column_label: Table label: Table 4 Kinetic constants. Row: Pcal_1031 | Oxidative deamination | NAD? (the paper's NAD+). Enzyme block: Pcal_1031, section Oxidative deamination. Columns read: Km (mM)a cell 0.028, kcat (s-1)a cell 14, kcat/Km (mM-1 s-1) cell 500. metric: kcat; raw value: 14; raw unit: s^-1; normalized value: 14.0 s^(-1); metric: Km; raw value: 0.028; raw unit: mM; normalized value: 0.028 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 500.0 s^-1 mM^-1; assay condition: Recombinant Pcal_1031, the NAD+-dependent glutamate dehydrogenase (EC 1.4.1.2) of Pyrobaculum calidifontis; the standard assay mixture for oxidative deamination (1 ml, pH 10.5 for Pcal_1031) contained 200 mM Gly-KOH, 50 mM L-glutamate, 1.25 mM NAD(P)+ and 60 nM protein; the standard assays were performed at 50 °C; per Table 4 footnote a, assays were performed at 50 °C, the enzyme was mixed with various concentrations of substrate, and Km and kcat were determined through nonlinear regression analysis of the assay data. Export row conditions: pH 10.5; 323.15 K.

normalized_value_unit_evidence: Pcal_1031 Oxidative deamination row NAD? (the paper's NAD+) of Table 4: kcat 14 s^-1 = 14.0 s^(-1) (no conversion, table already in s^-1); Km 0.028 mM = 0.028 mM (no conversion, table already in mM); kcat/Km 500.0 s^-1 mM^-1 (the table's mM^-1 s^-1 is the same unit as s^-1 mM^-1). In the PDF text extract the superscript plus of NAD+ renders as ?, so the printed row label `NAD?` is the paper's NAD+; the kcat column header `kcat (s-1)a` is the flattened kcat (s^-1) with footnote marker a, the Km header `Km (mM)a` likewise carries footnote marker a, the plus-minus error terms render as ±, and the thousands separator renders as a comma, so the printed cell `5,800` is the paper's 5800.

raw_value_unit_evidence: Table 4 Kinetic constants | header row of Table 4: Enzyme Substrate Km (mM)a kcat (s-1)a kcat/Km (mM-1 s-1); enzyme block anchor rows: Pcal_1031 Oxidative deamination / Reductive amination | row: NAD? 0.028 ± 0.0025 14 ± 0.54 500 | Pcal_1031 Oxidative deamination cells read: kcat = 14 s^-1; Km = 0.028 mM; kcat/Km = 500 mM^-1 s^-1. Table 4 footnote a: Assays were performed at 50 °C as described in Materials and methods. In these assays, the enzyme was mixed with various concentrations of substrate. Km and kcat were determined through nonlinear regression analysis of the assay data.


enzyme_display_name: glutamate dehydrogenase

organism: Pyrobaculum calidifontis

substrate_name: NADH

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NADH

column_label: Table label: Table 4 Kinetic constants. Row: Pcal_1031 | Reductive amination | NADH. Enzyme block: Pcal_1031, section Reductive amination. Columns read: Km (mM)a cell 0.010, kcat (s-1)a cell 58, kcat/Km (mM-1 s-1) cell 5,800. metric: kcat; raw value: 58; raw unit: s^-1; normalized value: 58.0 s^(-1); metric: Km; raw value: 0.010; raw unit: mM; normalized value: 0.01 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 5800.0 s^-1 mM^-1; assay condition: Recombinant Pcal_1031, the NAD+-dependent glutamate dehydrogenase (EC 1.4.1.2) of Pyrobaculum calidifontis; the standard assay mixture for reductive amination (1 ml, pH 9.5 for Pcal_1031) contained 200 mM Gly-KOH, 10 mM 2-oxoglutarate, 200 mM NH4Cl, 0.2 mM NAD(P)H and 6 nM protein; the standard assays were performed at 50 °C; per Table 4 footnote a, assays were performed at 50 °C, the enzyme was mixed with various concentrations of substrate, and Km and kcat were determined through nonlinear regression analysis of the assay data. Export row conditions: pH 9.5; 323.15 K.

normalized_value_unit_evidence: Pcal_1031 Reductive amination row NADH of Table 4: kcat 58 s^-1 = 58.0 s^(-1) (no conversion, table already in s^-1); Km 0.010 mM = 0.01 mM (no conversion, table already in mM); kcat/Km 5800.0 s^-1 mM^-1 (the table's mM^-1 s^-1 is the same unit as s^-1 mM^-1). In the PDF text extract the superscript plus of NAD+ renders as ?, so the printed row label `NAD?` is the paper's NAD+; the kcat column header `kcat (s-1)a` is the flattened kcat (s^-1) with footnote marker a, the Km header `Km (mM)a` likewise carries footnote marker a, the plus-minus error terms render as ±, and the thousands separator renders as a comma, so the printed cell `5,800` is the paper's 5800.

raw_value_unit_evidence: Table 4 Kinetic constants | header row of Table 4: Enzyme Substrate Km (mM)a kcat (s-1)a kcat/Km (mM-1 s-1); enzyme block anchor rows: Pcal_1031 Oxidative deamination / Reductive amination | row: NADH 0.010 ± 0.0013 58 ± 2.4 5,800 | Pcal_1031 Reductive amination cells read: kcat = 58 s^-1; Km = 0.010 mM; kcat/Km = 5,800 mM^-1 s^-1. Table 4 footnote a: Assays were performed at 50 °C as described in Materials and methods. In these assays, the enzyme was mixed with various concentrations of substrate. Km and kcat were determined through nonlinear regression analysis of the assay data.

row_label: Pcal_1031 | Reductive amination | NADH

table_label: Table 4 Kinetic constants

data_origin: experimental

enzyme: glutamate dehydrogenase

substrate: NADH

status: verified

source: oed


kcat_over_km_display: Not reported

smiles: N

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+

column_label: Table label: Table 4 Kinetic constants. Row: Pcal_1031 | Reductive amination | Ammonia. Enzyme block: Pcal_1031, section Reductive amination. Columns read: Km (mM)a cell 9.8, kcat (s-1)a cell 58, kcat/Km (mM-1 s-1) cell 5.9. metric: kcat; raw value: 58; raw unit: s^-1; normalized value: 58.0 s^(-1); metric: Km; raw value: 9.8; raw unit: mM; normalized value: 9.8 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 5.918367346938775 s^-1 mM^-1; assay condition: Recombinant Pcal_1031, the NAD+-dependent glutamate dehydrogenase (EC 1.4.1.2) of Pyrobaculum calidifontis; the standard assay mixture for reductive amination (1 ml, pH 9.5 for Pcal_1031) contained 200 mM Gly-KOH, 10 mM 2-oxoglutarate, 200 mM NH4Cl, 0.2 mM NAD(P)H and 6 nM protein; the standard assays were performed at 50 °C; per Table 4 footnote a, assays were performed at 50 °C, the enzyme was mixed with various concentrations of substrate, and Km and kcat were determined through nonlinear regression analysis of the assay data. Export row conditions: pH 9.5; 323.15 K.

normalized_value_unit_evidence: Pcal_1031 Reductive amination row Ammonia of Table 4: kcat 58 s^-1 = 58.0 s^(-1) (no conversion, table already in s^-1); Km 9.8 mM = 9.8 mM (no conversion, table already in mM); kcat/Km 5.918367346938775 s^-1 mM^-1 (the table's mM^-1 s^-1 is the same unit as s^-1 mM^-1). In the PDF text extract the superscript plus of NAD+ renders as ?, so the printed row label `NAD?` is the paper's NAD+; the kcat column header `kcat (s-1)a` is the flattened kcat (s^-1) with footnote marker a, the Km header `Km (mM)a` likewise carries footnote marker a, the plus-minus error terms render as ±, and the thousands separator renders as a comma, so the printed cell `5,800` is the paper's 5800.

raw_value_unit_evidence: Table 4 Kinetic constants | header row of Table 4: Enzyme Substrate Km (mM)a kcat (s-1)a kcat/Km (mM-1 s-1); enzyme block anchor rows: Pcal_1031 Oxidative deamination / Reductive amination | row: Ammonia 9.8 ± 0.36 58 ± 1.9 5.9 | Pcal_1031 Reductive amination cells read: kcat = 58 s^-1; Km = 9.8 mM; kcat/Km = 5.9 mM^-1 s^-1. Table 4 footnote a: Assays were performed at 50 °C as described in Materials and methods. In these assays, the enzyme was mixed with various concentrations of substrate. Km and kcat were determined through nonlinear regression analysis of the assay data.


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

column_label: Table label: Table 4 Kinetic constants. Row: Pcal_1031 | Reductive amination | 2-Oxoglutarate. Enzyme block: Pcal_1031, section Reductive amination. Columns read: Km (mM)a cell 0.92, kcat (s-1)a cell 65, kcat/Km (mM-1 s-1) cell 71. metric: kcat; raw value: 65; raw unit: s^-1; normalized value: 65.0 s^(-1); metric: Km; raw value: 0.92; raw unit: mM; normalized value: 0.92 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 70.65217391304347 s^-1 mM^-1; assay condition: Recombinant Pcal_1031, the NAD+-dependent glutamate dehydrogenase (EC 1.4.1.2) of Pyrobaculum calidifontis; the standard assay mixture for reductive amination (1 ml, pH 9.5 for Pcal_1031) contained 200 mM Gly-KOH, 10 mM 2-oxoglutarate, 200 mM NH4Cl, 0.2 mM NAD(P)H and 6 nM protein; the standard assays were performed at 50 °C; per Table 4 footnote a, assays were performed at 50 °C, the enzyme was mixed with various concentrations of substrate, and Km and kcat were determined through nonlinear regression analysis of the assay data. Export row conditions: pH 9.5; 323.15 K.

normalized_value_unit_evidence: Pcal_1031 Reductive amination row 2-Oxoglutarate of Table 4: kcat 65 s^-1 = 65.0 s^(-1) (no conversion, table already in s^-1); Km 0.92 mM = 0.92 mM (no conversion, table already in mM); kcat/Km 70.65217391304347 s^-1 mM^-1 (the table's mM^-1 s^-1 is the same unit as s^-1 mM^-1). In the PDF text extract the superscript plus of NAD+ renders as ?, so the printed row label `NAD?` is the paper's NAD+; the kcat column header `kcat (s-1)a` is the flattened kcat (s^-1) with footnote marker a, the Km header `Km (mM)a` likewise carries footnote marker a, the plus-minus error terms render as ±, and the thousands separator renders as a comma, so the printed cell `5,800` is the paper's 5800.

raw_value_unit_evidence: Table 4 Kinetic constants | header row of Table 4: Enzyme Substrate Km (mM)a kcat (s-1)a kcat/Km (mM-1 s-1); enzyme block anchor rows: Pcal_1031 Oxidative deamination / Reductive amination | row: 2-Oxoglutarate 0.92 ± 0.0078 65 ± 1.1 71 | Pcal_1031 Reductive amination cells read: kcat = 65 s^-1; Km = 0.92 mM; kcat/Km = 71 mM^-1 s^-1. Table 4 footnote a: Assays were performed at 50 °C as described in Materials and methods. In these assays, the enzyme was mixed with various concentrations of substrate. Km and kcat were determined through nonlinear regression analysis of the assay data.


organism: Peptoniphilus asaccharolyticus

substrate_name: glutamate

source_db: brenda

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

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

assay_conditions_summary: pH 7; cofactor NAD+

substrate: glutamate

source: brenda


substrate_name: NADPH

verification_status: corrected

assay_conditions_summary: pH 7; cofactor NADP+

normalized_value_unit_evidence: Km 1.640 mM; kcat 12 s^-1; table kcat/Km 7.3 s^-1*mM^-1; exported kcat/Km 7.317073170731708 is rounding-consistent with 12/1.64

raw_value_unit_evidence: Table 3 row NADPH: concentration range 50-250 uM; Km 1640 +/- 252 uM; kcat 12 +/- 2.9 s^-1; kcat/Km 7.3 x 10^-3 uM^-1 s^-1

row_label: NADPH

table_label: Table 3 Kinetic parameters calculated for Pa GDH at pH 7

substrate: NADPH

status: corrected


column_label: NH4+ row lines 365-366, 374, 382, 390, 398; Fig. 3 caption lines 337-340 identifies NH4Cl

normalized_value_unit_evidence: Km 144 mM; kcat 20.4 s^-1; table kcat/Km 0.14 s^-1*mM^-1; exported kcat/Km 0.14166666666666666 is rounding-consistent with 20.4/144

row_label: NH4+ / NH4Cl


assay_conditions_summary: pH 7; cofactor NADPH

normalized_value_unit_evidence: Km 0.0044 mM; kcat 31.4 s^-1; table kcat/Km 7140 s^-1*mM^-1; exported kcat/Km 7136.363636363636 is rounding-consistent with 31.4/0.0044

raw_value_unit_evidence: Table 3 row NADH: concentration range 5-30 uM; Km 4.4 +/- 0.4 uM; kcat 31.4 +/- 7.23 s^-1; kcat/Km 7.14 uM^-1 s^-1

row_label: NADH


enzyme_display_name: alanine dehydrogenase

organism: Rhizobium sp.

kcat_display: Not reported

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

assay_conditions_summary: cofactor NADH

column_label: PubMed abstract states apparent Michaelis constants for NADH, NH4+, pyruvate, L-alanine, and NAD were 86 microM, 8.9 mM, 0.49 mM, 1 mM, and 200 microM, respectively.

raw_value_unit_evidence: Km raw_value=86 raw_unit=microM for NADH

row_label: NADH in apparent Michaelis constants sentence

table_label: PubMed abstract PMID 8346914

enzyme: alanine dehydrogenase


substrate_name: L-Ala

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

raw_value_unit_evidence: Km raw_value=1 raw_unit=mM for L-alanine

row_label: L-alanine in apparent Michaelis constants sentence

substrate: L-Ala


substrate_name: pyruvate

raw_value_unit_evidence: Km raw_value=0.49 raw_unit=mM for pyruvate

row_label: pyruvate in apparent Michaelis constants sentence

substrate: pyruvate


raw_value_unit_evidence: Km raw_value=8.9 raw_unit=mM for NH4+

row_label: NH4+ in apparent Michaelis constants sentence


enzyme_display_name: glutamate dehydrogenase (NADP(+))

organism: Thermococcus waiotapuensis

substrate_name: L-glutamate

verification_status: unverified

kcat_over_km_origin: calculated

enzyme: glutamate dehydrogenase (NADP(+))

substrate: L-glutamate

status: unverified


substrate_name: NADP+

assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+

substrate: NADP+


organism: Klebsiella aerogenes

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

column_label: J-STAGE/PubMed abstract and rendered official PDF page 1 map NAD+ to Km 0.16 mM

raw_value_unit_evidence: Km 0.16 mM for NAD+

row_label: Km values list: L-alanine, NAD+, pyruvate, NADH, ammonia

table_label: J-STAGE/PubMed abstract; official PDF page 1

substrate: NAD+


assay_conditions_summary: pH 8.7; cofactor NAD+

column_label: J-STAGE/PubMed abstract and rendered official PDF page 1 map pyruvate to Km 0.22 mM

raw_value_unit_evidence: Km 0.22 mM for pyruvate


assay_conditions_summary: pH 10.9; cofactor NAD+

column_label: J-STAGE/PubMed abstract and rendered official PDF page 1 map L-alanine to Km 0.47 mM

raw_value_unit_evidence: Km 0.47 mM for L-alanine


column_label: J-STAGE/PubMed abstract and rendered official PDF page 1 map ammonia to Km 66.7 mM

raw_value_unit_evidence: Km 66.7 mM for ammonia


organism: Streptomyces clavuligerus

column_label: Abstract reports pyruvate (Km = 1.1 mM), ammonia (Km = 20 mM) and NADH (Km = 0.14 mM) were required for reductive amination.

raw_value_unit_evidence: Km raw_value=0.14 mM raw_unit=mM

row_label: Streptomyces clavuligerus alanine dehydrogenase / NADH

table_label: PubMed XML abstract PMID 7387330


raw_value_unit_evidence: Km raw_value=20 mM raw_unit=mM

row_label: Streptomyces clavuligerus alanine dehydrogenase / ammonia


enzyme_display_name: valine dehydrogenase (NADP+)

organism: Streptomyces fradiae

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

enzyme: valine dehydrogenase (NADP+)


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


substrate_name: L-valine

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

substrate: L-valine


substrate_name: L-leucine

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

substrate: L-leucine


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


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


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-norvaline

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

substrate: L-norvaline


smiles: CCCC(=O)C(=O)O


smiles: CCCCC(=O)C(=O)[O-]


enzyme_display_name: leucine dehydrogenase

organism: [Bacillus] caldolyticus

enzyme: leucine dehydrogenase


smiles: CSCCC(=O)C(=O)[O-]


substrate_name: L-Met

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

substrate: L-Met


organism: Clostridium symbiosum

substrate_name: L-Glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:P24295 and applied mutation signature A163G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

column_label: PDF page 5, Table 3, A163G / Glu / pH 8.0 row, Km, kcat, kcat/Km columns

table_label: PMID 11722565 Table 3. Kinetic parameters for glutamate and 2-oxoglutarate

substrate: L-Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_reviewed:P24295 and applied mutation signature S380A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PDF page 5, Table 3, S380A / Glu / pH 7.0 row, Km, kcat, kcat/Km columns


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: PDF page 5, Table 3, S380A / Glu / pH 8.0 row, Km, kcat, kcat/Km columns


column_label: PDF page 5, Table 3, WT / Glu / pH 7.0 row, Km, kcat, kcat/Km columns

row_label: WT / Glu / pH 7.0


column_label: PDF page 5, Table 3, WT / Glu / pH 8.0 row, Km, kcat, kcat/Km columns

row_label: WT / Glu / pH 8.0


substrate_name: L-Ile

substrate: L-Ile


substrate_name: L-Leu

substrate: L-Leu


substrate_name: L-tert-Leu

substrate: L-tert-Leu


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


substrate_name: L-Val

substrate: L-Val


substrate_name: L-norleucine

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

substrate: L-norleucine


organism: Kitasatospora aureofaciens


substrate_name: L-methionine

substrate: L-methionine


substrate_name: L-alanine

substrate: L-alanine


organism: Streptomyces virginiae


substrate_name: pyruvate

substrate: pyruvate


organism: Streptomyces albus

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


substrate_name: NADH

substrate: NADH


enzyme_display_name: 2,4-diaminopentanoate dehydrogenase

organism: Fervidobacterium nodosum

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

enzyme: 2,4-diaminopentanoate dehydrogenase


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 328.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 328.15 K; cofactor NAD+

substrate: NAD+


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Lathyrus oleraceus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


assay_conditions_summary: cofactor NADP+


substrate_name: L-valine

substrate: L-valine


enzyme_display_name: glutamate synthase (NADH)

organism: Derxia gummosa

enzyme: glutamate synthase (NADH)


substrate_name: L-glutamine

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

substrate: L-glutamine


organism: Streptomyces coelicolor


enzyme_display_name: glutamate synthase (NADPH)

organism: Sclerotinia sclerotiorum

enzyme: glutamate synthase (NADPH)


substrate_name: alpha-ketoglutarate

substrate: alpha-ketoglutarate


organism: Bacillus subtilis

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

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

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


organism: Escherichia coli

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

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


substrate_name: NADH; H+; 2-Oxoglutarate; L-Glutamine

substrate: NADH; H+; 2-Oxoglutarate; L-Glutamine


organism: Pseudoalteromonas sp. ANT 178

substrate_name: L-leucine

assay_conditions_summary: pH 9; 303.15 K; buffer pH 10; cofactor NAD+

column_label: PMID 30275355 Table 3 'Substrate specificity analysis of rPsLeuDH', row L-lecine, columns Km (mM), kcat (1/s), kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row L-lecine: Km=0.33 mM; kcat=30.13 1/s; kcat/Km=91.30 mM^-1 s^-1.

row_label: L-lecine

table_label: Table 3. Substrate specificity analysis of rPsLeuDH.

substrate: L-leucine


substrate_name: L-tyrosine

column_label: PMID 30275355 Table 3 'Substrate specificity analysis of rPsLeuDH', row L-tyrosine, columns Km (mM), kcat (1/s), kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: paper normalized: km=0.48 mM; kcat=26.39 s^-1; kcat_over_km=54.98 s^-1*mM^-1. export: km=0.48 mM; kcat=26.4 s^-1; kcat_over_km=55.0 s^-1*mM^-1.

raw_value_unit_evidence: Table 3 row L-tyrosine: Km=0.48 mM; kcat=26.39 1/s; kcat/Km=54.98 mM^-1 s^-1.

row_label: L-tyrosine

substrate: L-tyrosine


substrate_name: L-proline

column_label: PMID 30275355 Table 3 'Substrate specificity analysis of rPsLeuDH', row L-proline, columns Km (mM), kcat (1/s), kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: paper normalized: km=0.64 mM; kcat=20.80 s^-1; kcat_over_km=32.50 s^-1*mM^-1. export: km=0.64 mM; kcat=20.8 s^-1; kcat_over_km=32.5 s^-1*mM^-1.

raw_value_unit_evidence: Table 3 row L-proline: Km=0.64 mM; kcat=20.80 1/s; kcat/Km=32.50 mM^-1 s^-1.

row_label: L-proline

substrate: L-proline


substrate_name: DL-methionine

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

column_label: PMID 30275355 Table 3 'Substrate specificity analysis of rPsLeuDH', row DL-methionine, columns Km (mM), kcat (1/s), kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row DL-methionine: Km=0.75 mM; kcat=16.57 1/s; kcat/Km=22.09 mM^-1 s^-1.

row_label: DL-methionine

substrate: DL-methionine


substrate_name: L-Arginine

column_label: PMID 30275355 Table 3 'Substrate specificity analysis of rPsLeuDH', row L-arginine, columns Km (mM), kcat (1/s), kcat/Km (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row L-arginine: Km=0.84 mM; kcat=14.09 1/s; kcat/Km=16.77 mM^-1 s^-1.

row_label: L-arginine

substrate: L-Arginine


organism: Amycolatopsis mediterranei


organism: Euglena gracilis


enzyme_display_name: lysine dehydrogenase

organism: Agrobacterium tumefaciens

enzyme: lysine dehydrogenase


substrate_name: deamino-NAD+

substrate: deamino-NAD+


organism: Thiobacillus thioparus


enzyme_display_name: glycine dehydrogenase

organism: Mycobacterium tuberculosis

substrate_name: NADH

enzyme: glycine dehydrogenase

substrate: NADH


smiles: N


organism: Bacillus methanolicus

substrate_name: L-glutamate

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

substrate: L-glutamate


organism: Priestia megaterium


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


substrate_name: NAD+

assay_conditions_summary: pH 10.5; cofactor NAD+

substrate: NAD+


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


organism: Alloalcanivorax dieselolei

assay_conditions_summary: pH 7; cofactor NADH

proof_lines: pH 7.0, temperature not specified in the publication


assay_conditions_summary: pH 7


substrate_name: glyoxylate

proof_lines:
aerobic aerated bacilli - AB
anaerobic resting bacilli - RB
pH 8.5, 22°C, recombinant enzyme

substrate: glyoxylate


organism: Brevibacterium L5

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


organism: Streptomyces virginiae


organism: Exiguobacterium artemiae

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

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Table 4 columns Substrate/Km/Vmax/kcat/kcat/Km; unit row gives Km=(mM), kcat=(s^-1), kcat/Km=(L*mmol^-1*s^-1), numerically equivalent to s^-1*mM^-1.

raw_value_unit_evidence: Table 4 L-Leucine row: Km=0.88 mM; kcat=4.31 s^-1; kcat/Km=4.90 L*mmol^-1*s^-1.

row_label: L-Leucine

table_label: Table 4: Steady-state kinetic constants of EsiLeuDH


assay_conditions_summary: pH 9.5; cofactor NAD+


raw_value_unit_evidence: Table 4 NAD row: Km=1.46 mM; kcat=8.41 s^-1; kcat/Km=5.76 L*mmol^-1*s^-1.

row_label: NAD


substrate_name: trimethylpyruvate

assay_conditions_summary: pH 8.5; cofactor NADH

row_label: TMP

substrate: trimethylpyruvate


row_label: NADH


assay_conditions_summary: pH 9.5; cofactor NADH


organism: Laceyella sacchari


organism: Citrobacter freundii

proof_lines: pH not specified in the publication, temperature not specified in the publication


organism: Natrialba magadii

substrate_name: L-Ile

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

substrate: L-Ile


substrate_name: L-Val

substrate: L-Val


organism: Azospirillum brasilense

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G298A to reconstruct the assayed variant sequence.

proof_lines: of NADPH: iodonitrotetrazolium oxidoreductase activity of the G298A-beta subunit

substrate: NADPH


substrate_name: Unknown

proof_lines: inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit

substrate: Unknown


organism: Bacillus licheniformis


organism: [Brevibacterium] flavum

proof_lines: competitive inhibitor with respect to glutamine

proof_lines: uncompetitive inhibitor with respect to alpha-ketoglutarate

proof_lines: uncompetitive inhibitor with respect to NADPH


enzyme_display_name: Glutamate synthase [NADH]

organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

source_db: uniprot

enzyme: Glutamate synthase [NADH]

source: uniprot


organism: Roseibium aggregatum

substrate_name: L-tert-leucine

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

assay_conditions_summary: pH 8

substrate: L-tert-leucine


assay_conditions_summary: pH 8; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D153N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H191N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P130V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D153N/H191N to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; cofactor NAD+


organism: Fusobacterium nucleatum (subsp. nucleatum)

substrate_name: NAD+; (3S,5S)-3,5-Diaminohexanoate; H2O

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_source: multiple

assay_conditions_summary: cofactor NAD+

substrate: NAD+; (3S,5S)-3,5-Diaminohexanoate; H2O


substrate_name: H+; NADPH; Iodonitrotetrazolium

substrate: H+; NADPH; Iodonitrotetrazolium


organism: Saccharomyces cerevisiae

substrate_name: 2-Oxoglutarate; NADH; L-Glutamine; H+

assay_conditions_summary: cofactor NADH

substrate: 2-Oxoglutarate; NADH; L-Glutamine; H+


organism: Streptomyces albus

substrate_name: H2O; L-Valine; NAD+

substrate: H2O; L-Valine; NAD+


organism: Streptomyces fradiae

substrate_name: L-Valine; H2O; NAD+

assay_conditions_summary: pH 10.6; cofactor NAD+

column_label: Abstract/prose Michaelis-constant sentence reports Km 0.029 mM for NAD+ in the L-valine oxidative deamination context.

normalized_value_unit_evidence: Km 0.029 mM; exported Km 0.029 mM.

raw_value_unit_evidence: Abstract/prose states Km 0.029 mM for NAD+ in the L-valine oxidative deamination context.

row_label: NAD+ cofactor in L-valine oxidative deamination

substrate: L-Valine; H2O; NAD+


enzyme_display_name: Leucine dehydrogenase

organism: Thermoactinomyces intermedius

column_label: Table 3 row 2-Oxo-3-methylvaleate; column K_m (mM); PDF page 4.

raw_value_unit_evidence: Table 3 row 2-Oxo-3-methylvaleate: relative activity=82%; K_m=2.2 mM.

table_label: Table 3

enzyme: Leucine dehydrogenase


enzyme_display_name: Glutamate synthase [NADPH] large chain

organism: Escherichia coli (strain K12)

enzyme: Glutamate synthase [NADPH] large chain


substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: Glutamate synthase [NADPH] small chain

enzyme: Glutamate synthase [NADPH] small chain


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

assay_conditions_summary: pH 10.5; cofactor NADH

column_label: Kinetic mechanism text reports 2-Oxoisocaproate K value 1 mM; normalized 1 mM.

raw_value_unit_evidence: Km raw_value=1 raw_unit=mM; reductive amination K value for 2-oxoisocaproate

table_label: Kinetic mechanism section K values for leucine dehydrogenase

source_databases_merged: brenda uniprot


substrate_name: L-Leu

column_label: Kinetic mechanism text reports L-Leucine K value 2.1 mM; normalized 2.1 mM.

raw_value_unit_evidence: Km raw_value=2.1 raw_unit=mM; oxidative deamination K value for L-leucine

substrate: L-Leu


column_label: Kinetic mechanism text reports 2-Oxovalerate K value 2.4 mM; normalized 2.4 mM.

raw_value_unit_evidence: Km raw_value=2.4 raw_unit=mM; reductive amination K value for 2-oxovalerate


column_label: Kinetic mechanism text reports L-Isoleucine K value 3.3 mM; normalized 3.3 mM.

raw_value_unit_evidence: Km raw_value=3.3 raw_unit=mM; oxidative deamination K value for L-isoleucine

row_label: L-Isoleucine


column_label: Kinetic mechanism text reports 2-Oxoisovalerate K value 3.8 mM; normalized 3.8 mM.

raw_value_unit_evidence: Km raw_value=3.8 raw_unit=mM; reductive amination K value for 2-oxoisovalerate


column_label: Kinetic mechanism text reports L-Valine K value 12.5 mM; normalized 12.5 mM.

raw_value_unit_evidence: Km raw_value=12.5 raw_unit=mM; oxidative deamination K value for L-valine

row_label: L-Valine


column_label: Kinetic mechanism text reports Ammonia K value 330 mM; normalized 330 mM.

raw_value_unit_evidence: Km raw_value=330 raw_unit=mM; reductive amination K value for ammonia

row_label: Ammonia


substrate_name: NAD(+)

column_label: Kinetic mechanism text reports NAD+ K value 0.31 mM; normalized 0.31 mM.

raw_value_unit_evidence: Km raw_value=0.31 raw_unit=mM; oxidative deamination K value for NAD+

row_label: NAD+

substrate: NAD(+)


smiles: CCCC(=O)C(=O)O


organism: Bacillus cereus

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D126E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 303.15 K; buffer Tris-HCl; cofactor NADH

column_label: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row D126E; substrate NADH.

raw_value_unit_evidence: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH row D126E; substrate NADH: Km = 0.27 +/- 0.02 mM; kcat = 50.92 +/- 5.95 s^-1; kcat/Km = 188.59 mM^-1 s^-1.

row_label: D126E; substrate NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E116V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E116V; substrate NADH.

normalized_value_unit_evidence: Paper normalized values: Km 0.25 mM; kcat 60.48 s^-1; kcat/Km 241.92 s^-1*mM^-1. Export values: Km 0.25 mM; kcat 60.5 s^-1; kcat/Km 242.0 s^-1*mM^-1.

raw_value_unit_evidence: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH row E116V; substrate NADH: Km = 0.25 +/- 0.03 mM; kcat = 60.48 +/- 7.84 s^-1; kcat/Km = 241.92 mM^-1 s^-1.

row_label: E116V; substrate NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E24A/D126E with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E24A/D126E; substrate NADH.

raw_value_unit_evidence: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH row E24A/D126E; substrate NADH: Km = 0.154 +/- 0.009 mM; kcat = 42.62 +/- 3.01 s^-1; kcat/Km = 276.75 mM^-1 s^-1.

row_label: E24A/D126E; substrate NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E24V/E116V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E24V/E116V; substrate NADH.

normalized_value_unit_evidence: Paper normalized values: Km 0.100 mM; kcat 35.09 s^-1; kcat/Km 350.90 s^-1*mM^-1. Export values: Km 0.1 mM; kcat 35.1 s^-1; kcat/Km 351.0 s^-1*mM^-1.

raw_value_unit_evidence: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH row E24V/E116V; substrate NADH: Km = 0.100 +/- 0.003 mM; kcat = 35.09 +/- 3.78 s^-1; kcat/Km = 350.90 mM^-1 s^-1.

row_label: E24V/E116V; substrate NADH


assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH

column_label: Official Springer Table 2 row Wild type, columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km 0.28 mM; kcat 33.71 s^-1; printed kcat/Km 118.46 mM^-1 s^-1; exported kcat/Km 120.35714285714286 is within displayed-cell/assay precision but not the printed ratio.

row_label: Wild type

table_label: Table 2: Kinetic parameters of the wild type and mutant LeuDHs for substrates NADH


column_label: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row D126E; substrate TMP.

raw_value_unit_evidence: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP row D126E; substrate TMP: Km = 23.17+/-2.21 mM; kcat = 77.36 +/- 5.92 s^-1; kcat/Km = 3.34 mM^-1 s^-1.

row_label: D126E; substrate TMP


column_label: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E116V; substrate TMP.

normalized_value_unit_evidence: Paper normalized values: Km 10.74 mM; kcat 60.49 s^-1; kcat/Km 5.63 s^-1*mM^-1. Export values: Km 10.7 mM; kcat 60.5 s^-1; kcat/Km 5.654205607476636 s^-1*mM^-1.

raw_value_unit_evidence: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP row E116V; substrate TMP: Km = 10.74+/-2.33 mM; kcat = 60.49 +/- 4.54 s^-1; kcat/Km = 5.63 mM^-1 s^-1.

row_label: E116V; substrate TMP


column_label: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E24A/D126E; substrate TMP.

normalized_value_unit_evidence: Paper normalized values: Km 17.57 mM; kcat 93.27 s^-1; kcat/Km 5.31 s^-1*mM^-1. Export values: Km 17.6 mM; kcat 93.3 s^-1; kcat/Km 5.301136363636363 s^-1*mM^-1.

raw_value_unit_evidence: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP row E24A/D126E; substrate TMP: Km = 17.57+/-2.30 mM; kcat = 93.27 +/- 5.50 s^-1; kcat/Km = 5.31 mM^-1 s^-1.

row_label: E24A/D126E; substrate TMP


column_label: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP; columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); row E24V/E116V; substrate TMP.

normalized_value_unit_evidence: Paper normalized values: Km 7.92 mM; kcat 66.21 s^-1; kcat/Km 8.36 s^-1*mM^-1. Export values: Km 7.9 mM; kcat 66.2 s^-1; kcat/Km 8.379746835443038 s^-1*mM^-1.

raw_value_unit_evidence: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP row E24V/E116V; substrate TMP: Km = 7.92+/-1.11 mM; kcat = 66.21 +/- 4.89 s^-1; kcat/Km = 8.36 mM^-1 s^-1.

row_label: E24V/E116V; substrate TMP


column_label: Official Springer Table 1 row Wild type, columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1).

normalized_value_unit_evidence: Km 60.82 mM; kcat 94.14 s^-1; printed kcat/Km 1.55 mM^-1 s^-1, matching the exported values within displayed precision.

table_label: Table 1: Kinetic parameters of the wild type and mutant LeuDHs for substrates TMP


organism: Exiguobacterium sibiricum

substrate_name: L-leucine

substrate: L-leucine


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: trimethylpyruvate

column_label: Table label: TABLE 4. Steady-state kinetic constants of EsiLeuDH. Row: TMP. Columns read: K m (mM) cell 5.96, k cat (s^-1) cell 45.43, k cat / K m (L mmol^-1 s^-1) cell 7.62. metric: kcat; raw value: 45.43; raw unit: s^-1; normalized value: 45.4 s^(-1) at the export's stored precision; metric: Km; raw value: 5.96; raw unit: mM; normalized value: 5.96 mM; metric: kcat/Km; raw value: 7.62; raw unit: L mmol^-1 s^-1; normalized value: 7.61744966442953 s^-1 mM^-1 as stored by the export, agreeing with the printed cell 7.62 at the printed cell's own precision; assay condition: kinetic parameters from Lineweaver-Burk plots, kcat and kcat/Km calculated based on the molecular weight of the enzyme, TMP varied from 2 to 50 mM with NADH fixed at 0.3 mM. Export row conditions: pH 8.5; 303.15 K.

normalized_value_unit_evidence: Table 4 row TMP: Km 5.96 mM = 5.96 mM (already in the export unit); kcat printed cell 45.43 s^-1 = 45.43 s^(-1), which equals the export's stored kcat 45.4 s^(-1) at the export's stored one-decimal precision (45.43 rounds to 45.4); kcat/Km printed cell 7.62 L mmol^-1 s^-1 = 7.62 s^-1 mM^-1 because 1 L mmol^-1 s^-1 = 1 s^-1 mM^-1. The export stores the quotient of its own kcat and Km fields, 45.4 s^(-1) / 5.96 mM = 7.61744966442953 s^-1 mM^-1, which rounds to the paper's printed cell 7.62 at the printed cell's own two-decimal precision, so the printed ratio and the export ratio agree. In the article XML the units render with the micro sign and flattened superscripts, e.g. (L⋅mmol–1⋅s–1); the package source extract writes the same row as Table 4 TMP row: Km=5.96 mM; kcat=45.43 s^-1; kcat/Km=7.62 L*mmol^-1*s^-1.

raw_value_unit_evidence: TABLE 4. Steady-state kinetic constants of EsiLeuDH | metric header row of Table 4: Substrate K m V max k cat k cat / K m; unit header row: (mM) (umol min^-1 mg^-1) (s^-1) (L mmol^-1 s^-1) | row TMP, as carried in this package's source extract: Table 4 TMP row: Km=5.96 mM; kcat=45.43 s^-1; kcat/Km=7.62 L*mmol^-1*s^-1. | TMP cells read: K m = 5.96 mM; k cat = 45.43 s^-1; k cat / K m = 7.62 L mmol^-1 s^-1

row_label: EsiLeuDH | TMP

substrate: trimethylpyruvate


assay_conditions_summary: pH 9.5; 308.15 K; cofactor NADH

column_label: Table 1 row 2-keto-3-methylbutyric acid; E116V variant columns Km, kcat, kcat/Km; cells Km = 0.731 +/- 0.059 mM, kcat = 0.659 +/- 0.025 s^-1, printed kcat/Km = 0.902 s^-1 mM^-1.

row_label: 2-keto-3-methylbutyric acid; E116V

table_label: Table 1: Kinetic parameters of wild type BcLeuDH and its variants toward different alpha-keto acid substrates


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T45M to reconstruct the assayed variant sequence.

column_label: Table 1 row 2-keto-3-methylbutyric acid; T45M variant columns Km, kcat, kcat/Km; cells Km = 2.540 +/- 0.220 mM, kcat = 0.702 +/- 0.055 s^-1, printed kcat/Km = 0.276 s^-1 mM^-1.

row_label: 2-keto-3-methylbutyric acid; T45M


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A392 and applied mutation signature T45M/E116V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; 308.15 K; buffer Tris-HCl; cofactor NADH

column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'T45M/E116V', substrate row '2-Keto-3-methylbutyrate'; column 'Km [mM]' = 0.925; column 'kcat [s-1]' = 0.382; column 'kcat/Km [s-1 mM-1]' = 0.413. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.018 on Km and 0.014 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.382 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.382 s^(-1). Km: printed Table 1 cell 0.925 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 0.925 mM. kcat/Km: printed Table 1 cell 0.413 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.413 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.382 s^(-1), Km 0.93 mM and kcat_over_km 0.410752688172043 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'T45M/E116V', substrate row '2-Keto-3-methylbutyrate': Km = 0.925 in the column headed Km [mM]; kcat = 0.382 in the column headed kcat [s-1]; printed kcat/Km = 0.413 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group T45M/E116V, substrate row 2-Keto-3-methylbutyrate

table_label: Table 1: Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates (Biotechnol. J. 2019, 14, 1800253). Printed metric heads, repeated once for each enzyme column group: Km [mM]; kcat [s-1]; kcat/Km [s-1 mM-1]. Printed substrate rows: α-Ketobutyric acid; α-Oxovaleric acid; Trimethylpyruvic acid; 2-Keto-3-methylbutyrate; α-ketoisocaproic acid; Phenylglyoxylic acid; NADH.


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

assay_conditions_summary: pH 9.5; 308.15 K; buffer 50 mM Tris-HCl

column_label: Table 1 columns substrate, wild type Km (mM), wild type kcat (s^-1), and wild type kcat/Km (s^-1 mM^-1); row matched by paper substrate 2-keto-3-methylbutyrate and wild type BcLeuDH.

normalized_value_unit_evidence: kcat 0.478 s^-1; Km 2.47 mM; printed kcat/Km 0.194 s^-1 mM^-1; quotient of printed kcat and Km is 0.19352226720647772 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row 2-keto-3-methylbutyrate wild type: Km 2.470 +/- 0.135 mM; kcat 0.478 +/- 0.024 s^-1; kcat/Km 0.194 s^-1 mM^-1.

row_label: 2-keto-3-methylbutyrate; wild type BcLeuDH

table_label: Table 1, Kinetic parameters of wild type BcLeuDH and its variants toward different alpha-keto acid substrates


column_label: Table 1 row alpha-ketobutyric acid; E116V variant columns Km, kcat, kcat/Km; cells Km = 0.705 +/- 0.040 mM, kcat = 0.168 +/- 0.012 s^-1, printed kcat/Km = 0.238 s^-1 mM^-1.

row_label: alpha-ketobutyric acid; E116V


column_label: Table 1 row alpha-ketobutyric acid; T45M variant columns Km, kcat, kcat/Km; cells Km = 1.700 +/- 0.138 mM, kcat = 0.174 +/- 0.036 s^-1, printed kcat/Km = 0.102 s^-1 mM^-1.

row_label: alpha-ketobutyric acid; T45M


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T45M/E116V to reconstruct the assayed variant sequence.

column_label: Table 1 row alpha-ketobutyric acid; T45M/E116V variant columns Km, kcat, kcat/Km; cells Km = 2.650 +/- 0.115 mM, kcat = 0.284 +/- 0.008 s^-1, printed kcat/Km = 0.107 s^-1 mM^-1.

row_label: alpha-ketobutyric acid; T45M/E116V


column_label: Table 1 columns substrate, wild type Km (mM), wild type kcat (s^-1), and wild type kcat/Km (s^-1 mM^-1); row matched by paper substrate alpha-ketobutyric acid and wild type BcLeuDH.

normalized_value_unit_evidence: kcat 0.149 s^-1; Km 1.89 mM; printed kcat/Km 0.079 s^-1 mM^-1; quotient of printed kcat and Km is 0.07883597883597884 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row alpha-ketobutyric acid wild type: Km 1.890 +/- 0.123 mM; kcat 0.149 +/- 0.013 s^-1; kcat/Km 0.079 s^-1 mM^-1.

row_label: alpha-ketobutyric acid; wild type BcLeuDH


column_label: Table 1 row alpha-oxovaleric acid; E116V variant columns Km, kcat, kcat/Km; cells Km = 1.140 +/- 0.078 mM, kcat = 0.384 +/- 0.023 s^-1, printed kcat/Km = 0.337 s^-1 mM^-1.

row_label: alpha-oxovaleric acid; E116V


column_label: Table 1 row 4-methyl-2-oxopentanoic acid; E116V variant columns Km, kcat, kcat/Km; cells Km = 0.377 +/- 0.025 mM, kcat = 0.543 +/- 0.012 s^-1, printed kcat/Km = 1.440 s^-1 mM^-1.

row_label: 4-methyl-2-oxopentanoic acid; E116V


organism: Lysinibacillus sphaericus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A43V/D124E to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 10; 303.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G298A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines:
GltS
pyridine nucleotides
NADPH-binding site


proof_lines:
GltS
NADPH
pyridine nucleotides


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
NADPH-binding site
NADPH
GltS


column_label: Table 2 row L-Leucine; column K_m (mM); PDF page 4.

raw_value_unit_evidence: Table 2 row L-Leucine: relative activity=100%; K_m=2.0 mM.

row_label: L-Leucine

table_label: Table 2


substrate_name: L-isoleucine

column_label: Table 2 row L-Isoleucine; column K_m (mM); PDF page 4.

raw_value_unit_evidence: Table 2 row L-Isoleucine: relative activity=88.5%; K_m=0.4 mM.

row_label: L-Isoleucine

substrate: L-isoleucine


substrate_name: L-valine

column_label: Table 2 row L-Valine; column K_m (mM); PDF page 4.

raw_value_unit_evidence: Table 2 row L-Valine: relative activity=86.7%; K_m=2.4 mM.

row_label: L-Valine

substrate: L-valine


column_label: Steady-state kinetics prose tied to Fig. 3A; substrate label NAD; metric K_m; PDF page 5.

normalized_value_unit_evidence: K_m(NAD)=0.36 mM; package NAD(+) is paper NAD.

raw_value_unit_evidence: Steady-state kinetics prose: K_m values for NAD and L-leucine were calculated as 0.36 mM and 2.0 mM, respectively.

row_label: NAD

table_label: Steady-state kinetics prose / Fig. 3


column_label: Table 3 row 2-Oxoisocaproate; column K_m (mM); PDF page 4.

normalized_value_unit_evidence: K_m=0.63 mM; package substrate 4-methyl-2-oxopentanoate is synonymous with 2-oxoisocaproate.

raw_value_unit_evidence: Table 3 row 2-Oxoisocaproate: relative activity=100%; K_m=0.63 mM.


column_label: Steady-state kinetics prose tied to Fig. 3C-D; substrate label NADH; metric K_m; PDF page 5.

raw_value_unit_evidence: Steady-state kinetics prose: K_m values for NADH, 2-oxoisocaproate, and NH3 were determined as 0.042, 0.63, and 118 mM, respectively.

row_label: NADH


column_label: Steady-state kinetics prose tied to Fig. 3B-D; substrate label NH3; metric K_m; PDF page 5.

normalized_value_unit_evidence: K_m(NH3)=118 mM; package NH(3) is paper ammonia/NH3.


enzyme_display_name: valine dehydrogenase (NADP(+))

substrate_name: L-Valine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C251S to reconstruct the assayed variant sequence.

enzyme: valine dehydrogenase (NADP(+))

substrate: L-Valine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C29S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V305L to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

column_label: Table I; row Wild type; deamination Kcat column and L-Valine Km column.

raw_value_unit_evidence: Table I wild-type row: kcat 46 +/- 0.2 sec^-1; L-Valine Km 1.686 +/- 0.002 mM; kcat/Km is not printed.

row_label: Wild type

table_label: Table I. Steady-state kinetic parameters of the wild type and mutant enzymes


column_label: Table I; row Wild type; deamination Kcat column and NAD+ Km column.

raw_value_unit_evidence: Table I wild-type row: kcat 46 +/- 0.2 sec^-1; NAD+ Km 0.15 +/- 0.01 mM; kcat/Km is not printed.


organism: Planifilum fimeticola

assay_conditions_summary: pH 9.5; cofactor NAD+

column_label: Table 1 columns Km (mM) | Kcat (S^-1) | Kcat/Km (S^-1 mM^-1) for row NAD+

normalized_value_unit_evidence: package values Km 0.11 mM | kcat 1.8 s^-1 | kcat_over_km 16.363636363636363 s^-1 mM^-1 reflect rounded kcat and derived ratio

raw_value_unit_evidence: Table 1 row NAD+ gives Km 0.11 mM | Kcat 1.81 s^-1 | Kcat/Km 16.45 s^-1 mM^-1

row_label: NAD+

table_label: Table 1 | The kinetic parameter of PfLeuDH


column_label: Table 1 columns Km (mM) | Kcat (S^-1) | Kcat/Km (S^-1 mM^-1) for row L-Leucine

normalized_value_unit_evidence: package values Km 0.1 mM | kcat 2.3 s^-1 | kcat_over_km 23.0 s^-1 mM^-1 reflect rounded kcat and derived ratio

raw_value_unit_evidence: Table 1 row L-Leucine gives Km 0.1 mM | Kcat 2.33 s^-1 | Kcat/Km 23.3 s^-1 mM^-1


assay_conditions_summary: pH 9.5; cofactor NADH

column_label: Table 1 columns Km (mM) | Kcat (S^-1) | Kcat/Km (S^-1 mM^-1) for row NADH

normalized_value_unit_evidence: package values Km 0.06 mM | kcat 6.1 s^-1 | kcat_over_km 101.66666666666667 s^-1 mM^-1 reflect rounded kcat and derived ratio

raw_value_unit_evidence: Table 1 row NADH gives Km 0.06 mM | Kcat 6.06 s^-1 | Kcat/Km 101 s^-1 mM^-1


column_label: Table 1 columns Km (mM) | Kcat (S^-1) | Kcat/Km (S^-1 mM^-1) for row Trimethylpyruvate

normalized_value_unit_evidence: package values Km 3.08 mM | kcat 39.1 s^-1 | kcat_over_km 12.694805194805195 s^-1 mM^-1 reflect rounded kcat and derived ratio

raw_value_unit_evidence: Table 1 row Trimethylpyruvate gives Km 3.08 mM | Kcat 39.07 s^-1 | Kcat/Km 12.69 s^-1 mM^-1

row_label: Trimethylpyruvate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


organism: Medicago sativa

column_label: Official PMC article abstract/prose; substrate/cofactor NADH; Km = 4.2 micromolar.

normalized_value_unit_evidence: Km 0.0042 mM from 4.2 micromolar.

raw_value_unit_evidence: Official PMC article abstract reports: Km values for glutamine, alpha-ketoglutarate, and NADH were 466, 33, and 4.2 micromolar, respectively.

table_label: Abstract/prose: Km values for purified NADH-glutamate synthase from alfalfa root nodules


column_label: Official PMC article abstract/prose; substrate alpha-ketoglutarate/2-oxoglutarate; Km = 33 micromolar.

normalized_value_unit_evidence: Km 0.033 mM from 33 micromolar.

row_label: Alpha-ketoglutarate


column_label: Official PMC article abstract/prose; substrate glutamine; Km = 466 micromolar.

normalized_value_unit_evidence: Km 0.466 mM from 466 micromolar.

row_label: L-glutamine


organism: Clostridium pasteurianum


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Debaryomyces hansenii

substrate_name: NADPH

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

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
NADP-GDH activity
Debaryomyces hansenii
1 M NaCl

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADPH


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

assay_conditions_summary: pH 8


enzyme_display_name: Glutamate dehydrogenase, mitochondrial

organism: Dictyostelium discoideum

substrate_name: alpha-ketoglutarate

assay_conditions_summary: pH 7.25; cofactor NADH

column_label: Primary article abstract/prose reports Km values for alpha-ketoglutarate, NADH, and NH4+ in order; alpha-ketoglutarate is the first value, 0.36 +/- 0.03 mM.

row_label: Km sentence substrate order 1: alpha-ketoglutarate

table_label: ScienceDirect article abstract/prose

enzyme: Glutamate dehydrogenase, mitochondrial

substrate: alpha-ketoglutarate


column_label: Primary article abstract/prose reports Km values for alpha-ketoglutarate, NADH, and NH4+ in order; NADH is the second value, 16.0 +/- 0.1 uM, normalized to 0.016 mM.

row_label: Km sentence substrate order 2: NADH


column_label: Primary article abstract/prose reports Km values for alpha-ketoglutarate, NADH, and NH4+ in order; NH4+ is the third value, 34.5 +/- 2.7 mM, matching the CatLog NH(3) row.

row_label: Km sentence substrate order 3: NH4+


column_label: Table 1 row 4-methyl-2-oxopentanoic acid; T45M variant columns Km, kcat, kcat/Km; cells Km = 1.720 +/- 0.119 mM, kcat = 0.532 +/- 0.045 s^-1, printed kcat/Km = 0.309 s^-1 mM^-1.

row_label: 4-methyl-2-oxopentanoic acid; T45M


column_label: Table 1 row 4-methyl-2-oxopentanoic acid; T45M/E116V variant columns Km, kcat, kcat/Km; cells Km = 0.890 +/- 0.067 mM, kcat = 0.385 +/- 0.024 s^-1, printed kcat/Km = 0.433 s^-1 mM^-1.


column_label: Table 1 columns substrate, wild type Km (mM), wild type kcat (s^-1), and wild type kcat/Km (s^-1 mM^-1); row matched by paper substrate alpha-ketoisocaproic acid and wild type BcLeuDH.

normalized_value_unit_evidence: kcat 0.467 s^-1; Km 1.41 mM; printed kcat/Km 0.332 s^-1 mM^-1; quotient of printed kcat and Km is 0.3312056737588653 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row alpha-ketoisocaproic acid wild type: Km 1.410 +/- 0.083 mM; kcat 0.467 +/- 0.034 s^-1; kcat/Km 0.332 s^-1 mM^-1.

row_label: alpha-ketoisocaproic acid; wild type BcLeuDH


column_label: Table 1 row NADH; E116V variant columns Km, kcat, kcat/Km; cells Km = 0.070 +/- 0.004 mM, kcat = 1.300 +/- 0.021 s^-1, printed kcat/Km = 18.700 s^-1 mM^-1.

row_label: NADH; E116V


column_label: Table 1 row NADH; T45M variant columns Km, kcat, kcat/Km; cells Km = 0.224 +/- 0.012 mM, kcat = 0.552 +/- 0.043 s^-1, printed kcat/Km = 2.460 s^-1 mM^-1.

row_label: NADH; T45M


column_label: Table 1 row NADH; T45M/E116V variant columns Km, kcat, kcat/Km; cells Km = 0.090 +/- 0.009 mM, kcat = 0.286 +/- 0.016 s^-1, printed kcat/Km = 3.180 s^-1 mM^-1.

row_label: NADH; T45M/E116V


assay_conditions_summary: pH 9.5; 308.15 K; buffer 50 mM Tris-HCl; cofactor NADH

column_label: Table 1 columns substrate, wild type Km (mM), wild type kcat (s^-1), and wild type kcat/Km (s^-1 mM^-1); row matched by substrate NADH and wild type BcLeuDH.

normalized_value_unit_evidence: kcat 0.544 s^-1; Km 0.171 mM; printed kcat/Km 3.180 s^-1 mM^-1; export value 3.2 is table-rounding compatible.

row_label: NADH; wild type BcLeuDH


substrate_name: oxo(phenyl)acetate

column_label: Table 1 row Phenylglyoxylic acid; E116V variant columns Km, kcat, kcat/Km; cells Km = 0.752 +/- 0.034 mM, kcat = 0.101 +/- 0.006 s^-1, printed kcat/Km = 0.134 s^-1 mM^-1.

row_label: Phenylglyoxylic acid; E116V

substrate: oxo(phenyl)acetate


column_label: Table 1 row Phenylglyoxylic acid; T45M variant columns Km, kcat, kcat/Km; cells Km = 1.990 +/- 0.154 mM, kcat = 0.060 +/- 0.014 s^-1, printed kcat/Km = 0.030 s^-1 mM^-1.

row_label: Phenylglyoxylic acid; T45M


column_label: Table 1 row Phenylglyoxylic acid; T45M/E116V variant columns Km, kcat, kcat/Km; cells Km = 1.120 +/- 0.092 mM, kcat = 0.214 +/- 0.017 s^-1, printed kcat/Km = 0.191 s^-1 mM^-1.

row_label: Phenylglyoxylic acid; T45M/E116V


enzyme_display_name: NADP-specific glutamate dehydrogenase

enzyme: NADP-specific glutamate dehydrogenase


substrate_name: ammonia

substrate: ammonia


enzyme_display_name: alanine dehydrogenase

organism: Carnobacterium sp.

assay_conditions_summary: cofactor NAD+

proof_lines:
NAD(+)-dependent alanine dehydrogenase
Carnobacterium sp. strain St2
CarAlaDH

enzyme: alanine dehydrogenase


substrate_name: L-Ala

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

proof_lines:
Carnobacterium sp. strain St2
alanine dehydrogenase
CarAlaDH

substrate: L-Ala


organism: Psychrobacter sp. (strain TAD1)

substrate_name: NADP (at 20 degrees Celsius and at pH 8)

assay_conditions_summary: cofactor NADP+

column_label: PMID 10601858 Table 2; row NADP+; column Km (mM), TAD1.

raw_value_unit_evidence: Table 2 NADP+ row under TAD1 Km: 0.043 plus/minus 0.06 mM.

row_label: NADP+ / Psychrobacter sp. TAD1 GDH

table_label: Table 2. Kinetic parameters measured for Psychrobacter sp. TAD1 and E. coli GDH


substrate_name: ammonium (at 20 degrees Celsius and at pH 8)

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
NADP+-dependent glutamate dehydrogenase
Psychrobacter sp. TAD1
2-oxoglutarate


substrate_name: L-glutamate (at 20 degrees Celsius and at pH 8)


organism: Bacillus subtilis

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

proof_lines: NAD L-alanine


assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: glutamine

proof_lines:
GS/GOGAT
Km values
crude cell-free extracts

substrate: glutamine


assay_conditions_summary: pH 9.5; 308.15 K; buffer Tris-HCl; cofactor NADH

column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'Wild type', substrate row 'Phenylglyoxylic acid'; column 'Km [mM]' = 9.380; column 'kcat [s-1]' = 0.182; column 'kcat/Km [s-1 mM-1]' = 0.019. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.672 on Km and 0.015 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.182 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.182 s^(-1). Km: printed Table 1 cell 9.380 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 9.380 mM. kcat/Km: printed Table 1 cell 0.019 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.019 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.182 s^(-1), Km 9.38 mM and kcat_over_km 0.019402985074626865 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'Wild type', substrate row 'Phenylglyoxylic acid': Km = 9.380 in the column headed Km [mM]; kcat = 0.182 in the column headed kcat [s-1]; printed kcat/Km = 0.019 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group Wild type, substrate row Phenylglyoxylic acid


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A392 and applied mutation signature E116V to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'E116V', substrate row 'Trimethylpyruvic acid'; column 'Km [mM]' = 1.71; column 'kcat [s-1]' = 0.033; column 'kcat/Km [s-1 mM-1]' = 0.0195. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.113 on Km and 0.005 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.033 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.033 s^(-1). Km: printed Table 1 cell 1.71 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 1.71 mM. kcat/Km: printed Table 1 cell 0.0195 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.0195 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.033 s^(-1), Km 1.71 mM and kcat_over_km 0.01929824561403509 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'E116V', substrate row 'Trimethylpyruvic acid': Km = 1.71 in the column headed Km [mM]; kcat = 0.033 in the column headed kcat [s-1]; printed kcat/Km = 0.0195 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group E116V, substrate row Trimethylpyruvic acid


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0A392 and applied mutation signature T45M to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'T45M', substrate row 'Trimethylpyruvic acid'; column 'Km [mM]' = 1.150; column 'kcat [s-1]' = 0.006; column 'kcat/Km [s-1 mM-1]' = 0.005. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.103 on Km and 0.001 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.006 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.006 s^(-1). Km: printed Table 1 cell 1.150 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 1.150 mM. kcat/Km: printed Table 1 cell 0.005 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.005 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.006 s^(-1), Km 1.15 mM and kcat_over_km 0.0052173913043478265 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'T45M', substrate row 'Trimethylpyruvic acid': Km = 1.150 in the column headed Km [mM]; kcat = 0.006 in the column headed kcat [s-1]; printed kcat/Km = 0.005 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group T45M, substrate row Trimethylpyruvic acid


column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'T45M/E116V', substrate row 'Trimethylpyruvic acid'; column 'Km [mM]' = 2.650; column 'kcat [s-1]' = 0.036; column 'kcat/Km [s-1 mM-1]' = 0.0137. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.209 on Km and 0.007 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.036 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.036 s^(-1). Km: printed Table 1 cell 2.650 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 2.650 mM. kcat/Km: printed Table 1 cell 0.0137 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.0137 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.036 s^(-1), Km 2.65 mM and kcat_over_km 0.013584905660377358 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'T45M/E116V', substrate row 'Trimethylpyruvic acid': Km = 2.650 in the column headed Km [mM]; kcat = 0.036 in the column headed kcat [s-1]; printed kcat/Km = 0.0137 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group T45M/E116V, substrate row Trimethylpyruvic acid


column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'Wild type', substrate row 'Trimethylpyruvic acid'; column 'Km [mM]' = 3.750; column 'kcat [s-1]' = 0.016; column 'kcat/Km [s-1 mM-1]' = 0.004. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.229 on Km and 0.001 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.016 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.016 s^(-1). Km: printed Table 1 cell 3.750 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 3.750 mM. kcat/Km: printed Table 1 cell 0.004 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.004 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.016 s^(-1), Km 4.35 mM and kcat_over_km 0.00367816091954023 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'Wild type', substrate row 'Trimethylpyruvic acid': Km = 3.750 in the column headed Km [mM]; kcat = 0.016 in the column headed kcat [s-1]; printed kcat/Km = 0.004 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group Wild type, substrate row Trimethylpyruvic acid


column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'T45M', substrate row 'α-Oxovaleric acid'; column 'Km [mM]' = 1.990; column 'kcat [s-1]' = 0.588; column 'kcat/Km [s-1 mM-1]' = 0.295. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.124 on Km and 0.048 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.588 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.588 s^(-1). Km: printed Table 1 cell 1.990 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 1.990 mM. kcat/Km: printed Table 1 cell 0.295 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.295 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.588 s^(-1), Km 1.99 mM and kcat_over_km 0.29547738693467335 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'T45M', substrate row 'α-Oxovaleric acid': Km = 1.990 in the column headed Km [mM]; kcat = 0.588 in the column headed kcat [s-1]; printed kcat/Km = 0.295 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group T45M, substrate row α-Oxovaleric acid


column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'T45M/E116V', substrate row 'α-Oxovaleric acid'; column 'Km [mM]' = 0.409; column 'kcat [s-1]' = 0.129; column 'kcat/Km [s-1 mM-1]' = 0.315. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.008 on Km and 0.010 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.129 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.129 s^(-1). Km: printed Table 1 cell 0.409 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 0.409 mM. kcat/Km: printed Table 1 cell 0.315 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.315 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.129 s^(-1), Km 0.41 mM and kcat_over_km 0.3146341463414634 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'T45M/E116V', substrate row 'α-Oxovaleric acid': Km = 0.409 in the column headed Km [mM]; kcat = 0.129 in the column headed kcat [s-1]; printed kcat/Km = 0.315 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group T45M/E116V, substrate row α-Oxovaleric acid


column_label: Table 1 (Kinetic parameters of wild type BcLeuDH and its variants toward different α-keto acid substrates), enzyme column group 'Wild type', substrate row 'α-Oxovaleric acid'; column 'Km [mM]' = 1.430; column 'kcat [s-1]' = 0.332; column 'kcat/Km [s-1 mM-1]' = 0.232. The value printed after the plus/minus sign beside the Km and kcat cells of this line is the printed uncertainty (0.107 on Km and 0.016 on kcat) and is not an exported metric; the kcat/Km head prints a single value with no plus/minus term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.332 under the head kcat [s-1]; s-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.332 s^(-1). Km: printed Table 1 cell 1.430 under the head Km [mM]; mM is already canonical, so no unit conversion applies and the value is 1.430 mM. kcat/Km: printed Table 1 cell 0.232 under the head kcat/Km [s-1 mM-1]; 1 s^-1 mM^-1 is 1 s^(-1)*mM^(-1), so no unit conversion applies and the value is 0.232 s^(-1)*mM^(-1). The exported values on this catalog line are kcat 0.332 s^(-1), Km 1.43 mM and kcat_over_km 0.23216783216783218 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column group 'Wild type', substrate row 'α-Oxovaleric acid': Km = 1.430 in the column headed Km [mM]; kcat = 0.332 in the column headed kcat [s-1]; printed kcat/Km = 0.232 in the column headed kcat/Km [s-1 mM-1].

row_label: Table 1, enzyme column group Wild type, substrate row α-Oxovaleric acid


organism: Acetoanaerobium sticklandii

substrate_name: NADP+

column_label: Table 1 row DAPDH / NADP+ columns Km, kcat, kcat/Km

row_label: DAPDH / NADP+

table_label: Table 1

substrate: NADP+


enzyme_display_name: NAD-specific glutamate dehydrogenase

organism: Clostridium symbiosum

substrate_name: NADH (at 25 degrees Celsius and at pH 7)

assay_conditions_summary: cofactor NADH

enzyme: NAD-specific glutamate dehydrogenase


substrate_name: 2-oxoglutarate (at 25 degrees Celsius and at pH 7)


enzyme_display_name: glutamate dehydrogenase

organism: Clostridioides difficile

substrate_name: NAD+

enzyme: glutamate dehydrogenase


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: glutamate dehydrogenase [NAD(P)(+)]

organism: Homo sapiens

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

enzyme: glutamate dehydrogenase [NAD(P)(+)]


column_label: Table III; row Wild-type; columns kcat, Km-NAD+, and kcat/Km.

raw_value_unit_evidence: Table III row Wild-type: kcat=65 s^-1; Km-NAD+=0.71 mM; kcat/Km=91.55 s^-1 mM^-1.

row_label: Wild-type

table_label: Table III


organism: Alkalihalophilus pseudofirmus

assay_conditions_summary: pH 10.5; 313.15 K; cofactor NAD+


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 7.6; 363.15 K; buffer pH 7; cofactor NADPH

column_label: Table 1; NADPH row; Apparent Km (mM) column = 0.037 +/- 0.003; kcat (s^-1) column = 387.5 +/- 28.87; no separate kcat/Km column is printed.

raw_value_unit_evidence: Table 1 NADPH row reports Apparent Km = 0.037 +/- 0.003 mM and kcat = 387.5 +/- 28.87 s^-1.

row_label: NADPH row; Apparent Km and kcat columns

table_label: PMID 12590923, Table 1: Km values of Pho-GDH for various substrates


assay_conditions_summary: pH 7.6; 363.15 K; buffer phosphate; cofactor NADP+

column_label: Table 1 ammonia row: apparent Km 2.82 +/- 0.188 mM and kcat 43.8 +/- 2.92 s^-1; the table has no separate kcat/Km column.

raw_value_unit_evidence: Ammonia row: apparent Km 2.82 +/- 0.188 mM; kcat 43.8 +/- 2.92 s^-1; no independently printed kcat/Km cell.

row_label: Ammonia

table_label: Table 1. Apparent kinetic parameters for Pho-GDH


organism: Bacillus licheniformis

assay_conditions_summary: cofactor NADPH

column_label: Abstract states classical hyperbolic kinetics were seen for NADPH affinity and gave an apparent Km value of 13 microM.

raw_value_unit_evidence: Km raw_value=13 raw_unit=microM

row_label: Bacillus licheniformis glutamate synthase with NADPH

table_label: PubMed/PMC abstract PMID 6501215


enzyme_display_name: 2,4-diaminopentanoate dehydrogenase

proof_lines:
ornithine metabolism
2,4-diaminopentanoic acid
2-amino-4-ketopentanoic acid

enzyme: 2,4-diaminopentanoate dehydrogenase


organism: Amycolatopsis sulphurea

substrate_name: L-alanine

column_label: PubMed abstract for PMID 33818657 lists the enzyme kinetic values as Km 2.03 mM, kcat 13.24 s^-1, and kcat/Km 6.53 s^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=2.03 normalized_unit=mM; kcat normalized_value=13.24 normalized_unit=s^-1; kcat/Km paper_value=6.53 normalized_unit=s^-1 mM^-1; CatLog stores computed 13.24/2.03=6.5221674876847295

raw_value_unit_evidence: Km raw_value=2.03 raw_unit=mM; kcat raw_value=13.24 raw_unit=s^-1; kcat/Km raw_value=6.53 raw_unit=s^-1 mM^-1

row_label: L-alanine row

table_label: PubMed abstract kinetic prose

substrate: L-alanine


enzyme_display_name: Glutamate dehydrogenase 2

enzyme: Glutamate dehydrogenase 2


enzyme_display_name: UniProt P9WQB1

organism: Mycobacterium tuberculosis

source_db: skid

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

proof_lines:
Raw SKiD Env: Temp=-----, pH=10.2
Raw SKiD Env: Temp=37°C, pH=10.2

source_databases_merged: skid uniprot

enzyme: UniProt P9WQB1

source: skid


assay_conditions_summary: pH 10.2; 310.15 K; cofactor NAD+

column_label: Paper abstract/results prose gives L-alanine Km 13.8 mM, contradicting expected 0.049 mM.

raw_value_unit_evidence: Paper prose reports Km values in oxidative deamination were 13.8 mM for L-alanine and 0.31 mM for NAD+.

row_label: L-alanine / oxidative deamination

table_label: Abstract and Results prose: oxidative deamination kinetic constants


column_label: Paper abstract/results prose gives NAD+ Km 0.31 mM, matching expected.

row_label: NAD+ / oxidative deamination


substrate_name: glutamate

substrate: glutamate


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: NAD

column_label: Results prose reports a linear NAD plot yielding a Km value of 0.13 mM.

raw_value_unit_evidence: Km raw_value=0.13 raw_unit=mM

row_label: Purified Pseudomonas aeruginosa PAO1 NAD-GDH / NAD deamination activity

table_label: PMC94904 results prose

substrate: NAD


enzyme_display_name: Glutamate dehydrogenase 1, mitochondrial

organism: Bos taurus

substrate_name: NAD(+)

column_label: Abstract reports the Km and Vmax values for NAD+ were 0.1 mM and 1.08 micromol/min/mg, respectively.

raw_value_unit_evidence: Km raw_value=0.1 mM raw_unit=mM

row_label: Bovine brain glutamate dehydrogenase / NAD+

table_label: PubMed XML abstract PMID 14659072

substrate: NAD(+)


organism: Streptomyces clavuligerus

assay_conditions_summary: pH 7; buffer 100 mM phosphate; cofactor NADH

column_label: PMID 10924516 page 39533, Table II; NH4+ block; row [Asp] = 0; column Km (mM).

raw_value_unit_evidence: Table II NH4+ block, [Asp] 0 row: Km 33.9 mM.

row_label: NH4+ / reductive amination / [Asp] = 0

table_label: Table II. Initial rate kinetic parameters for NAD-GDH from S. clavuligerus


enzyme_display_name: Alanine dehydrogenase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: pyruvate (at pH 7.4 and at 25 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines:
Mycobacterium tuberculosis
alanine dehydrogenase
pyruvate

enzyme: Alanine dehydrogenase


substrate_name: NADH (at pH 7.4 and at 37 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Paper abstract/results prose gives NADH Km,app 98.2 uM in reductive amination, matching expected 0.0982 mM at pH 7.4 and 37 deg C.

raw_value_unit_evidence: Paper abstract/results prose reports Km,app values in reductive amination were 35.4 mM, 1.45 mM, and 98.2 uM for ammonium, pyruvate, and NADH, respectively.

row_label: NADH / reductive amination

table_label: Abstract and Results prose: reductive amination kinetic constants


substrate_name: ammonium (at pH 7.4 and at 37 degrees Celsius)

column_label: Paper abstract/results prose gives ammonium Km,app 35.4 mM in reductive amination, matching expected.

row_label: ammonium / reductive amination


enzyme_display_name: UniProt P00370

organism: Escherichia coli

substrate_name: NADPH

assay_conditions_summary: pH 8; 295.15 K; cofactor NADP+

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=-----, pH=8

enzyme: UniProt P00370


organism: Mus musculus

enzyme: Glutamate dehydrogenase 1, mitochondrial


organism: Mycobacterium smegmatis

substrate_name: L-Glutamate

substrate: L-Glutamate


enzyme_display_name: glutamate synthase (NADPH)

organism: Geobacillus stearothermophilus

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

enzyme: glutamate synthase (NADPH)


substrate_name: L-glutamine

substrate: L-glutamine


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Leucine dehydrogenase

substrate_name: NADH

proof_lines: found to produce a thermostable and halophilic leucine dehydrogenase (EC 1.4.1.9)

proof_lines: stereospecificity for hydrogen transfer from the C-4 of NADH

enzyme: Leucine dehydrogenase

substrate: NADH


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


assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: pyruvate

substrate: pyruvate


substrate_name: L-serine

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

proof_lines: wild-type, pH 10.2, temperature not specified in the publication

substrate: L-serine


proof_lines: wild type enzyme, in 125 mM glycine/KOH (pH 10.2), at 25°C


proof_lines: mutant F94S/Y117L, pH 10.2, temperature not specified in the publication


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: L-leucine

proof_lines: mutant F94S, pH 10.2, temperature not specified in the publication

substrate: L-leucine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-alanine


substrate_name: L-valine

substrate: L-valine


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-homoserine

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

substrate: L-homoserine


substrate_name: L-homophenylalanine

substrate: L-homophenylalanine


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: ammonium

column_label: Results prose reports that the Km of GDH (MSMEG_4699) for ammonium was calculated as 45 mM at 4 mM alpha-ketoglutarate (Fig. 7C).

raw_value_unit_evidence: Km raw_value=45 raw_unit=mM

row_label: Recombinant GDH (MSMEG_4699)

table_label: Results prose and Fig. 7C - Characterization of GDH and its regulation by GarA

substrate: ammonium


organism: Bacillus subtilis


substrate_name: NAD+


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


smiles: CCCCC(=O)C(=O)[O-]


substrate_name: glyoxalate

substrate: glyoxalate


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


substrate_name: L-Ser

substrate: L-Ser


substrate_name: L-Val

substrate: L-Val


proof_lines:
at pH 8.6
at pH 7.4


substrate_name: L-Ile

substrate: L-Ile


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

substrate_name: NADH

proof_lines:
mutant C119G, hGDH1
mutant C119G, hGDH2

enzyme: glutamate dehydrogenase [NAD(P)+]

substrate: NADH


proof_lines:
mutant C119Y, hGDH1
mutant C119Y, hGDH2


proof_lines:
mutant C119A, hGDH1
mutant C119A, hGDH2


proof_lines:
mutant C59Y, hGDH1
mutant C59Y, hGDH2


proof_lines:
mutant C274Y, hGDH1
mutant C274Y, hGDH2


proof_lines:
mutant C59A, hGDH1
mutant C59A, hGDH2


proof_lines:
mutant C274A, hGDH1
mutant C274A, hGDH2


proof_lines:
mutant C59G, hGDH1
mutant C59G, hGDH2


proof_lines:
mutant C274G, hGDH1
mutant C274G, hGDH2


proof_lines:
pH 9.5, 25°C, mutant enzyme hGDH1K130Y
pH 9.5, 25°C, mutant enzyme hGDH1K94Y
pH 9.5, 25°C, mutant enzyme hGDH1K118Y

substrate: NAD+


substrate_name: L-glutamate

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

substrate: L-glutamate


proof_lines:
pH 9.5, 25°C, mutant enzyme hGDH2K130Y
pH 9.5, 25°C, mutant enzyme hGDH2K94Y
pH 9.5, 25°C, mutant enzyme hGDH2K118Y


proof_lines:
pH 9.5, 25°C, wild-type enzyme hGDH1
pH 9.5, 25°C, wild-type enzyme
pH 9.5, 25°C, wild-type enzyme hGDH2


enzyme_display_name: leucine dehydrogenase

organism: Bacillus cereus

enzyme: leucine dehydrogenase


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


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


substrate_name: L-norvaline


substrate_name: L-Met

substrate: L-Met


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Aspergillus niger

substrate_name: NADPH

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: recombinant wild-type, pH 8.0, temperature not specified in the publication

proof_lines: wild-type inactivated by 2-hydroxyethyl disulfide, pH 8.0, temperature not specified in the publication

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: pH 9.3; cofactor NADP+

proof_lines: wild-type inactivated by 2-hydroxyethyl disulfide, pH 9.3, temperature not specified in the publication

proof_lines: recombinant wild-type, pH 9.3, temperature not specified in the publication

substrate: NADP+


smiles: N

assay_conditions_summary: pH 8

proof_lines: wild-type, pH 8.0, temperature not specified in the publication


proof_lines: mutant C141S, pH 8.0, temperature not specified in the publication


proof_lines: mutant C141S, S0.5 value, Hill coefficient 2.3, pH 8.0, temperature not specified in the publication


proof_lines: wild-type, S0.5 value, Hill coefficient 3.2, pH 8.0, temperature not specified in the publication

proof_lines: recombinant wild-type, S0.5 value, Hill coefficient 3.5, pH 8.0, temperature not specified in the publication

proof_lines: wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 2.4, pH 8.0, temperature not specified in the publication


proof_lines: mutant C415S, S0.5 value, Hill coefficient 4.9, pH 8.0, temperature not specified in the publication


proof_lines: mutant C141S, pH 9.3, temperature not specified in the publication


proof_lines: wild-type, pH 9.3, temperature not specified in the publication

proof_lines: wild-type inactivated by 2-hydroxyethyl disulfide, S0.5 value, Hill coefficient 1.9, pH 9.3, temperature not specified in the publication


proof_lines: mutant C415S, pH 9.3, temperature not specified in the publication


enzyme_display_name: UniProt P04964

organism: Corynebacterium glutamicum

substrate_name: pyruvate

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P04964

substrate: pyruvate


substrate_name: oxaloacetate

substrate: oxaloacetate


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

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=10


enzyme_display_name: UniProt Q67PI3

organism: Symbiobacterium thermophilum

substrate_name: phenylpyruvate

enzyme: UniProt Q67PI3

substrate: phenylpyruvate


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=10
Raw SKiD Env: Temp=30°C, pH=8.5


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=30°C, pH=9


enzyme_display_name: Meso-diaminopimelate D-dehydrogenase

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

substrate_name: NADP(+)

enzyme: Meso-diaminopimelate D-dehydrogenase

substrate: NADP(+)


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


substrate_name: ammonia

substrate: ammonia


enzyme_display_name: phenylalanine dehydrogenase

organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

enzyme: phenylalanine dehydrogenase


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


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: L-Trp

substrate: L-Trp


enzyme_display_name: UniProt Q59771

organism: Rhodococcus sp.

substrate_name: phenylacetone

enzyme: UniProt Q59771

substrate: phenylacetone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K66Q/S149G/N262C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


organism: Homo sapiens

substrate_name: NAD+

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+


substrate_name: trimethylpyruvate

substrate: trimethylpyruvate


proof_lines:
wild-type, pH 9.5, 35°C
wild-type, pH 8.5, 30°C


proof_lines:
mutant E116V, pH 9.5, 35°C
mutant E116V, pH 8.5, 30°C


substrate_name: oxo(phenyl)acetate

substrate: oxo(phenyl)acetate


substrate_name: NADH

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NADH

substrate: NADH


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


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


organism: Brevibacterium sp.

assay_conditions_summary: cofactor NADH


substrate: NAD+


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Tyr

substrate: L-Tyr


substrate_name: L-Met

substrate: L-Met


substrate_name: indolylpyruvate

substrate: indolylpyruvate


organism: Pseudobacillus badius

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


organism: Microbacterium sp.


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: L-norleucine

substrate: L-norleucine


organism: Dietzia maris

substrate_name: thionicotinamide-NAD+

substrate: thionicotinamide-NAD+


substrate_name: deamino-NAD+

substrate: deamino-NAD+


organism: Nocardia sp.


proof_lines:
25°C, pH 10.4, dextran-modified enzyme
25°C, pH 10.4, native enzyme
PheDH after glycosidation


enzyme_display_name: lysine 6-dehydrogenase

organism: Agrobacterium tumefaciens

enzyme: lysine 6-dehydrogenase


enzyme_display_name: tryptophan dehydrogenase

organism: Nicotiana tabacum

proof_lines:
tumor C-58 cell culture
tumor T-24 cell culture
normal cell culture

enzyme: tryptophan dehydrogenase


assay_conditions_summary: pH 10.4; buffer 100 mM glycine-KCl-KOH; cofactor NAD+

proof_lines: in 100 mM glycine-KCl-KOH buffer (pH 10.4)


enzyme_display_name: glutamate dehydrogenase

substrate_name: L-glutamate

enzyme: glutamate dehydrogenase

substrate: L-glutamate


proof_lines: mutant Q144R, 1.3 times higher than that of the wild-type


organism: Achromobacter denitrificans

column_label: The abstract reports Km values for L-lysine and NAD+ were 5.0 and 0.09 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.09 mM raw_unit=mM

row_label: Prose segment: NAD+ Km

table_label: PubMed PMID 19017491 abstract


substrate_name: nicotinamide guanine dinucleotide

substrate: nicotinamide guanine dinucleotide


substrate_name: L-lysine

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

raw_value_unit_evidence: Km raw_value=5.0 mM raw_unit=mM

row_label: Prose segment: L-lysine Km

substrate: L-lysine


organism: Thermoactinomyces intermedius

substrate_name: L-ethionine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F124M/V125S/H126I/A127I/A128Y/R129Q to reconstruct the assayed variant sequence.

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

substrate: L-ethionine


substrate_name: L-norvaline

substrate: L-norvaline


substrate_name: L-Leu

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

substrate: L-Leu


substrate_name: L-Ile

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

column_label: Table III (article page 74); row L-Isoleucine; PheDH sub-column of Km (mM) raw value 0.09 mM; PheDH sub-column of kcat (s^-1) raw value 0.24 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 0.24 s^-1 is already in s^-1, so normalized kcat = 0.24 s^-1. Km 0.09 mM is already in mM, so normalized Km = 0.09 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 0.24 / 0.09 = 2.6666666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row L-Isoleucine: Km (mM) PheDH cell 0.09; kcat (s^-1) PheDH cell 0.24. Verbatim table line as extracted: L-Isoleucine 0.09 10 0.24 0.28 2.6 0.028 (1.1)

row_label: L-Isoleucine

table_label: TABLE m. Kinetic constants of CS2 and the wild-type phenylalanlne dehydrogenase

substrate: L-Ile


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

column_label: Table III (article page 74); row L-Norvaline; PheDH sub-column of Km (mM) raw value 0.53 mM; PheDH sub-column of kcat (s^-1) raw value 0.59 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 0.59 s^-1 is already in s^-1, so normalized kcat = 0.59 s^-1. Km 0.53 mM is already in mM, so normalized Km = 0.53 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 0.59 / 0.53 = 1.1132075471698113 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row L-Norvaline: Km (mM) PheDH cell 0.53; kcat (s^-1) PheDH cell 0.59. Verbatim table line as extracted: L-Norvaline 0.53 10 0.59 0.15 1.1 0.015 (1.4)

row_label: L-Norvaline


substrate_name: L-Phe

substrate: L-Phe


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

column_label: Table III (article page 74); row L-Methionine; PheDH sub-column of Km (mM) raw value 0.34 mM; PheDH sub-column of kcat (s^-1) raw value 0.84 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 0.84 s^-1 is already in s^-1, so normalized kcat = 0.84 s^-1. Km 0.34 mM is already in mM, so normalized Km = 0.34 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 0.84 / 0.34 = 2.4705882352941173 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row L-Methionine: Km (mM) PheDH cell 0.34; kcat (s^-1) PheDH cell 0.84. Verbatim table line as extracted: L-Methionine 0.34 7.5 0.84 0.16 2.5 0.021 (0.84)

row_label: L-Methionine


column_label: Table III (article page 74); row L-Ethionine; PheDH sub-column of Km (mM) raw value 0.27 mM; PheDH sub-column of kcat (s^-1) raw value 1.1 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 1.1 s^-1 is already in s^-1, so normalized kcat = 1.1 s^-1. Km 0.27 mM is already in mM, so normalized Km = 0.27 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 1.1 / 0.27 = 4.074074074074074 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row L-Ethionine: Km (mM) PheDH cell 0.27; kcat (s^-1) PheDH cell 1.1. Verbatim table line as extracted: L-Ethionine 0.27 4.0 1.1 0.10 4.0 0.025 (0.63)

row_label: L-Ethionine


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


column_label: Table III (article page 74); row L-Leucine; PheDH sub-column of Km (mM) raw value 0.09 mM; PheDH sub-column of kcat (s^-1) raw value 3.6 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 3.6 s^-1 is already in s^-1, so normalized kcat = 3.6 s^-1. Km 0.09 mM is already in mM, so normalized Km = 0.09 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 3.6 / 0.09 = 40.0 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row L-Leucine: Km (mM) PheDH cell 0.09; kcat (s^-1) PheDH cell 3.6. Verbatim table line as extracted: L-Leucine 0.09 4.7 3.6 0.21 40 0.045 (0.11)

row_label: L-Leucine


source_databases_merged: brenda oed


assay_conditions_summary: pH 10.8; cofactor NAD+

column_label: Table III (Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase), oxidative deamination rows, substrate row 'L-Phenylalanine', wild-type PheDH columns; column 'Km (mM)' = 0.11; column 'kcat (s^-1)' = 45; column 'kcat/Km (mM^-1 s^-1)' = 410.

normalized_value_unit_evidence: Km: printed Table III cell 0.11 in the column headed Km (mM); mM is already the export unit, so no unit conversion applies; the exported value is 0.1 mM. kcat: printed Table III cell 45 in the column headed kcat (s^-1); s^-1 is already the export unit, so no unit conversion applies; the exported value is 45.0 s^(-1). kcat/Km: printed Table III cell 410 in the column headed kcat/Km (mM^-1 s^-1); mM^-1 s^-1 is the export unit s^(-1)*mM^(-1), so no unit conversion applies; the exported value is 450.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, oxidative deamination rows, substrate row 'L-Phenylalanine', wild-type PheDH columns: Km = 0.11 mM; kcat = 45 s^-1; printed kcat/Km = 410 mM^-1 s^-1.

row_label: Table III, oxidative deamination rows, substrate row 'L-Phenylalanine', wild-type phenylalanine dehydrogenase (PheDH) columns

table_label: Table III: Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase (J. Biochem. 1993, 114(1):69-75)


smiles: CCCCC(=O)C(=O)[O-]

column_label: Table III (article page 74); row a-Ketocaproate; PheDH sub-column of Km (mM) raw value 2.5 mM; PheDH sub-column of kcat (s^-1) raw value 79 s^-1; the PheDH kcat/Km sub-column is printed only at two significant figures, so the absolute kcat/Km is derived by dividing this row's own printed kcat cell by its own printed Km cell.

normalized_value_unit_evidence: kcat 79 s^-1 is already in s^-1, so normalized kcat = 79.0 s^-1. Km 2.5 mM is already in mM, so normalized Km = 2.5 mM. Table III prints no absolute kcat/Km at the exported precision for this row, so paper kcat/Km is the quotient of this same row's own two printed cells: 79 / 2.5 = 31.6 s^-1 mM^-1.

raw_value_unit_evidence: Table III, row a-Ketocaproate: Km (mM) PheDH cell 2.5; kcat (s^-1) PheDH cell 79. Verbatim table line as extracted: a-Ketocaproate 2.5 47 79 22 31 0.47 (1.5)

row_label: a-Ketocaproate


assay_conditions_summary: pH 9.5; 295.15 K; buffer Gly-KCl-KOH; cofactor NAD+

column_label: TABLE III. Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase; substrate row 'alpha-Ketovalerate'; column group 'Km (mM)' sub-column 'PheDH' = 35; column group 'kcat (s^-1)' sub-column 'PheDH' = 82; column group 'kcat/Km (mM^-1 s^-1)' sub-column 'PheDH' = 2.3.

normalized_value_unit_evidence: Km: printed cell 35 mM, already the catalog unit mM (no uM/1000 step applies). kcat: printed cell 82 s^-1, already the catalog unit s^(-1) (no min^-1/60 step applies). kcat/Km: printed cell 2.3 mM^-1 s^-1 is already s^(-1)*mM^(-1); the exact quotient of this row's own printed cells is 82 / 35 = 2.342857142857143 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III (printed page 74), row 'alpha-Ketovalerate', wild-type PheDH sub-columns: Km = 35 mM; kcat = 82 s^-1; printed kcat/Km = 2.3 mM^-1 s^-1. Printed line: alpha-Ketovalerate | 35 | 107 | 82 | 4.8 | 2.3 | 0.045 (2.0)

row_label: Table III, substrate row 'alpha-Ketovalerate', wild-type PheDH column group


assay_conditions_summary: pH 10.8; buffer Gly-KCl-KOH; cofactor NAD+

column_label: TABLE III. Kinetic constants of CS2 and the wild-type phenylalanine dehydrogenase; substrate row 'Phenylpyruvate'; column group 'Km (mM)' sub-column 'PheDH' = 0.06; column group 'kcat (s^-1)' sub-column 'PheDH' = 91; column group 'kcat/Km (mM^-1 s^-1)' sub-column 'PheDH' = 1,500.

normalized_value_unit_evidence: Km: printed cell 0.06 mM, already the catalog unit mM (no uM/1000 step applies). kcat: printed cell 91 s^-1, already the catalog unit s^(-1) (no min^-1/60 step applies). kcat/Km: printed cell 1,500 mM^-1 s^-1 is already s^(-1)*mM^(-1); the exact quotient of this row's own printed cells is 91 / 0.06 = 1516.6666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III (printed page 74), row 'Phenylpyruvate', wild-type PheDH sub-columns: Km = 0.06 mM; kcat = 91 s^-1; printed kcat/Km = 1,500 mM^-1 s^-1. Printed line: Phenylpyruvate | 0.06 | 23 | 91 | 12 | 1,500 | 0.52 (0.035)

row_label: Table III, substrate row 'Phenylpyruvate', wild-type PheDH column group


organism: Lysinibacillus sphaericus

substrate_name: DL-propargylglycine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K224Q/L283F/E313G to reconstruct the assayed variant sequence.

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

substrate: DL-propargylglycine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G124A/E313N with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q18H/I336F/E313G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V135I/I308N/Q363H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G124A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F110Y/G124C/G293A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G124A/E313G with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q18H/I336F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E313G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K224Q/L283F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D209G/Q18H/I336F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V33A/A206D/L283F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D209G with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


enzyme_display_name: valine dehydrogenase (NAD+)

organism: Kitasatospora aureofaciens

proof_lines: pH 10.4, temperature not specified in the publication

enzyme: valine dehydrogenase (NAD+)


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


substrate_name: L-valine

substrate: L-valine


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


substrate_name: L-isoleucine

substrate: L-isoleucine


substrate_name: L-leucine

substrate: L-leucine


substrate_name: L-alanine

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

substrate: L-alanine


enzyme_display_name: diaminopimelate dehydrogenase

organism: Numidum massiliense

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

proof_lines: pH 10.5, temperature not specified in the publication

enzyme: diaminopimelate dehydrogenase


substrate_name: NADP+

assay_conditions_summary: pH 10.5; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 10.5; cofactor NAD+

substrate: NAD+


enzyme_display_name: L-tryptophan dehydrogenase

organism: Nostoc punctiforme

substrate_name: L-tryptophan

proof_lines: kcat is 4.2 sec(-1) with L-tryptophan as substrate. kcat is 4.3 sec(-1) with NAD(+) as substrate. kcat is 16 sec(-1) with indole-3-pyruvate as substrate. kcat is 21 sec(-1) with NADH as substrate. kcat is 17 sec(-1) with NH4(+) as substrate

enzyme: L-tryptophan dehydrogenase

substrate: L-tryptophan


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


substrate_name: NADH

substrate: NADH