sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D107A to reconstruct the assayed variant sequence.


enzyme_display_name: methanol dehydrogenase

organism: Lysinibacillus xylanilyticus

substrate_name: methanol

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

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

smiles: CO

mutation_type: substitution

enzyme: methanol dehydrogenase

substrate: methanol

status: unverified

source: brenda


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: NAD+

mutation_signature: Unknown

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

assay_conditions_summary: pH 9.5; 328.15 K; cofactor NAD+

substrate: NAD+


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


enzyme_display_name: tetrahydroxynaphthalene reductase

organism: Pyricularia grisea

substrate_name: Scytalone

enzyme: tetrahydroxynaphthalene reductase

substrate: Scytalone


substrate_name: Phenanthrenequinone

substrate: Phenanthrenequinone


substrate_name: NADPH

kcat_display: Not reported

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: with 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one as cosubstrate

substrate: NADP+


assay_conditions_summary: cofactor NAD+


enzyme_display_name: D-arabinitol 2-dehydrogenase

organism: Thermotoga maritima

substrate_name: D-arabitol

smiles: C(C(C(C(CO)O)O)O)O

proof_lines:
85°C, pH 8.5, Strep-tagged enzyme
85°C, pH 8.5, tag-less enzyme

enzyme: D-arabinitol 2-dehydrogenase

substrate: D-arabitol


substrate_name: D-ribulose

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

proof_lines:
85°C, pH 7.5, Strep-tagged enzyme
85°C, pH 7.5, tag-less enzyme

substrate: D-ribulose


substrate_name: NADH

assay_conditions_summary: pH 7.5; 358.15 K; cofactor NADH

proof_lines: 85°C, pH 7.5, Strep-tagged enzyme, cosubstrate D-ribulose

proof_lines: 85°C, pH 7.5, tag-less enzyme, cosubstrate D-ribulose

substrate: NADH


assay_conditions_summary: pH 8.5; 358.15 K; cofactor NAD+

proof_lines: 85°C, pH 8.5, tag-less enzyme, cosubstrate D-arabitol

proof_lines: 85°C, pH 8.5, Strep-tagged enzyme, cosubstrate D-arabitol


enzyme_display_name: (S)-carnitine 3-dehydrogenase

organism: Agrobacterium sp.

assay_conditions_summary: cofactor NADH

enzyme: (S)-carnitine 3-dehydrogenase


substrate_name: (S)-carnitine

substrate: (S)-carnitine


enzyme_display_name: cyclohexanol dehydrogenase

organism: Xanthobacter sp.

substrate_name: Cyclohexanol

enzyme: cyclohexanol dehydrogenase

substrate: Cyclohexanol


organism: Agrobacterium sp. 525a


substrate_name: D-carnitine

substrate: D-carnitine


organism: Bacillus methanolicus

substrate_name: NAD+; Ethanol

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

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

substrate: NAD+; Ethanol


enzyme_display_name: codeinone reductase (NADPH)

organism: Papaver somniferum

substrate_name: codeine

source_db: oed

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

data_origin: experimental

enzyme: codeinone reductase (NADPH)

substrate: codeine

source: oed


substrate_name: codeinone

kcat_over_km_origin: calculated

substrate: codeinone


assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 6.8; 303.15 K; cofactor NADPH


enzyme_display_name: NADPH-dependent codeinone reductase 1-3

substrate_name: codeine (at pH 9.0 and 30 degrees Celsius)

source_db: uniprot

protein_accession_database: UniProt

assay_conditions_summary: pH 9; cofactor NADPH

proof_lines: kcat is 0.040 sec(-1) with codeinone as substrate (PubMed:29779229). kcat is 0.015 sec(-1) with codeine as substrate (PubMed:29779229). kcat is 0.060 sec(-1) with NADPH as substrate (PubMed:29779229). kcat is 0.044 sec(-1) with NADP(+) as s

enzyme: NADPH-dependent codeinone reductase 1-3

source: uniprot


substrate_name: codeinone (at pH 9.0 and 30 degrees Celsius)


substrate_name: NADPH (at pH 9.0 and 30 degrees Celsius)


substrate_name: NADP (at pH 9.0 and 30 degrees Celsius)

substrate: NADP (at pH 9.0 and 30 degrees Celsius)


substrate_name: morphine (at pH 9.0 and 30 degrees Celsius)


substrate_name: dihydrocodeine (at pH 9.0 and 30 degrees Celsius)


substrate_name: morphinone (at pH 9.0 and 30 degrees Celsius)


substrate_name: hydrocodone (at pH 9.0 and 30 degrees Celsius)


substrate_name: hydromorphone (at pH 9.0 and 30 degrees Celsius)


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

sequence_source: multiple

source_databases_merged: brenda uniprot


smiles: CCCCC(CO)O


substrate_name: Cyclopentanol

substrate: Cyclopentanol


enzyme_display_name: salutaridine reductase (NADPH)

organism: Papaver bracteatum

substrate_name: NADPH

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: pH 6.0, 40°C, recombinant enzyme, with salutaridine

proof_lines: The enzyme does not obey Michaelis-Menten kinetics because the theorectical Vmax cannot be achieved due to strong substrate inhibition, instead the optimal velocity, Vopt, is taken as the measure of enzyme performance.

enzyme: salutaridine reductase (NADPH)


substrate_name: salutaridine

substrate: salutaridine


substrate_name: NADH


substrate_name: NADP+

assay_conditions_summary: pH 6; cofactor NADP+

proof_lines: pH 6.0, 40°C, recombinant enzyme, with salutaridinol


enzyme_display_name: Salutaridine reductase

substrate_name: NADP(+)

enzyme: Salutaridine reductase

substrate: NADP(+)


organism: Cupriavidus necator

substrate_name: methanol

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

source_databases_merged: brenda oed

substrate: methanol


proof_lines: pH 9.5, 30°C, recombinant mutant A26V/A31V/A169V


proof_lines: pH 9.5, 30°C, recombinant mutant A26V/A169V


substrate_name: n-butanol

substrate: n-butanol


enzyme_display_name: NADPH-dependent codeinone reductase 1-5

substrate_name: codeinone

proof_lines: kcat is 0.023 sec(-1) with codeinone as substrate (PubMed:29779229). kcat is 0.027 sec(-1) with codeine as substrate (PubMed:29779229). kcat is 0.045 sec(-1) with NADPH as substrate (PubMed:29779229). kcat is 0.067 sec(-1) with NADP(+) as s

enzyme: NADPH-dependent codeinone reductase 1-5


substrate_name: codeine


substrate: NADPH


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F104A/I275A to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S97T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines: S97T mutant enzyme without added Mg2+, pH 9.5, 50°C

substrate: NAD+


sequence_variant_note: Mutation signature S97G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: S97G mutant enzyme without added Mg2+, pH 9.5, 50°C


assay_conditions_summary: pH 6

proof_lines: pH 6.0, 30°C, recombinant enzyme, reduction reaction


assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: pH 9.5, 30°C, recombinant enzyme, oxidation reaction

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A164P/A363L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A363L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A164P to reconstruct the assayed variant sequence.


enzyme_display_name: NADPH-dependent codeinone reductase 1-1

substrate_name: NADPH (at pH 9.0 and 30 degrees Celsius)

verification_status: verified

column_label: Table 3 row 'Km NADPH (uM)', COR1.1 column = 180 uM.

raw_value_unit_evidence: Km raw_value=180 raw_unit=uM

row_label: COR1.1; Km NADPH

table_label: Table 3

enzyme: NADPH-dependent codeinone reductase 1-1

status: verified


substrate_name: NADP (at pH 9.0 and 30 degrees Celsius)

assay_conditions_summary: pH 9

column_label: Table 3 row 'Km NADP (uM)', COR1.1 column = 53 uM.

raw_value_unit_evidence: Km raw_value=53 raw_unit=uM

row_label: COR1.1; Km NADP


enzyme_display_name: NADPH-dependent codeinone reductase 1-2

substrate_name: codeine (at pH 9.0 and 30 degrees Celsius)

proof_lines: NADPH-dependent reduction of codeinone to codeine

enzyme: NADPH-dependent codeinone reductase 1-2


substrate_name: codeinone (at pH 9.0 and 30 degrees Celsius)


substrate: NADPH (at pH 9.0 and 30 degrees Celsius)


enzyme_display_name: NADPH-dependent codeinone reductase 1-4

enzyme: NADPH-dependent codeinone reductase 1-4

substrate: codeine (at pH 9.0 and 30 degrees Celsius)


substrate: codeinone (at pH 9.0 and 30 degrees Celsius)


organism: Candida tropicalis

column_label: Abstract states the apparent Km for NAD+ at DA concentration 384 mM is 0.12 mM.

raw_value_unit_evidence: Km raw_value=0.12 raw_unit=mM

row_label: Candida tropicalis D-arabinitol dehydrogenase with NAD+

table_label: PubMed abstract PMID 8250887


substrate_name: D-arabinitol

substrate: D-arabinitol


enzyme_display_name: NAD-dependent methanol dehydrogenase

proof_lines:
Bacillus methanolicus
methanol dehydrogenase
NAD-dependent methanol dehydrogenase

enzyme: NAD-dependent methanol dehydrogenase

substrate: NADH


substrate_name: D-xylitol

substrate: D-xylitol


substrate_name: D-Ribulose

substrate: D-Ribulose


substrate_name: D-Arabitol

substrate: D-Arabitol


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


substrate_name: NAD

column_label: Table IV lists bMDH row with Km NAD+ = 0.02 mM.

raw_value_unit_evidence: Km raw_value=0.02 mM raw_unit=mM

row_label: bMDH row

table_label: JBC full text Table IV: Kinetic characteristics and metal composition of bMDH and cMDH

substrate: NAD


enzyme_display_name: NADH-dependent L-xylulose reductase

organism: Ambrosiozyma monospora

substrate_name: L-xylulose

enzyme: NADH-dependent L-xylulose reductase

substrate: L-xylulose


proof_lines:
D-ribulose
D-arabinitol
L-xylulose reductase


substrate_name: formaldehyde (without activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: ethanol (with the activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: methanol (with the activator protein at pH 9.5 and 50 degrees Celsius)


substrate_name: salutaridinol

verification_status: corrected

column_label: Table 2 reports salutaridinol substrate Km as 23.0 +/- 6.9 microM, not the CatLog value 0.018 mM.

raw_value_unit_evidence: Km raw_value=23.0 +/- 6.9 microM raw_unit=microM

row_label: Salutaridine reductase / salutaridinol reverse-reaction substrate row

table_label: Wiley/The Plant Journal full text Table 2

substrate: salutaridinol

status: corrected


organism: Curvularia lunata

assay_conditions_summary: pH 7


organism: Escherichia coli (strain K12)

substrate_name: 4-(phosphooxy)-L-threonine (at 0.1 M Tris-HCl and pH 7.5)


enzyme_display_name: UniProt P9WNS1

organism: Mycobacterium tuberculosis

substrate_name: 1-deoxy-D-xylulose 5-phosphate

source_db: skid

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt P9WNS1

substrate: 1-deoxy-D-xylulose 5-phosphate

source: skid


enzyme_display_name: UniProt P45568

organism: Escherichia coli

enzyme: UniProt P45568


substrate_name: NADPH


enzyme_display_name: methanol dehydrogenase

substrate_name: Methanol; NAD+

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

enzyme: methanol dehydrogenase

substrate: Methanol; NAD+


substrate_name: Unknown

km_display: Not reported

assay_conditions_summary: cofactor NADPH

substrate: Unknown


substrate_name: DNA with apurinic site

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADPH

substrate: DNA with apurinic site


substrate_name: salutaridine (Termination and extraction with NaHCO(3) and ethylacetate, respectively)


enzyme_display_name: tetrahydroxynaphthalene reductase

ki_unit: mM

proof_lines: at 0.04 mM 2,3-dihydro-2,5-dihydroxy-4H-benzopyran-4-one, at pH 7.0 and 25°C

enzyme: tetrahydroxynaphthalene reductase


enzyme_display_name: L-idonate 5-dehydrogenase

organism: Gluconobacter oxydans

enzyme: L-idonate 5-dehydrogenase

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: D-gluconate

substrate: D-gluconate


organism: Fusarium sp.


organism: synthetic construct


organism: Aspergillus niger

substrate_name: L-Idonate

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

assay_conditions_summary: pH 8

proof_lines: pH 8, temperature not specified in the publication

proof_lines: pH 7, temperature not specified in the publication

substrate: L-Idonate


enzyme_display_name: 1,5-anhydro-D-fructose reductase

organism: Ensifer adhaerens

proof_lines: mutant G206I in the presence of 1,5-anhydro-D-fructose

enzyme: 1,5-anhydro-D-fructose reductase


proof_lines: mutant K94G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant S10G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant A13G/S10G in the presence of 1,5-anhydro-D-fructose


proof_lines: mutant A13G/S33D in the presence of 1,5-anhydro-D-fructose


substrate_name: NADH

proof_lines: mutant A13G in the presence of 1,5-anhydro-D-fructose


substrate_name: D-glucosone

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

substrate: D-glucosone


enzyme_display_name: 3-methylbutanal reductase

organism: Saccharomyces cerevisiae

sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y128A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

smiles: CC(C)CC=O

enzyme: 3-methylbutanal reductase


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature F85A with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y198A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y198F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature Y128F with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature V162A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature F132A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 7; cofactor NADPH

enzyme: sn-glycerol-1-phosphate dehydrogenase


substrate_name: dihydroxyacetone phosphate

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

proof_lines: wild-type, cosubstrate NADPH, pH 7.0, 50°C

proof_lines: wild-type, cosubstrate NADH, pH 7.0, 50°C

substrate: dihydroxyacetone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S40A/T42A to reconstruct the assayed variant sequence.

proof_lines: mutant S40A/T42A, cosubstrate NADPH, pH 7.0, 50°C

proof_lines: mutant S40A/T42A, cosubstrate NADH, pH 7.0, 50°C


assay_conditions_summary: pH 7; cofactor NADH

substrate: NADH


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


proof_lines: mutant A13G/S10G in the presence of NADH

proof_lines: mutant A13G/S10Gin the presence of NADPH


proof_lines: mutant A13G/S33D in the presence of NADPH

proof_lines: mutant A13G/S33D in the presence of NADH


proof_lines:
mutant A13G in the presence of NADH
mutant A13G in the presence of NADPH


assay_conditions_summary: cofactor NADH


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

proof_lines: recombinant wild type enzyme in the presence of NADPH

proof_lines: native wild type enzyme in the presence of NADPH


proof_lines: recombinant wild type enzyme in the presence of 1,5-anhydro-D-fructose

proof_lines: native wild type enzyme in the presence of 1,5-anhydro-D-fructose


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W204A to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature W204L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature W204V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


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

proof_lines: pH 7.8, 37°C, recombinant wild-type enzyme


enzyme_display_name: dTDP-4-dehydro-6-deoxyglucose reductase

organism: Aggregatibacter actinomycetemcomitans

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

enzyme: dTDP-4-dehydro-6-deoxyglucose reductase


organism: Vitis vinifera


enzyme_display_name: NADPH-dependent methylglyoxal reductase GRE2

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 31.3 min(-1) with 3-chloro-1-phenyl-1-propanol as substrate and 29.1 min(-1) for NADPH.


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

enzyme: NADPH-dependent methylglyoxal reductase GRE2


smiles: CC(CCC(C)O)O


proof_lines: kcat is 406 min(-1) for the reduction reaction with NADPH, and 1594 min(-1) for that with NADH.


organism: Methanocaldococcus jannaschii

proof_lines: with NADH as cosubstrate, at pH 7.8 and 65°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines:
pH 7.5, 37°C, presence of 1 mM Co2+
pH 7.5, 37°C, presence of 1 mM Mn2+
pH 7.5, 37°C, presence of 1 mM Mg2+


proof_lines:
pH 7.5, 37°C, presence of 1 mM Co2+
pH 7.5, 37°C, presence of 1 mM Mg2+
pH 7.5, 37°C, presence of 1 mM Mn2+


organism: Plectranthus barbatus

assay_conditions_summary: pH 8; cofactor NADPH


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: phenylglyoxal

substrate: phenylglyoxal


organism: Mus musculus


substrate_name: Hexanol

smiles: CCCCCCO

proof_lines:
in the presence of NADP+
presence of NADP+

substrate: Hexanol


substrate_name: acetaldehyde

smiles: CC=O

proof_lines:
in the presence of NADPH
pH 7.0, 30°C
presence of NADPH

substrate: acetaldehyde


smiles: CCCC=CCO


substrate_name: Butanal

smiles: CCCC=O

proof_lines:
presence of NADH
presence of NADPH

substrate: Butanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: propanal

smiles: CCC=O

proof_lines:
presence of NADPH
presence of NADH

substrate: propanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


smiles: CCC(C)C=O


organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)

substrate_name: DHAP (in the presence of NADH as coenzyme)


substrate_name: NADPH


substrate_name: G1P (in the presence of NAD as coenzyme)


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


organism: Aeropyrum pernix

substrate_name: glycerone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D144A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 8; 338.15 K; buffer 50 mM Tris-HCl; cofactor NADH

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D144A': the line 'k cat (min -1)' cell reads 1126.5 ± 158.6 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.12 ± 0.34. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1126.5 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 1126.5 / 60 = 18.775 and the paper value is 18.775 s^(-1). Km: printed Table 1 cell 1.12 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.12 mM. kcat/Km: Table 1 carries no kcat/Km line, so 16.763392857142854 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 18.775 / 1.12 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D144A': the 'k cat (min -1)' cell reads 1126.5 ± 158.6 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.12 ± 0.34. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D144A'

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D144N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D144N': the line 'k cat (min -1)' cell reads 3628.2 ± 380.5 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.12 ± 0.20. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3628.2 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 3628.2 / 60 = 60.47 and the paper value is 60.47 s^(-1). Km: printed Table 1 cell 1.12 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.12 mM. kcat/Km: Table 1 carries no kcat/Km line, so 53.99107142857142 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 60.47 / 1.12 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D144N': the 'k cat (min -1)' cell reads 3628.2 ± 380.5 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.12 ± 0.20. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D144N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature D191N with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'D191N': the line 'k cat (min -1)' cell reads 196.2 ± 38.4 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 0.633 ± 0.32. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 196.2 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 196.2 / 60 = 3.27 and the paper value is 3.27 s^(-1). Km: printed Table 1 cell 0.633 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 0.633 mM. kcat/Km: Table 1 carries no kcat/Km line, so 5.165876777251185 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 3.27 / 0.633 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'D191N': the 'k cat (min -1)' cell reads 196.2 ± 38.4 and the 'Kb (mM)' cell, the Km for DHAP, reads 0.633 ± 0.32. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'D191N'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature H271A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'H271A': the line 'k cat (min -1)' cell reads 29.58 ± 16.6 and the line 'Kb (mM)' cell, which the table caption defines as the Km for DHAP, reads 1.09 ± 0.13. The same column also prints a 'Ka (mM)' cell, the Km for the coenzyme NADH, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 29.58 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 29.58 / 60 = 0.493 and the paper value is 0.493 s^(-1). Km: printed Table 1 cell 1.09 in the 'Kb (mM)' line, the Km for DHAP; the unit is already mM, so no unit conversion applies and the paper value is 1.09 mM. kcat/Km: Table 1 carries no kcat/Km line, so 0.4522935779816513 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.493 / 1.09 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'H271A': the 'k cat (min -1)' cell reads 29.58 ± 16.6 and the 'Kb (mM)' cell, the Km for DHAP, reads 1.09 ± 0.13. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'H271A'


substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YER2 and applied mutation signature H287A with inferred residue-numbering offset -18 to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic constants for the wild-type and sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) mutants in dihydroxyacetone phosphate (DHAP) reduction with NADH as the coenzyme (Archaea 2005), column 'H287A': the line 'k cat (min -1)' cell reads 176.7 ± 4.99 and the line 'Ka (mM)' cell, which the table caption defines as the Km for the coenzyme NADH, reads 0.036 ± 0.004. The same column also prints a 'Kb (mM)' cell, the Km for DHAP, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 1 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 1 cell 176.7 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 176.7 / 60 = 2.945 and the paper value is 2.945 s^(-1). Km: printed Table 1 cell 0.036 in the 'Ka (mM)' line, the Km for the coenzyme NADH; the unit is already mM, so no unit conversion applies and the paper value is 0.036 mM. kcat/Km: Table 1 carries no kcat/Km line, so 81.80555555555556 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 2.945 / 0.036 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, column 'H287A': the 'k cat (min -1)' cell reads 176.7 ± 4.99 and the 'Ka (mM)' cell, the Km for the coenzyme NADH, reads 0.036 ± 0.004. Table 1 carries no kcat/Km line.

row_label: Table 1, column 'H287A'


assay_conditions_summary: pH 8; 338.15 K; buffer 50 mM Tris-HCl; cofactor NADPH

column_label: Table 2: Kinetic parameters for the wild-type and mutant sn-glycerol-1-phosphate dehydrogenases (Gro1PDH) in dihydroxyacetone phosphate (DHAP) reduction with NADPH as the coenzyme (Archaea 2005), column 'D144N': the line 'k cat (min -1)' cell reads 284.1 ± 50.8 and the line 'Ka (mM)' cell, which the table caption defines as the Km for the coenzyme NADPH, reads 0.165 ± 0.06. The same column also prints a 'Kb (mM)' cell, the Km for DHAP, a 'Kia (mM)' cell, the dissociation constant for the coenzyme, and the fit-quality lines '% Fit' and 'SD'. Table 2 carries no kcat/Km line.

normalized_value_unit_evidence: kcat: printed Table 2 cell 284.1 in the 'k cat (min -1)' line; per minute becomes per second on division by 60, so 284.1 / 60 = 4.735 and the paper value is 4.735 s^(-1). Km: printed Table 2 cell 0.165 in the 'Ka (mM)' line, the Km for the coenzyme NADPH; the unit is already mM, so no unit conversion applies and the paper value is 0.165 mM. kcat/Km: Table 2 carries no kcat/Km line, so 28.6969696969697 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.735 / 0.165 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 2, column 'D144N': the 'k cat (min -1)' cell reads 284.1 ± 50.8 and the 'Ka (mM)' cell, the Km for the coenzyme NADPH, reads 0.165 ± 0.06. Table 2 carries no kcat/Km line.

row_label: Table 2, column 'D144N'

substrate: NADPH


enzyme_display_name: UniProt Q2VEQ7

organism: Haloferax mediterranei

enzyme: UniProt Q2VEQ7


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


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


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


substrate_name: pyruvate

substrate: pyruvate


substrate_name: dihydroxyacetone phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S40A/T42A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 323.15 K; cofactor NADPH


column_label: Table 2; NADPH row; columns Km, kcat, kcat/Km.

row_label: NADPH row

table_label: Carbone et al. 2015, J Biol Chem, Structure and Evolution of the Archaeal Lipid Synthesis Enzyme sn-Glycerol-1-phosphate Dehydrogenase; kinetic table evidence


column_label: Table 2; NADH row; columns Km, kcat, kcat/Km.

row_label: NADH row


column_label: Table 2; DHAP (NADPH) row; columns Km, kcat, kcat/Km.

row_label: DHAP (NADPH) row


assay_conditions_summary: pH 7; 323.15 K; cofactor NADH


substrate_name: glycolaldehyde

smiles: C(C=O)O

proof_lines: three aliphatic aldehydes (acetaldehyde, glycolaldehyde, and 3-methylbutanal)

substrate: glycolaldehyde


substrate_name: furfural

proof_lines: two furan aldehydes (furfural and 5-hydroxymethylfurfural)

substrate: furfural


substrate_name: acetaldehyde

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: when acetaldehyde was used as the substrate


smiles: O=CCO


substrate_name: NAD+

assay_conditions_summary: pH 7; 338.15 K; cofactor NAD+

substrate: NAD+


assay_conditions_summary: pH 7; 338.15 K; cofactor NADPH

column_label: PMID 11846799 Table 2, Dihydroxyacetone phosphate reduction section, row NADH (4 mM dihydroxyacetone phosphate): Km 0.032 +/- 0.005 mM and kcat 143.96 +/- 6.81 min^-1. The same-row central-value ratio after minute-to-second conversion is 74.979166666666666666666666666666666666666666666666 s^-1*mM^-1.

raw_value_unit_evidence: Table 2 row NADH (4 mM dihydroxyacetone phosphate): Km 0.032 +/- 0.005 mM; kcat 143.96 +/- 6.81 min^-1.

row_label: NADH (4 mM dihydroxyacetone phosphate)

table_label: Table 2. Substrate specificity of Gro1P dehydrogenase from A. pernix

substrate: NADH


substrate_name: sn-Glycerol 1-phosphate

substrate: sn-Glycerol 1-phosphate


enzyme_display_name: vellosimine dehydrogenase

organism: Rauvolfia serpentina

substrate_name: vellosimine

enzyme: vellosimine dehydrogenase

substrate: vellosimine


substrate_name: geissoschizal

substrate: geissoschizal


enzyme_display_name: 3beta-hydroxysteroid 3-dehydrogenase

organism: Eggerthella sp. CAG:298

substrate_name: 3-oxodeoxycholic acid

assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: coenzyme: NADPH, pH 6.5, temperature not specified in the publication

enzyme: 3beta-hydroxysteroid 3-dehydrogenase

substrate: 3-oxodeoxycholic acid


substrate_name: isodeoxycholic acid

assay_conditions_summary: pH 9.5; cofactor NADP+

proof_lines: coenzyme: NADP+, pH 9.5, temperature not specified in the publication

substrate: isodeoxycholic acid


enzyme_display_name: D-2-hydroxyacid dehydrogenase (NADP+)

substrate_name: NADPH

assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADPH

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisocaproate

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxoisoleucine

proof_lines: pH 8.5, 40°C, recombinant enzyme, substrate 2-oxobutyrate

enzyme: D-2-hydroxyacid dehydrogenase (NADP+)


assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADH


proof_lines: pH 8.5, 40°C, recombinant enzyme, cofactor NADPH

proof_lines: pH 8.5, 40°C, recombinant enzyme, cofactor NADH


assay_conditions_summary: pH 5; 313.15 K; cofactor NADPH

proof_lines: pH 5.0, 40°C, recombinant enzyme, cofactor NADPH


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: DHAP (in the presence of NADH as coenzyme)

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

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

assay_conditions_summary: cofactor NADPH


assay_conditions_summary: pH 7; cofactor NADH

column_label: Table 2; section Dihydroxyacetone phosphate reduction; row NADH (4 mM dihydroxyacetone phosphate); column Km (mM); cell 0.032 +/- 0.005.

normalized_value_unit_evidence: Km=0.032 mM for NADH.

raw_value_unit_evidence: Table 2 row NADH (4 mM dihydroxyacetone phosphate); Km (mM) cell = 0.032 +/- 0.005.

table_label: Table 2: Substrate specificity of Gro1P dehydrogenase from A. pernix


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 2; section Dihydroxyacetone phosphate reduction; row NADPH (4 mM dihydroxyacetone phosphate); column Km (mM); cell 0.044 +/- 0.022.

normalized_value_unit_evidence: Km=0.044 mM for NADPH.

raw_value_unit_evidence: Table 2 row NADPH (4 mM dihydroxyacetone phosphate); Km (mM) cell = 0.044 +/- 0.022.

row_label: NADPH (4 mM dihydroxyacetone phosphate)


assay_conditions_summary: pH 7

column_label: Table 2; section Gro1P oxidation; row Gro1P (5 mM NAD); column Km (mM); cell 8.92 +/- 0.64.

normalized_value_unit_evidence: Km=8.92 mM for G1P/Gro1P.

raw_value_unit_evidence: Table 2 row Gro1P (5 mM NAD); Km (mM) cell = 8.92 +/- 0.64.

row_label: Gro1P (5 mM NAD)


substrate_name: NAD(+)

assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 2; section Gro1P oxidation; row NAD (50 mM Gro1P); column Km (mM); cell 1.57 +/- 0.44.

normalized_value_unit_evidence: Km=1.57 mM for NAD(+).

raw_value_unit_evidence: Table 2 row NAD (50 mM Gro1P); Km (mM) cell = 1.57 +/- 0.44.

row_label: NAD (50 mM Gro1P)


enzyme_display_name: (R)-2-hydroxyacid dehydrogenase

organism: Enterococcus faecalis

substrate_name: H+; NADH; 2-Oxobutyrate

assay_conditions_summary: cofactor NADH

enzyme: (R)-2-hydroxyacid dehydrogenase

substrate: H+; NADH; 2-Oxobutyrate


organism: Zea mays

mutation_signature: Δ7

mutation_type: deletion


substrate_name: cycloartenone

substrate: cycloartenone


substrate_name: cyclolaudenone

substrate: cyclolaudenone


substrate_name: cycloeucalenone

substrate: cycloeucalenone


substrate_name: cholestanone

substrate: cholestanone


organism: Escherichia coli

substrate_name: 1-Deoxy-D-xylulose 5-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E231K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: 1-Deoxy-D-xylulose 5-phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H153Q with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H209Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H257Q with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


enzyme_display_name: 4-methyl-2-oxopentanoate reductase A

organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40)

substrate_name: 4-methyl-2-oxopentanoate (MOA)

proof_lines: kcat is 15.0 sec(-1) with 4-methyl-2-oxopentanoate (MOA) as substrate. kcat is 140.0 sec(-1) with pyruvate as substrate. kcat is 10.0 sec(-1) with hydroxypyruvate as substrate. kcat is 11.0 sec(-1) with glyoxylate as substrate. kcat is 0.74

enzyme: 4-methyl-2-oxopentanoate reductase A

substrate: 4-methyl-2-oxopentanoate (MOA)


substrate_name: pyruvate

substrate: pyruvate


substrate_name: hydroxypyruvate

substrate: hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate: NADPH


substrate_name: NADH

substrate: NADH


enzyme_display_name: 2-hydroxyacid dehydrogenase A

proof_lines: kcat is 14.0 sec(-1) with pyruvate as substrate. kcat is 170.0 sec(-1) with hydroxypyruvate as substrate. kcat is 591.0 sec(-1) with glyoxylate as substrate.

enzyme: 2-hydroxyacid dehydrogenase A


organism: Corynebacterium sp.

sequence_variant_note: Mutation signature F22Y/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature F22Y/S233T/R235S/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/S233T/R235S/R238H/A272G isoenzyme A mutant


column_label: Table 6: Full Kinetic Parameters with NADH as a Cofactor, row wild type, substrate/cofactor context NADH: kcat 170 min^-1; Ka 1.4 mM for NADH; normalized kcat 2.83333 s^-1; Km 1.4 mM; kcat/Km 2.02381 s^-1*mM^-1.

raw_value_unit_evidence: kcat 170 min^-1; Ka 1.4 mM for NADH

row_label: wild type


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232G/R238H to reconstruct the assayed variant sequence.

column_label: Table 8: Full Kinetic Parameters with NADPH as a Cofactor, row K232G/R238H, substrate/cofactor context NADPH: kcat 200 min^-1; Ka 0.13 mM for NADPH; normalized kcat 3.33333 s^-1; Km 0.13 mM; kcat/Km 25.641 s^-1*mM^-1.

raw_value_unit_evidence: kcat 200 min^-1; Ka 0.13 mM for NADPH


sequence_variant_note: Mutation signature F22Y/K232G/R235T/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235T/R238H/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R238H/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R235G/R238E/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235G/R238E/A272G isoenzyme A mutant


sequence_variant_note: Mutation signature F22Y/K232G/R235G/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235G/R238H/A272G isoenzyme A mutant


column_label: Table 6: Full Kinetic Parameters with NADH as a Cofactor, row K232G/R238H, substrate/cofactor context NADH: kcat 1200 min^-1; Ka 0.66 mM for NADH; normalized kcat 20 s^-1; Km 0.66 mM; kcat/Km 30.303 s^-1*mM^-1.

raw_value_unit_evidence: kcat 1200 min^-1; Ka 0.66 mM for NADH


sequence_variant_note: Mutation signature F22Y/K232G/R235T/R238E/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/K232G/R235T/R238E/A272G isoenzyme A mutant


column_label: Table 8: Full Kinetic Parameters with NADPH as a Cofactor, row K232G/R238H, substrate/cofactor context 2,5-didehydro-D-gluconate: Kb 13 mM for 2,5-DKG substrate; normalized Km 13 mM.

normalized_value_unit_evidence: Km 13 mM

raw_value_unit_evidence: Kb 13 mM for 2,5-DKG substrate


sequence_variant_note: Mutation signature F22Y/S232T/R235S/R238H/A272G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: F22Y/S232T/R235S/R238H/A272G isoenzyme A mutant


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter autotrophicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R203A to reconstruct the assayed variant sequence.

smiles: CCC(=O)C

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase


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

assay_conditions_summary: pH 7.5; 303.15 K; buffer GPT; cofactor NAD+

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-butanone span, enzyme row WT; column Vmax (units per mg) = 0.058; column Km (mM) = 52; column kcat (s^-1) = 0.027; column kcat/Km (M^-1 s^-1) = 0.52. captured primary segment: Table 2 row WT | ketone substrate 2-butanone | Vmax 0.058 units per mg | Km 52 mM | kcat 0.027 s^-1 | kcat/Km 0.52 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 52 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 52.0 mM. kcat: printed Table 2 cell 0.027 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 0.027 s^(-1). kcat/Km: printed Table 2 cell 0.52 M^-1 s^-1, that is 0.52 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.52 / 1000 = 0.0005200000000000001 s^-1 mM^-1. Quotient disclosure for this row: 0.027 / 52.0 = 0.0005192307692307692 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 0.5192307692307693 M^-1 s^-1, and the printed cell 0.52 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 2, 2-butanone span, enzyme row WT: Km = 52 mM; kcat = 0.027 s^-1; printed kcat/Km = 0.52 M^-1 s^-1.

row_label: Table 2, 2-butanone span, enzyme row WT


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R152A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R209A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56840 and applied mutation signature R196A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-butanone span, enzyme row R196A; column Vmax (units per mg) = 0.069; column Km (mM) = 23; column kcat (s^-1) = 0.033; column kcat/Km (M^-1 s^-1) = 1.4. captured primary segment: Table 2 row R196A | ketone substrate 2-butanone | Vmax 0.069 units per mg | Km 23 mM | kcat 0.033 s^-1 | kcat/Km 1.4 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 23 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 23.0 mM. kcat: printed Table 2 cell 0.033 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 0.033 s^(-1). kcat/Km: printed Table 2 cell 1.4 M^-1 s^-1, that is 1.4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.4 / 1000 = 0.0014 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 0.033 / 23.0 = 0.0014347826086956522 s^-1 mM^-1, that is 1.434782608695652 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.4 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 2, 2-butanone span, enzyme row R196A: Km = 23 mM; kcat = 0.033 s^-1; printed kcat/Km = 1.4 M^-1 s^-1.


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

smiles: CCC(C)O

assay_conditions_summary: pH 7.5; 303.15 K; buffer mix (50 mM glycine; cofactor NAD+

column_label: Table 5 'Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol' (Biochemistry 2010, 49(16): 3487-3498); Table 5, enzyme block 'rR-HPCDH1', substrate row '(R)-2-butanol': column 'kcat (s^-1)' = 1.9; column 'Km (mM)' = 220; column 'kcat/Km (M^-1 s^-1)' = 8.69.

normalized_value_unit_evidence: kcat: printed Table 5 cell 1.9 s^-1; already in s^-1, no conversion; the value is 1.9 s^(-1) and the exported value is 9.3 s^(-1). Km: printed cell 220 mM; already in mM, no conversion; the value is 220.0 mM and the exported value is 220.0 mM. kcat/Km: printed cell 8.69 M^-1 s^-1; the column header prints M^-1 s^-1 and 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.69 x 0.001 = 0.00869 s^-1 mM^-1; the exported value is 0.042272727272727274 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5, decoded plain-numeral transcription, Table 5, enzyme block 'rR-HPCDH1', substrate row '(R)-2-butanol': Km = 220 mM; kcat = 1.9 s^-1; printed kcat/Km = 8.69 M^-1 s^-1.

source_databases_merged: brenda skid uniprot


smiles: CCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-pentanol; column Vmax (units per mg) = 2.36; column Km (mM) = 20; column kcat (s^-1) = 1.1; column kcat/Km (M^-1 s^-1) = 5.6 x 10^1. captured primary segment: Table 1 row (R)-2-pentanol | Vmax 2.36 units per mg | Km 20 mM | kcat 1.1 s^-1 | kcat/Km 5.6 x 10^1 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 20 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 20.0 mM. kcat: printed Table 1 cell 1.1 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.1 s^(-1). kcat/Km: printed Table 1 cell 5.6 x 10^1 M^-1 s^-1, that is 56.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 56.0 / 1000 = 0.056 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 1.1 / 20.0 = 0.05500000000000001 s^-1 mM^-1, that is 55.00000000000001 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 5.6 x 10^1 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-pentanol: Km = 20 mM; kcat = 1.1 s^-1; printed kcat/Km = 5.6 x 10^1 M^-1 s^-1.


smiles: CCCCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-octanol; column Vmax (units per mg) = 3.54; column Km (mM) = 1.08; column kcat (s^-1) = 1.7; column kcat/Km (M^-1 s^-1) = 1.5 x 10^3. captured primary segment: Table 1 row (R)-2-octanol | Vmax 3.54 units per mg | Km 1.08 mM | kcat 1.7 s^-1 | kcat/Km 1.5 x 10^3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1.08 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 1.08 mM. kcat: printed Table 1 cell 1.7 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.7 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^3 M^-1 s^-1, that is 1500.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1500.0 / 1000 = 1.5 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 1.7 / 1.08 = 1.574074074074074 s^-1 mM^-1, that is 1574.074074074074 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.5 x 10^3 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-octanol: Km = 1.08 mM; kcat = 1.7 s^-1; printed kcat/Km = 1.5 x 10^3 M^-1 s^-1.


smiles: CCCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-heptanol; column Vmax (units per mg) = 3.80; column Km (mM) = 2.64; column kcat (s^-1) = 1.8; column kcat/Km (M^-1 s^-1) = 6.8 x 10^2. captured primary segment: Table 1 row (R)-2-heptanol | Vmax 3.80 units per mg | Km 2.64 mM | kcat 1.8 s^-1 | kcat/Km 6.8 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 2.64 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 2.64 mM. kcat: printed Table 1 cell 1.8 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 1.8 s^(-1). kcat/Km: printed Table 1 cell 6.8 x 10^2 M^-1 s^-1, that is 680.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 680.0 / 1000 = 0.68 s^-1 mM^-1. Quotient disclosure for this row: 1.8 / 2.64 = 0.6818181818181818 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 681.8181818181818 M^-1 s^-1, and the printed cell 6.8 x 10^2 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-heptanol: Km = 2.64 mM; kcat = 1.8 s^-1; printed kcat/Km = 6.8 x 10^2 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R196A to reconstruct the assayed variant sequence.


smiles: CCCCC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row (R)-2-hexanol; column Vmax (units per mg) = 5.66; column Km (mM) = 4.6; column kcat (s^-1) = 2.7; column kcat/Km (M^-1 s^-1) = 5.8 x 10^2. captured primary segment: Table 1 row (R)-2-hexanol | Vmax 5.66 units per mg | Km 4.6 mM | kcat 2.7 s^-1 | kcat/Km 5.8 x 10^2 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 4.6 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 4.6 mM. kcat: printed Table 1 cell 2.7 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 2.7 s^(-1). kcat/Km: printed Table 1 cell 5.8 x 10^2 M^-1 s^-1, that is 580.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 580.0 / 1000 = 0.58 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 2.7 / 4.6 = 0.5869565217391305 s^-1 mM^-1, that is 586.9565217391305 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 5.8 x 10^2 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 1, secondary-alcohol row (R)-2-hexanol: Km = 4.6 mM; kcat = 2.7 s^-1; printed kcat/Km = 5.8 x 10^2 M^-1 s^-1.


smiles: CC(C)O

column_label: Table 1: Kinetic Parameters for R-HPCDH with Various Secondary Alcohols at 30 °C and pH 7.5 (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads secondary alcohol | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) | enantioselectivity (E). Cited cell set: Table 1, secondary-alcohol row 2-propanol; column Vmax (units per mg) = 6.2; column Km (mM) = 1726; column kcat (s^-1) = 2.9; column kcat/Km (M^-1 s^-1) = 1.7 x 10^0. captured primary segment: Table 1 row 2-propanol | Vmax 6.2 units per mg | Km 1726 mM | kcat 2.9 s^-1 | kcat/Km 1.7 x 10^0 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1726 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 1726.0 mM. kcat: printed Table 1 cell 2.9 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 2.9 s^(-1). kcat/Km: printed Table 1 cell 1.7 x 10^0 M^-1 s^-1, that is 1.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 / 1000 = 0.0017 s^-1 mM^-1. Quotient disclosure for this row: 2.9 / 1726.0 = 0.0016801853997682502 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 1.6801853997682503 M^-1 s^-1, and the printed cell 1.7 x 10^0 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 1, secondary-alcohol row 2-propanol: Km = 1726 mM; kcat = 2.9 s^-1; printed kcat/Km = 1.7 x 10^0 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56840 and applied mutation signature R209A to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-KPC span, enzyme row R209A; column Vmax (units per mg) = 32; column Km (mM) = 0.15; column kcat (s^-1) = 15; column kcat/Km (M^-1 s^-1) = 1.0 x 10^5. captured primary segment: Table 2 row R209A | ketone substrate 2-KPC | Vmax 32 units per mg | Km 0.15 mM | kcat 15 s^-1 | kcat/Km 1.0 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.15 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 0.15 mM. kcat: printed Table 2 cell 15 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 15.0 s^(-1). kcat/Km: printed Table 2 cell 1.0 x 10^5 M^-1 s^-1, that is 100000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 100000.0 / 1000 = 100.0 s^-1 mM^-1. Quotient disclosure for this row: the two printed component cells give 15.0 / 0.15 = 100.0 s^-1 mM^-1, that is 100000.0 M^-1 s^-1, while the paper's own printed catalytic-efficiency cell for the same row is 1.0 x 10^5 M^-1 s^-1; this record reports the printed cell.

raw_value_unit_evidence: Table 2, 2-KPC span, enzyme row R209A: Km = 0.15 mM; kcat = 15 s^-1; printed kcat/Km = 1.0 x 10^5 M^-1 s^-1.

row_label: Table 2, 2-KPC span, enzyme row R209A


column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-KPC span, enzyme row WT; column Vmax (units per mg) = 51.9; column Km (mM) = 0.092; column kcat (s^-1) = 24.5; column kcat/Km (M^-1 s^-1) = 2.7 x 10^5. captured primary segment: Table 2 row WT | ketone substrate 2-KPC | Vmax 51.9 units per mg | Km 0.092 mM | kcat 24.5 s^-1 | kcat/Km 2.7 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.092 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 0.092 mM. kcat: printed Table 2 cell 24.5 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 24.5 s^(-1). kcat/Km: printed Table 2 cell 2.7 x 10^5 M^-1 s^-1, that is 270000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 270000.0 / 1000 = 270.0 s^-1 mM^-1. Quotient disclosure for this row: 24.5 / 0.092 = 266.30434782608694 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 266304.3478260869 M^-1 s^-1, and the printed cell 2.7 x 10^5 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 2, 2-KPC span, enzyme row WT: Km = 0.092 mM; kcat = 24.5 s^-1; printed kcat/Km = 2.7 x 10^5 M^-1 s^-1.

row_label: Table 2, 2-KPC span, enzyme row WT


organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

proof_lines: kcat is 25.8 sec(-1) for R-HPC oxidation (at pH 7.5). kcat is 24.5 sec(-1) for 2-KPC reduction (at pH 7.5) (PubMed:11851420). kcat is 26.8 sec(-1) with R-HPC as substrate. kcat is 0.044 sec(-1) with S-HPC as substrate. kcat is 2.9 sec(-1) w


substrate_name: NADH (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADH

substrate: NADH (at pH 7.5)


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

organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

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


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

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

substrate: dihydrotestosterone (in the presence of NADPH)


enzyme_display_name: D-specific alpha-keto acid dehydrogenase

organism: Enterococcus faecium

substrate_name: pyruvate (in the presence of NADPH at pH 5.6)

assay_conditions_summary: pH 5.6; buffer 50 mM sodium phosphate; cofactor NADPH

column_label: Table II row pyruvate; VanH column Km (mM).

raw_value_unit_evidence: Table II VanH row pyruvate: Km 1.45 mM.

row_label: pyruvate

table_label: Table II, Kinetic Data for VanH and D-Lactate Dehydrogenases


substrate_name: alpha-ketobutyrate (in the presence of NADPH at pH 5.6)

column_label: Table II row alpha-ketobutyrate; VanH column Km (mM).

normalized_value_unit_evidence: Km 2.6 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketobutyrate: Km 2.6 mM.

row_label: alpha-ketobutyrate

enzyme: D-specific alpha-keto acid dehydrogenase


substrate_name: alpha-ketovalerate (in the presence of NADPH at pH 5.6)

column_label: Table II row alpha-ketovalerate; VanH column Km (mM).

normalized_value_unit_evidence: Km 40 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketovalerate: Km 40 mM.

row_label: alpha-ketovalerate


substrate_name: alpha-ketocaproate (in the presence of NADPH at pH 5.6)

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

column_label: Table II row alpha-ketocaproate; VanH column Km (mM).

normalized_value_unit_evidence: Km 20 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketocaproate: Km 20 mM.

row_label: alpha-ketocaproate


substrate_name: alpha-ketoisocaproate (in the presence of NADPH at pH 5.6)

column_label: Table II row alpha-ketoisocaproate; VanH column Km (mM).

normalized_value_unit_evidence: Km 31 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketoisocaproate: Km 31 mM.

row_label: alpha-ketoisocaproate


substrate_name: NADPH (at pH 5.6)

assay_conditions_summary: pH 5.6; cofactor NADPH

proof_lines: kcat is 40 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:1931965). kcat is 10.7 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:9605319). kcat is 35 sec(-1) with alpha-ketobu

substrate: NADPH (at pH 5.6)


substrate_name: NADH (at pH 5.6)

assay_conditions_summary: pH 5.6; cofactor NADH

column_label: Table II VanH cofactor row Km (NADH) (uM).

normalized_value_unit_evidence: Km 0.021 mM after converting 21 uM to mM.

raw_value_unit_evidence: Table II row Km (NADH): 21 uM.

row_label: Km (NADH)

substrate: NADH (at pH 5.6)


enzyme_display_name: Aldo-keto reductase family 1 member C1

organism: Homo sapiens

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: 2-(S)-hydroxypropyl-CoM dehydrogenase 3

proof_lines: kcat is 5.5 sec(-1) with R-HPC as substrate. kcat is 25 sec(-1) with S-HPC as substrate. kcat is 11 sec(-1) with 2-KPC as substrate. kcat is 0.044 sec(-1) with 2-butanone as substrate. kcat is 2.0 sec(-1) with 2-propanol as substrate. kcat

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase 3


substrate_name: NAD(+)

substrate: NAD(+)


organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M304S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: 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 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.


assay_conditions_summary: pH 7; cofactor NADP+

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.


smiles: CC(CSCCS(=O)(=O)O)O

proof_lines: recombinant enzyme, pH and temperature not specified in the publication

source_databases_merged: brenda skid


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase

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

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase


smiles: CC(=O)CSCCS(=O)(=O)O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R238H with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232Q to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R235G 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_ec_organism_unique and applied mutation signature R238E with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


proof_lines:
isoenzyme I
isoenzyme II


substrate_name: NADPH


organism: Xanthobacter sp.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F22Y with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


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


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


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

substrate_name: 5-beta-androstane-3,17-dione (at 37 degrees Celsius)

column_label: Table 1; row 3,17-Diketosteroids / 5beta-Androstane-3,17-dione; Km column

normalized_value_unit_evidence: Km=0.0052 mM converted from 5.2 uM

raw_value_unit_evidence: Table 1 3,17-Diketosteroids / 5beta-Androstane-3,17-dione Km 5.2 uM

table_label: Table 1


substrate_name: 4-androstene-3,17-dione (at 37 degrees Celsius)

column_label: Table 1; row 3,17-Diketosteroids / 4-Androstene-3,17-dione; Km column

normalized_value_unit_evidence: Km=0.0046 mM converted from 4.6 uM

raw_value_unit_evidence: Table 1 3,17-Diketosteroids / 4-Androstene-3,17-dione Km 4.6 uM

enzyme: Dehydrogenase/reductase SDR family member 11


substrate_name: progesterone (at 37 degrees Celsius)

column_label: Table 1; row 3,20-Diketosteroids / Progesterone; Km column

normalized_value_unit_evidence: Km=0.0034 mM converted from 3.4 uM

raw_value_unit_evidence: Table 1 3,20-Diketosteroids / Progesterone Km 3.4 uM

row_label: 3,20-Diketosteroids / Progesterone

substrate: progesterone (at 37 degrees Celsius)


substrate_name: 5-beta-pregnane-3,20-dione (at 37 degrees Celsius)

column_label: Table 1; row 3,20-Diketosteroids / 5beta-Pregnane-3,20-dione; Km column

normalized_value_unit_evidence: Km=0.015 mM converted from 15 uM

raw_value_unit_evidence: Table 1 3,20-Diketosteroids / 5beta-Pregnane-3,20-dione Km 15 uM


substrate_name: 17-beta-estradiol (at 37 degrees Celsius)

column_label: Table 2; row C18-steroid / 17beta-Estradiol; Km column

normalized_value_unit_evidence: Km=0.016 mM converted from 16 uM

raw_value_unit_evidence: Table 2 C18-steroid / 17beta-Estradiol Km 16 uM

row_label: C18-steroid / 17beta-Estradiol

table_label: Table 2


substrate_name: testosterone (at 37 degrees Celsius)

column_label: Table 2; row C19-steroids / Testosterone; Km column

normalized_value_unit_evidence: Km=0.03 mM converted from 30 uM

raw_value_unit_evidence: Table 2 C19-steroids / Testosterone Km 30 uM

row_label: C19-steroids / Testosterone

substrate: testosterone (at 37 degrees Celsius)


substrate_name: 5-alpha-androstane-3-alpha,17-beta-diol (at 37 degrees Celsius)


substrate_name: isolithocholic acid (at 37 degrees Celsius)

proof_lines:
DHRS11
bile acid isomerization
7beta-OH dehydrogenases


substrate_name: 1-phenyl-1,2-propanedione (at 37 degrees Celsius)


substrate_name: 2,3-hexanedione (at 37 degrees Celsius)

substrate: 2,3-hexanedione (at 37 degrees Celsius)


substrate_name: 2,3-heptanedione (at 37 degrees Celsius)

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

column_label: Table 3; row alpha-Dicarbonyl compounds / 2,3-Heptanedione; Km column

normalized_value_unit_evidence: Km=0.201 mM converted from 201 uM

raw_value_unit_evidence: Table 3 alpha-Dicarbonyl compounds / 2,3-Heptanedione Km 201 uM


substrate_name: 3,4-hexanedione (at 37 degrees Celsius)

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

column_label: Table 3; row alpha-Dicarbonyl compounds / 3,4-Hexanedione; Km column

normalized_value_unit_evidence: Km=0.42 mM converted from 420 uM

raw_value_unit_evidence: Table 3 alpha-Dicarbonyl compounds / 3,4-Hexanedione Km 420 uM

substrate: 3,4-hexanedione (at 37 degrees Celsius)


substrate_name: alpha-tetralone (at 37 degrees Celsius)

column_label: Table 3; row Alicyclic ketones / alpha-Tetralone; Km column

normalized_value_unit_evidence: Km=0.178 mM converted from 178 uM

raw_value_unit_evidence: Table 3 Alicyclic ketones / alpha-Tetralone Km 178 uM

row_label: Alicyclic ketones / alpha-Tetralone

substrate: alpha-tetralone (at 37 degrees Celsius)


substrate_name: loxoprofen (at 37 degrees Celsius)

column_label: Table 3; row Alicyclic ketones / Loxoprofen; Km column

normalized_value_unit_evidence: Km=0.74 mM converted from 740 uM

raw_value_unit_evidence: Table 3 Alicyclic ketones / Loxoprofen Km 740 uM

row_label: Alicyclic ketones / Loxoprofen

substrate: loxoprofen (at 37 degrees Celsius)


column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / 2-KPC: Km=68 uM; kcat=29 s^-1; kcat/Km=4.2 x 10^5 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / 2-KPC


column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / R-HPC: Km=96 uM; kcat=48 s^-1; kcat/Km=5.0 x 10^5 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / R-HPC


column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / S-HPC: Km=220 uM; kcat=0.12 s^-1; kcat/Km=5.3 x 10^2 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / S-HPC


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rR-HPCDH1 / (R)-2-butanol: Km=220 mM; kcat=1.9 s^-1; kcat/Km=8.69 M^-1 s^-1.

row_label: Table 5 / rR-HPCDH1 / (R)-2-butanol


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rR-HPCDH1 / (S)-2-butanol: Km=350 mM; kcat=9.3 s^-1; kcat/Km=26.4 M^-1 s^-1.

row_label: Table 5 / rR-HPCDH1 / (S)-2-butanol


substrate_name: dehydroepiandrosterone

sequence_variant_note: Mutation signature S194G matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: dehydroepiandrosterone


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K214A 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 R211A 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 S143A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 2. Summary of Amino Acid Substitutions Made to the Putative rS-HPCDH3 Catalytic Residues Using Site-Directed Mutagenesis, Table 2 / S143A / S-HPC: Km=9500 uM; kcat=0.013 s^-1; kcat/Km=1.4 x 10^0 M^-1 s^-1.

row_label: Table 2 / S143A / S-HPC


sequence_variant_note: Mutation signature Y156A matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rS-HPCDH3 / (R)-2-butanol: Km=68 mM; kcat=1.0 s^-1; kcat/Km=14.8 M^-1 s^-1.

row_label: Table 5 / rS-HPCDH3 / (R)-2-butanol


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rS-HPCDH3 / (S)-2-butanol: Km=28 mM; kcat=2.6 s^-1; kcat/Km=92.8 M^-1 s^-1.

row_label: Table 5 / rS-HPCDH3 / (S)-2-butanol


smiles: CCC(C)=O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56841 and applied mutation signature K214A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM glycine; cofactor NAD+

column_label: Table 3 (Kinetic Parameters for wild-type rS-HPCDH3 and its alanine variants), block 'Substrate: 2-KPC', enzyme row 'K214A'; column 'Km (mM)' = 12 ± 0. 9; column 'kcat (s-1)' = 9.6 ± 0.3; column 'kcat/Km (M-1 s-1)' = 8.1 x 10^2; column 'Change in Km (x-fold)' and column 'Change in kcat (x-fold)' print unitless ratios to the wild-type row.

normalized_value_unit_evidence: Km: printed Table 3 cell 12 under the column head Km (mM); millimolar is already the canonical unit, so no unit conversion applies and the value is 12.0 mM. kcat: printed Table 3 cell 9.6 under the column head kcat (s-1); per-second is already the canonical unit, so no unit conversion applies and the value is 9.6 s^(-1). kcat/Km: printed Table 3 cell 8.1 x 10^2 under the column head kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.1 x 10^2 / 1000 = 0.81 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, block 'Substrate: 2-KPC', enzyme row 'K214A': the column headed Km (mM) prints 12 ± 0. 9; the column headed kcat (s-1) prints 9.6 ± 0.3; the column headed kcat/Km (M-1 s-1) prints 8.1 x 10^2.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56841 and applied mutation signature R211A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Parameters for wild-type rS-HPCDH3 and its alanine variants), block 'Substrate: 2-KPC', enzyme row 'R211A'; column 'Km (mM)' = 11 ± 0.4; column 'kcat (s-1)' = 8.6 ± 0.2; column 'kcat/Km (M-1 s-1)' = 7.5 x 10^2; column 'Change in Km (x-fold)' and column 'Change in kcat (x-fold)' print unitless ratios to the wild-type row.

normalized_value_unit_evidence: Km: printed Table 3 cell 11 under the column head Km (mM); millimolar is already the canonical unit, so no unit conversion applies and the value is 11.0 mM. kcat: printed Table 3 cell 8.6 under the column head kcat (s-1); per-second is already the canonical unit, so no unit conversion applies and the value is 8.6 s^(-1). kcat/Km: printed Table 3 cell 7.5 x 10^2 under the column head kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.5 x 10^2 / 1000 = 0.75 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, block 'Substrate: 2-KPC', enzyme row 'R211A': the column headed Km (mM) prints 11 ± 0.4; the column headed kcat (s-1) prints 8.6 ± 0.2; the column headed kcat/Km (M-1 s-1) prints 7.5 x 10^2.


proof_lines: kcat is 28 sec(-1) with S-HPC as substrate. kcat is 20 sec(-1) with 2-KPC as substrate. kcat is 2.4 sec(-1) with R-HPC as substrate.


substrate_name: NADPH

substrate: NADPH


substrate_name: estrone (at 37 degrees Celsius)

proof_lines:
DHRS11
sex steroids
17beta-OH activities

substrate: estrone (at 37 degrees Celsius)


substrate_name: 5-alpha-androstan-3-alpha-ol-17-one (at 37 degrees Celsius)

column_label: Table 1; row 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one; Km column

normalized_value_unit_evidence: Km=0.0013 mM converted from 1.3 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one Km 1.3 uM


substrate_name: dehydroepiandrosterone (DHEA) (at 37 degrees Celsius)

column_label: Table 1; row 17-Ketosteroids / DHEA; Km column

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA Km 11 uM

row_label: 17-Ketosteroids / DHEA


substrate_name: DHEA sulfate (at 37 degrees Celsius)

column_label: Table 1; row 17-Ketosteroids / DHEA sulfate; Km column

normalized_value_unit_evidence: Km=0.012 mM converted from 12 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA sulfate Km 12 uM

row_label: 17-Ketosteroids / DHEA sulfate

substrate: DHEA sulfate (at 37 degrees Celsius)


substrate_name: dehydrolithocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Dehydrolithocholic acid; Km column

normalized_value_unit_evidence: Km=0.0011 mM converted from 1.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Dehydrolithocholic acid Km 1.1 uM


substrate_name: 20-alpha-hydroxyprogesterone (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / 20alpha-Hydroxyprogesterone; Km column

normalized_value_unit_evidence: Km=0.0051 mM converted from 5.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / 20alpha-Hydroxyprogesterone Km 5.1 uM


substrate_name: taurodehydrocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Taurodehydrocholic acid; Km column

normalized_value_unit_evidence: Km=0.044 mM converted from 44 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Taurodehydrocholic acid Km 44 uM


substrate_name: dehydrocholic acid (at 37 degrees Celsius)


substrate_name: 5-beta-dihydrotestosterone (DHT) (at 37 degrees Celsius)


organism: Yersinia pestis

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH

proof_lines:
pH 7.8, 37°C
Raw SKiD Env: Temp=37°C, pH=7.8


substrate_name: 1-deoxy-D-xylulose 5-phosphate

column_label: Table 1; row label Y. pestis; column label Kcat DXP/Km DXP (M^-1 min^-1); raw value 4.6 x 10^5; raw unit M^-1 min^-1; normalized value kcat/Km=7.66667 s^-1*mM^-1; assay condition DXP varied. Table 1 also labels Km DXP (uM) and Kcat DXP (s^-1).

normalized_value_unit_evidence: Km normalized_value=0.2215 normalized_unit=mM; kcat normalized_value=1.7 normalized_unit=s^-1; kcat/Km=7.66667 s^-1*mM^-1 from explicit Kcat DXP/Km DXP table value conversion.

raw_value_unit_evidence: Table 1 row Y. pestis reports Km DXP=221.5 +/- 34.3 uM, Kcat DXP=1.7 s^-1, and Kcat DXP/Km DXP=4.6 x 10^5 M^-1 min^-1.

row_label: Y. pestis

table_label: Table 1, MEP synthase Apparent Kinetic Parameters

substrate: 1-deoxy-D-xylulose 5-phosphate


substrate_name: glycerol

smiles: C(C(CO)O)O

assay_conditions_summary: cofactor NADPH

substrate: glycerol


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


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


enzyme_display_name: GDP-L-fucose synthase

organism: Escherichia coli (strain K12)

enzyme: GDP-L-fucose synthase


substrate_name: NADH

substrate: NADH


organism: Bacillus subtilis (strain 168)

substrate_name: DHAP

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

assay_conditions_summary: pH 8.2; cofactor NADH

column_label: Table 1, substrate row DHAP, KM (uM) column; condition footnote a.

row_label: DHAP

substrate: DHAP


column_label: Table 1, substrate row NADH, KM (uM) column; condition footnote a.

row_label: NADH


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

column_label: Table 1, substrate row G1P, KM (uM) column; condition footnote a.


substrate_name: NAD(+)

assay_conditions_summary: pH 8.2; cofactor NAD+

column_label: Table 1, substrate row NAD+, KM (uM) column; condition footnote a.

row_label: NAD+

substrate: NAD(+)


enzyme_display_name: 1,5-anhydro-D-fructose reductase

substrate_name: NADPH (at 25 degrees Celsius)

enzyme: 1,5-anhydro-D-fructose reductase

substrate: NADPH (at 25 degrees Celsius)


substrate_name: NADH (at 25 degrees Celsius)

substrate: NADH (at 25 degrees Celsius)


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Bacillus subtilis

substrate_name: NAD+

assay_conditions_summary: pH 8.2; 318.15 K; cofactor NAD+

column_label: Literal AraM Table 1 NAD+ row under the reverse reaction with saturating 10 mM G1P; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.008 s^-1; Km=0.059 mM; deterministic same-row quotient=0.13559322033898305 s^-1 mM^-1. Direct literal conversions are kcat=0.007666666666666667 s^-1 and Km=0.0593 mM; independently printed efficiency converts to 0.13 s^-1 mM^-1 and is not substituted for the component quotient.

table_label: Table 1. Steady-State Kinetic Constants of the G1PDH Activity of AraM

enzyme: sn-glycerol-1-phosphate dehydrogenase


assay_conditions_summary: pH 8.2; 318.15 K; cofactor NADH

column_label: Literal AraM Table 1 NADH row under the forward reaction with saturating 0.1 mM DHAP; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.222 s^-1; Km=0.016 mM; deterministic same-row quotient=13.875 s^-1 mM^-1. Direct literal conversions are kcat=0.22166666666666668 s^-1 and Km=0.016 mM; independently printed efficiency converts to 13.833333333333334 s^-1 mM^-1 and is not substituted for the component quotient.


substrate_name: sn-Glycerol 1-phosphate

column_label: Literal AraM Table 1 G1P row under the reverse reaction with saturating 4 mM NAD+; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.008 s^-1; Km=1.37 mM; deterministic same-row quotient=0.00583941605839416 s^-1 mM^-1. Direct literal conversions are kcat=0.008333333333333333 s^-1 and Km=1.37 mM; independently printed efficiency converts to 0.006 s^-1 mM^-1 and is not substituted for the component quotient.

substrate: sn-Glycerol 1-phosphate


substrate_name: glycerone phosphate

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

substrate: glycerone phosphate


substrate_name: 9,10-phenanthrenequinone with NADPH as cofactor


organism: Thermotoga maritima

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 358.15 K; cofactor NADPH


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


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Section 3 Results and discussion prose gives the DXP reductoisomerase Km value as 0.3 mM.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM

row_label: DXP reductoisomerase substrate DXP

table_label: Section 3 Results and discussion prose


column_label: Section 3 Results and discussion prose states NADPH is the cofactor with Km of 5 uM.

raw_value_unit_evidence: Km raw_value=5 raw_unit=uM

row_label: DXP reductoisomerase cofactor NADPH


organism: Sus scrofa

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Abstract states the purified enzyme showed a Km value of 0.44 mM for AF at the optimum pH of 7.0.

raw_value_unit_evidence: Km raw_value=0.44 raw_unit=mM

row_label: porcine liver NADPH-dependent reductase with 1,5-anhydro-D-fructose

table_label: PubMed abstract PMID 9504428


enzyme_display_name: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7

organism: Mus musculus

substrate_name: estrone

substrate: estrone


enzyme: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7


column_label: Table 2: Kinetic parameters of purified recombinant human and mouse 17HSD type 7; row E1 -> E2; Human 17HSD type 7 Km (uM) column = 3.25 +/- 0.38 uM.

normalized_value_unit_evidence: Km normalized_value=0.00325 normalized_unit=mM from 3.25 uM / 1000.

raw_value_unit_evidence: Table 2 row E1 -> E2, Human 17HSD type 7 Km column reports Km 3.25 +/- 0.38 uM.


column_label: Table 2: Kinetic parameters of purified recombinant human and mouse 17HSD type 7; row DHT -> 3betaA-diol; Human 17HSD type 7 Km (uM) column = 2.60 +/- 0.30 uM.

normalized_value_unit_evidence: Km normalized_value=0.00260 normalized_unit=mM from 2.60 uM / 1000.

raw_value_unit_evidence: Table 2 row DHT -> 3betaA-diol, Human 17HSD type 7 Km column reports Km 2.60 +/- 0.30 uM.

row_label: DHT -> 3betaA-diol


organism: Escherichia coli


substrate_name: 1,2-Dideoxy-D-hexulose 6-phosphate

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

proof_lines:
Et-DXP
poor substrate

substrate: 1,2-Dideoxy-D-hexulose 6-phosphate


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W203F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W203Y to reconstruct the assayed variant sequence.


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


substrate_name: dihydrotestosterone

column_label: Abstract reports expressed 3 beta HSD V has an apparent Km value for DHT of 0.47 microM.

raw_value_unit_evidence: Km raw_value=0.47 microM raw_unit=microM

row_label: Mouse expressed 3 beta HSD V / DHT

table_label: PubMed XML abstract PMID 7491113

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

substrate: dihydrotestosterone


enzyme_display_name: NADPH-dependent 3-keto-steroid reductase Hsd3b4

column_label: PMID 7491113 abstract reports expressed 3 beta HSD V has lower DHT Km than 3 beta HSD IV: 0.47 microM vs 2.2 microM respectively; PMID 8145763 establishes 3 beta HSD IV converts DHT to 5 alpha-androstanediol with NADPH.

raw_value_unit_evidence: Km raw_value=2.2 raw_unit=microM for DHT

row_label: mouse 3 beta HSD IV / Hsd3b4 converting dihydrotestosterone to 5 alpha-androstanediol

table_label: PubMed abstract PMID 7491113 with lead context PMID 8145763


substrate_name: 1-Fluoro-1-deoxy-D-xylulose 5-phosphate

substrate: 1-Fluoro-1-deoxy-D-xylulose 5-phosphate


organism: Taiwanofungus camphoratus

substrate_name: S-nitrosoglutathione

substrate: S-nitrosoglutathione


substrate_name: S-(hydroxymethyl)glutathione

substrate: S-(hydroxymethyl)glutathione


enzyme_display_name: UniProt P11766

enzyme: UniProt P11766


enzyme_display_name: UniProt Q5JFV8

organism: Thermococcus kodakarensis

substrate_name: homoisocitrate

enzyme: UniProt Q5JFV8

substrate: homoisocitrate


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


substrate_name: isocitrate

substrate: isocitrate


enzyme_display_name: UniProt Q72IW9

organism: Thermus thermophilus

enzyme: UniProt Q72IW9


substrate: NAD+


substrate_name: dihydrotestosterone (in the presence of NADH)

assay_conditions_summary: cofactor NADH

proof_lines:
3 beta-hydroxysteroid dehydrogenase
dihydrotestosterone
Homo sapiens

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


enzyme_display_name: xanthoxin dehydrogenase

organism: Arabidopsis thaliana

substrate_name: xanthoxin

proof_lines: no activity with xanthoxic acid, ethanol, isopropanol, butanol, cyclohexanol and 2,6-dimethylcyclohexanol.

enzyme: xanthoxin dehydrogenase

substrate: xanthoxin


enzyme_display_name: sorbose reductase

organism: Candida albicans

substrate_name: D-fructose

proof_lines:
pH 7.5, 25°C, positive cooperativity
pH 7.5, 25°C, Michaelis-Menten kinetics
K0.5-value, positive cooperativity

enzyme: sorbose reductase

substrate: D-fructose


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

proof_lines:
pH 7.5, 30 C
Raw SKiD Env: Temp=30 C, pH=7.5

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase


enzyme_display_name: momilactone-A synthase

organism: Oryza sativa

substrate_name: oryzalexin A

assay_conditions_summary: pH 8

enzyme: momilactone-A synthase

substrate: oryzalexin A


assay_conditions_summary: pH 8; cofactor NAD+


organism: Gluconobacter oxydans

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

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: D-mannitol

smiles: C(C(C(C(C(CO)O)O)O)O)O

assay_conditions_summary: pH 10; 298.15 K; cofactor NADPH

substrate: D-mannitol


substrate_name: L-sorbose

substrate: L-sorbose


organism: Ensifer adhaerens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A13G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A13G/S10G with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature A13G/S33D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature D176A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature G206I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature H180A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature K94G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature S10G to reconstruct the assayed variant sequence.


organism: Eubacterium barkeri

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


organism: Bacillus cereus

proof_lines:
pH 8.5, 37°C
pH 8.5, 37°C, recombinant enzyme


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


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+


organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature T71V to reconstruct the assayed variant sequence.

substrate: Unknown

source: unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature S80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature I82N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature L81P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature L83R to reconstruct the assayed variant sequence.


enzyme_display_name: diacetyl reductase [(R)-acetoin forming]

organism: Shouchella clausii

substrate_name: diacetyl

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

substrate: diacetyl


organism: Metallosphaera sedula

substrate_name: malonate semialdehyde

substrate: malonate semialdehyde


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 338.15 K; cofactor NADPH


enzyme_display_name: NADP-retinol dehydrogenase

protein_accession_database: NCBI Protein

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

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NADPH reduction; Km column raw 40 +/- 1.0 uM; kcat column raw 0.033 +/- 0.00 min^-1; kcat/Km column raw 0.83 +/- 0.05 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM; kcat normalized_value=0.00055 normalized_unit=s^-1; kcat/Km normalized_value=0.01375 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=40 +/- 1.0 raw_unit=uM; kcat raw_value=0.033 +/- 0.00 raw_unit=min^-1; kcat/Km raw_value=0.83 +/- 0.05 raw_unit=mM^-1 min^-1

row_label: NADPH reduction

enzyme: NADP-retinol dehydrogenase


assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NAD+ oxidation; Km column raw 4.0 +/- 0.2 uM; kcat column raw 0.10 +/- 0.01 min^-1; kcat/Km column raw 25 +/- 0.1 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.004 normalized_unit=mM; kcat normalized_value=0.0017 normalized_unit=s^-1; kcat/Km normalized_value=0.425 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.0 +/- 0.2 raw_unit=uM; kcat raw_value=0.10 +/- 0.01 raw_unit=min^-1; kcat/Km raw_value=25 +/- 0.1 raw_unit=mM^-1 min^-1

row_label: NAD+ oxidation


assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NADP+ oxidation; Km column raw 4.2 +/- 0.3 uM; kcat column raw 0.11 +/- 0.02 min^-1; kcat/Km column raw 26 +/- 0.2 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.0042 normalized_unit=mM; kcat normalized_value=0.0018 normalized_unit=s^-1; kcat/Km normalized_value=0.4285714285714286 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.2 +/- 0.3 raw_unit=uM; kcat raw_value=0.11 +/- 0.02 raw_unit=min^-1; kcat/Km raw_value=26 +/- 0.2 raw_unit=mM^-1 min^-1

row_label: NADP+ oxidation


substrate_name: retinal

column_label: Table 1. Kinetic parameters for aldehyde substrates of BcALDH in oxidation activity using NAD+ as a cosubstrate; row all-trans-retinal -> all-trans-retinoic acid; Km column raw 7 +/- 0.1 uM; kcat column raw 0.28 +/- 0.03 min^-1; kcat/Km column raw 40 +/- 0.2 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.007 normalized_unit=mM; kcat normalized_value=0.0047 normalized_unit=s^-1; kcat/Km normalized_value=0.6714285714285715 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=7 +/- 0.1 raw_unit=uM; kcat raw_value=0.28 +/- 0.03 raw_unit=min^-1; kcat/Km raw_value=40 +/- 0.2 raw_unit=mM^-1 min^-1

substrate: retinal


enzyme_display_name: Aldo-keto reductase family 1 member B15

organism: Homo sapiens

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) u

enzyme: Aldo-keto reductase family 1 member B15

substrate: all-trans-retinal


substrate_name: D,L-glyceraldehyde

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

substrate: D,L-glyceraldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC(=O)C


substrate_name: farnesal

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

substrate: farnesal


assay_conditions_summary: cofactor NADPH