substrate_name: Coniferaldehyde

column_label: Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8 row AtCAD7 substrate 3 (coniferyl aldehyde), column kcat sec^-1, raw cell 0.99, normalized 0.99 s^-1; Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8 row AtCAD7 substrate 3 (coniferyl aldehyde), column kenz M^-1 sec^-1, raw cell 1500, normalized 1.5 s^-1*mM^-1; Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8 row AtCAD7 substrate 3 (coniferyl aldehyde), column Km uM, raw cell 675, normalized 0.675 mM

normalized_value_unit_evidence: kcat normalized_value=0.99 normalized_unit=s^-1; kcat/Km normalized_value=1.5 normalized_unit=s^-1*mM^-1; Km normalized_value=0.675 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=0.99 raw_unit=s^-1 raw_cell=0.99; kcat/Km raw_value=1500 raw_unit=M^-1*s^-1 raw_cell=1500; Km raw_value=675 raw_unit=uM raw_cell=675

row_label: AtCAD7 substrate 3 (coniferyl aldehyde)


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Arabidopsis thaliana

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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 6.25; 303.15 K; buffer pH 6; cofactor NADPH

column_label: Table 2 row AtCAD8, substrate 3 (coniferyl aldehyde / coniferaldehyde) lists Km 141 uM, kcat 0.44 sec-1, and kenz 3,100 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.141 normalized_unit=mM; kcat normalized_value=0.44 normalized_unit=s^-1; kcat/Km calculated from same row as 0.44/0.141=3.1205673758865253 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=141 raw_unit=uM; kcat raw_value=0.44 raw_unit=sec-1; kenz raw_value=3,100 raw_unit=M-1 sec-1

row_label: AtCAD8 / substrate 3 (coniferyl aldehyde / coniferaldehyde)

table_label: Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8.

data_origin: experimental

enzyme: cinnamyl-alcohol dehydrogenase

substrate: Coniferaldehyde

status: verified

source: oed


column_label: Table 2 row AtCAD3, substrate 3 (coniferyl aldehyde / coniferaldehyde) lists Km 362 uM, kcat 0.39 sec-1, and kenz 1,100 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.362 normalized_unit=mM; kcat normalized_value=0.39 normalized_unit=s^-1; kcat/Km calculated from same row as 0.39/0.362=1.0773480662983426 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=362 raw_unit=uM; kcat raw_value=0.39 raw_unit=sec-1; kenz raw_value=1,100 raw_unit=M-1 sec-1

row_label: AtCAD3 / substrate 3 (coniferyl aldehyde / coniferaldehyde)


column_label: Table 2 row AtCAD2, substrate 3 (coniferyl aldehyde / coniferaldehyde) lists Km 452 uM, kcat 0.65 sec-1, and kenz 1,400 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.452 normalized_unit=mM; kcat normalized_value=0.65 normalized_unit=s^-1; kcat/Km calculated from same row as 0.65/0.452=1.4380530973451326 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=452 raw_unit=uM; kcat raw_value=0.65 raw_unit=sec-1; kenz raw_value=1,400 raw_unit=M-1 sec-1

row_label: AtCAD2 / substrate 3 (coniferyl aldehyde / coniferaldehyde)


substrate_name: Sinapoyl aldehyde

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD5 / substrate 5 (sinapyl aldehyde / sinapoyl aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).

normalized_value_unit_evidence: Km=0.02 mM; kcat=13.72 s^-1; kcat_over_km=686.0 s^-1 mM^-1 from same-row kcat/Km

substrate: Sinapoyl aldehyde


column_label: Table 2 row AtCAD4, substrate 5 (sinapyl aldehyde / sinapaldehyde) lists Km 274 uM, kcat 0.72 sec-1, and kenz 2,600 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.274 normalized_unit=mM; kcat normalized_value=0.72 normalized_unit=s^-1; kcat/Km calculated from same row as 0.72/0.274=2.627737226277372 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=274 raw_unit=uM; kcat raw_value=0.72 raw_unit=sec-1; kenz raw_value=2,600 raw_unit=M-1 sec-1

row_label: AtCAD4 / substrate 5 (sinapyl aldehyde / sinapaldehyde)


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD7 / substrate 5 (sinapyl aldehyde / sinapoyl aldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


column_label: Table 2 row AtCAD8, substrate 5 (sinapyl aldehyde / sinapaldehyde) lists Km 898 uM, kcat 2.25 sec-1, and kenz 2,500 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.898 normalized_unit=mM; kcat normalized_value=2.25 normalized_unit=s^-1; kcat/Km calculated from same row as 2.25/0.898=2.505567928730512 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=898 raw_unit=uM; kcat raw_value=2.25 raw_unit=sec-1; kenz raw_value=2,500 raw_unit=M-1 sec-1

row_label: AtCAD8 / substrate 5 (sinapyl aldehyde / sinapaldehyde)


column_label: Table 2 row AtCAD3, substrate 5 (sinapyl aldehyde / sinapaldehyde) lists Km 629 uM, kcat 0.74 sec-1, and kenz 1,200 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=0.629 normalized_unit=mM; kcat normalized_value=0.74 normalized_unit=s^-1; kcat/Km calculated from same row as 0.74/0.629=1.1764705882352942 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=629 raw_unit=uM; kcat raw_value=0.74 raw_unit=sec-1; kenz raw_value=1,200 raw_unit=M-1 sec-1

row_label: AtCAD3 / substrate 5 (sinapyl aldehyde / sinapaldehyde)


column_label: Table 2 row AtCAD2, substrate 5 (sinapyl aldehyde / sinapaldehyde) lists Km 2,161 uM, kcat 3.93 sec-1, and kenz 1,800 M-1 sec-1.

normalized_value_unit_evidence: Km normalized_value=2.161 normalized_unit=mM; kcat normalized_value=3.93 normalized_unit=s^-1; kcat/Km calculated from same row as 3.93/2.161=1.8186024988431282 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=2,161 raw_unit=uM; kcat raw_value=3.93 raw_unit=sec-1; kenz raw_value=1,800 raw_unit=M-1 sec-1

row_label: AtCAD2 / substrate 5 (sinapyl aldehyde / sinapaldehyde)


substrate_name: 4-Hydroxycinnamyl aldehyde

assay_conditions_summary: pH 6.25; 303.15 K; cofactor NADPH

column_label: The literal AtCAD5 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the independently printed kenz cell is retained as a distinct primary cell and is not substituted for the quotient.

normalized_value_unit_evidence: Km=0.013 mM; kcat=14.52 s^-1; current same-row quotient=1116.923076923077 s^-1 mM^-1; printed kenz=1091 s^-1 mM^-1; printed value is preserved separately without an equality record.

raw_value_unit_evidence: AtCAD5 substrate-1 cells: Km 13 μM; kcat 14.52 sec^-1; printed kenz 1,091,000 M^-1 sec^-1.

row_label: AtCAD5 / substrate 1

table_label: Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8

substrate: 4-Hydroxycinnamyl aldehyde


column_label: The literal AtCAD4 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the printed kenz cell independently corroborates the same row but is not substituted.

normalized_value_unit_evidence: Km=0.047 mM; kcat=3.44 s^-1; current same-row quotient=73.19148936170212 s^-1 mM^-1; printed kenz=74 s^-1 mM^-1; printed rounding is preserved separately.

raw_value_unit_evidence: AtCAD4 substrate-1 cells: Km 47 μM; kcat 3.44 sec^-1; printed kenz 74,000 M^-1 sec^-1.

row_label: AtCAD4 / substrate 1


column_label: The literal AtCAD7 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the printed kenz cell independently corroborates the same row but is not substituted.

normalized_value_unit_evidence: Km=0.320 mM; kcat=2.18 s^-1; current same-row quotient=6.8125 s^-1 mM^-1; printed kenz=6.8 s^-1 mM^-1; printed rounding is preserved separately.

raw_value_unit_evidence: AtCAD7 substrate-1 cells: Km 320 μM; kcat 2.18 sec^-1; printed kenz 6,800 M^-1 sec^-1.

row_label: AtCAD7 / substrate 1


column_label: The literal AtCAD8 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the printed kenz cell independently corroborates the same row but is not substituted.

normalized_value_unit_evidence: Km=0.302 mM; kcat=1.59 s^-1; current same-row quotient=5.264900662251656 s^-1 mM^-1; printed kenz=5.3 s^-1 mM^-1; printed rounding is preserved separately.

raw_value_unit_evidence: AtCAD8 substrate-1 cells: Km 302 μM; kcat 1.59 sec^-1; printed kenz 5,300 M^-1 sec^-1.

row_label: AtCAD8 / substrate 1


column_label: The literal AtCAD3 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the printed kenz cell independently corroborates the same row but is not substituted.

normalized_value_unit_evidence: Km=0.292 mM; kcat=1.65 s^-1; current same-row quotient=5.6506849315068495 s^-1 mM^-1; printed kenz=5.6 s^-1 mM^-1; printed rounding is preserved separately.

raw_value_unit_evidence: AtCAD3 substrate-1 cells: Km 292 μM; kcat 1.65 sec^-1; printed kenz 5,600 M^-1 sec^-1.

row_label: AtCAD3 / substrate 1


column_label: The literal AtCAD2 substrate-1 row binds the exact Km and kcat cells. The current stored efficiency is their deterministic quotient; the printed kenz cell independently corroborates the same row but is not substituted.

normalized_value_unit_evidence: Km=0.114 mM; kcat=0.27 s^-1; current same-row quotient=2.368421052631579 s^-1 mM^-1; printed kenz=2.4 s^-1 mM^-1; printed rounding is preserved separately.

raw_value_unit_evidence: AtCAD2 substrate-1 cells: Km 114 μM; kcat 0.27 sec^-1; printed kenz 2,400 M^-1 sec^-1.

row_label: AtCAD2 / substrate 1


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD5 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD4 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


verification_status: corrected

column_label: Table 2: Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8; row AtCAD7 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde); Km 0.756 mM; Vmax 2.7e-06 mol s^-1 g^-1; kcat 0.21 s^-1; kcat/Km 0.28 s^-1 mM^-1.

raw_value_unit_evidence: Km 756 uM; Vmax 2.7 pKat/ug; kcat 0.21 sec^-1; kenz 280 M^-1 sec^-1

status: corrected


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD8 / substrate 4 (5-hydroxyconiferyl aldehyde / 5-hydroxyconiferaldehyde), columns Km (uM), kcat (sec^-1), kenz (M^-1 sec^-1).


enzyme_display_name: Cinnamyl alcohol dehydrogenase 7

substrate_name: 4-coumaraldehyde (at pH 6.25-6.5 and 30 degrees Celsius)

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

kcat_over_km_display: Not reported

enzyme: Cinnamyl alcohol dehydrogenase 7

status: unverified

source: uniprot


substrate_name: caffeyl aldehyde (at pH 6.25 and 30 degrees Celsius)


substrate_name: coniferaldehyde (at pH 6.25 and 30 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 6.25 and 30 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25 and 30 degrees Celsius)


enzyme_display_name: Cinnamyl alcohol dehydrogenase 8

substrate_name: 4-coumaraldehyde (at pH 6.25 and 42 degrees Celsius)

enzyme: Cinnamyl alcohol dehydrogenase 8


substrate_name: caffeyl aldehyde (at pH 6.0 and 35 degrees Celsius)


substrate_name: coniferaldehyde (at pH 6.25 and 42 degrees Celsius)


substrate_name: 5-hydroxyconiferaldehyde (at pH 6.25 and 42 degrees Celsius)


substrate_name: sinapaldehyde (at pH 6.25-6.5 and 25 degrees Celsius)


enzyme_display_name: prostaglandin-F synthase

organism: Bos taurus

substrate_name: Prostaglandin D2

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

mutation_type: substitution

enzyme: prostaglandin-F synthase

substrate: Prostaglandin D2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H170C to reconstruct the assayed variant sequence.

proof_lines:
H170C
phenanthrenequinone
liver-type PGF synthase


proof_lines: K225S phenanthrenequinone PQ


proof_lines:
N306Y
phenanthrenequinone
PGF synthase


proof_lines: R223L phenanthrenequinone PQ


proof_lines: R27E phenanthrenequinone PQ


substrate_name: Prostaglandin H2

substrate: Prostaglandin H2


organism: Leucaena leucocephala

substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: NADP+

assay_conditions_summary: pH 8.8; 313.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: pH 6.5; 313.15 K; cofactor NADPH

substrate: NADPH


substrate_name: p-coumaryl aldehyde

substrate: p-coumaryl aldehyde


substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


substrate_name: sinapyl aldehyde

substrate: sinapyl aldehyde


organism: Aralia cordata

source_db: brenda

source: brenda


assay_conditions_summary: cofactor NADP+


assay_conditions_summary: cofactor NADPH


organism: Populus tremuloides

substrate_name: Coniferaldehyde

sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature L122W/G302F to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.0227 normalized_unit=mM; kcat normalized_value=11.111666666666666 normalized_unit=s^-1; kcat/Km normalized_value=490 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=22.7 +/- 6.2 raw_unit=uM; kcat raw_value=666.7 raw_unit=min^-1; kcat/Km raw_value=29.4 raw_unit=uM^-1 min^-1

table_label: PMC PMID 15829607 Table 2 - kinetic constants for wild-type and mutant aspen SAD


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W61L/F289P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_fasta_exact_accession and applied mutation signature W61L/L122W/F289P/G302F to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: km normalized_value=0.5047 normalized_unit=mM; kcat normalized_value=21.323333333333334 normalized_unit=s^-1; kcat/Km normalized_value=41.666666666666664 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=504.7 +/- 132.5 raw_unit=uM; kcat raw_value=1279.4 raw_unit=min^-1; kcat/Km raw_value=2.5 raw_unit=uM^-1 min^-1


column_label: PMC PMID 15829607 Table 2; column SAD/CLD; rows Km=78.0 +/- 16.0 uM, kcat=975.5 min^-1, kcat/Km=12.5 uM^-1 min^-1.

normalized_value_unit_evidence: km normalized_value=0.078 normalized_unit=mM; kcat normalized_value=16.258333333333333 normalized_unit=s^-1; kcat/Km normalized_value=208.33333333333334 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=78.0 +/- 16.0 raw_unit=uM; kcat raw_value=975.5 raw_unit=min^-1; kcat/Km raw_value=12.5 raw_unit=uM^-1 min^-1

row_label: SAD / CLD


substrate_name: Sinapoyl aldehyde

normalized_value_unit_evidence: km normalized_value=0.3998 normalized_unit=mM; kcat normalized_value=13.131666666666666 normalized_unit=s^-1; kcat/Km normalized_value=33.333333333333336 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=399.8 +/- 56.6 raw_unit=uM; kcat raw_value=787.9 raw_unit=min^-1; kcat/Km raw_value=2.0 raw_unit=uM^-1 min^-1


column_label: PMC PMID 15829607 Table 2; column SAD/SLD; rows Km=28.6 +/- 3.6 uM, kcat=2434.1 min^-1, kcat/Km=85.1 uM^-1 min^-1.

normalized_value_unit_evidence: km normalized_value=0.0286 normalized_unit=mM; kcat normalized_value=40.568333333333335 normalized_unit=s^-1; kcat/Km normalized_value=1418.3333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=28.6 +/- 3.6 raw_unit=uM; kcat raw_value=2434.1 raw_unit=min^-1; kcat/Km raw_value=85.1 raw_unit=uM^-1 min^-1

row_label: SAD / SLD


organism: Sorghum bicolor

substrate_name: 4-coumaryl aldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A278V to reconstruct the assayed variant sequence.

substrate: 4-coumaryl aldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L119W with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


proof_lines:
wild type
Prostaglandin D2
PGD2


organism: Ocimum basilicum

substrate_name: Geraniol

smiles: CC(C)=CCC/C(C)=C/CO

substrate: Geraniol


enzyme_display_name: Cinnamyl alcohol dehydrogenase 1

enzyme: Cinnamyl alcohol dehydrogenase 1


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


enzyme_display_name: Carbonyl reductase [NADPH] 1

organism: Homo sapiens

substrate_name: prostaglandin E1

column_label: Table IV; row PGE1; Michaelis constant column for the middle carbonyl reductase molecular form = 0.45 mM

normalized_value_unit_evidence: Km=0.45 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row PGE1; Michaelis constant middle molecular-form column = 0.45 mM

row_label: PGE1; middle molecular-form Michaelis constant column matching exported Km

table_label: Table IV / Michaelis constants and relative maximal velocities of the molecular forms of human brain carbonyl reductase

enzyme: Carbonyl reductase [NADPH] 1

substrate: prostaglandin E1


substrate_name: phenylglyoxal

column_label: Table IV; row Phenylglyoxal; Michaelis constant column for the middle carbonyl reductase molecular form = 4.0 mM

normalized_value_unit_evidence: Km=4.0 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row Phenylglyoxal; Michaelis constant middle molecular-form column = 4.0 mM

row_label: Phenylglyoxal; middle molecular-form Michaelis constant column matching exported Km

substrate: phenylglyoxal


column_label: Table IV; row 4-Nitrobenzaldehyde; Michaelis constant column for the middle carbonyl reductase molecular form = 1.6 mM

normalized_value_unit_evidence: Km=1.6 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row 4-Nitrobenzaldehyde; Michaelis constant middle molecular-form column = 1.6 mM

row_label: 4-Nitrobenzaldehyde; middle molecular-form Michaelis constant column matching exported Km


column_label: Table IV; row Ubiquinone-1; Michaelis constant column for the middle carbonyl reductase molecular form = 0.017 mM

normalized_value_unit_evidence: Km=0.017 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row Ubiquinone-1; Michaelis constant middle molecular-form column = 0.017 mM

row_label: Ubiquinone-1; middle molecular-form Michaelis constant column matching exported Km


substrate_name: Prostaglandin D2


organism: Artemisia annua

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

column_label: Figure 2D p-coumaryl aldehyde column reports Km 11.05 +/- 1.4, Kcat 12.36, and Kcat/Km 1.12.

raw_value_unit_evidence: Figure 2D p-coumaryl aldehyde column: Km 11.05 +/- 1.4 uM; Kcat 12.36 s^-1; Kcat/Km 1.12 uM^-1 s^-1

row_label: p-coumaryl aldehyde

table_label: Figure 2D


column_label: Figure 2D coniferyl aldehyde column reports Km 10.76 +/- 0.46, Kcat 13.82, and Kcat/Km 1.28.

raw_value_unit_evidence: Figure 2D coniferyl aldehyde column: Km 10.76 +/- 0.46 uM; Kcat 13.82 s^-1; Kcat/Km 1.28 uM^-1 s^-1

row_label: coniferyl aldehyde


column_label: Figure 2D sinapyl aldehyde column reports Km 1.94 +/- 0.71, Kcat 14.03, and Kcat/Km 7.23.

raw_value_unit_evidence: Figure 2D sinapyl aldehyde column: Km 1.94 +/- 0.71 uM; Kcat 14.03 s^-1; Kcat/Km 7.23 uM^-1 s^-1

row_label: sinapyl aldehyde


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


substrate_name: NADH

substrate: NADH


substrate_name: 9alpha,11beta-Prostaglandin F2

proof_lines:
9alpha,11beta-Prostaglandin F2
prostaglandin F synthase
Homo sapiens

substrate: 9alpha,11beta-Prostaglandin F2


proof_lines:
Prostaglandin D2
prostaglandin F synthase
Homo sapiens

substrate: Prostaglandin D2


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

sequence_source: multiple

assay_conditions_summary: pH 7; 310.15 K; buffer pH 7

column_label: PMC Table 1 row AKR1C3 / Delta4-androstene-3,17-dione reports Km 6.6 +/- 2.4 uM, kcat 0.16 +/- 0.02 min^-1, kcat/Km 24 min^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.002666667 s^-1; Km normalized_value=0.0066 mM; kcat/Km normalized_value=0.4 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.16 raw_unit=min^-1; Km raw_value=6.6 raw_unit=uM; kcat/Km raw_value=24 raw_unit=min^-1*mM^-1

row_label: AKR1C3 / Delta4-androstene-3,17-dione

table_label: Table 1

source_databases_merged: brenda skid


proof_lines:
pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7


assay_conditions_summary: pH 7; 310.15 K; buffer pH 7; cofactor NADPH

column_label: PMC Table 1 row AKR1C3 / PQ reports Km 1.5 +/- 0.7 uM, kcat 84 +/- 18 min^-1, kcat/Km 55000 min^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.4 s^-1; Km normalized_value=0.0015 mM; kcat/Km normalized_value=916.666667 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=84 raw_unit=min^-1; Km raw_value=1.5 raw_unit=uM; kcat/Km raw_value=55000 raw_unit=min^-1*mM^-1

row_label: AKR1C3 / PQ


column_label: PMC Table 1 row AKR1C2 / PQ reports Km 1.1 +/- 0.4 uM, kcat 110 +/- 18 min^-1, kcat/Km 100000 min^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.833333 s^-1; Km normalized_value=0.0011 mM; kcat/Km normalized_value=1666.666667 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=110 raw_unit=min^-1; Km raw_value=1.1 raw_unit=uM; kcat/Km raw_value=100000 raw_unit=min^-1*mM^-1

row_label: AKR1C2 / PQ


column_label: PMC Table 1 row AKR1C1 / PQ reports Km 0.73 +/- 0.2 uM, kcat 35 +/- 6.1 min^-1, kcat/Km 48000 min^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.5833333 s^-1; Km normalized_value=0.00073 mM; kcat/Km normalized_value=800 s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=35 raw_unit=min^-1; Km raw_value=0.73 raw_unit=uM; kcat/Km raw_value=48000 raw_unit=min^-1*mM^-1

row_label: AKR1C1 / PQ


organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

substrate_name: NADP

substrate: NADP


substrate_name: NAD

substrate: NAD


column_label: Table 4 reports sp2/AKR3C2 with isatin substrate: Km,NADPH 34 +/- 9.6 uM and kcat,NADPH 11.8 +/- 0.9 s^-1.

raw_value_unit_evidence: Km raw_value=34 raw_unit=uM

row_label: sp2/AKR3C2 / Isatin

table_label: Table 4 - Co-substrate utilization


assay_conditions_summary: cofactor NADH

column_label: Table 4 reports sp2/AKR3C2 with isatin substrate: Km,NADH 53.3 +/- 11 uM and kcat,NADH 4.2 +/- 0.6 s^-1.

raw_value_unit_evidence: Km raw_value=53.3 raw_unit=uM


substrate_name: menadione

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: Official PMC Table 3, Menadione row, CBR1 V88 Km (microM) column = 42 +/- 23; the adjacent I88 Km is 55 +/- 21 microM and neither column reports 22 microM.

normalized_value_unit_evidence: 42 +/- 23 microM = 0.042 mM; the current corrected top-level Km is 0.042 mM; the preserved source value was 0.022 mM.

raw_value_unit_evidence: Table 3 Menadione row, CBR1 V88 Km column: 42 +/- 23 microM.

row_label: Menadione row / CBR1 V88

table_label: Table 3 / CBR1 V88 and CBR1 I88 kinetic constants for prototypical substrates

substrate: menadione


substrate_name: daunorubicin

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 3 reports Daunorubicin row, CBR1 V88 Km column = 173 +/- 26 uM; normalized Km = 0.173 mM.

normalized_value_unit_evidence: Km=0.173 mM after converting 173 +/- 26 uM from uM to mM.

row_label: Daunorubicin row / CBR1 V88 Km column

substrate: daunorubicin


organism: Oryza sativa

substrate: Coniferaldehyde


substrate: Sinapoyl aldehyde


substrate_name: NADPH

substrate: NADPH


organism: Rattus norvegicus


substrate_name: prostaglandin E2

substrate: prostaglandin E2


substrate_name: retinal

assay_conditions_summary: pH 6.5; cofactor NADPH

column_label: Results text reports the K m value and specific activity for retinal of PGF synthase were 20 uM and 4 nmol/min/mg of protein, respectively.

raw_value_unit_evidence: Km raw_value=20 uM raw_unit=uM

row_label: Purified bovine lung PGF synthase / retinal reduction to retinol

table_label: Results text and Fig. 1C, PMID 11573958 PDF

substrate: retinal


proof_lines: PubMed abstract preserves NADPH-dependent reduction of PGH2, but the Km values reported there are for PGH2 rather than NADPH.


enzyme_display_name: prostaglandin-E2 9-reductase

column_label: Abstract states the Michaelis constant Km for PGE2 is 80 microM.

raw_value_unit_evidence: Km raw_value=80 raw_unit=microM

row_label: human decidua vera prostaglandin E2-9-oxoreductase with prostaglandin E2

table_label: PubMed abstract PMID 6586494

source_databases_merged: brenda uniprot

enzyme: prostaglandin-E2 9-reductase


substrate_name: D-xylose

proof_lines: prostaglandin D2 11-ketoreductase activity

substrate: D-xylose


organism: Trypanosoma brucei

substrate_name: Prostaglandin H2

substrate: Prostaglandin H2


column_label: Abstract reports that for NADPH, the equilibrium constant was 1.0 microM and Km was 1.6 microM.

raw_value_unit_evidence: Km raw_value=1.6 microM raw_unit=microM

row_label: prostaglandin-E2 9-ketoreductase / NADPH

table_label: PubMed XML abstract PMID 3459656


substrate_name: S-nitrosoglutathione

assay_conditions_summary: pH 6.8; cofactor NADPH

column_label: Table 2 row hCBR1 / GSNO, column Km (uM), gives 30.1 +/- 3.6

raw_value_unit_evidence: Km (uM) = 30.1 +/- 3.6 uM; article abstract/discussion round the same hCBR1 GSNO value to Km = 30 uM

row_label: hCBR1 / GSNO

table_label: Table 2

substrate: S-nitrosoglutathione


enzyme_display_name: 7alpha-hydroxysteroid dehydrogenase

organism: Pseudomonas sp.

substrate_name: cholic acid

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

enzyme: 7alpha-hydroxysteroid dehydrogenase

substrate: cholic acid


enzyme_display_name: aldose-6-phosphate reductase (NADPH)

organism: Malus domestica

smiles: C(C(C(C(C(COP(=O)(O)O)O)O)O)O)O

assay_conditions_summary: pH 9

enzyme: aldose-6-phosphate reductase (NADPH)


enzyme_display_name: 1,3-propanediol dehydrogenase

organism: Klebsiella pneumoniae

smiles: O=CCCO

enzyme: 1,3-propanediol dehydrogenase


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: NAD+

substrate: NAD+


substrate_name: NADH

substrate: NADH


smiles: OCCCO


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


enzyme_display_name: UniProt Q1QUN7

organism: Chromohalobacter salexigens

substrate_name: beta-D-glucuronate

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q1QUN7

substrate: beta-D-glucuronate

source: skid


enzyme_display_name: UniProt Q7CRQ0

organism: Agrobacterium tumefaciens

substrate_name: beta-D-galacturonate

enzyme: UniProt Q7CRQ0

substrate: beta-D-galacturonate


enzyme_display_name: uronate dehydrogenase

organism: Chromohalobacter israelensis

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

proof_lines: mutant enzyme L158A/N159C/I160V, at pH 8.0 and 25°C

enzyme: uronate dehydrogenase


proof_lines: mutant enzyme T113V/M175I/D246N, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/D246N, at pH 8.0 and 25°C


organism: [Ruminococcus] torques

substrate_name: 7-oxo-lithocholic acid

proof_lines: mutant enzyme I112V/T189I/N240D, at pH 8.0 and 30°C

substrate: 7-oxo-lithocholic acid


substrate_name: NADPH

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

substrate: NADPH


proof_lines: mutant enzyme K44E/T189I, at pH 8.0 and 30°C


proof_lines: mutant enzyme I28V/V38A/I76V/V207M, at pH 8.0 and 30°C


proof_lines: mutant enzyme I112V/N240D, at pH 8.0 and 30°C


proof_lines: mutant enzyme T189V/V207M, at pH 8.0 and 30°C


proof_lines: mutant enzyme G57S/I163V/V207M, at pH 8.0 and 30°C


proof_lines: mutant enzyme N99K/L100H/K102V/P103K/I105V, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I, at pH 8.0 and 25°C


proof_lines: mutant enzyme T113V/A172V/M175I/D236N, at pH 8.0 and 25°C


organism: Penicillium camemberti

proof_lines: with NADPH as cosubstrate, at pH 7.5 and 25°C


substrate_name: L-galactonate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, at pH 7.5 and 25°C

substrate: L-galactonate


substrate_name: L-Gulonic acid

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

substrate: L-Gulonic acid


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: D-glucuronic acid

proof_lines: with NADH as cosubstrate, at pH 7.5 and 25°C

substrate: D-glucuronic acid


proof_lines: with D-glucuronic acid as cosubstrate, at pH 7.5 and 25°C


organism: Lentilactobacillus buchneri


assay_conditions_summary: cofactor NAD+


smiles: C(CO)CO


substrate_name: glyceraldehyde

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

substrate: glyceraldehyde


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


organism: Blautia producta

substrate_name: 3,7-Diketo-5beta-cholanoic acid

substrate: 3,7-Diketo-5beta-cholanoic acid


substrate_name: 3,7,12-Triketo-5beta-cholanoic acid

substrate: 3,7,12-Triketo-5beta-cholanoic acid


substrate_name: 3,7,12-triketo-5beta-cholanoyl taurine

substrate: 3,7,12-triketo-5beta-cholanoyl taurine


enzyme_display_name: (+)-borneol dehydrogenase

organism: Pseudomonas putida

substrate_name: (+)-borneol

enzyme: (+)-borneol dehydrogenase

substrate: (+)-borneol


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: NAD+


organism: Pseudomonas sp. ATCC 17453

km_display: Not reported


substrate_name: (-)-borneol

proof_lines: mutant enzyme S146A/Y188A, at pH 7.5 and 30°C

substrate: (-)-borneol


proof_lines: mutant enzyme S146A/Y188T, at pH 7.5 and 30°C


organism: Hathewaya limosa


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Levilactobacillus brevis

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+


organism: Thermobispora bispora

substrate_name: D-galacturonic acid

substrate: D-galacturonic acid


substrate_name: D-glucuronic acid from a beechwood xylan


assay_conditions_summary: pH 7; 333.15 K; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

substrate: NADH


smiles: C(CO)C=O


organism: Oceanicola granulosus

substrate_name: beta-D-galacturonate

protein_accession_database: NCBI Protein

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

assay_conditions_summary: buffer recombinant His-tagged enzyme

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, potassium phosphate buffer

proof_lines: recombinant His-tagged enzyme, pH and temperature not specified in the publication, Tris buffer

substrate: beta-D-galacturonate


substrate_name: D-Mannuronate

substrate: D-Mannuronate


assay_conditions_summary: buffer recombinant His-tagged enzyme; cofactor NAD+


organism: Artemisia annua

substrate_name: (-)-cis-carveol

substrate: (-)-cis-carveol


substrate_name: (-)-artemisia alcohol

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

substrate: (-)-artemisia alcohol


organism: Pseudomonas sp. TCU-HL1

proof_lines: refolded isoform BDH1, at pH 7.0, temperature not specified in the publication

proof_lines: refolded recombinant protein, pH 7, 25°C

proof_lines: soluble isoform BDH1, at pH 7.0, temperature not specified in the publication


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Fulvimarina pelagi

sequence_source: NCBI protein accession ZP_01440880.1


assay_conditions_summary: pH 8; buffer recombinant His-tagged enzyme; cofactor NAD+

column_label: Table 1; row F. pelagi / NAD+; KP i-Buffer columns kcat, Km, and kcat/Km; expected kcat/Km 565 does not match explicit table value 785.

row_label: F. pelagi / NAD+


organism: Streptomyces viridochromogenes

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


organism: Cinnamomum camphora

proof_lines:
isoform BDH3, at pH 9.0 and 32°C
isoform BDH3, at pH 8.5 and 30°C


organism: Polaromonas naphthalenivorans

proof_lines:
pH 8.0, 25°C, method A
pH 8.0, 25°C, method B


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
pH 8.0, 25°C, method B
pH 8.0, 25°C, method A


organism: Pseudomonas monteilii

assay_conditions_summary: pH 7

proof_lines:
at pH 7.0 and 25°C
at pH 11.0 and 25°C
pH 7, 25°C


proof_lines:
pH 7, 25°C
at pH 7.0 and 25°C
pH 11, 25°C


organism: Ectopseudomonas mendocina

assay_conditions_summary: pH 8


assay_conditions_summary: pH 8; cofactor NAD+


organism: Pseudomonas sp.


organism: Chromohalobacter israelensis


assay_conditions_summary: pH 9


organism: Lavandula x intermedia


enzyme_display_name: 7beta-hydroxysteroid dehydrogenase

organism: Clostridium sardiniense

substrate_name: ursocholate

proof_lines: kcat is 407000 sec(-1) for the oxidation of ursocholate. kcat is 203000 sec(-1) for the reduction of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate. kcat is 430000 sec(-1) for the oxidation of ursodeoxycholate. kcat is 639000 sec(-1) for th

enzyme: 7beta-hydroxysteroid dehydrogenase

substrate: ursocholate


substrate_name: ursodeoxycholate

substrate: ursodeoxycholate


substrate_name: dehydrocholate

substrate: dehydrocholate


organism: Sus scrofa

substrate_name: prostaglandin E2

proof_lines: kcats are 2 min(-1), 285 min(-1), 460 min(-1), 58 min(-1) for prostaglandin E2, menadione, 9,1 O-phenanthrene-quinone and 4-nitrobenzaldehyde as substrates, respectively.

substrate: prostaglandin E2


substrate_name: menadione

substrate: menadione


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Collinsella aerofaciens (strain ATCC 25986 / DSM 3979 / JCM 10188 / KCTC 3647 / NCTC 11838 / VPI 1003)

substrate_name: NADP(+)

proof_lines: kcat is 1179 min(-1) for the oxidation of ursodeoxycholate. kcat is 951 min(-1) for the reduction of 7-oxolithocholate. kcat is 875 min(-1) for the reduction of dehydrocholate.

substrate: NADP(+)


organism: Collinsella aerofaciens

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table 1 row NADPH columns KM (uM)=4.50 and Kcat (min^-1)=1033.44

normalized_value_unit_evidence: KM=0.00450 mM; Kcat=17.2240 s^-1; kcat_over_km=3822.2222 s^-1*mM^-1 from rounded source values; full table-cell quotient=3827.56 s^-1*mM^-1

raw_value_unit_evidence: Table 1 cells: KM=4.50 uM; Kcat=1033.44 min^-1

row_label: NADPH

table_label: Table 1 Summary of kinetic constants for 7beta-HSDH from C. aerofaciens


substrate_name: Ursodeoxycholic acid

substrate: Ursodeoxycholic acid


organism: Agrobacterium tumefaciens

substrate_name: D-glucuronate

proof_lines: kcat is 190 sec(-1) and 92 sec(-1) with D-glucuronate and D-galacturonate as substrate, respectively.

source_databases_merged: skid uniprot

substrate: D-glucuronate


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: Uronate dehydrogenase

organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)

proof_lines: kcat is 74 sec(-1) and 24 sec(-1) with D-glucuronate and D-galacturonate as substrate, respectively.

enzyme: Uronate dehydrogenase


substrate_name: NAD(+)

column_label: Table 2 row P. syringae / NAD+ reports Km 0.17 ± 0.07 mM.

row_label: P. syringae / NAD+

table_label: PMC2648182 Table 2

substrate: NAD(+)


organism: Malus domestica

substrate_name: D-glucose 6-phosphate

smiles: C(C(C(C(C(C=O)O)O)O)O)OP(=O)(O)O

proof_lines:
C-term tagged enzyme
N-term tagged enzyme
pH 9.0, presence of 2.5 mM MgCl2

substrate: D-glucose 6-phosphate


organism: Pseudomonas putida KT2440

substrate_name: D-galacturonate

proof_lines: kcat is 55 sec(-1) and 30 sec(-1) with D-glucuronate and D-galacturonate as substrate, respectively.

substrate: D-galacturonate


substrate_name: tauroursodeoxycholate

substrate: tauroursodeoxycholate


organism: Salvia officinalis


substrate_name: (+)-borneol

substrate: (+)-borneol


organism: Mediterraneibacter gnavus

assay_conditions_summary: pH 6; 310.15 K; cofactor NADPH

column_label: Table 1 row Ruminococcus gnavus N53 / 7-oxo-LCA reports K_m (uM) = 38.8.

raw_value_unit_evidence: Km raw_value=38.8 raw_unit=uM

row_label: Ruminococcus gnavus N53 / 7-oxo-LCA

table_label: PMC3793610 Table 1, Kinetic parameters of 7beta-HSDHs purified from UDCA-producing bacteria


substrate_name: 7-oxolithocholate (7-oxo-LCA) (at pH 6 and 37 degrees Celsius)


proof_lines: kcat is 700 min(-1) for the reduction of 7-oxolithocholate (7-oxo-LCA) (at pH 6 and 37 degrees Celsius). kcat is 326 min(-1) for the oxidation of ursodeoxycholate (UDCA) (at pH 10 and 37 degrees Celsius).


organism: Chromohalobacter salexigens

substrate_name: beta-D-glucuronate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature T113V/M175L/D246N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

column_label: Table 3 (GluUA column group); enzyme row 'TMD'; column 'kcat (s^-1)' = 179; column 'Km (mM)' = 1.1; column 'kcat/ Km (s^-1 mM^-1)' = 164

normalized_value_unit_evidence: kcat: printed Table 3 cell 179 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 179.0 s^(-1), which is the exported value. Km: printed Table 3 cell 1.1 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 1.1 mM, which is the exported value. kcat/Km: printed Table 3 cell 164 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 164.0 s^(-1)*mM^(-1). The catalog holds 162.72727272727272 for this metric, which is the full-precision quotient of the two component cells; the paper's own fitted efficiency cell replaces it.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'TMD': kcat = 179 s^-1; Km = 1.1 mM; printed kcat/Km = 164 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'TMD', the mutation combination T113V/M175L/D246N under the abbreviations the text assigns

table_label: Table 3: Thermal stability Kt0.5 and Michaelis-Menten kinetic parameter values for enzymes acting on glucuronic acid (GluUA) and galacturonic acid (GalUA) at 25 C (Process Biochem author manuscript, GluUA column group)

substrate: beta-D-glucuronate


organism: Homo sapiens


substrate_name: toluquinone

substrate: toluquinone


substrate_name: prostaglandin A1

substrate: prostaglandin A1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature D246N to reconstruct the assayed variant sequence.

column_label: Table 3 (GluUA column group); enzyme row 'D246N'; column 'kcat (s^-1)' = 192; column 'Km (mM)' = 1.3; column 'kcat/ Km (s^-1 mM^-1)' = 146

normalized_value_unit_evidence: kcat: printed Table 3 cell 192 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 192.0 s^(-1), which is the exported value. Km: printed Table 3 cell 1.3 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 1.3 mM, which is the exported value. kcat/Km: printed Table 3 cell 146 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 146.0 s^(-1)*mM^(-1). The catalog holds 147.69230769230768 for this metric, which is the full-precision quotient of the two component cells; the paper's own fitted efficiency cell replaces it.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'D246N': kcat = 192 s^-1; Km = 1.3 mM; printed kcat/Km = 146 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'D246N (D)'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature I114T to reconstruct the assayed variant sequence.

column_label: Table 3 (GluUA column group); enzyme row 'I114T'; column 'kcat (s^-1)' = 155; column 'Km (mM)' = 3.2; column 'kcat/ Km (s^-1 mM^-1)' = 48

normalized_value_unit_evidence: kcat: printed Table 3 cell 155 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 155.0 s^(-1), which is the exported value. Km: printed Table 3 cell 3.2 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 3.2 mM, which is the exported value. kcat/Km: printed Table 3 cell 48 s^-1 mM^-1, a two-significant-figure cell whose rounding interval spans 47.5 to 48.5 s^-1 mM^-1; the exported 48.4375 is the exact quotient of the two component cells above and lies inside that interval, so the printed cell corroborates the exported value at the precision the paper prints.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'I114T': kcat = 155 s^-1; Km = 3.2 mM; printed kcat/Km = 48 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'I114T'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature I88L to reconstruct the assayed variant sequence.

column_label: Table 3 (GluUA column group); enzyme row 'I88L'; column 'kcat (s^-1)' = 192; column 'Km (mM)' = 1.5; column 'kcat/ Km (s^-1 mM^-1)' = 125

normalized_value_unit_evidence: kcat: printed Table 3 cell 192 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 192.0 s^(-1), which is the exported value. Km: printed Table 3 cell 1.5 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 1.5 mM, which is the exported value. kcat/Km: printed Table 3 cell 125 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 125.0 s^(-1)*mM^(-1). The catalog holds 128.0 for this metric, which is the full-precision quotient of the two component cells; the paper's own fitted efficiency cell replaces it.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'I88L': kcat = 192 s^-1; Km = 1.5 mM; printed kcat/Km = 125 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'I88L'


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M175I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature N99K/L100H/K102V/P103K/I105V to reconstruct the assayed variant sequence.

column_label: Table 3 (GluUA column group); enzyme row 'CsUDH99'; column 'kcat (s^-1)' = 142; column 'Km (mM)' = 0.9; column 'kcat/ Km (s^-1 mM^-1)' = 162

normalized_value_unit_evidence: kcat: printed Table 3 cell 142 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 142.0 s^(-1), which is the exported value. Km: printed Table 3 cell 0.9 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 0.9 mM, which is the exported value. kcat/Km: printed Table 3 cell 162 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 162.0 s^(-1)*mM^(-1). The catalog holds 157.77777777777777 for this metric, which is the full-precision quotient of the two component cells; the paper's own fitted efficiency cell replaces it.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'CsUDH99': kcat = 142 s^-1; Km = 0.9 mM; printed kcat/Km = 162 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'CsUDH99', whose footnote c reads Mutation CsUDH99 = N99K, L100H, K102V, P103K, I105V


sequence_variant_note: Mutation signature N99K/L100H/K102V/P103K/I105V/Y116F/T113V/A172V/M175I/D236N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1QUN7 and applied mutation signature Q55R to reconstruct the assayed variant sequence.

column_label: Table 3 (GluUA column group); enzyme row 'Q55R'; column 'kcat (s^-1)' = 270; column 'Km (mM)' = 1.7; column 'kcat/ Km (s^-1 mM^-1)' = 161

normalized_value_unit_evidence: kcat: printed Table 3 cell 270 s^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 270.0 s^(-1), which is the exported value. Km: printed Table 3 cell 1.7 mM; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 1.7 mM, which is the exported value. kcat/Km: printed Table 3 cell 161 s^-1 mM^-1; the printed unit is already the canonical unit, so no unit conversion applies and the value carries over as 161.0 s^(-1)*mM^(-1). The catalog holds 158.8235294117647 for this metric, which is the full-precision quotient of the two component cells; the paper's own fitted efficiency cell replaces it.

raw_value_unit_evidence: Table 3, GluUA column group, enzyme row 'Q55R': kcat = 270 s^-1; Km = 1.7 mM; printed kcat/Km = 161 s^-1 mM^-1.

row_label: Table 3, GluUA half, enzyme row 'Q55R'


sequence_variant_note: Mutation signature T113V/A172V/D246N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature T113V/A172V/M175I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature T113V/A172V/M175I/D236N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Klebsiella pneumoniae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D41G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


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


substrate_name: NADH

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


substrate_name: prostaglandin E1

column_label: Table IV; row PGE1; Michaelis constant column for the middle carbonyl reductase molecular form = 0.45 mM

normalized_value_unit_evidence: Km=0.45 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row PGE1; Michaelis constant middle molecular-form column = 0.45 mM

row_label: PGE1; middle molecular-form Michaelis constant column matching exported Km

substrate: prostaglandin E1


substrate_name: phenylglyoxal

column_label: Table IV; row Phenylglyoxal; Michaelis constant column for the middle carbonyl reductase molecular form = 4.0 mM

normalized_value_unit_evidence: Km=4.0 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row Phenylglyoxal; Michaelis constant middle molecular-form column = 4.0 mM

row_label: Phenylglyoxal; middle molecular-form Michaelis constant column matching exported Km

substrate: phenylglyoxal


column_label: Table IV; row 4-Nitrobenzaldehyde; Michaelis constant column for the middle carbonyl reductase molecular form = 1.6 mM

normalized_value_unit_evidence: Km=1.6 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row 4-Nitrobenzaldehyde; Michaelis constant middle molecular-form column = 1.6 mM

row_label: 4-Nitrobenzaldehyde; middle molecular-form Michaelis constant column matching exported Km


column_label: Table IV; row Ubiquinone-1; Michaelis constant column for the middle carbonyl reductase molecular form = 0.017 mM

normalized_value_unit_evidence: Km=0.017 mM; paper reports Michaelis constant directly in mM

raw_value_unit_evidence: Table IV row Ubiquinone-1; Michaelis constant middle molecular-form column = 0.017 mM

row_label: Ubiquinone-1; middle molecular-form Michaelis constant column matching exported Km


substrate_name: menadione

proof_lines:
menadione
CBR1 V88I
wild-type CBR1

substrate: menadione


substrate_name: prostaglandin E2

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 3 reports PGE2 row, CBR1 V88 Km column = 309 +/- 94 uM; normalized Km = 0.309 mM.

normalized_value_unit_evidence: Km=0.309 mM after converting 309 +/- 94 uM from uM to mM.

row_label: PGE2 row / CBR1 V88 Km column

substrate: prostaglandin E2


substrate_name: daunorubicin

column_label: Table 3 reports Daunorubicin row, CBR1 V88 Km column = 173 +/- 26 uM; normalized Km = 0.173 mM.

row_label: Daunorubicin row / CBR1 V88 Km column

substrate: daunorubicin


substrate_name: NADPH

column_label: Table 3 reports NADPH row, CBR1 V88 Km column = 247 +/- 29 uM; normalized Km = 0.247 mM; footnote b says menadione was held constant at 250 uM.

normalized_value_unit_evidence: Km=0.247 mM after converting 247 +/- 29 uM from uM to mM.

row_label: NADPH row / CBR1 V88 Km column

substrate: NADPH


organism: Citrobacter freundii

assay_conditions_summary: pH 7.5; buffer 100 mM triethanolamine; cofactor NADH

column_label: PMID 7721705 / DOI 10.1128/jb.177.8.2151-2156.1995, Results paragraph, apparent Km for 3-hydroxypropionaldehyde = 0.14 mM; paper label is synonym of 3-hydroxypropanal.

raw_value_unit_evidence: Results paragraph reports apparent Km value of 0.14 mM for 3-hydroxypropionaldehyde.

table_label: Results prose: Substrate specificity and kinetic properties


assay_conditions_summary: pH 9; buffer pH 9; cofactor NAD+

column_label: PMID 7721705 / DOI 10.1128/jb.177.8.2151-2156.1995, Results paragraph, apparent Km for 1,3-propanediol = 1.25 mM.

raw_value_unit_evidence: Results paragraph reports apparent Km value of 1.25 mM for 1,3-propanediol.


substrate_name: propionaldehyde

column_label: PMID 7721705 / DOI 10.1128/jb.177.8.2151-2156.1995, Results paragraph, apparent Km for propionaldehyde = 11 mM.

raw_value_unit_evidence: Results paragraph reports apparent Km value of 11 mM for propionaldehyde.

row_label: propionaldehyde

substrate: propionaldehyde


substrate_name: NAD(+) (with 1,3-propanediol as substrate)

column_label: PMID 7721705 / DOI 10.1128/jb.177.8.2151-2156.1995, Results paragraph, apparent Km for NAD+ with 1,3-propanediol = 0.3 mM.

normalized_value_unit_evidence: Km=0.3 mM

raw_value_unit_evidence: Results paragraph reports apparent Km value for NAD+ was 0.3 mM with 1,3-propanediol.

row_label: NAD+ with 1,3-propanediol


substrate_name: NADH (with propionaldehyde as substrate)

column_label: PMID 7721705 / DOI 10.1128/jb.177.8.2151-2156.1995, Results paragraph, apparent Km for NADH with propionaldehyde = 0.033 mM.

raw_value_unit_evidence: Results paragraph reports apparent Km value for NADH was 0.033 mM with propionaldehyde.

row_label: NADH with propionaldehyde


organism: Oenococcus oeni

substrate_name: NAD+

assay_conditions_summary: pH 9; cofactor NAD+

substrate: NAD+


smiles: CC(CO)O


organism: Prunus persica

column_label: Official Oxford article HTML Table 1 row Glc-6P reduction / NADPH, column Km (mM), reports 0.031 +/- 0.001.

normalized_value_unit_evidence: Km normalized 0.031 mM.

raw_value_unit_evidence: Km raw 0.031 +/- 0.001 mM for NADPH.

row_label: Glc-6P reduction; NADPH

table_label: Table 1. Kinetic parameters for the substrates of Ald6PRase from peach


assay_conditions_summary: pH 8; cofactor NADP+

column_label: Official Oxford article HTML Table 1 row Gol-6P oxidation / NADP+, column Km (mM), reports 0.059 +/- 0.006.

normalized_value_unit_evidence: Km normalized 0.059 mM.

row_label: Gol-6P oxidation; NADP+


substrate_name: D-sorbitol 6-phosphate

smiles: OCC(O)C(O)C(O)C(O)COP(=O)(O)O

substrate: D-sorbitol 6-phosphate


substrate_name: Dehydrocholic acid

column_label: Table 1 row Dehydrocholic acid columns KM (uM)=9.23 and Kcat (min^-1)=875.35

normalized_value_unit_evidence: KM=0.00923 mM; Kcat=14.5892 s^-1; kcat_over_km=1586.9565 s^-1*mM^-1 from rounded source values; full table-cell quotient=1580.62 s^-1*mM^-1

raw_value_unit_evidence: Table 1 cells: KM=9.23 uM; Kcat=875.35 min^-1

row_label: Dehydrocholic acid

substrate: Dehydrocholic acid


column_label: Table 1 row NADP+ columns KM (uM)=5.32 and Kcat (min^-1)=944.95

normalized_value_unit_evidence: KM=0.00532 mM; Kcat=15.7492 s^-1; kcat_over_km=2962.2642 s^-1*mM^-1 from rounded source values; full table-cell quotient=2960.37 s^-1*mM^-1

raw_value_unit_evidence: Table 1 cells: KM=5.32 uM; Kcat=944.95 min^-1

row_label: NADP+


substrate_name: 7-ketolithocholic acid

column_label: Table 1 row KLA columns KM (uM)=5.20 and Kcat (min^-1)=950.77

normalized_value_unit_evidence: KM=0.00520 mM; Kcat=15.8462 s^-1; kcat_over_km=3038.4615 s^-1*mM^-1 from rounded source values; full table-cell quotient=3047.34 s^-1*mM^-1

raw_value_unit_evidence: Table 1 cells: KM=5.20 uM; Kcat=950.77 min^-1

row_label: KLA (7-ketolithocholic acid)

substrate: 7-ketolithocholic acid


organism: Oryza sativa

column_label: Abstract states K m values for glucose-6-phosphate and sorbitol-6-phosphate were 15.9 +/- 0.2 and 7.21 +/- 0.5 mM, respectively.

raw_value_unit_evidence: Km raw_value=7.21 mM raw_unit=mM

row_label: Oryza sativa S6PDH / sorbitol-6-phosphate

table_label: PubMed XML abstract


substrate_name: D-glucose 6-phosphate

raw_value_unit_evidence: Km raw_value=15.9 mM raw_unit=mM

row_label: Oryza sativa S6PDH / glucose-6-phosphate

substrate: D-glucose 6-phosphate


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

organism: Mesocricetus auratus

substrate_name: corticosterone

column_label: PMID 14973125 Table II, Oxidation of corticosterone, Hamster row, Km (nM) = 321 +/- 48.

normalized_value_unit_evidence: Km normalized_value=0.000321 mM.

raw_value_unit_evidence: Table II row Oxidation of corticosterone / Hamster, Km column: 321 +/- 48 nM.

row_label: Oxidation of corticosterone / Hamster

table_label: Table II. Oxidation and reduction of glucocorticoids and 7-oxycholesterols in intact HEK-293 cells expressing recombinant 11beta-HSD1

enzyme: 11-beta-hydroxysteroid dehydrogenase 1

substrate: corticosterone


column_label: PMID 14973125 Table II, Reduction of 11-dehydrocorticosterone, Hamster row, Km (nM) = 726 +/- 118.

normalized_value_unit_evidence: Km normalized_value=0.000726 mM.

raw_value_unit_evidence: Table II row Reduction of 11-dehydrocorticosterone / Hamster, Km column: 726 +/- 118 nM.


table_label: Table II

row_label: Reduction of 7-ketocholesterol / Hamster

column_label: Km

metric_label: Km

raw_unit: nM

normalized_unit: mM

assay_condition: Intact HEK-293 cells transiently expressing hamster recombinant 11beta-HSD1; steroid-free medium; reduction of 7-ketocholesterol; data are mean +/- S.D. from at least four independent experiments; apparent Km calculated by Eadie-Hofstee assuming first-order rate kinetics.


organism: Rattus norvegicus


column_label: Table II, Reduction of 7-ketocholesterol, row Rat, Km column = 776 +/- 154 nM

row_label: Reduction of 7-ketocholesterol / Rat


organism: Saimiri sciureus

substrate_name: cortisol

substrate: cortisol


substrate_name: cortisone

substrate: cortisone


organism: Mus musculus

column_label: Table 2 row 7-Ketocholesterol / Reduction; Km (uM) column = 1 269 +/- 282.

raw_value_unit_evidence: Km raw_value=1269 +/- 282 raw_unit=uM

row_label: Recombinant protein / 7-Ketocholesterol / Reduction

table_label: PMC3694296 Table 2, Kinetic parameters describing metabolism of 7-oxysterols and glucocorticoids by murine 11betaHSD1


assay_conditions_summary: cofactor NADP+

column_label: Table 2 row Corticosterone / Oxidation; Km (uM) column = 1.78 +/- 0.56.

raw_value_unit_evidence: Km raw_value=1.78 +/- 0.56 raw_unit=uM

row_label: Recombinant protein / Corticosterone / Oxidation


proof_lines:
11 beta-HSD
cortisone
Michaelis-Menten constant


proof_lines:
11 beta-HSD
cortisol
K(M) values


organism: Thermobispora bispora

substrate_name: D-galacturonic acid

substrate: D-galacturonic acid


assay_conditions_summary: pH 7; 333.15 K; cofactor NAD+


substrate_name: S-nitrosoglutathione

assay_conditions_summary: pH 6.8; cofactor NADPH

column_label: Table 2 row hCBR1 / GSNO, column Km (uM), gives 30.1 +/- 3.6

raw_value_unit_evidence: Km (uM) = 30.1 +/- 3.6 uM; article abstract/discussion round the same hCBR1 GSNO value to Km = 30 uM

row_label: hCBR1 / GSNO

substrate: S-nitrosoglutathione


column_label: Abstract reports Km values for D-sorbitol 6-phosphate oxidation and D-glucose 6-phosphate reduction were 3.9 and 20 millimolar, respectively.

raw_value_unit_evidence: Km raw_value=3.9 millimolar raw_unit=mM

row_label: Apple leaf aldose-6-phosphate reductase / D-sorbitol 6-phosphate oxidation

table_label: PubMed XML abstract PMID 16661614


organism: Cavia porcellus


organism: Clostridium sardiniense

substrate_name: NADP+

substrate: NADP+


row_label: Reduction of 7-ketocholesterol / Human

metric: Km

assay_condition: Intact HEK-293 cells transiently expressing human recombinant 11beta-HSD1; steroid-free medium; reduction of 7-ketocholesterol; data are mean +/- S.D. from at least four independent experiments; apparent Km calculated by Eadie-Hofstee assuming first-order rate kinetics.


column_label: Abstract states the Km values for corticosterone and 7alpha-hydroxycholesterol were 1.2 and 1.9 microM, respectively, for purified 7alpha-HCD.

raw_value_unit_evidence: Km raw_value=1.9 raw_unit=microM

row_label: hamster liver microsomal 7alpha-hydroxycholesterol dehydrogenase with 7alpha-hydroxycholesterol

table_label: PubMed abstract PMID 9632680


assay_conditions_summary: pH 6; cofactor NADPH

column_label: Results prose reports the Km for 11-DHC (11beta-reductase) was 120 +/- 10 nM in wild-type liver.

raw_value_unit_evidence: Km raw_value=120 +/- 10 nM raw_unit=nM

row_label: Wild-type mouse liver homogenate / 11-DHC (11beta-reductase)

table_label: Official PMC Results prose: 11beta-HSD-1 knockout liver 11-DHC reductase Km


enzyme_display_name: UniProt A0A6L8P2U9

organism: Bacillus anthracis

enzyme: UniProt A0A6L8P2U9


substrate_name: IMP

substrate: IMP


enzyme_display_name: UniProt Q756Z6

organism: Eremothecium gossypii

enzyme: UniProt Q756Z6


enzyme_display_name: UniProt Q8T6T2

organism: Cryptosporidium parvum

substrate_name: 3-acetylpyridine adenine dinucleotide

enzyme: UniProt Q8T6T2

substrate: 3-acetylpyridine adenine dinucleotide


enzyme_display_name: IMP dehydrogenase

organism: Saccharomyces cerevisiae

enzyme: IMP dehydrogenase


enzyme_display_name: UniProt Q91WR5

substrate_name: lithocholic acid

enzyme: UniProt Q91WR5

substrate: lithocholic acid


proof_lines:
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=-----, pH=-----


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


enzyme_display_name: tropinone reductase I

organism: Pseudomonas sp.

substrate_name: Tropine

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

enzyme: tropinone reductase I

substrate: Tropine


substrate_name: nortropine

substrate: nortropine


organism: Homo sapiens

substrate_name: H2O; IMP; NAD+

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

assay_conditions_summary: cofactor NAD+

substrate: H2O; IMP; NAD+


substrate_name: NAD+; H2O; IMP

substrate: NAD+; H2O; IMP


enzyme_display_name: UniProt A0A2R4D3F6

organism: Campylobacter jejuni

substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

enzyme: UniProt A0A2R4D3F6

substrate: NAD+


enzyme_display_name: (-)-menthol dehydrogenase

organism: Mentha arvensis

substrate_name: (-)-menthol

enzyme: (-)-menthol dehydrogenase

substrate: (-)-menthol


organism: Mentha x piperita


substrate_name: (-)-menthone

substrate: (-)-menthone


enzyme_display_name: (+)-neomenthol dehydrogenase

enzyme: (+)-neomenthol dehydrogenase


substrate_name: NADPH

assay_conditions_summary: pH 7; 304.15 K; cofactor NADPH

substrate: NADPH


proof_lines: recombinant His6-tagged enzyme, pH 7.0, 30°C


assay_conditions_summary: pH 9.3; 304.15 K; cofactor NADPH

proof_lines:
pH 9.3, 31°C, recombinant enzyme
(-)-menthone


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


assay_conditions_summary: pH 9.3; 304.15 K; cofactor NADP+


organism: Dendrobium nobile

proof_lines: pH 8.0, 25°C, recombinant His-tagged enzyme


substrate_name: tropinone

substrate: tropinone


organism: Oryctolagus cuniculus

substrate_name: Epitestosterone

proof_lines: liver isozyme IB, androsterone, kidney, isozyme IB

substrate: Epitestosterone


substrate_name: androsterone

proof_lines:
liver isozyme IC
kidney isozyme II, liver isozyme IB

substrate: androsterone


proof_lines:
type II enzyme
type I enzyme
at pH 8.0 and 25°C


organism: Withania somnifera

sequence_source: paper_cDNA_translation: KF360055.1

assay_conditions_summary: pH 6.7; buffer MES-NaOH; cofactor NADP+

column_label: Table 2; row NADP+; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=0.54 s^-1; Km paper=0.09615 mM; kcat/Km paper=0.559 s^-1 mM^-1

table_label: Table 2. Kinetic parameters of Withania somnifera tropine forming tropinone reductase (WsTR-I) catalyzed reaction


column_label: Table 2; row Tropine; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=1.67 s^-1; Km paper=114.94 mM; kcat/Km paper=0.014 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row Tropine: Km 114.94 mM; kcat 1.67 s^-1; kcat/Km 0.14 x 10^2 M^-1 s^-1; dimer kcat 3.33 s^-1.

row_label: Tropine


column_label: Table 2; row 3-methyl-cyclohexanone; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=9.23 s^-1; Km paper=2.11 mM; kcat/Km paper=4.38 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row 3-methyl-cyclohexanone: Km 2.11 mM; kcat 9.23 s^-1; kcat/Km 4.38 x 10^3 M^-1 s^-1; dimer kcat 18.46 s^-1.


substrate_name: N-methylpiperidine

column_label: Table 2; row N-methyl-piperidine; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=8.97 s^-1; Km paper=1.74 mM; kcat/Km paper=5.17 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row N-methyl-piperidine: Km 1.74 mM; kcat 8.97 s^-1; kcat/Km 5.17 x 10^3 M^-1 s^-1; dimer kcat 17.95 s^-1.

row_label: N-methyl-piperidine

substrate: N-methylpiperidine


column_label: Table 2; row Tropinone; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=9.51 s^-1; Km paper=1.27 mM; kcat/Km paper=7.49 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row Tropinone: Km 1.27 mM; kcat 9.51 s^-1; kcat/Km 7.49 x 10^3 M^-1 s^-1; dimer kcat 19.03 s^-1.

row_label: Tropinone


assay_conditions_summary: pH 6.7; buffer MES-NaOH; cofactor NADPH

column_label: Table 2; row NADPH; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=33.34 s^-1; Km paper=0.00043 mM; kcat/Km paper=77400 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row NADPH: Km 0.43 uM; kcat 33.34 s^-1; kcat/Km 7.74 x 10^7 M^-1 s^-1; dimer kcat 66.68 s^-1.

row_label: NADPH


substrate_name: Unknown

proof_lines:
type I isoform
against type II isoform
at pH 8.0 and 25°C

substrate: Unknown


organism: Chlorocebus aethiops


organism: Przewalskia tangutica

proof_lines:
pH 6.4, 30°C, enzyme TRI
pH 6.4, 30°C


proof_lines:
type II
type I
at pH 8.0 and 25°C


organism: Artemisia annua

sequence_source: GenBank GU167953.1 CDS translation (RED1; PMID 20483909)

assay_conditions_summary: pH 7; buffer 500 uM NADPH in; cofactor NADPH

column_label: Table 3, row (-)-Menthone, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); primary PDF page 7, journal page 1225.

row_label: (-)-Menthone

table_label: Table 3


substrate_name: (+)-neomenthol

assay_conditions_summary: pH 7; buffer 500 uM NADP+ in; cofactor NADP+

column_label: Table 3, row (+)-Neomenthol, columns Km (uM), kcat (s^-1), and kcat/Km (M^-1 s^-1); primary PDF page 7, journal page 1225.

row_label: (+)-Neomenthol

substrate: (+)-neomenthol


organism: Tritrichomonas suis

substrate_name: inosine 5'-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50097 and applied mutation signature R322E with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer assay

column_label: kcat (s^-1) under R322E column

row_label: R322E column; substrate IMP / inosine 5-phosphate

table_label: Table 1. Steady-state kinetic parameters and isotope effects for reactions of T. foetus IMPDH mutants.

substrate: inosine 5'-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R322A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Q324A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E323A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; cofactor NADH

column_label: Table 1; W.T. column; substrate IMP / inosine 5'-phosphate; kcat (s^-1) 1.9 +/- 0.2; Km IMP (uM) 1.7 +/- 0.4; same-row quotient.

table_label: Table 1. Steady-state kinetic parameters and isotope effects for reactions of T. foetus IMPDH mutants


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50097 and applied mutation signature Q324A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer assay; cofactor NAD+

column_label: Km NAD+ (uM) under Q324A column

row_label: Q324A column; substrate NAD+


column_label: Km NAD+ (uM) under W.T. column

row_label: W.T. column; substrate NAD+


column_label: Km NAD+ (uM) under E323A column

row_label: E323A column; substrate NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50097 and applied mutation signature R322A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.

column_label: Km NAD+ (uM) under R322A column

row_label: R322A column; substrate NAD+


column_label: Km NAD+ (uM) under R322E column

normalized_value_unit_evidence: Km=2.6 mM

row_label: R322E column; substrate NAD+


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


enzyme_display_name: Aldo-keto reductase family 1 member C2

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2: Km 22.0 uM; kcat 0.24 min^-1; kcat/Km 11 min^-1 mM^-1.

enzyme: Aldo-keto reductase family 1 member C2


substrate_name: progesterone (reduction)

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1: Km 2.65 uM; kcat 0.29 min^-1; kcat/Km 109 min^-1 mM^-1.

row_label: Progesterone reduction / AKR1C1

substrate: progesterone (reduction)


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1: Km 16.2 uM; kcat 1.10 min^-1; kcat/Km 68 min^-1 mM^-1.


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1: Km 14.7 uM; kcat 1.20 min^-1; kcat/Km 82 min^-1 mM^-1.


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R): Km 80.6 uM; kcat 0.66 min^-1; kcat/Km 8 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C1 (R)


substrate_name: testosterone (oxidation)

column_label: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R): Km 39.8 uM; kcat 0.044 min^-1; kcat/Km 1.1 min^-1 mM^-1.

row_label: Testosterone oxidation / AKR1C1 (R)

substrate: testosterone (oxidation)


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1: Km 19.4 uM; kcat 3.23 min^-1; kcat/Km 167 min^-1 mM^-1.


enzyme_display_name: Aldo-keto reductase family 1 member C4

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4: Km 10.5 uM; kcat 2.1 min^-1; kcat/Km 200 min^-1 mM^-1.

enzyme: Aldo-keto reductase family 1 member C4


proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4: Km 1.44 uM; kcat 1.79 min^-1; kcat/Km 1243 min^-1 mM^-1.


organism: Mus musculus

substrate_name: testosterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G225P/G226P to reconstruct the assayed variant sequence.

substrate: testosterone


enzyme_display_name: Aldo-keto reductase family 1 member C3

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

enzyme: Aldo-keto reductase family 1 member C3


table_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms


row_label: 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1


row_label: 20alpha-Hydroxyprogesterone oxidation / AKR1C1


table_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms


table_label: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms


row_label: 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1


row_label: 3alpha-Androstanediol oxidation / AKR1C4


row_label: 5alpha-Androstane-3,17-dione reduction / AKR1C4


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.


enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Aspergillus nidulans

substrate_name: IMP

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl; cofactor NADH

column_label: Table 1: Steady-state kinetic parameters of fungal IMPDHs (Protein Science 2020, 29:686-694); Table 1, row AnIMPDH; the kcat value 1.9 s-1 comes from the column headed kcat (s-1) and the Michaelis constant 15 uM comes from the column headed Km IMP (uM). Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.9 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the exported value is 1.9 s^(-1). Km: printed Table 1 cell 15 uM; 15 / 1000 = 0.015 mM; the exported value is 0.015 mM. kcat/Km: Table 1 carries no kcat/Km column and this article prints no kcat/Km value for this enzyme form, so the exported 126.66666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.9 / 0.015 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, row AnIMPDH: kcat = 1.9 s-1 (printed column kcat (s-1)); Km IMP = 15 uM (printed column Km IMP (uM)). No kcat/Km value is printed for this measurement.

row_label: Table 1, row AnIMPDH

substrate: IMP


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris-HCl; cofactor NAD+

column_label: Table 1: Steady-state kinetic parameters of fungal IMPDHs (Protein Science 2020, 29:686-694); Table 1, row AnIMPDH; the kcat value 1.9 s-1 comes from the column headed kcat (s-1) and the Michaelis constant 120 uM comes from the column headed Km NAD+ (uM). Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.9 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the exported value is 1.9 s^(-1). Km: printed Table 1 cell 120 uM; 120 / 1000 = 0.12 mM; the exported value is 0.12 mM. kcat/Km: Table 1 carries no kcat/Km column and this article prints no kcat/Km value for this enzyme form, so the exported 15.833333333333334 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.9 / 0.12 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, row AnIMPDH: kcat = 1.9 s-1 (printed column kcat (s-1)); Km NAD+ = 120 uM (printed column Km NAD+ (uM)). No kcat/Km value is printed for this measurement.

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:C8V6R6 and applied mutation signature A267S with inferred residue-numbering offset -244 to reconstruct the assayed variant sequence.

column_label: Table 1: Steady-state kinetic parameters of fungal IMPDHs (Protein Science 2020, 29:686-694); Table 1, row AnIMPDH-A267S; the kcat value 1.9 s-1 comes from the column headed kcat (s-1) and the Michaelis constant 15 uM comes from the column headed Km IMP (uM). Table 1 has no kcat/Km column.

raw_value_unit_evidence: Table 1, row AnIMPDH-A267S: kcat = 1.9 s-1 (printed column kcat (s-1)); Km IMP = 15 uM (printed column Km IMP (uM)). No kcat/Km value is printed for this measurement.

row_label: Table 1, row AnIMPDH-A267S


column_label: Table 1: Steady-state kinetic parameters of fungal IMPDHs (Protein Science 2020, 29:686-694); Table 1, row AnIMPDH-A267S; the kcat value 1.9 s-1 comes from the column headed kcat (s-1) and the Michaelis constant 190 uM comes from the column headed Km NAD+ (uM). Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.9 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the exported value is 1.9 s^(-1). Km: printed Table 1 cell 190 uM; 190 / 1000 = 0.19 mM; the exported value is 0.19 mM. kcat/Km: Table 1 carries no kcat/Km column and this article prints no kcat/Km value for this enzyme form, so the exported 10.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.9 / 0.19 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, row AnIMPDH-A267S: kcat = 1.9 s-1 (printed column kcat (s-1)); Km NAD+ = 190 uM (printed column Km NAD+ (uM)). No kcat/Km value is printed for this measurement.


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

proof_lines:
isoform IMPDH1(595), pH 8.0, 25°C
isoform IMPDH1(546), pH 8.0, 25°C
isoform IMPDH1(514), pH 8.0, 25°C

source_databases_merged: brenda skid uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature D226N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant D226N of isoform IMPDH1(595), pH 8.0, 25°C

proof_lines: mutant D226N of isoform IMPDH1(546), pH 8.0, 25°C


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines:
isoform IMPDH1(514), pH 8.0, 25°C
isoform IMPDH1(546), pH 8.0, 25°C
isoform IMPDH1(595), pH 8.0, 25°C


assay_conditions_summary: pH 8; cofactor NAD+


proof_lines: The kinetic parameters were determined using microsomes from transfected cells.


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: androsterone

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


substrate_name: (s)-tetralol (oxidation)

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


substrate_name: (s)-tetralol

substrate: (s)-tetralol


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


organism: Withania coagulans

substrate_name: Tropine

proof_lines: pH 6.6, 30°C, recombinant His-tagged enzyme

substrate: Tropine


substrate_name: NADP+

assay_conditions_summary: pH 6.6; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 6.6; cofactor NADPH


substrate_name: tropinone

substrate: tropinone


organism: Vibrio cholerae serotype O1

substrate_name: IMP

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

substrate: IMP


sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: deletion

proof_lines: pH 8.0, 25°C, recombinant short enzyme CBS-deletion mutant VcIMPDHDELTAL


substrate_name: NAD+

mutation_signature: recombinant short enzyme CBS-deletion mutant VcIMPDHDELTAL

substrate: NAD+


organism: Macaca fuscata fuscata

proof_lines: kcat is 4.9 min(-1) for 5-beta-pregnan-20-alpha-ol-3-one as substrate. kcat is 4.9 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one as substrate. kcat is 23 min(-1) for 5alpha-pregnane-3alpha,21-diol-20-one.


organism: Penicillium brevicompactum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S267A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S267A of isoform IMPDHA, at pH 8.0 and 25°C


substrate_name: inosine 5'-phosphate

proof_lines: pH 8.0, 25°C, recombinant alphabeta core domain, in presence of 100 mM KCl

proof_lines: pH 8.0, 25°C, recombinant full-length enzyme, in presence of 100 mM KCl

substrate: inosine 5'-phosphate


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Eremothecium gossypii

proof_lines: recombinant wild-type enzyme, pH 8.0, 28°C


proof_lines: recombinant AgIMPDH-DELTABateman mutant enzyme, pH 8.0, 28°C


enzyme_display_name: UniProt P9WKI7

organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8; 295.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8

enzyme: UniProt P9WKI7


proof_lines:
Raw SKiD Env: Temp=22°C, pH=8
kcat is 0.53 sec(-1).


organism: Homo sapiens


substrate_name: (s)-indan-1-ol (oxidation)

substrate: (s)-indan-1-ol (oxidation)


substrate_name: progesterone

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1

substrate_name: dihydrotestosterone (in the presence of NADPH)

proof_lines: Vmax for dihydrotestosterone reduction is 15-fold higher in the presence of NADH than in the presence of NADPH.


enzyme_display_name: NADPH-dependent 3-keto-steroid reductase Hsd3b5

proof_lines: Catalytic efficiency for dihydrotestosterone reduction is 20-fold better in the presence of NADPH than in the presence of NADH.

substrate: dihydrotestosterone (in the presence of NADPH)


organism: Arabidopsis thaliana

smiles: CCC=CC=O

proof_lines: kcat is 0.27 sec(-1) for (E)-2-pentenal. kcat is 0.4 sec(-1) for (E)-2-hexenal.


smiles: CCCC=CC=O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A285T to reconstruct the assayed variant sequence.


substrate_name: prostaglandin H2

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

substrate: prostaglandin H2


substrate_name: progesterone (reduction)

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

substrate: progesterone (reduction)


organism: Bacillus amyloliquefaciens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P166S/K481E to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 40°C, recombinant mutant enzymes, P166S, K481E, and IMPDHDELTACBS


assay_conditions_summary: pH 7; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: PDF Table 2 row DhtS has AKR1C1 Km=5.2 +/- 0.8 uM; 5.2 uM normalizes to 0.0052 mM

raw_value_unit_evidence: Km raw_value=5.2 raw_unit=uM; S.D.=0.8 uM

row_label: DhtS; enzyme AKR1C1

table_label: Table 2 Kinetic parameters for the reduction of Dht, DhtG, and DhtS catalyzed by AKR1C isoforms


substrate_name: 5alpha-androstan-3,17-dione (reduction)

substrate: 5alpha-androstan-3,17-dione (reduction)


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 2, row '5b-Pregnane-3,20-dione', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 19 min^-1; kcat/Km 38 min^-1 uM^-1; Km 0.5 uM

row_label: 5b-Pregnane-3,20-dione / AKR1C21* (DD1/Q91WR5)

table_label: Table 2


proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=7


substrate_name: Epitestosterone

column_label: J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; Km (uM) = 0.6; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; kcat (min^-1) = 18; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; kcat/Km (min^-1 uM^-1) = 30

normalized_value_unit_evidence: normalized km=0.0006 mM; export km=0.0006 mM; normalized kcat=0.3 s^-1; export kcat=0.57 s^-1; normalized kcat_over_km=5 s^-1 mM^-1; export kcat_over_km=950.0 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.6 uM for AKR1C21 (DD3) / Epitestosterone; kcat (min^-1) 18 min^-1 for AKR1C21 (DD3) / Epitestosterone; kcat/Km (min^-1 uM^-1) 30 min^-1 uM^-1 for AKR1C21 (DD3) / Epitestosterone

row_label: AKR1C21 (DD3) / Epitestosterone

table_label: J-STAGE PDF page 1942 Table 1

substrate: Epitestosterone


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); Androst-4-ene-3,17-dione; Km (uM) = 0.2; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); Androst-4-ene-3,17-dione; kcat (min^-1) = 10; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); Androst-4-ene-3,17-dione; kcat/Km (min^-1 uM^-1) = 50

raw_value_unit_evidence: Km (uM) 0.2 uM for AKR1C21 (DD3) / Androst-4-ene-3,17-dione; kcat (min^-1) 10 min^-1 for AKR1C21 (DD3) / Androst-4-ene-3,17-dione; kcat/Km (min^-1 uM^-1) 50 min^-1 uM^-1 for AKR1C21 (DD3) / Androst-4-ene-3,17-dione

table_label: J-STAGE PDF page 1942 Table 2


column_label: Table 2, row '5b-Dihydrocorticosterone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 7 min^-1; kcat/Km 1 min^-1 uM^-1; Km 6.2 uM

row_label: 5b-Dihydrocorticosterone / AKR1C21* (DD1/Q91WR5)


column_label: Table 2, row 'Deoxycorticosterone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 0.5 min^-1; kcat/Km 0.3 min^-1 uM^-1; Km 1.5 uM

row_label: Deoxycorticosterone / AKR1C21* (DD1/Q91WR5)


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 16-Ketoestrone; Km (uM) = 0.8; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 16-Ketoestrone; kcat (min^-1) = 35; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 16-Ketoestrone; kcat/Km (min^-1 uM^-1) = 44

raw_value_unit_evidence: Km (uM) 0.8 uM for AKR1C21 (DD3) / 16-Ketoestrone; kcat (min^-1) 35 min^-1 for AKR1C21 (DD3) / 16-Ketoestrone; kcat/Km (min^-1 uM^-1) 44 min^-1 uM^-1 for AKR1C21 (DD3) / 16-Ketoestrone

row_label: AKR1C21 (DD3) / 16-Ketoestrone


column_label: Table 2, row '5b-Dihydrocortisone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 3.5 min^-1; kcat/Km 0.4 min^-1 uM^-1; Km 8.4 uM

row_label: 5b-Dihydrocortisone / AKR1C21* (DD1/Q91WR5)


column_label: Table 1, row '17a-Hydroxy-5a-androstan-3-one', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 8.4 min^-1; kcat/Km 21 min^-1 uM^-1; Km 0.4 uM

row_label: 17a-Hydroxy-5a-androstan-3-one / AKR1C21* (DD1/Q91WR5)

table_label: Table 1


column_label: J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Hydroxy-5b-androstan-3-one; Km (uM) = 0.4; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Hydroxy-5b-androstan-3-one; kcat (min^-1) = 8.4; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Hydroxy-5b-androstan-3-one; kcat/Km (min^-1 uM^-1) = 21

normalized_value_unit_evidence: normalized km=0.0004 mM; export km=0.0004 mM; normalized kcat=0.14 s^-1; export kcat=0.14 s^-1; normalized kcat_over_km=350 s^-1 mM^-1; export kcat_over_km=350.0 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.4 uM for AKR1C21 (DD3) / 17a-Hydroxy-5b-androstan-3-one; kcat (min^-1) 8.4 min^-1 for AKR1C21 (DD3) / 17a-Hydroxy-5b-androstan-3-one; kcat/Km (min^-1 uM^-1) 21 min^-1 uM^-1 for AKR1C21 (DD3) / 17a-Hydroxy-5b-androstan-3-one


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D138A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D13A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D243A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D248A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D338A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D50A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E369A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E373A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E469A to reconstruct the assayed variant sequence.


substrate_name: K+

substrate: K+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E54A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


column_label: Page 13370 Table 2, row wild-type: the `kcat s-1` cell and the `K m K+ (mM)` cell of that one row reproduce the export values exactly after the normalizations recorded in conversion_arithmetic_note, and their same-row quotient reproduces the exported kcat/Km. Table 2 prints a `kcat/KmKm [(sM2)-1 x 107]` column, but that column is NOT a kcat/Km cell: its unit is the reciprocal of (s x M^2), i.e. kcat divided by the PRODUCT of the two Michaelis constants (Km IMP x Km NAD+), which is not the same quantity as kcat/Km (s^-1 mM^-1). This was checked against the printed cells of every row used here: e.g. wild-type 13 s^-1 / (61 uM x 2.0 mM) = 1.07e8 (s M2)^-1 = 10.7 x 10^7, which is the printed cell 11 at that cell's printed precision; D200A 14 / (44 uM x 1.5 mM) = 2.12e8 = 21.2 x 10^7 versus the printed 21; D338A 0.02 / (710 uM x 3.3 mM) = 8.5e3 = 0.00085 x 10^7 versus the printed 0.0009. So the paper prints no kcat/Km cell for these rows, there is no printed ratio cell to back-convert the quotient against, and no correction is claimed against the printed kcat/KmKm column.

normalized_value_unit_evidence: metric: kcat; raw value: 13 s-1; raw unit: s-1; normalized value: 13.0 s^-1; normalized unit: s^-1; metric: Km; raw value: 2.8 mM; raw unit: mM; normalized value: 2.8 mM; normalized unit: mM; metric: kcat/Km; normalized value: 4.642857142857143 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Enzyme Assays: Standard E. coli IMPDH activity assays contained 50 mM Tris, pH 8.0, 100 mM KCl, 3 mM EDTA, 1 mM DTT, 1 mM IMP, and 2.5 mM NAD+; the production of NADH was monitored at 25 C. Data Analysis (Block C): Wild-type and all mutant enzyme activities were assayed at saturating IMP and NAD+ concentrations and varied K+ concentrations. The export row carries pH 8.0 and 298.15 K (25 C). This row's Km is the apparent Michaelis-Menten constant of K+ (Block C: 'where Km is the apparent Michaelis-Menten constant of K+'), read from Table 2's own `K m K+ (mM)` column. Note that the wild-type row's `Kii NAD+ (mM)` cell happens to print the same number 2.8; the value used here is taken from the `K m K+ (mM)` column, not from the Kii NAD+ column, and the Kii NAD+ cell is not used anywhere in this record.

raw_value_unit_evidence: Table 2, row wild-type: kcat cell 13 s-1; K m K+ (mM) cell 2.8 mM. Column headers as printed: `kcat        kcat/KmKm        Km IMP     Km NAD+       Kii NAD+      K m K+    Kis GMP      Kis XMP      Ki MMP      Kii TAD` / `enzyme        s-1      [(sM2)-1 × 107]      (µM)       (mM)           (mM)        (mM)       (µM)         (µM)         (nM)        (µM)`. Table title as printed: `Table 2: Kinetic Charaterization of E. coli IMPDH and Mutants (Unless Otherwise Noted, Error Was e15%)`. Footnotes as printed: `a Error was e25%. b Kinetic constants determined at 400 mM KCl. cProgress curve analysis. dTight binding analysis. ena, not applicable. end,`.

row_label: wild-type

table_label: Table 2: Kinetic Charaterization of E. coli IMPDH and Mutants (Unless Otherwise Noted, Error Was e15%) - Biochemistry 1997, 36, page 13370


substrate_name: testosterone

column_label: Table 2, row 'Testosterone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 0.9 min^-1; kcat/Km 1 min^-1 uM^-1; Km 0.9 uM

row_label: Testosterone / AKR1C21* (DD1/Q91WR5)

substrate: testosterone


substrate_name: estrone

column_label: Table 2, row 'Estrone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 0.3 min^-1; kcat/Km 0.4 min^-1 uM^-1; Km 0.8 uM

row_label: Estrone / AKR1C21* (DD1/Q91WR5)

substrate: estrone


substrate_name: acenaphthenequinone

column_label: Table 2, row 'Acenaphthenequinone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 22 min^-1; kcat/Km 44 min^-1 uM^-1; Km 0.5 uM

row_label: Acenaphthenequinone / AKR1C21* (DD1/Q91WR5)

substrate: acenaphthenequinone