column Km (mM) = 0.33

row_label: delta1-Piperidine 2-carboxylate


substrate_name: (R)-lanthionine ketimine (at pH 5.0 and 37 degrees Celsius)

column_label: Table V (Apparent kinetic constants), row Lanthionine ketimine, column Km (mM), value 1.17; Table V note says pH 5.0 and 4 units purified reductase for LK; Materials and Methods says 37 C

raw_value_unit_evidence: Table V row Lanthionine ketimine, column Km (mM) = 1.17

row_label: Lanthionine ketimine


substrate_name: (S)-cystathionine ketimine (at pH 5.0 and 37 degrees Celsius)

column_label: Table V (Apparent kinetic constants), row Cystathionine ketimine, column Km (mM), value 10; Table V note says pH 5.0; Materials and Methods says spectrophotometry at 340 nm and 37 C

raw_value_unit_evidence: Table V row Cystathionine ketimine, column Km (mM) = 10

row_label: Cystathionine ketimine


organism: Colwellia psychrerythraea

proof_lines:
CpLhpI
Pyr4S H2C
Colwellia psychrerythraea


column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row CpLhpI / Pip2C / NADPH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 7.26 ± 1.22 mM | kcat 82.9 ± 13.7 min^-1 | kcat/Km 11.4 ± 0.2 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=1.38 normalized_unit=s^-1; Km normalized_value=7.26 normalized_unit=mM; kcat/Km normalized_value=0.19008264462809915 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=82.9 ± 13.7 raw_unit=min^-1; Km raw_value=7.26 ± 1.22 raw_unit=mM; kcat/Km raw_value=11.4 ± 0.2 raw_unit=min^-1*mM^-1

row_label: CpLhpI / Pip2C / NADPH


column_label: Table 1. Kinetic parameters of AbLhpI, CpLhpI, and PaLhpD in the forward direction; row CpLhpI / Pyr2C / NADPH; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 5.90 ± 0.36 mM | kcat 7470 ± 470 min^-1 | kcat/Km 1270 ± 2 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=124.5 normalized_unit=s^-1; Km normalized_value=5.9 normalized_unit=mM; kcat/Km normalized_value=21.101694915254235 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=7470 ± 470 raw_unit=min^-1; Km raw_value=5.90 ± 0.36 raw_unit=mM; kcat/Km raw_value=1270 ± 2 raw_unit=min^-1*mM^-1

row_label: CpLhpI / Pyr2C / NADPH


assay_conditions_summary: pH 10.5; 303.15 K; cofactor NADP+

column_label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. Row CpLhpI (Colwellia psychrerythraea) | l-Proline | NADP+; pH cell 10.5; column 'K m (mM)' = 18.3 ± 2.4; column 'k cat (min^-1)' = 65.3 ± 6.9; column 'k cat / K m (min^-1 mM^-1)' = 3.57 ± 0.09.

normalized_value_unit_evidence: kcat: printed Table 2 cell 65.3 ± 6.9 min^-1; 65.3 / 60 = 1.0883333333333334 s^(-1); the exported value is 1.09 s^(-1). Km: printed Table 2 cell 18.3 ± 2.4 mM; the paper prints Km in mM already, so the value stands at 18.3 mM; the exported value is 18.8 mM. kcat/Km: printed Table 2 cell 3.57 ± 0.09 min^-1 mM^-1; 3.57 / 60 = 0.0595 s^-1 mM^-1; the exported value is 0.05797872340425532 s^(-1)*mM^(-1), which is the bare quotient 1.09 / 18.8 of the export's own two stored numbers.

raw_value_unit_evidence: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction. | metric header row of the table: Enzymes Substrates pH a Coenzymes Specific activity (units/mg protein) K m (mM) k cat (min −1 ) k cat / K m b (min −1 mM −1 ) | row CpLhpI (Colwellia psychrerythraea) | l-Proline | NADP+ cells read: specific activity 0.630 units/mg protein, K m = 18.3 ± 2.4 mM, k cat = 65.3 ± 6.9 min^-1, k cat / K m = 3.57 ± 0.09 min^-1 mM^-1.

row_label: Table 2, row CpLhpI (Colwellia psychrerythraea) | l-Proline | NADP+


column_label: Table 2. Kinetic parameters of AbLhpI, CpLhpI and PaLhpD in the reverse direction; row CpLhpI / L-Pipecolate / NADP+; columns Km (mM); kcat (min^-1); kcat/Km (min^-1*mM^-1); raw table cells: Km 80.1 ± 2.8 mM | kcat 1.28 ± 0.04 min^-1 | kcat/Km 0.016 ± 0.001 min^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=0.02 normalized_unit=s^-1; Km normalized_value=80.1 normalized_unit=mM; kcat/Km normalized_value=0.0002496878901373284 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.28 ± 0.04 raw_unit=min^-1; Km raw_value=80.1 ± 2.8 raw_unit=mM; kcat/Km raw_value=0.016 ± 0.001 raw_unit=min^-1*mM^-1

row_label: CpLhpI / L-Pipecolate / NADP+


organism: Lactobacillus casei

substrate_name: folate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D26N to reconstruct the assayed variant sequence.

proof_lines:
D26N
folate reduction
Lactobacillus casei

substrate: folate


proof_lines:
D26N
dihydrofolate reduction
Lactobacillus casei


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T238A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


column_label: PMC5409489 Table 2, Wild type / 1-pyrroline-5-carboxylate / fixed NADPH row: Km 667 +/- 88 uM, kcat 31 +/- 2 s^-1, kcat/Km 0.47 +/- 0.07 x 10^5 M^-1 s^-1. The explicit efficiency is 47; the preserved OED source tuple says 470 and must be repaired with audit preservation.

normalized_value_unit_evidence: Km normalized_value=0.667 normalized_unit=mM; kcat normalized_value=31 normalized_unit=s^-1; kcat_over_km normalized_value=47 normalized_unit=s^-1*mM^-1.

row_label: Wild type; variable 1-pyrroline-5-carboxylate; fixed NADPH

table_label: Table 2. Steady-state kinetic parameters for PYCR1


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: PMC5409489 Table 2, Wild type / NADH / fixed 1-pyrroline-5-carboxylate row: Km 70 +/- 11 uM, kcat 218 +/- 8 s^-1, kcat/Km 31 +/- 5 x 10^5 M^-1 s^-1. The explicit table efficiency normalizes to 3100, not the recomputed export value 3114.2857142857138.

normalized_value_unit_evidence: Km normalized_value=0.07 normalized_unit=mM; kcat normalized_value=218 normalized_unit=s^-1; kcat_over_km normalized_value=3100 normalized_unit=s^-1*mM^-1.

row_label: Wild type; variable NADH; fixed 1-pyrroline-5-carboxylate

substrate: NADH


column_label: PMC5409489 Table 2, Wild type / NADPH / fixed 1-pyrroline-5-carboxylate row: Km 283 +/- 119 uM, kcat 74 +/- 8 s^-1, kcat/Km 2.6 +/- 1.1 x 10^5 M^-1 s^-1. The explicit table efficiency normalizes to 260, not the recomputed export value 261.48409893992937.

normalized_value_unit_evidence: Km normalized_value=0.283 normalized_unit=mM; kcat normalized_value=74 normalized_unit=s^-1; kcat_over_km normalized_value=260 normalized_unit=s^-1*mM^-1.

row_label: Wild type; variable NADPH; fixed 1-pyrroline-5-carboxylate


organism: Pneumocystis carinii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K37Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P16184 and applied mutation signature K37Q to reconstruct the assayed variant sequence.

column_label: Official PMC Table 2 pcDHFR K37Q row under Km DHFA, kcat, and kcat/Km DHFA columns.

normalized_value_unit_evidence: Km 0.0085 mM; kcat 36 s^-1; explicit kcat/Km 4000 s^-1 mM^-1.

raw_value_unit_evidence: Km DHFA 8.5 +/- 0.87 microM (n=7); kcat 36 +/- 2.4 s^-1 (n=9); printed DHFA kcat/Km 4 s^-1 microM^-1.

row_label: pcDHFR K37Q; Km DHFA, kcat, and kcat/Km DHFA


substrate_name: delta(1)-piperideine-2-carboxylate (at pH 7.2 and 37 degrees Celsius)

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


substrate_name: 1-pyrroline-2-carboxylate (at pH 7.2 and 37 degrees Celsius)


substrate_name: delta(2)-thiazoline-2-carboxylate (at pH 7.2 and 37 degrees Celsius)


organism: Bacillus anthracis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F96I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y102F to reconstruct the assayed variant sequence.


substrate_name: NADPH

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


proof_lines:
R67 DHFR
NADPH


substrate_name: ATP

assay_conditions_summary: cofactor ATP

substrate: ATP


substrate_name: formate

substrate: formate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH


organism: Mus musculus


substrate_name: NAD+

assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

column_label: PMC full-text Table 2 row NAD+, columns Km, kcat, and kcat/Km for redox cofactor kinetic parameters; Methods states cofactor parameters were measured with saturating CH2-H4PteGlu1.

normalized_value_unit_evidence: kcat=3.6 s^-1; Km=0.147 mM; kcat/Km=25 s^-1 mM^-1 from explicit paper kcat/Km 0.025 s^-1 uM^-1.

raw_value_unit_evidence: NAD+ row reports Km 147 uM, kcat 3.6 s^-1, kcat/Km 0.025 s^-1 uM^-1.

row_label: NAD+

table_label: PMC Table 2, Kinetic parameters for MTHFD2L


substrate_name: NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: PMC full-text Table 2 row NADP+, columns Km, kcat, and kcat/Km for redox cofactor kinetic parameters; Methods states cofactor parameters were measured with saturating CH2-H4PteGlu1.

normalized_value_unit_evidence: kcat=1.1 s^-1; Km=0.537 mM; kcat/Km=2 s^-1 mM^-1 from explicit paper kcat/Km 0.002 s^-1 uM^-1.

raw_value_unit_evidence: NADP+ row reports Km 537 uM, kcat 1.1 s^-1, kcat/Km 0.002 s^-1 uM^-1.

row_label: NADP+


enzyme_display_name: Bifunctional protein MdtA

organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)

substrate_name: methylenetetrahydromethanopterin

assay_conditions_summary: cofactor NADP+

enzyme: Bifunctional protein MdtA

substrate: methylenetetrahydromethanopterin


substrate_name: methylenetetrahydrofolate

substrate: methylenetetrahydrofolate


substrate_name: NADP(+) (in the presence of methylenetetrahydromethanopterin)


source_db: brenda

source: brenda


organism: Medicago truncatula

assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADH

column_label: Table 2 reports KM(app) NADH 468 +/- 22 uM, Vmax NADH 92.4 +/- 2.1 ukat (mg protein)^-1, kcat (NADH) 2972 s^-1, kcat/KM (NADH) 6.35 x 10^6 M^-1 s^-1; Km matches after unit normalization, but kcat and kcat/KM differ from current export

normalized_value_unit_evidence: KM normalized_value=0.468 normalized_unit=mM; kcat normalized_value=2972 normalized_unit=s^-1; kcat_over_km normalized_value=6350 normalized_unit=s^-1*mM^-1; current_export_kcat=2.972 s^-1; current_export_kcat_over_km=6.35042735042735 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=468 +/- 22 raw_unit=uM; kcat raw_value=2972 raw_unit=s^-1; kcat_over_km raw_value=6.35 x 10^6 raw_unit=M^-1*s^-1 for NADH

row_label: Table 2 NADH rows; KM(app) NADH, kcat (NADH), and kcat/KM (NADH)

table_label: PMID 26579138 PMC HTML Table 2


assay_conditions_summary: pH 7.5; 308.15 K; cofactor NADPH

column_label: Table 2 reports KM(app) NADPH 39 +/- 3 uM, Vmax NADPH 36.1 +/- 0.7 ukat (mg protein)^-1, kcat (NADPH) 1113 s^-1, kcat/KM (NADPH) 2.85 x 10^7 M^-1 s^-1; Km matches after unit normalization, but kcat and kcat/KM differ from current export

normalized_value_unit_evidence: KM normalized_value=0.039 normalized_unit=mM; kcat normalized_value=1113 normalized_unit=s^-1; kcat_over_km normalized_value=28500 normalized_unit=s^-1*mM^-1; current_export_kcat=1.113 s^-1; current_export_kcat_over_km=28.538461538461537 s^-1*mM^-1

raw_value_unit_evidence: KM raw_value=39 +/- 3 raw_unit=uM; kcat raw_value=1113 raw_unit=s^-1; kcat_over_km raw_value=2.85 x 10^7 raw_unit=M^-1*s^-1 for NADPH

row_label: Table 2 NADPH rows; KM(app) NADPH, kcat (NADPH), and kcat/KM (NADPH)


enzyme_display_name: Dihydromonapterin reductase

organism: Escherichia coli (strain K12)

substrate_name: 7,8-dihydrofolate (at pH 6.0)

assay_conditions_summary: cofactor NADPH

enzyme: Dihydromonapterin reductase

substrate: 7,8-dihydrofolate (at pH 6.0)


substrate_name: NADPH (at pH 6.0)

substrate: NADPH (at pH 6.0)


enzyme_display_name: UniProt P00374

substrate_name: dihydrofolate

source_db: skid

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: multiple

proof_lines:
human DHFR inhibitor complexes
dihydrofolate reductase
NADPH

source_databases_merged: skid uniprot

enzyme: UniProt P00374

source: skid


proof_lines:
ternary complexes with NADPH
hDHFR
dihydrofolate reductase


organism: Zymomonas mobilis subsp. mobilis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F31R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q35E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: Dihydrofolate reductase 2, mitochondrial


enzyme: Dihydrofolate reductase 2, mitochondrial


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H45R/W47Y/I50F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H45R/W47Y/I50F/G51P to reconstruct the assayed variant sequence.

proof_lines: Escherichia coli dihydrofolate reductase


organism: Lactobacillus leichmannii


organism: Leishmania major

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M53R to reconstruct the assayed variant sequence.


organism: Moritella yayanosii

assay_conditions_summary: pH 7; 298.15 K; buffer used was 20 mM TrisHCl; cofactor NADPH

column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: myDHFR. Column group: DHF. Columns read: Km (uM) cell 1.8 ± 0.2, kcat (s^-1) cell 83.8 ± 2.4, kcat/Km (uM^-1 s^-1) cell 46.6 ± 6.5. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 1.8 ± 0.2; raw unit: uM; normalized value: 0.0018; normalized unit: mM; metric: kcat; raw value: 83.8 ± 2.4; raw unit: s^-1; normalized value: 83.8; normalized unit: s^(-1); metric: kcat/Km; normalized value: 46555.555555555555; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: myDHFR | column group: DHF | Km (uM) cell 1.8 ± 0.2; kcat (s^-1) cell 83.8 ± 2.4; kcat/Km (uM^-1 s^-1) cell 46.6 ± 6.5. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: myDHFR | DHF column group


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines:
Moritella yayanosii
dihydrofolate reductase
DHFR


organism: Moritella japonica

column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: mjDHFR. Column group: DHF. Columns read: Km (uM) cell 238 ± 26, kcat (s^-1) cell 144.5 ± 3.2, kcat/Km (uM^-1 s^-1) cell 0.6 ± 0.1. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 238 ± 26; raw unit: uM; normalized value: 0.238; normalized unit: mM; metric: kcat; raw value: 144.5 ± 3.2; raw unit: s^-1; normalized value: 144.5; normalized unit: s^(-1); metric: kcat/Km; normalized value: 607.1428571428572; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: mjDHFR | column group: DHF | Km (uM) cell 238 ± 26; kcat (s^-1) cell 144.5 ± 3.2; kcat/Km (uM^-1 s^-1) cell 0.6 ± 0.1. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: mjDHFR | DHF column group


column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: mjDHFR. Column group: NADPH. Columns read: Km (uM) cell 58.4 ± 1.9, kcat (s^-1) cell 109.2 ± 1.1, kcat/Km (uM^-1 s^-1) cell 1.9 ± 0.1. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 58.4 ± 1.9; raw unit: uM; normalized value: 0.0584; normalized unit: mM; metric: kcat; raw value: 109.2 ± 1.1; raw unit: s^-1; normalized value: 109.2; normalized unit: s^(-1); metric: kcat/Km; normalized value: 1869.86301369863; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: mjDHFR | column group: NADPH | Km (uM) cell 58.4 ± 1.9; kcat (s^-1) cell 109.2 ± 1.1; kcat/Km (uM^-1 s^-1) cell 1.9 ± 0.1. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: mjDHFR | NADPH column group


organism: Photobacterium profundum

column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: ppDHFR. Column group: DHF. Columns read: Km (uM) cell 6.2 ± 0.8, kcat (s^-1) cell 156.0 ± 5.6, kcat/Km (uM^-1 s^-1) cell 25.2 ± 4.2. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 6.2 ± 0.8; raw unit: uM; normalized value: 0.0062; normalized unit: mM; metric: kcat; raw value: 156.0 ± 5.6; raw unit: s^-1; normalized value: 156.0; normalized unit: s^(-1); metric: kcat/Km; normalized value: 25161.290322580648; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: ppDHFR | column group: DHF | Km (uM) cell 6.2 ± 0.8; kcat (s^-1) cell 156.0 ± 5.6; kcat/Km (uM^-1 s^-1) cell 25.2 ± 4.2. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: ppDHFR | DHF column group


column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: ppDHFR. Column group: NADPH. Columns read: Km (uM) cell 19.8 ± 0.8, kcat (s^-1) cell 150.5 ± 2.3, kcat/Km (uM^-1 s^-1) cell 7.6 ± 0.4. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 19.8 ± 0.8; raw unit: uM; normalized value: 0.0198; normalized unit: mM; metric: kcat; raw value: 150.5 ± 2.3; raw unit: s^-1; normalized value: 150.5; normalized unit: s^(-1); metric: kcat/Km; normalized value: 7601.010101010101; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: ppDHFR | column group: NADPH | Km (uM) cell 19.8 ± 0.8; kcat (s^-1) cell 150.5 ± 2.3; kcat/Km (uM^-1 s^-1) cell 7.6 ± 0.4. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: ppDHFR | NADPH column group


organism: Plasmodium falciparum


organism: Pneumocystis jiroveci


assay_conditions_summary: pH 7.4; 310.15 K; buffer 41 mM sodium phosphate; cofactor NADPH

column_label: Table 2 row pjDHFR lists K_m DHFA 2.8 +/- 0.04 uM, K_m NADPH 22.9 +/- 2.1 uM, kcat 53 +/- 4.2 sec^-1, and kcat/K_m DHFA 19 sec^-1 uM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0028 normalized_unit=mM; kcat normalized_value=53 normalized_unit=s^-1; kcat/Km normalized_value=19000 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m DHFA raw_value=2.8 +/- 0.04 raw_unit=uM; kcat raw_value=53 +/- 4.2 raw_unit=sec^-1; kcat/Km raw_value=19 raw_unit=sec^-1 uM^-1

row_label: pjDHFR

table_label: Table 2. Kinetic constants for substrate and cofactor for pj-, pc- and hDHFR and its active site mutants that reflect human to Pneumocystis changes


organism: Mycolicibacterium phlei


organism: Schistosoma mansoni

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADP+


organism: Shewanella violacea

column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: svDHFR. Column group: DHF. Columns read: Km (uM) cell 1.9 ± 0.2, kcat (s^-1) cell 90.1 ± 2.9, kcat/Km (uM^-1 s^-1) cell 47.4 ± 6.5. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 1.9 ± 0.2; raw unit: uM; normalized value: 0.0019; normalized unit: mM; metric: kcat; raw value: 90.1 ± 2.9; raw unit: s^-1; normalized value: 90.1; normalized unit: s^(-1); metric: kcat/Km; normalized value: 47421.05263157895; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: svDHFR | column group: DHF | Km (uM) cell 1.9 ± 0.2; kcat (s^-1) cell 90.1 ± 2.9; kcat/Km (uM^-1 s^-1) cell 47.4 ± 6.5. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: svDHFR | DHF column group


column_label: Table label: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure. Row label: svDHFR. Column group: NADPH. Columns read: Km (uM) cell 3.4 ± 0.3, kcat (s^-1) cell 86.8 ± 2.0, kcat/Km (uM^-1 s^-1) cell 25.5 ± 2.8. Every value is taken from this one row and this one column group; no value is taken from another row, another column group, another table, or another paper. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

normalized_value_unit_evidence: metric: Km; raw value: 3.4 ± 0.3; raw unit: uM; normalized value: 0.0034; normalized unit: mM; metric: kcat; raw value: 86.8 ± 2.0; raw unit: s^-1; normalized value: 86.8; normalized unit: s^(-1); metric: kcat/Km; normalized value: 25529.411764705885; normalized unit: s^(-1)*mM^(-1);

raw_value_unit_evidence: Table II. Steady-state kinetic parameters of ecDHFR and deep-sea DHFR enzymatic reactions at 25 C and pH 7.0 under atmospheric pressure | row label: svDHFR | column group: NADPH | Km (uM) cell 3.4 ± 0.3; kcat (s^-1) cell 86.8 ± 2.0; kcat/Km (uM^-1 s^-1) cell 25.5 ± 2.8. In the PDF text layer the micro sign is dropped, so the printed headers Km (uM) and kcat/Km (uM^-1 s^-1) appear as Km (mM) and (mM1 s1) and superscript -1 appears as 1; the rendered page image shows the printed headers.

row_label: svDHFR | NADPH column group


organism: Streptococcus pneumoniae

sequence_variant_note: Mutation signature H26Y/Q60K/A77V/V78A/Q81H/Q91S/L100V/E133A/A149T could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Strigomonas oncopelti


column_label: Page 453 Summary gives 1 x 10^-5 M for NADPH; page 455 prose repeats cofactor Km 1 x 10^-5 M

normalized_value_unit_evidence: Paper-supported NADPH Km is 0.01 mM; sheet value is 0.05 mM

raw_value_unit_evidence: Paper reports cofactor Km values for the two enzymes essentially the same at 1 x 10^-5 M for NADPH

row_label: C. oncopelti / NADPH cofactor Km

table_label: BBA 178:453-458 summary and page 455 prose


assay_conditions_summary: pH 7.3; 300.15 K; cofactor NADP+


organism: Oryctolagus cuniculus

column_label: Table II, Km (uM) column, Parent enzyme subcolumn, Methylene-tetrahydrofolate row shows 2; Dehydrogenase-cyclohydrolase fragment also shows 2.

raw_value_unit_evidence: Km = 2 uM

row_label: Methylenetetrahydrofolate dehydrogenase; substrate Methylene-tetrahydrofolate

table_label: Table II: Kinetic constants for C1-tetrahydrofolate synthase reactions and the two purified fragments


column_label: Table II, Km (uM) column, Parent enzyme subcolumn, NADP+ row shows 4; Dehydrogenase-cyclohydrolase fragment also shows 4.

raw_value_unit_evidence: Km = 4 uM

row_label: Methylenetetrahydrofolate dehydrogenase; substrate NADP+


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Photobacterium phosphoreum

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADP+


organism: Ovis aries

proof_lines:
Table III
NADP+


enzyme_display_name: D-arginine dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: D-histidine

enzyme: D-arginine dehydrogenase

substrate: D-histidine


substrate_name: D-Leucine

substrate: D-Leucine


organism: Neurospora crassa

proof_lines:
pyrroline-5-carboxylate reductase
Neurospora crassa
NADPH


substrate_name: D-arginine

substrate: D-arginine


organism: Homo sapiens

substrate_name: NADH (at pH 5.0 and 37 degrees Celsius)

assay_conditions_summary: pH 5; cofactor NADH

column_label: PDF p.383 and Fig. 5 caption report Km=3.6 +/- 1.4 uM for NADH under the human CRYM assay conditions.

normalized_value_unit_evidence: 3.6 uM converts to 0.0036 mM for NADH Km.

raw_value_unit_evidence: Results/Fig. 5 report a Km of 3.6 +/- 1.4 uM for NADH.

row_label: Recombinant human CRYM/ketimine reductase / NADH

table_label: Journal of Neurochemistry PDF p.383 Results and Fig. 5 caption

substrate: NADH (at pH 5.0 and 37 degrees Celsius)


organism: Crithidia fasciculata


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y69L with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

proof_lines:
PMID 15333637
R67 dihydrofolate reductase
Y69L


organism: Escherichia coli (strain K12)

substrate_name: 7,8-dihydromonapterin (at pH 6.0)

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines:
FolM
dihydromonapterin reductase
Escherichia coli

substrate: 7,8-dihydromonapterin (at pH 6.0)


organism: Moritella profunda

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

source_databases_merged: brenda skid

substrate: NADPH


proof_lines:
at pH 7.0 and 5°C
at pH 7.0 and 10°C
at pH 7.0 and 15°C


proof_lines:
human DHFR
OAAG324
trimethoprim


organism: Trypanosoma brucei brucei


organism: Trypanosoma cruzi


organism: Mycobacterium avium

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


proof_lines: mutant enzyme R44P, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44D, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44E, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44Y, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44L, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44I, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44V, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44F, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44H, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44G, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44Q, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44T, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44W, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44C, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44A, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44N, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44M, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44K, at 15°C, pH not specified in the publication


proof_lines: mutant enzyme R44S, at 15°C, pH not specified in the publication


organism: Plasmodium falciparum

assay_conditions_summary: pH 7


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH


proof_lines: recombinant mutants S108G, S108A and S108C


proof_lines: recombinant mutants S108G, S108N and S108C


organism: Pneumocystis carinii

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

proof_lines:
recombinant mutant K37Q, pH 7.4, 37°C
pH 7.4, 37°C, mutant K37Q


proof_lines: recombinant mutant K37S/F69S, pH 7.4, 37°C


proof_lines: recombinant mutant K37Q/F69S, pH 7.4, 37°C


proof_lines: recombinant mutant K37S/F69N, pH 7.4, 37°C


proof_lines: recombinant mutant K37Q/F69N, pH 7.4, 37°C


proof_lines: recombinant wild-type enzyme, pH 7.4, 37°C


organism: Pneumocystis jirovecii


proof_lines: recombinant mutant S37Q/S69F, pH 7.4, 37°C


proof_lines: recombinant mutant S37K/S69F, pH 7.4, 37°C


proof_lines: recombinant mutant S37K/S69N, pH 7.4, 37°C


proof_lines: recombinant mutant S37Q/S69N, pH 7.4, 37°C


proof_lines:
recombinant mutant N64F, pH 7.4, 37°C
pH 7.4, 37°C, mutant N64F


proof_lines:
recombinant mutant N64S, pH 7.4, 37°C
pH 7.4, 37°C, mutant N64S


proof_lines: recombinant mutant Q35K/N64S, pH 7.4, 37°C


proof_lines: recombinant mutant Q35S/N64F, pH 7.4, 37°C


proof_lines: recombinant mutant Q35S/N64S, pH 7.4, 37°C


proof_lines:
recombinant mutant Q35S, pH 7.4, 37°C
pH 7.4, 37°C, mutant Q35S


proof_lines:
recombinant mutant Q35K, pH 7.4, 37°C
pH 7.4, 37°C, mutant Q35K


proof_lines: recombinant mutant Q35K/N64F, pH 7.4, 37°C


mutation_signature: deletion mutant DELTAGly121/DELTAAla145

mutation_type: deletion

proof_lines: deletion mutant DELTAGly121/DELTAAla145, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAArg52/DELTAGly121

proof_lines: deletion mutant DELTAArg52/DELTAGly121, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAGly67/DELTAGly121

proof_lines: deletion mutant DELTAGly67/DELTAGly121, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAGly121

proof_lines: deletion mutant DELTAGly121, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAGly67

proof_lines: deletion mutant DELTAGly67, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAArg52/DELTAGly67

proof_lines: deletion mutant DELTAArg52/DELTAGly67, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAAla145

proof_lines: deletion mutant DELTAAla145, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAArg52/DELTAAla145

proof_lines: deletion mutant DELTAArg52/DELTAAla145, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAGly67/DELTAAla145

proof_lines: deletion mutant DELTAGly67/DELTAAla145, at pH 7.0 and 25°C


mutation_signature: deletion mutant DELTAArg52

proof_lines: deletion mutant DELTAArg52, at pH 7.0 and 25°C


assay_conditions_summary: pH 5; 298.15 K; cofactor NADPH


proof_lines: triple mutant L16M/L20M/L42M from plasmid


assay_conditions_summary: cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

proof_lines: pH 7.5, 37°C, recombinant mutant R119C, with 1-pyrroline-5-carboxylate


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: mutant R119C, cosubstrate NADH, pH 7.5, 37°C

proof_lines: pH 7.5, 37°C, recombinant mutant R119C, with NADH

proof_lines: mutant R119C, cosubstrate NADPH, pH 7.5, 37°C


proof_lines: pH 7.5, 37°C, recombinant mutant R251C, with 1-pyrroline-5-carboxylate


proof_lines: mutant R251C, cosubstrate NADPH, pH 7.5, 37°C

proof_lines: pH 7.5, 37°C, recombinant mutant R251C, with NADPH

proof_lines: mutant R251C, cosubstrate NADH, pH 7.5, 37°C


proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, with 1-pyrroline-5-carboxylate


substrate_name: L-Pro

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, competitive inhibition

substrate: L-Pro


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADP+

substrate: NADP+


proof_lines: recombinant mutant Q35K/N64F, pH 7.4, 37°C


proof_lines: recombinant mutant N64F enzyme, pH 7.4, 37°C


organism: Bacillus anthracis


organism: Streptococcus pneumoniae

proof_lines: mutant H26Y/Q60K/A77V/V78A/Q81H/Q91S/L100V/E133A/A149T, pH 7.0, 25°C, value below

proof_lines: mutant H26Y/Q60K/A77V/V78A/Q81H/Q91S/L100V/E133A/A149T, pH 7.0, 25°C, value above

substrate: dihydrofolate


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


proof_lines:
wild-type, 25°C, pH 7.0
recombinant wild-type enzyme
wild-type, pH 5.0, 25°C


enzyme_display_name: protein-lysine 6-oxidase

smiles: C(CCN)CCN

proof_lines: pH 8.2, temperature not specified in the publication

enzyme: protein-lysine 6-oxidase


assay_conditions_summary: pH 5

proof_lines:
pH 5.0
above pH 7.4


organism: Mycobacterium tuberculosis

proof_lines:
cofactor NADPH
cofactor NADH


assay_conditions_summary: cofactor NADP+


substrate_name: L-proline

substrate: L-proline


substrate: NADH


enzyme_display_name: L-aspartate oxidase

organism: Pseudomonas putida

substrate_name: L-aspartate

proof_lines: mutant enzyme R290A, at pH 7.5, temperature not specified in the publication

enzyme: L-aspartate oxidase

substrate: L-aspartate


proof_lines: mutant enzyme Q242A, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme S389A, at pH 7.5, temperature not specified in the publication


proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme H244A, at pH 7.5, temperature not specified in the publication


organism: Plasmodium vivax


organism: Rattus norvegicus


proof_lines:
cosubstrate NADPH
cosubstrate NADH


proof_lines:
cosubstrate NADPH
cosubstrate NADH
against DL-pyrroline-5-carboxylate


substrate_name: NADP+

proof_lines:
against NADH
against NADPH


enzyme_display_name: diamine oxidase

organism: Sus scrofa

substrate_name: Butylamine

smiles: CCCCN

proof_lines:
at pH 8.5
at pH 6.3
at pH 7.4

enzyme: diamine oxidase

substrate: Butylamine


substrate_name: lysine methylester

proof_lines:
at pH 7.4
vs. p-dimethylaminomethylbenzylamine
vs. O2

substrate: lysine methylester


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


substrate_name: ethylenediamine

smiles: C(CN)N

substrate: ethylenediamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


enzyme_display_name: leucine dehydrogenase

organism: Bacillus cereus

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: leucine dehydrogenase

substrate: NAD+


substrate_name: L-Leu

smiles: CC(C)CC(C(=O)O)N

substrate: L-Leu


enzyme_display_name: glycine oxidase

organism: Bacillus subtilis

substrate_name: glycine

smiles: C(C(=O)O)N

proof_lines: apparent value for mutant enzyme H244N, at 25°C and pH 8.5

enzyme: glycine oxidase

substrate: glycine


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


substrate_name: D-proline

proof_lines: apparent value for mutant enzyme H244F, at 25°C and pH 8.5

substrate: D-proline


substrate_name: D-alanine

smiles: CC(C(=O)O)N

substrate: D-alanine


enzyme_display_name: glutamate synthase (NADPH)

organism: Azospirillum brasilense

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES/KOH; cofactor NADPH

proof_lines: of NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, co-substrate: iodonitrotetrazolium, inhibitor: 2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose

proof_lines: of NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, co-substrate: ferricyanide, inhibitor: 2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose

proof_lines: of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme, acceptor: iodonitrotetrazolium

enzyme: glutamate synthase (NADPH)

substrate: NADPH


substrate_name: iodonitrotetrazolium

proof_lines: of NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, co-substrate: NADPH, inhibitor: 2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose

proof_lines: of NADPH:acceptor oxidoreductase acitivity of the beta subunit of the enzyme

proof_lines: of NADPH: acceptor oxidoreductase activity of the beta subunit of the enzyme

substrate: iodonitrotetrazolium


substrate_name: menadione

substrate: menadione


substrate_name: ferricyanide

proof_lines: of NADPH:acceptor oxidoreductase activity of the beta subunit of the enzyme, co-substrate: NADPH, inhibitor: 2'-phosphoadenosine-5'-diphospho-5'beta-D-ribose

substrate: ferricyanide


proof_lines: in the presence of a fixed concentration of L-glutamine, and varied concentrations of alpha-ketoglutarate

proof_lines: in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of L-glutamine


substrate_name: alpha-ketoglutarate

proof_lines: in the presence of a fixed concentration of NADPH, and varied concentrations of L-glutamine

proof_lines: in the presence of a fixed concentration of NADH, and varied concentrations of L-glutamine

proof_lines: in the presence of a fixed concentration of L-glutamine, and varied concentrations of NADH

substrate: alpha-ketoglutarate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: L-glutamine

smiles: C(CC(=O)N)C(C(=O)O)N

proof_lines: in the presence of a fixed concentration of NADPH, and varied concentrations of alpha-ketoglutarate

proof_lines: in the presence of a fixed concentration of NADH, and varied concentrations of alpha-ketoglutarate

proof_lines: in the presence of a fixed concentration of alpha-ketoglutarate, and varied concentrations of NADPH

substrate: L-glutamine


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Bos taurus

enzyme: glutamate dehydrogenase [NAD(P)+]


proof_lines:
NADH + NH4Cl
NADPH + NH4Cl


smiles: N

proof_lines:
NADPH + 2-oxoglutarate
NADH + 2-oxoglutarate


organism: Gluconobacter oxydans


substrate_name: Unknown

proof_lines: competitive inhibitor with respect to alpha-keto-glutarate

proof_lines: mixed-type inhibition with alpha-ketoglutarate

substrate: Unknown


organism: Glycine max

proof_lines: glutamate dehydrogenase 1, 5 mM 2-oxoglutarate

proof_lines: glutamate dehydrogenase 2, 5 mM 2-oxoglutarate


proof_lines: glutamate dehydrogenase 1, 10 mM 2-oxoglutarate

proof_lines: glutamate dehydrogenase 2, 10 mM 2-oxoglutarate


proof_lines:
glutamate dehydrogenase 2, 0.1 mM NADH
glutamate dehydrogenase 2, 80 mM NH4+
glutamate dehydrogenase 1, 0.1 mM NADH


organism: Haloferax volcanii

proof_lines: lowest Km value in 3.0 M KCl, recombinant wild-type enzyme


organism: Homo sapiens

substrate_name: NADP+

proof_lines: E221A mutant, 1 mM fixed thioproline, thioproline dehydrogenase activity assay

substrate: NADP+


proof_lines: wild type enzyme, 1 mM fixed thioproline, thioproline dehydrogenase activity assay


proof_lines: inhibition of recombinant S448P mutant enzyme


proof_lines: inhibition of recombinant H454Y mutant enzyme


proof_lines: inhibition of recombinant wild-type enzyme


proof_lines: inhibition of recombinant R463A mutant enzyme


organism: Klebsiella aerogenes


organism: Lysinibacillus sphaericus


assay_conditions_summary: pH 10; 303.15 K; cofactor NADH


enzyme_display_name: diaminopimelate dehydrogenase

enzyme: diaminopimelate dehydrogenase


smiles: C(CC(C(=O)O)N)CC(=O)C(=O)O


organism: Plasmodium falciparum


proof_lines:
wild-type, pH 8.0, 25°C
recombinant wild-type enzyme
wild-type, pH 5.0, 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


organism: Pseudomonas fluorescens

substrate_name: methylene blue

proof_lines: specific acceptor, cosubstrate: D-kynurenine

substrate: methylene blue


substrate_name: D-kynurenine

proof_lines: both methylene blue and 2,6-dichlorophenolindophenol specific enzymes

substrate: D-kynurenine


substrate_name: D-tryptophan

substrate: D-tryptophan


organism: Priestia megaterium


organism: Pseudomonas putida


substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

substrate: N-ethylglycine


enzyme_display_name: aralkylamine dehydrogenase (azurin)

organism: Pseudomonas sp.

substrate_name: tyramine

enzyme: aralkylamine dehydrogenase (azurin)

substrate: tyramine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Salmonella enterica subsp. enterica serovar Typhimurium

enzyme: glutamate dehydrogenase (NADP+)


enzyme_display_name: alanine dehydrogenase

organism: Thermus thermophilus

enzyme: alanine dehydrogenase


substrate_name: NAD+

substrate: NAD+


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: UniProt E3NZ06

organism: Danio rerio

source_license: CC BY-NC-ND 4.0

enzyme: UniProt E3NZ06


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

organism: Candida maltosa


enzyme: saccharopine dehydrogenase (NAD+, L-lysine-forming)


substrate_name: L-lysine

smiles: C(CCN)CC(C(=O)O)N

substrate: L-lysine


enzyme_display_name: D-octopine dehydrogenase

organism: Mytilus edulis

substrate_name: D-lysopine

smiles: CC(C(=O)O)NC(CCCCN)C(=O)O

enzyme: D-octopine dehydrogenase

substrate: D-lysopine


smiles: CCC(=O)C(=O)O


organism: Catharanthus roseus

substrate_name: NADPH

substrate: NADPH


substrate_name: L-Orn

substrate: L-Orn


substrate_name: oxaloacetate

proof_lines: L-Lys, with pyruvate and NADPH as cosubstrates

substrate: oxaloacetate


substrate_name: L-Gln

substrate: L-Gln


substrate_name: L-canavanine

smiles: C(CON=C(N)N)C(C(=O)O)N

substrate: L-canavanine


substrate_name: L-Arg

smiles: C(CC(C(=O)O)N)CN=C(N)N

substrate: L-Arg


substrate_name: L-Cys

smiles: C(C(C(=O)O)N)S

substrate: L-Cys


substrate_name: L-citrulline

smiles: C(CC(C(=O)O)N)CNC(=O)N

proof_lines: L-Met, with pyruvate and NADPH as cosubstrate

substrate: L-citrulline


substrate_name: L-His

substrate: L-His


organism: Buccinum undatum

substrate_name: NADH

proof_lines:
foot muscle enzyme
digestive gland enzyme
NAD+, digestive gland enzyme

substrate: NADH


substrate_name: D-octopine

smiles: CC(C(=O)O)NC(CCCN=C(N)N)C(=O)O

proof_lines:
NAD+, foot muscle enzyme
digestive gland enzyme
foot muscle enzyme

substrate: D-octopine


substrate_name: Arg

proof_lines:
digestive gland enzyme
foot muscle enzyme

substrate: Arg


organism: Cerastoderma edule


proof_lines:
with pyruvate as cosubstrate
with 2-ketobutanoate as cosubstrate
with oxaloacetate as cosubstrate


organism: Cerebratulus lacteus


substrate_name: octopine

substrate: octopine


proof_lines: depending on concentration of the cosubstrates NADH and Arg


proof_lines: dependent on concentration of the cosubstrates NADH and pyruvate


organism: Glycymeris glycymeris


substrate_name: Lys

substrate: Lys


proof_lines:
with 2-ketobutanoate as cosubstrate
L-Lys
2-ketobutanoate


substrate_name: NAD+

substrate: NAD+


organism: Pecten jacobaeus


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: saccharopine dehydrogenase (NADP+, L-lysine-forming)

organism: Oryza sativa

substrate_name: L-Lysine; NADPH; H+; 2-Oxoglutarate

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: L-Lysine; NADPH; H+; 2-Oxoglutarate


substrate_name: NADPH

enzyme: saccharopine dehydrogenase (NADP+, L-lysine-forming)

substrate: NADPH


substrate_name: L-lysine

substrate: L-lysine


smiles: C(CCNC(CCC(=O)O)C(=O)O)CC(C(=O)O)N


organism: Concholepas concholepas


organism: Helianthus annuus

substrate_name: L-Orn

substrate: L-Orn


substrate_name: L-Met

smiles: CSCCC(C(=O)O)N

substrate: L-Met


substrate_name: oxaloacetate

substrate: oxaloacetate


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-glutamate-forming)


substrate_name: saccharopine

enzyme: saccharopine dehydrogenase (NAD+, L-glutamate-forming)

substrate: saccharopine


enzyme_display_name: saccharopine dehydrogenase (NADP+, L-glutamate-forming)

organism: Meyerozyma guilliermondii

substrate_name: NADP+

substrate: NADP+


enzyme: saccharopine dehydrogenase (NADP+, L-glutamate-forming)


organism: Glycine max

substrate_name: 2-Oxoglutarate; NADPH; L-Lysine; H+

substrate: 2-Oxoglutarate; NADPH; L-Lysine; H+


organism: Zea mays


organism: Haemonchus contortus

proof_lines: enzyme from L3 larva, at pH 7.0, temperature not specified in the publication

proof_lines: enzyme from adult, at pH 7.0, temperature not specified in the publication


organism: Nautilus pompilius

substrate_name: NADH; Pyruvate; H+; L-Arginine

substrate: NADH; Pyruvate; H+; L-Arginine


smiles: C(CSCC(C(=O)O)N)N


organism: Sorghum bicolor

substrate_name: H+; 2-Oxoglutarate; NADPH; L-Lysine

substrate: H+; 2-Oxoglutarate; NADPH; L-Lysine


organism: Teladorsagia circumcincta


organism: Pecten maximus

substrate_name: L-Arg

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BHM6 and applied mutation signature D329A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM triethanolamine hydrochloride; cofactor NADH

column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'D329A' in the L-arginine substrate group; column 'Km (mmol/L)' = 9.8; column 'kcat (s-1)' = 28; column 'kcat/Km (L mol-1 s-1)' = 2.85 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 28 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 28.0 s^(-1). Km: printed Table 3 cell 9.8 mmol/L; one millimole per litre is one millimolar, so the paper value is 9.8 mM. kcat/Km: printed Table 3 cell 2.85 x 10^3 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.85 x 10^3 / 1000 = 2.85 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'D329A', L-arginine substrate group: kcat = 28 s^-1; Km = 9.8 mmol/L; printed kcat/Km = 2.85 x 10^3 L mol^-1 s^-1.

table_label: Table 3: Kinetic properties of residues potentially involved in the catalytic triad (FEBS J. 274, 6329-6339, 2007)

substrate: L-Arg


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BHM6 and applied mutation signature H212A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'H212A' in the L-arginine substrate group; column 'Km (mmol/L)' = 3.5; column 'kcat (s-1)' = 5.1; column 'kcat/Km (L mol-1 s-1)' = 1.47 x 10^3.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.1 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 5.1 s^(-1). Km: printed Table 3 cell 3.5 mmol/L; one millimole per litre is one millimolar, so the paper value is 3.5 mM. kcat/Km: printed Table 3 cell 1.47 x 10^3 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.47 x 10^3 / 1000 = 1.47 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'H212A', L-arginine substrate group: kcat = 5.1 s^-1; Km = 3.5 mmol/L; printed kcat/Km = 1.47 x 10^3 L mol^-1 s^-1.


substrate_name: NADH

column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'H212A' in the NADH substrate group; column 'Km (mmol/L)' = 64.9 x 10^-3; column 'kcat (s-1)' = 7.3; column 'kcat/Km (L mol-1 s-1)' = 1.13 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 7.3 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 7.3 s^(-1). Km: printed Table 3 cell 64.9 x 10^-3 mmol/L; one millimole per litre is one millimolar, so the paper value is 0.0649 mM. kcat/Km: printed Table 3 cell 1.13 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.13 x 10^5 / 1000 = 113.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'H212A', NADH substrate group: kcat = 7.3 s^-1; Km = 64.9 x 10^-3 mmol/L; printed kcat/Km = 1.13 x 10^5 L mol^-1 s^-1.

substrate: NADH


column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'D329A' in the NADH substrate group; column 'Km (mmol/L)' = 21.4 x 10^-3; column 'kcat (s-1)' = 9.3; column 'kcat/Km (L mol-1 s-1)' = 4.34 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.3 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 9.3 s^(-1). Km: printed Table 3 cell 21.4 x 10^-3 mmol/L; one millimole per litre is one millimolar, so the paper value is 0.0214 mM. kcat/Km: printed Table 3 cell 4.34 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.34 x 10^5 / 1000 = 434.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'D329A', NADH substrate group: kcat = 9.3 s^-1; Km = 21.4 x 10^-3 mmol/L; printed kcat/Km = 4.34 x 10^5 L mol^-1 s^-1.


column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'H212A' in the pyruvate substrate group; column 'Km (mmol/L)' = 59; column 'kcat (s-1)' = 13.0; column 'kcat/Km (L mol-1 s-1)' = 2.17 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13.0 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 13.0 s^(-1). Km: printed Table 3 cell 59 mmol/L; one millimole per litre is one millimolar, so the paper value is 59.0 mM. kcat/Km: printed Table 3 cell 2.17 x 10^2 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.17 x 10^2 / 1000 = 0.217 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'H212A', pyruvate substrate group: kcat = 13.0 s^-1; Km = 59 mmol/L; printed kcat/Km = 2.17 x 10^2 L mol^-1 s^-1.


column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'D329A' in the pyruvate substrate group; column 'Km (mmol/L)' = 33; column 'kcat (s-1)' = 15.4; column 'kcat/Km (L mol-1 s-1)' = 4.64 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 15.4 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 15.4 s^(-1). Km: printed Table 3 cell 33 mmol/L; one millimole per litre is one millimolar, so the paper value is 33.0 mM. kcat/Km: printed Table 3 cell 4.64 x 10^2 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.64 x 10^2 / 1000 = 0.464 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'D329A', pyruvate substrate group: kcat = 15.4 s^-1; Km = 33 mmol/L; printed kcat/Km = 4.64 x 10^2 L mol^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BHM6 and applied mutation signature R324A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'R324A' in the pyruvate substrate group; column 'Km (mmol/L)' = 92; column 'kcat (s-1)' = 22.5; column 'kcat/Km (L mol-1 s-1)' = 2.34 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22.5 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 22.5 s^(-1). Km: printed Table 3 cell 92 mmol/L; one millimole per litre is one millimolar, so the paper value is 92.0 mM. kcat/Km: printed Table 3 cell 2.34 x 10^2 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.34 x 10^2 / 1000 = 0.234 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'R324A', pyruvate substrate group: kcat = 22.5 s^-1; Km = 92 mmol/L; printed kcat/Km = 2.34 x 10^2 L mol^-1 s^-1.


column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'R324A' in the NADH substrate group; column 'Km (mmol/L)' = 90.4 x 10^-3; column 'kcat (s-1)' = 25; column 'kcat/Km (L mol-1 s-1)' = 2.77 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 25 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 25.0 s^(-1). Km: printed Table 3 cell 90.4 x 10^-3 mmol/L; one millimole per litre is one millimolar, so the paper value is 0.0904 mM. kcat/Km: printed Table 3 cell 2.77 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.77 x 10^5 / 1000 = 277.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'R324A', NADH substrate group: kcat = 25 s^-1; Km = 90.4 x 10^-3 mmol/L; printed kcat/Km = 2.77 x 10^5 L mol^-1 s^-1.


column_label: Table 3 (Kinetic properties of residues potentially involved in the catalytic triad), enzyme-form row 'R324A' in the L-arginine substrate group; column 'Km (mmol/L)' = 159; column 'kcat (s-1)' = 43; column 'kcat/Km (L mol-1 s-1)' = 2.70 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 3 cell 43 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 43.0 s^(-1). Km: printed Table 3 cell 159 mmol/L; one millimole per litre is one millimolar, so the paper value is 159.0 mM. kcat/Km: printed Table 3 cell 2.70 x 10^2 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.70 x 10^2 / 1000 = 0.27 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme-form row 'R324A', L-arginine substrate group: kcat = 43 s^-1; Km = 159 mmol/L; printed kcat/Km = 2.70 x 10^2 L mol^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BHM6 and applied mutation signature C148S to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148S' in the NADH substrate group; column 'Km (mmol/L)' = 38.9 x 10^-3; column 'kcat (s-1)' = 410; column 'kcat/Km (L mol-1 s-1)' = 1.05 x 10^7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 410 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 410.0 s^(-1). Km: printed Table 2 cell 38.9 x 10^-3 mmol/L; one millimole per litre is one millimolar, so the paper value is 0.0389 mM. kcat/Km: printed Table 2 cell 1.05 x 10^7 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.05 x 10^7 / 1000 = 10500.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148S', NADH substrate group: kcat = 410 s^-1; Km = 38.9 x 10^-3 mmol/L; printed kcat/Km = 1.05 x 10^7 L mol^-1 s^-1.

table_label: Table 2: Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants (FEBS J. 274, 6329-6339, 2007)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9BHM6 and applied mutation signature C148A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148A' in the NADH substrate group; column 'Km (mmol/L)' = 40 x 10^-3; column 'kcat (s-1)' = 422; column 'kcat/Km (L mol-1 s-1)' = 1.05 x 10^7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 422 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 422.0 s^(-1). Km: printed Table 2 cell 40 x 10^-3 mmol/L; one millimole per litre is one millimolar, so the paper value is 0.04 mM. kcat/Km: printed Table 2 cell 1.05 x 10^7 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.05 x 10^7 / 1000 = 10500.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148A', NADH substrate group: kcat = 422 s^-1; Km = 40 x 10^-3 mmol/L; printed kcat/Km = 1.05 x 10^7 L mol^-1 s^-1.


column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148A' in the L-arginine substrate group; column 'Km (mmol/L)' = 1.6; column 'kcat (s-1)' = 444; column 'kcat/Km (L mol-1 s-1)' = 2.73 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 444 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 444.0 s^(-1). Km: printed Table 2 cell 1.6 mmol/L; one millimole per litre is one millimolar, so the paper value is 1.6 mM. kcat/Km: printed Table 2 cell 2.73 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.73 x 10^5 / 1000 = 273.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148A', L-arginine substrate group: kcat = 444 s^-1; Km = 1.6 mmol/L; printed kcat/Km = 2.73 x 10^5 L mol^-1 s^-1.


column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148S' in the L-arginine substrate group; column 'Km (mmol/L)' = 1.7; column 'kcat (s-1)' = 446; column 'kcat/Km (L mol-1 s-1)' = 2.68 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 446 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 446.0 s^(-1). Km: printed Table 2 cell 1.7 mmol/L; one millimole per litre is one millimolar, so the paper value is 1.7 mM. kcat/Km: printed Table 2 cell 2.68 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.68 x 10^5 / 1000 = 268.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148S', L-arginine substrate group: kcat = 446 s^-1; Km = 1.7 mmol/L; printed kcat/Km = 2.68 x 10^5 L mol^-1 s^-1.


column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148A' in the pyruvate substrate group; column 'Km (mmol/L)' = 2.5; column 'kcat (s-1)' = 499; column 'kcat/Km (L mol-1 s-1)' = 1.98 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 499 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 499.0 s^(-1). Km: printed Table 2 cell 2.5 mmol/L; one millimole per litre is one millimolar, so the paper value is 2.5 mM. kcat/Km: printed Table 2 cell 1.98 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.98 x 10^5 / 1000 = 198.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148A', pyruvate substrate group: kcat = 499 s^-1; Km = 2.5 mmol/L; printed kcat/Km = 1.98 x 10^5 L mol^-1 s^-1.


column_label: Table 2 (Kinetic parameters for the forward reaction (NADH oxidation) catalyzed by recombinant wild-type ODH and Cys148 mutants), enzyme-form row 'C148S' in the pyruvate substrate group; column 'Km (mmol/L)' = 2.6; column 'kcat (s-1)' = 511; column 'kcat/Km (L mol-1 s-1)' = 1.97 x 10^5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 511 s^-1; the turnover column of this table is already per second, so no unit conversion applies and the paper value is 511.0 s^(-1). Km: printed Table 2 cell 2.6 mmol/L; one millimole per litre is one millimolar, so the paper value is 2.6 mM. kcat/Km: printed Table 2 cell 1.97 x 10^5 L mol^-1 s^-1, which is M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.97 x 10^5 / 1000 = 197.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme-form row 'C148S', pyruvate substrate group: kcat = 511 s^-1; Km = 2.6 mmol/L; printed kcat/Km = 1.97 x 10^5 L mol^-1 s^-1.


enzyme_display_name: Octopine dehydrogenase

substrate_name: pyruvate for the reverse reaction of the octopine dehydrogenase activity

proof_lines: The kinetic constants are determined for the recombinant His(5)-tagged protein.

enzyme: Octopine dehydrogenase


substrate_name: L-arginine for the reverse reaction of the octopine dehydrogenase activity


substrate_name: ketobutyrate for the reverse reaction of the octopine dehydrogenase activity


organism: Mytilus edulis

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


substrate_name: NAD+

proof_lines:
NADH, adductor muscle enzyme
adductor muscle enzyme
digestive gland enzyme


substrate_name: octopine

proof_lines:
NADH, gill enzyme
gill enzyme
pyruvate, adductor muscle enzyme

substrate: octopine


substrate_name: pyruvate

proof_lines:
digestive gland enzyme
pyruvate
oxaloacetate


proof_lines:
octopine, foot muscle enzyme
with pyruvate as cosubstrate
with 2-ketobutanoate as cosubstrate


organism: Sepia officinalis

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines:
brain enzyme
mantle muscle enzyme
mantle enzyme


proof_lines: L-Arg, with pyruvate as cosubstrate, brain enzyme


proof_lines:
brain enzyme
mantle enzyme


proof_lines:
NAD+, mantle muscle enzyme
brain enzyme
Arg, brain enzyme


substrate_name: Arg

proof_lines:
pyruvate, mantle muscle enzyme
D-octopine, mantle enzyme
L-Lys, brain enzyme

substrate: Arg


substrate_name: D-lysopine

substrate: D-lysopine


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q9BHM6 and applied mutation signature Q118D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; buffer 50 mM triethanolamine; cofactor NADH

column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row NADH / Q118D; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); NADH / Q118D: Km 175 x 10^-3 mmol L^-1; kcat 47 s^-1; kcat/Km 2.7 x 10^5 L mol^-1 s^-1. The independently printed efficiency normalizes to 270 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

row_label: NADH / Q118D


column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row pyruvate / Q118D; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); pyruvate / Q118D: Km 162 mmol L^-1; kcat 73 s^-1; kcat/Km 4.5 x 10^2 L mol^-1 s^-1. The independently printed efficiency normalizes to 0.45 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

row_label: pyruvate / Q118D

substrate: pyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:Q9BHM6 and applied mutation signature Q118A to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row L-Arg / Q118A; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); L-Arg / Q118A: Km 5.8 mmol L^-1; kcat 120 s^-1; kcat/Km 2.1 x 10^4 L mol^-1 s^-1. The independently printed efficiency normalizes to 21 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

normalized_value_unit_evidence: Km=5.8 mM; kcat=120 s^-1; printed kcat/Km=21 s^-1*mM^-1.

row_label: L-Arg / Q118A


column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row L-Arg / Q118D; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); L-Arg / Q118D: Km 81 mmol L^-1; kcat 122 s^-1; kcat/Km 1.5 x 10^3 L mol^-1 s^-1. The independently printed efficiency normalizes to 1.5 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

normalized_value_unit_evidence: Km=81 mM; kcat=122 s^-1; printed kcat/Km=1.5 s^-1*mM^-1.

row_label: L-Arg / Q118D


column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row NADH / Q118A; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); NADH / Q118A: Km 104 x 10^-3 mmol L^-1; kcat 173 s^-1; kcat/Km 1.7 x 10^6 L mol^-1 s^-1. The independently printed efficiency normalizes to 1700 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

row_label: NADH / Q118A


column_label: Table 5: Activity of different alpha-keto acid substrates; Ketovalerate row; Ketovalerate: Km 49.8 mM; kcat 272 s^-1; kcat/Km 5 L mmol^-1 s^-1.

normalized_value_unit_evidence: Km values are in mM; Table 4 L mol^-1 s^-1 kcat/Km values are normalized to s^-1 mM^-1 by dividing by 1000; Table 5 L mmol^-1 s^-1 equals s^-1 mM^-1.

row_label: Ketovalerate row


column_label: Table 4. Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; row pyruvate / Q118A; columns Km (mmol L^-1), kcat (s^-1), and kcat/Km (L mol^-1 s^-1); pyruvate / Q118A: Km 27 mmol L^-1; kcat 283 s^-1; kcat/Km 1 x 10^4 L mol^-1 s^-1. The independently printed efficiency normalizes to 10 s^-1*mM^-1 and is preserved instead of the quotient-derived export value.

normalized_value_unit_evidence: Km=27 mM; kcat=283 s^-1; printed kcat/Km=10 s^-1*mM^-1.

row_label: pyruvate / Q118A


column_label: Table 5: Activity of different alpha-keto acid substrates; Ketobutyrate row; Ketobutyrate: Km 5.9 mM; kcat 526 s^-1; kcat/Km 90 L mmol^-1 s^-1.

row_label: Ketobutyrate row


raw_value_unit_evidence: Ketobutyrate: Km 5.9 mM; kcat 526 s^-1; kcat/Km 90 L mmol^-1 s^-1.

table_label: Table 5: Activity of different alpha-keto acid substrates


column_label: Table 4: Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; l-Arginine / Wild type row; l-Arginine wild type: Km 0.5 mM; kcat 640 s^-1; kcat/Km 1.28 x 10^6 L mol^-1 s^-1 = 1280 s^-1 mM^-1.

row_label: l-Arginine / Wild type row


column_label: Table 4: Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; NADH / Wild type row; NADH wild type: Km 19.8 x 10^-3 mM; kcat 652 s^-1; kcat/Km 3.3 x 10^7 L mol^-1 s^-1 = 33000 s^-1 mM^-1.

row_label: NADH / Wild type row


column_label: Table 4: Kinetic parameters of the forward reaction (NADH oxidation) catalyzed by recombinant wild-type OcDH and Gln118 mutants; Pyruvate / Wild type row; Pyruvate wild type: Km 0.77 mM; kcat 775 s^-1; kcat/Km 1.0 x 10^6 L mol^-1 s^-1 = 1000 s^-1 mM^-1.

row_label: Pyruvate / Wild type row


proof_lines:
digestive gland enzyme
gill enzyme
Arg, foot muscle enzyme


substrate_name: Lys

substrate: Lys


proof_lines: with 2-ketobutanoate as cosubstrate, brain enzyme

proof_lines: with pyruvate as cosubstrate, mantle enzyme


substrate_name: oxaloacetate

proof_lines:
brain enzyme
D-lysopine, brain enzyme
mantle enzyme


substrate_name: L-Lys

proof_lines:
2-ketobutanoate, brain enzyme
mantle enzyme

substrate: L-Lys


organism: Mytilus galloprovincialis

assay_conditions_summary: pH 6.2; buffer citrate phosphate; cofactor NADH

proof_lines: GST-tagged enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication

proof_lines: crude extract enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication

proof_lines: recombinant enzyme, in 100 mM citrate phosphate buffer, pH 6.2, temperature not specified in the publication


substrate_name: L-lysine

assay_conditions_summary: pH 6.2; buffer 100 mM citrate phosphate; cofactor NADH

substrate: L-lysine


organism: Arabidopsis thaliana

substrate_name: saccharopine

assay_conditions_summary: pH 7

proof_lines: pH 9, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein

proof_lines: pH 7, bifunctional enzyme, lysine-ketoglutarate reductase (EC 1. 5.1.8) and saccharopine dehydrogenase activity (EC 1.5.1.9) occur on a single protein

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 7; cofactor NAD+

substrate: NAD+


proof_lines: The kinetic constants are determined for the recombinant His(5)-tagged protein.


substrate_name: D-octopine

substrate: D-octopine


enzyme_display_name: formyltetrahydrofolate dehydrogenase

organism: Rattus norvegicus

substrate_name: 10-Formyltetrahydrofolate; H2O; NADP+

enzyme: formyltetrahydrofolate dehydrogenase

substrate: 10-Formyltetrahydrofolate; H2O; NADP+


substrate_name: H+; L-Lysine; 2-Oxoglutarate; NADPH

assay_conditions_summary: cofactor NADPH

substrate: H+; L-Lysine; 2-Oxoglutarate; NADPH


organism: Homo sapiens

substrate_name: 2-Oxoglutarate; L-Lysine; NADPH; H+

substrate: 2-Oxoglutarate; L-Lysine; NADPH; H+


substrate_name: 2-Oxoglutarate; H+; L-Lysine; NADPH

substrate: 2-Oxoglutarate; H+; L-Lysine; NADPH


substrate_name: ketovalerate for the reverse reaction of the octopine dehydrogenase activity


substrate_name: L-Orn

substrate: L-Orn


organism: Saccharomyces cerevisiae


enzyme_display_name: saccharopine dehydrogenase (NAD(+), L-lysine-forming)

smiles: O=C(O)CCC(=O)C(=O)O

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


substrate_name: L-Lysine

column_label: Table 1, reverse reaction rows K_Lys, V2/Et, V2/K_Lys Et.

row_label: reverse reaction: lysine

table_label: Table 1

enzyme: saccharopine dehydrogenase (NAD(+), L-lysine-forming)

substrate: L-Lysine


column_label: Table 1, forward reaction rows K_sacc, V1/Et, V1/K_sacc Et.

row_label: forward reaction: saccharopine


substrate_name: NAD+

column_label: Table 1, forward reaction rows K_NAD, V1/Et, V1/K_NAD Et.

row_label: forward reaction: NAD


substrate_name: NADH


enzyme_display_name: Alpha-aminoadipic semialdehyde synthase

substrate_name: lysine (isoform Long at pH 7.5 and 30 degrees Celsius)

enzyme: Alpha-aminoadipic semialdehyde synthase


substrate_name: alpha-ketoglutarate (isoform Long at pH 7.5 and 30 degrees Celsius)


substrate_name: NADPH (isoform Long at pH 7.5 and 30 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor NADPH


substrate_name: saccharopine (isoform Long at pH 7 and 30 degrees Celsius)


substrate_name: NAD (isoform Long at pH 7 and 30 degrees Celsius)


proof_lines: Regulation of the lysine biosynthesis in Pichia guilliermondii


substrate_name: L-lysine


enzyme_display_name: Saccharopine dehydrogenase [NAD(+), L-lysine-forming]

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADH (at pH 6.8 and 22 degrees Celsius)

assay_conditions_summary: pH 6.8; cofactor NADH

substrate: NADH (at pH 6.8 and 22 degrees Celsius)


substrate_name: NAD(+) (at pH 6.8 and 22 degrees Celsius)

assay_conditions_summary: pH 6.8; cofactor NAD+

enzyme: Saccharopine dehydrogenase [NAD(+), L-lysine-forming]


substrate_name: saccharopine (at pH 6.8 and 22 degrees Celsius)


proof_lines:
saccharopine
nicotinamide adenine dinucleotide

substrate: lysine (isoform Long at pH 7.5 and 30 degrees Celsius)


substrate: alpha-ketoglutarate (isoform Long at pH 7.5 and 30 degrees Celsius)


substrate: NADPH (isoform Long at pH 7.5 and 30 degrees Celsius)


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines:
NADP+
Michaelis constants
0.022 mM

substrate: NADP+


substrate_name: saccharopine

proof_lines:
saccharopine
Michaelis constants
0.92 mM

substrate: saccharopine


enzyme_display_name: UniProt P38998

enzyme: UniProt P38998


substrate_name: Orn

smiles: C(CC(C(=O)O)N)CN

proof_lines: The lysopine and octopine dehydrogenase activities of Mytilus edulis are catalyzed by a single enzyme

substrate: Orn


assay_conditions_summary: cofactor NAD+


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADH

substrate: NADH


proof_lines:
wild-type, 25°C, pH 7.2
wild type enzyme, at pH 7.0 and 25°C


proof_lines: wild type enzyme, in 100 mM HEPES, pH 7.0, at 25°C


substrate: L-lysine


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


proof_lines: mutant enzyme H96Q, in 100 mM HEPES, pH 7.0, at 25°C


proof_lines: mutant enzyme K77M, in 100 mM HEPES, pH 7.0, at 25°C


proof_lines: mutant enzyme K77M/H96Q, in 100 mM HEPES, pH 7.0, at 25°C


substrate_name: pyruvate

substrate: pyruvate


substrate_name: alpha-ketoadipate

smiles: C(CC(=O)C(=O)O)CC(=O)O

substrate: alpha-ketoadipate


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: alpha-ketomalonate

proof_lines:
at pH 7.0
at pH 6.0

substrate: alpha-ketomalonate


substrate_name: alpha-ketovalerate

substrate: alpha-ketovalerate


substrate_name: alpha-Ketobutyrate

substrate: alpha-Ketobutyrate


enzyme_display_name: pyrroline-5-carboxylate reductase

assay_conditions_summary: pH 7.8; 308.15 K; cofactor NADPH

enzyme: pyrroline-5-carboxylate reductase


substrate_name: NADH


proof_lines:
cofactor NADPH, pH 7.8, 35°C
cofactor NADH, pH 7.8, 35°C


organism: Aspergillus niger

smiles: N


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: UniProt P0AEZ1

organism: Escherichia coli

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7.2

enzyme: UniProt P0AEZ1


enzyme_display_name: UniProt P42898

enzyme: UniProt P42898


enzyme_display_name: UniProt Q5SLG6

organism: Thermus thermophilus

enzyme: UniProt Q5SLG6


enzyme_display_name: glutamate dehydrogenase (NADP+)

assay_conditions_summary: pH 8; 301.15 K; cofactor NADP+

enzyme: glutamate dehydrogenase (NADP+)


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: glycine oxidase

organism: Bacillus cereus

substrate_name: glyphosate

smiles: C(C(=O)O)NCP(=O)(O)O

proof_lines: mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C

enzyme: glycine oxidase

substrate: glyphosate


proof_lines: mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C


substrate_name: glycine

smiles: C(C(=O)O)N

proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication

substrate: glycine


enzyme_display_name: D-lysopine dehydrogenase

organism: Nicotiana tabacum

enzyme: D-lysopine dehydrogenase

substrate: NADPH


substrate: NADP+


substrate_name: D(+)-lysopine

substrate: D(+)-lysopine


substrate_name: L-lysine

smiles: C(CCN)CC(C(=O)O)N


substrate_name: D-(+)-octopine

substrate: D-(+)-octopine


substrate_name: L-methionine

substrate: L-methionine


substrate_name: L-ornithine

substrate: L-ornithine


substrate_name: L-arginine

substrate: L-arginine


substrate_name: L-glutamine

smiles: C(CC(=O)N)C(C(=O)O)N

substrate: L-glutamine


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-citrulline

substrate: L-citrulline


enzyme_display_name: alanopine dehydrogenase

organism: Aphrodita aculeata

substrate_name: L-Val

smiles: CC(C)C(C(=O)O)N

enzyme: alanopine dehydrogenase

substrate: L-Val


substrate_name: Gly

substrate: Gly


substrate_name: pyruvate

substrate: pyruvate


substrate_name: NAD+

substrate: NAD+


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: meso-Alanopine

substrate: meso-Alanopine


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate