assay_conditions_summary: cofactor NAD+


organism: Pseudomonas putida

substrate_name: deoxycholate

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

substrate: deoxycholate

status: unverified

source: brenda


substrate_name: cholate

substrate: cholate


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)(+)]

organism: Bacillus sp. (in: Bacteria)

substrate_name: D-glucose

source_db: oed

verification_status: corrected

protein_accession_database: UniProt

sequence_source: genbank:KJ701281.2 (Bacillus sp. strain ZJ gdh; PMID 28587256)

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

column_label: Table 2 columns are Substrate/Cofactor, Km (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); D-glucose row cells are 17.126 +/- 0.946, 87.844 +/- 1.362, and 5.129.

normalized_value_unit_evidence: Km 17.126 mM; kcat 87.844 s^-1; printed kcat/Km 5.129 s^-1 mM^-1. Export expected kcat/Km 5.129043559500175 is within table precision/rounding.

row_label: BzGDH / D-glucose

table_label: Table 2, Kinetic constants of BzGDH

data_origin: experimental

enzyme: glucose 1-dehydrogenase [NAD(P)(+)]

substrate: D-glucose

status: corrected

source: oed


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 2 columns are Substrate/Cofactor, Km (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); NAD row cells are 0.072 +/- 0.009, 84.521 +/- 2.175, and 1166.294.

normalized_value_unit_evidence: Km 0.072 mM; kcat 84.521 s^-1; printed kcat/Km 1166.294 s^-1 mM^-1. Export expected kcat/Km 1173.888888888889 is a recomputation from displayed rounded fields; the primary table metric is preserved.

row_label: BzGDH / NAD

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 2 columns are Substrate/Cofactor, Km (mM), kcat (s^-1), and kcat/Km (mM^-1*s^-1); NADP row cells are 0.404 +/- 0.088, 73.960 +/- 2.677, and 182.978.

normalized_value_unit_evidence: Km 0.404 mM; kcat 73.960 s^-1; printed kcat/Km 182.978 s^-1 mM^-1. Export expected kcat/Km 183.06930693069305 is within table precision/rounding.

row_label: BzGDH / NADP

substrate: NADP+


organism: Rattus norvegicus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: 5alpha-dihydrotestosterone as substrate, 3-beta-hydroxysteroid dehydrogenase activity

proof_lines: estrone as substrate, 17beta-hydroxysteroid dehydrogenase activity

substrate: NADPH


assay_conditions_summary: cofactor NADP+

proof_lines: testosterone as substrate, 17beta-hydroxysteroid dehydrogenase activity

proof_lines: 3beta-hydroxy-5alpha-androstan-17-one as substrate, 3beta-hydroxysteroid dehydrogenase activity


substrate_name: testosterone

substrate: testosterone


organism: Homo sapiens

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


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

mutation_type: substitution


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)+]

organism: Priestia megaterium

substrate_name: beta-D-glucose

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: pH 8.0, 30°C, coenzyme NADP+, isoenzyme GlcDH II

proof_lines: pH 8.0, 30°C, coenzyme NAD+, isoenzymes GlcDH I and GlcDH II

enzyme: glucose 1-dehydrogenase [NAD(P)+]

substrate: beta-D-glucose


proof_lines:
pH 8.0, 30°C, isoenzyme GlcDH II
pH 8.0, 30°C, isoenzyme GlcDH I
pH 8.0, 30°C, isoenzyme GlcDH IV


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+

proof_lines:
pH 8.0, 30°C, isoenzyme GlcDH I
pH 8.0, 30°C, isoenzyme GlcDH IV
pH 8.0, 30°C, isoenzyme GlcDH III


enzyme_display_name: L-gulonate 3-dehydrogenase

organism: Schwanniomyces occidentalis

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: cosubstrate L-gulonate, pH 7.5 and pH 8.5

enzyme: L-gulonate 3-dehydrogenase


substrate_name: D-gluconate

assay_conditions_summary: pH 8.5; cofactor NAD+

substrate: D-gluconate


substrate_name: L-gulonate

proof_lines:
cofactor NAD+, pH 8.5
cofactor NAD+, pH 7.5

substrate: L-gulonate


organism: Mus musculus

substrate_name: 3-oxo-5beta-cholan-24-oic acid

substrate: 3-oxo-5beta-cholan-24-oic acid


proof_lines: also in this range: 17alpha,21-dihydroxy-5beta-pregnan-3,11,20-trione, acenaphthequinone

proof_lines: also in this range: 3alpha-hydroxy-5beta-pregnan-17-one


substrate_name: glycolithocholic acid

substrate: glycolithocholic acid


substrate_name: androsterone

substrate: androsterone


substrate_name: Camphorquinone

substrate: Camphorquinone


proof_lines: also in this range: 2,3-hexanedione, 1-phenyl-1,2-propanedione, 2,3-pentanedione, pyridine-4-aldehyde, 2,3-butanedione


organism: Mesocricetus auratus

protein_accession_database: NCBI Protein

kcat_over_km_origin: calculated

sequence_source: genbank:LC006028.1 protein_id:BAP76083.1 via PMID:26002966 paper_sequence_manual_review


substrate_name: androstanedione

proof_lines:
detection spectrophotometrically
NADPH, detection spectrophotometrically

substrate: androstanedione


organism: Meleagris gallopavo


substrate_name: D-glucose 6-phosphate

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

substrate: D-glucose 6-phosphate


substrate_name: allopregnanolone

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

assay_conditions_summary: pH 7

substrate: allopregnanolone


assay_conditions_summary: pH 7; cofactor NADP+


assay_conditions_summary: pH 7; cofactor NADPH


sequence_source: genbank:LC006028.1 protein_id:BAP76083.1 via PMID:26002966 AKR1C35


substrate_name: geranylgeraniol

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

substrate: geranylgeraniol


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: farnesol

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

substrate: farnesol


substrate_name: beta-ionol

substrate: beta-ionol


enzyme_display_name: D-galactose 1-dehydrogenase

organism: Azotobacter vinelandii

substrate_name: NAD+

enzyme: D-galactose 1-dehydrogenase

substrate: NAD+


substrate_name: D-galactose

substrate: D-galactose


organism: Digitalis purpurea

assay_conditions_summary: cofactor NADH

proof_lines: cytosolic NADH-linked 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase


substrate_name: NADH

substrate: NADH


substrate_name: NADPH

proof_lines: microsomal NADPH-linked 5beta-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase

substrate: NADPH


organism: Oncorhynchus mykiss

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines:
coenzyme NADP+
coenzyme NAD+
pH 7.5, 25°C, coenzyme NADP+


substrate_name: D-glucose

assay_conditions_summary: pH 10; 298.15 K; cofactor NADP+

proof_lines:
coenzyme NAD+
coenzyme NADP+
pH 10, 25°C, coenzyme NAD+

substrate: D-glucose


substrate_name: deamino-NADP+

proof_lines: pH and temperature not specified in the publication

substrate: deamino-NADP+


substrate_name: D-galactose 6-phosphate

proof_lines:
isoenzyme II
isoenzyme I

substrate: D-galactose 6-phosphate


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: Unknown


organism: Coriandrum sativum


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

substrate: NADP+


organism: Cavia porcellus

substrate_name: testosterone

substrate: testosterone


enzyme_display_name: glucose 1-dehydrogenase

organism: Lagothrix lagotricha

substrate_name: beta-D-Glucose; NAD+

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

assay_conditions_summary: cofactor NAD+

enzyme: glucose 1-dehydrogenase

substrate: beta-D-Glucose; NAD+


substrate_name: D-glucose 6-phosphate

proof_lines:
at pH 8.0 and 37°C
native G6PD
refolded G6PD

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: isoenzymes I and II, with glucose 6-phosphate


enzyme_display_name: L-arabinose 1-dehydrogenase

organism: Haloferax volcanii

verification_status: verified

sequence_source: uniprot:D4GP33 gene:HVO_B0032 via PMID:23949136 paper_sequence_manual_review

column_label: Downloaded Springer PDF Results section states that rate dependence on L-arabinose, NADP+ and NAD+ followed Michaelis-Menten kinetics with apparent Km values of 2.1, 1 and 2 mM, respectively.

normalized_value_unit_evidence: Km normalized_value=2 normalized_unit=mM for NAD+.

raw_value_unit_evidence: Results text reports apparent Km values of 2.1, 1 and 2 mM for L-arabinose, NADP+ and NAD+, respectively.

row_label: Haloferax volcanii L-AraDH dependence on NAD+

table_label: PDF Results section; Supplemental Fig. 3S referenced

enzyme: L-arabinose 1-dehydrogenase

status: verified


assay_conditions_summary: pH 8.5; cofactor NADP+


organism: Paralabrax clathratus


organism: Scomber scombrus

substrate_name: NAD+; beta-D-Glucose

substrate: NAD+; beta-D-Glucose


substrate_name: NADP+; D-Glucose

substrate: NADP+; D-Glucose


organism: Pituophis catenifer


organism: Salmo salar


organism: Roseateles saccharophilus


organism: Sus scrofa

assay_conditions_summary: cofactor NADPH

proof_lines: isoenzyme II, with 6-phosphonogluconate 0.1 mM


organism: Alburnus tarichi


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


organism: Homo sapiens

proof_lines: below, pH 7.0, 37?, isozymes AKR1C1 and AKR1C3


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines:
pH 7.0, 25°C, isozyme AKR1C3
pH 7.0, 25°C, isozyme AKR1C1
pH 7.0, 37°C with NADP+


organism: Canis lupus familiaris


organism: Gallus gallus


sequence_source: uniprot:P52895 gene:AKR1C2 via PMID:17059222 paper_sequence_manual_review


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

proof_lines:
pH 7.0, 37°C, with NAD(P)H
isozyme AKR1C2
pH 7.0, 25°C, recombinant enzyme


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+


organism: Rattus norvegicus

substrate_name: pregnenolone

substrate: pregnenolone


proof_lines:
microsomal enzyme
mitochondrial enzyme
cytosolic enzyme


organism: Ictalurus punctatus

proof_lines: pH 7.4, 35°C, 3alpha-hydroxysteroid dehydrogenase activity


organism: [Clostridium] innocuum


enzyme_display_name: 3alpha-hydroxycholanate dehydrogenase

organism: Clostridium perfringens

assay_conditions_summary: cofactor NADP+

enzyme: 3alpha-hydroxycholanate dehydrogenase


proof_lines: testicular microsome, inhibition of 17beta-hydroxysteroid dehydrogenase, pH and temperature not specified in the publication

proof_lines: testicular microsome, pH and temperature not specified in the publication, inhibition of 3beta-hydroxysteroid dehydrogenase

proof_lines: intact Leydig cells, pH and temperature not specified in the publication, inhibition of 3beta-hydroxysteroid dehydrogenase


organism: Bifidobacterium sp.


organism: Pseudomonas sp. B-0831

substrate_name: cholate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH

substrate: cholate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S114A/Y153F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y153F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S114A to reconstruct the assayed variant sequence.


substrate_name: dehydrocholate

substrate: dehydrocholate


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

column_label: Table 2. Steady-state kinetic constants for Ps3aHSD and its mutants with steroids, printed column heads substrate | cofactor | enzyme | Km (mM) | kcat (s-1). Journal page 1704 (PDF page 3). Substrate row cholic acid; cofactor NAD+; enzyme row wild-type; Km cell = 56; kcat cell = 23 s^-1. Discussion, journal page 1705 (PDF page 4): kcat/Km cell = 4.2 x 10^5 M-1 sec-1. captured primary segment: Table 2, cholic acid / NAD+ / wild-type row and Discussion kcat/Km sentence, wild-type value: Km 56 uM (printed Table 2 numeral 56, true unit uM per section 3.3, printed under the mislabeled column head Km (mM)); kcat 23 s-1; kcat/Km 4.2 x 10^5 M-1 sec-1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23 s^-1; the printed turnover column is already per second, so the cell is carried across unchanged as 23 s^-1; the export already stores 23 s^-1, the same value, and does not change. Km: printed Table 2 cell 56, printed under the column head Km (mM); 1 uM = 1/1000 mM, so 56 / 1000 = 0.056 mM; the export currently stores 56 mM, which is the printed cell carrying the table's own mislabeled unit without conversion, and is corrected to 0.056 mM. kcat/Km: printed Discussion value 4.2 x 10^5 M-1 sec-1 = 420000 M^-1 s^-1; 1 M^-1 s^-1 = 1/1000 s^-1 mM^-1, so 420000 / 1000 = 420.0 s^-1 mM^-1; the export already stores 420.0 s^-1 mM^-1, the same value, and does not change.

raw_value_unit_evidence: Journal page 1704, Table 2, cholic acid / NAD+ / wild-type row: Km = 56 (printed under the column head Km (mM), true unit uM); kcat = 23 under the printed column head kcat (s-1). Journal page 1705, Discussion: kcat/Km = 4.2 x 10^5 under the printed unit M-1 sec-1.


enzyme_display_name: Aldo-keto reductase family 1 member C2

substrate_name: (s)-tetralol (oxidation)

source_db: uniprot

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

enzyme: Aldo-keto reductase family 1 member C2

substrate: (s)-tetralol (oxidation)

source: uniprot


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

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

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


organism: Zymomonas mobilis subsp. mobilis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature A117S/F277I/Q324H/M381I/V443I/S470I to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L99I/A117S/G225S/F277I/Q324H/M381I/V443I/S470I/A476V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature A117S/Q324H/M381I/V443I/S470I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A117S/Q324H/M381I/V443I/S470I, pH 7.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature A117S/Q324H/V443I/S470I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A117S/Q324H/V443I/S470I, pH 7.5, 30°C


organism: Mus musculus

proof_lines: also in this range: 5beta-pregnan-3,20-dione, 5alpha-androstan-3,17-dione


organism: Digitalis lanata

assay_conditions_summary: pH 7.8; cofactor NADH

column_label: Table 1, row NAD + Pregnenolone, column Km pQ3betaHSD (uM): 90 +/- 9; product Isoprogesterone + Progesterone.

row_label: NAD + Pregnenolone

table_label: Table 1


column_label: Table 1, row NADH + 5alpha-Pregnane-3,20-dione, column Km pQ3betaHSD (uM): 106 +/- 1; product 5alpha-Pregnan-3beta-ol-20-one.

row_label: NADH + 5alpha-Pregnane-3,20-dione


column_label: Table 1, row NAD + 5alpha-Pregnan-3beta-ol-20-one, column Km pQ3betaHSD (uM): 116 +/- 23; product 5alpha-Pregnane-3,20-dione.

row_label: NAD + 5alpha-Pregnan-3beta-ol-20-one


substrate_name: NAD+

assay_conditions_summary: pH 7.8; cofactor NAD+

column_label: Table 1, row NAD, column Km pQ3betaHSD (uM): 260; paper labels oxidized cofactor as NAD.

row_label: NAD

substrate: NAD+


column_label: Table 1, row NAD + 5-Androsten-3beta-ol-17-one, column Km pQ3betaHSD (uM): 642; product 5-Androstene-3,17-dione.

row_label: NAD + 5-Androsten-3beta-ol-17-one


substrate_name: NADH

column_label: Table 1, row NADH, column Km pQ3betaHSD (uM): 642.

row_label: NADH

substrate: NADH


organism: Comamonas testosteroni

substrate_name: androsterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S114A/Y155F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; cofactor NAD+

column_label: PMID 15572373 Table II. The molecular masses and kinetic constants for wild-type and 3alpha-HSD/CR mutants; row S114A/Y155F; columns kcat/Km=(6.2 +/- 0.8) x 10^3 M^-1 s^-1, kcat=0.0028 +/- 0.0001 s^-1, Km=0.44 +/- 0.07 uM; strict kcat/Km value is locked from the same-row kcat and Km central values for androsterone.

normalized_value_unit_evidence: kcat_over_km normalized_value=6.363636363636363 normalized_unit=s^-1*mM^-1; kcat normalized_value=0.0028 normalized_unit=s^-1; km normalized_value=0.00044 normalized_unit=mM.

substrate: androsterone


sequence_variant_note: Mutation signature Y155F/K159A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 9

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F/K159A


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

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant S114A


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K159A to reconstruct the assayed variant sequence.

column_label: PMID 15572373 Table II. The molecular masses and kinetic constants for wild-type and 3alpha-HSD/CR mutants; row K159A; columns kcat/Km=(2.9 +/- 0.1) x 10^5 M^-1 s^-1, kcat=18.9 +/- 0.1 s^-1, Km=65 +/- 5 uM; strict kcat/Km value is locked from the same-row kcat and Km central values for androsterone.

normalized_value_unit_evidence: kcat_over_km normalized_value=290.7692307692307 normalized_unit=s^-1*mM^-1; kcat normalized_value=18.9 normalized_unit=s^-1; km normalized_value=0.065 normalized_unit=mM.


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

proof_lines: pH 9.0, 25°C, recombinant His-tagged wild-type

proof_lines: pH 10.4, 25°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D249S with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10.2; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 10.2; buffer 0.1 M CAPS; cofactor NAD+

column_label: Table 1, Km (uM) row, WT column; footnote specifies saturated NAD+ and varied androsterone.

normalized_value_unit_evidence: Androsterone Km 3.8 +/- 0.5 uM = 0.0038 mM.

raw_value_unit_evidence: Table 1 Km 3.8 +/- 0.5 uM for varied androsterone at saturated NAD+.

row_label: WT 3a-HSD/CR


assay_conditions_summary: pH 10.2; 298.15 K; buffer 0.1 M CAPS; cofactor NAD+

proof_lines: mutant enzyme D249S, in 0.1 M CAPS buffer, at pH 10.2, at 25°C


sequence_variant_note: Resolved canonical sequence from uniprotkb:P80702;rcsb_sifts:1FJH and applied mutation signature D249K to reconstruct the assayed variant sequence.

column_label: Table 1, Km (uM) row, D249K column; footnote specifies saturated NAD+ and varied androsterone.

normalized_value_unit_evidence: Androsterone Km 9 +/- 1 uM = 0.009 mM.

raw_value_unit_evidence: Table 1 Km 9 +/- 1 uM for varied androsterone at saturated NAD+.

row_label: D249K 3a-HSD/CR


assay_conditions_summary: pH 10.2; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprotkb:P80702;rcsb_sifts:1FJH and applied mutation signature D249A to reconstruct the assayed variant sequence.

column_label: Table 1, Km (uM) row, D249A column; footnote specifies saturated NAD+ and varied androsterone.

normalized_value_unit_evidence: Androsterone Km 16 +/- 3.0 uM = 0.016 mM.

raw_value_unit_evidence: Table 1 Km 16 +/- 3.0 uM for varied androsterone at saturated NAD+.

row_label: D249A 3a-HSD/CR


enzyme_display_name: Aldo-keto reductase family 1 member C4

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

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

enzyme: Aldo-keto reductase family 1 member C4


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


assay_conditions_summary: pH 10.5; cofactor NAD+

column_label: Table 1 row 2-decalol lists kcat 2.2 +/- 0.2 s^-1.

raw_value_unit_evidence: kcat raw_value=2.2 raw_unit=s^-1

table_label: Table 1. Kinetic parameters and the free energy changes for the oxidoreduction of androsterone and the truncated analogs with NAD+ by 3a-HSD/CR.


substrate_name: Cyclohexanol

column_label: Table 1 row cyclohexanol lists kcat 2.5 +/- 0.2 s^-1.

raw_value_unit_evidence: kcat raw_value=2.5 raw_unit=s^-1

row_label: cyclohexanol

substrate: Cyclohexanol


substrate_name: androstenol

column_label: Table 1 row androstenol lists kcat 230 +/- 20 s^-1.

raw_value_unit_evidence: kcat raw_value=230 raw_unit=s^-1

row_label: androstenol

substrate: androstenol


source_databases_merged: brenda uniprot


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S114A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADH


proof_lines: wild type enzyme, in 0.1 M HEPES at pH 7.5

proof_lines: wild-type, pH 7.5, 25°C, steady-state kinetic study


proof_lines: mutant enzyme S114A, in 0.1 M HEPES at pH 7.5


organism: Thermoproteus tenax

substrate_name: beta-D-glucose

assay_conditions_summary: pH 7; cofactor NADP+

column_label: The extracted paper text states the Km values for glucose and xylose in the presence of NADP+ are 0.3 mM and 8 mM, respectively, matching the expected beta-D-glucose row.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM

row_label: beta-D-glucose

table_label: Kinetic parameters paragraph

substrate: beta-D-glucose


substrate_name: NADP+

column_label: The extracted paper text states that in the presence of glucose the enzyme had a Km value of 0.7 mM for NADP+, matching the expected row.

raw_value_unit_evidence: Km raw_value=0.7 raw_unit=mM

row_label: NADP+

substrate: NADP+


assay_conditions_summary: pH 7; cofactor NAD+


substrate_name: xylose

column_label: The extracted paper text states the Km values for glucose and xylose in the presence of NADP+ are 0.3 mM and 8 mM, respectively, matching the expected xylose row.

raw_value_unit_evidence: Km raw_value=8 raw_unit=mM

row_label: xylose

substrate: xylose


organism: Thermotoga maritima

assay_conditions_summary: pH 7.4; 353.15 K; cofactor NAD+


substrate_name: 2-deoxy-D-glucose 6-phosphate

substrate: 2-deoxy-D-glucose 6-phosphate


substrate_name: D-glucose 6-phosphate

proof_lines:
pH 7.4, 80°C, recombinant enzyme
pH 7.8, 85°C, recombinant enzyme

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 7.4; 353.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N86A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y155F to reconstruct the assayed variant sequence.


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

organism: Gluconobacter oxydans (strain 621H)

substrate_name: glucose 6-phosphate

proof_lines: kcat is 44.1 sec(-1). Can use NAD or NADP in vitro, but primarily functions in a NADP-dependent manner in vivo.

enzyme: Glucose-6-phosphate 1-dehydrogenase

substrate: glucose 6-phosphate


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: L-iditol 2-dehydrogenase

substrate_name: xylitol (at pH 10.0)

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

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

column_label: Table III: Steady-State Kinetic Parameters for Human Liver Sorbitol Dehydrogenase (Biochemistry 1988, volume 27, pages 1622-1628); printed column heads substrate | pH | kcat (s^-1) | Km (M). Table III, substrate row xylitol; column pH = 10.0; column kcat (s^-1) = 5.9; column Km (M) = 2.2 x 10^-4. Table III prints no kcat/Km column. captured primary segment: xylitol | pH 10.0 | kcat 5.9 s^-1 | Km 2.2 x 10^-4 M

normalized_value_unit_evidence: Km: printed Table III cell 2.2 x 10^-4 M under the column head 'Km (M)'; 1 M is 1000 mM, so 2.2 x 10^-4 x 1000 = 0.22 mM; the exported value is 0.22 mM. kcat: printed Table III cell 5.9 s^-1 under the column head 'kcat (s^-1)'; the printed unit is already the export unit, so no unit conversion applies; the exported value is 5.9 s^(-1). kcat/Km: Table III prints no kcat/Km column and the article prints no kcat/Km value for xylitol, so nothing is converted; the exported 26.81818181818182 s^(-1)*mM^(-1) is carried unchanged and typed as the quotient of this row's own two confirmed printed components: 5.9 / 0.22 = 26.81818181818182 s^-1 mM^-1.

raw_value_unit_evidence: Table III, substrate row xylitol: pH = 10.0; kcat = 5.9 s^-1; Km = 2.2 x 10^-4 M. Table III prints no kcat/Km column and the article prints no kcat/Km value for xylitol.

row_label: Table III, substrate row xylitol

enzyme: L-iditol 2-dehydrogenase

substrate: xylitol (at pH 10.0)


substrate_name: L-threitol (at pH 10.0)

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

column_label: Table III: Steady-State Kinetic Parameters for Human Liver Sorbitol Dehydrogenase (Biochemistry 1988, volume 27, pages 1622-1628); printed column heads substrate | pH | kcat (s^-1) | Km (M). Table III, substrate row L-threitol; column pH = 10.0; column kcat (s^-1) = 5.3; column Km (M) = 2.7 x 10^-3. Table III prints no kcat/Km column. captured primary segment: L-threitol | pH 10.0 | kcat 5.3 s^-1 | Km 2.7 x 10^-3 M

normalized_value_unit_evidence: Km: printed Table III cell 2.7 x 10^-3 M under the column head 'Km (M)'; 1 M is 1000 mM, so 2.7 x 10^-3 x 1000 = 2.7 mM; the exported value is 2.7 mM. kcat: printed Table III cell 5.3 s^-1 under the column head 'kcat (s^-1)'; the printed unit is already the export unit, so no unit conversion applies; the exported value is 5.3 s^(-1). kcat/Km: Table III prints no kcat/Km column and the article prints no kcat/Km value for L-threitol, so nothing is converted; the exported 1.9629629629629628 s^(-1)*mM^(-1) is carried unchanged and typed as the quotient of this row's own two confirmed printed components: 5.3 / 2.7 = 1.9629629629629628 s^-1 mM^-1.

raw_value_unit_evidence: Table III, substrate row L-threitol: pH = 10.0; kcat = 5.3 s^-1; Km = 2.7 x 10^-3 M. Table III prints no kcat/Km column and the article prints no kcat/Km value for L-threitol.

row_label: Table III, substrate row L-threitol

substrate: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

smiles: CC(C(C)O)O

assay_conditions_summary: pH 10; cofactor NAD+

column_label: The copied official ACS PDF extract identifies Table III row (2R,3R)-2,3-butanediol and its exact kcat and Km cells; the target efficiency is the transparent quotient of those same-row central values, following packet 006 precedent.

raw_value_unit_evidence: Table III row (2R,3R)-2,3-butanediol: kcat 4.2 s^-1; Km 9.5 mM; kcat/Km derived transparently from those same-row central values.

table_label: Table III: Steady-State Kinetic Parameters for Human Liver Sorbitol Dehydrogenase

substrate: (2R,3R)-2,3-butanediol (at pH 10.0)


organism: Bos taurus

substrate_name: NADH (at pH 7.4)

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol oxidation (at pH 8.0). kcat is 24 sec(-1) f

substrate: NADH (at pH 7.4)


substrate_name: 3-pyridinealdehyde adenine dinucleotide

assay_conditions_summary: cofactor NADH

substrate: 3-pyridinealdehyde adenine dinucleotide


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: Thionicotinamide adenine dinucleotide

substrate: Thionicotinamide adenine dinucleotide


substrate_name: 3-acetylpyridine adenine dinucleotide

substrate: 3-acetylpyridine adenine dinucleotide


organism: Macaca fuscata fuscata

column_label: Table 2; row 5a-Pregnane-3a,21-diol-20-one; jpDD4 (AKR1C4) Km column; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

normalized_value_unit_evidence: normalized required Km-only paper value: 0.6 uM = 0.0006 mM.

raw_value_unit_evidence: Table 2 row 5a-Pregnane-3a,21-diol-20-one, jpDD4 column: Km=0.6 uM.

row_label: jpDD4 / 5a-Pregnane-3a,21-diol-20-one

table_label: Table 2


column_label: Table 2; row 5a-Androstan-3a-ol-17-one; jpDD4 (AKR1C4) Km column; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

normalized_value_unit_evidence: normalized required Km-only paper value: 0.7 uM = 0.0007 mM.

raw_value_unit_evidence: Table 2 row 5a-Androstan-3a-ol-17-one, jpDD4 column: Km=0.7 uM.

row_label: jpDD4 / 5a-Androstan-3a-ol-17-one


organism: Homo sapiens

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


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_display_name: Glucose 1-dehydrogenase

organism: Priestia megaterium

substrate_name: NAD(+) (at pH 8.0 and 25 degrees Celsius)

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

column_label: PMCID PMC1151818 HTML Table 1; row Wild type; column Apparent Km (NAD+) (mM); raw value 0.17 mM; normalized value 0.17 mM.

normalized_value_unit_evidence: 0.17 mM is already normalized as 0.17 mM.

raw_value_unit_evidence: Table 1 reports Apparent Km (NAD+) = 0.17 mM for the wild-type enzyme.

row_label: Wild type glucose dehydrogenase / NAD+ apparent Km

table_label: PMC HTML Table 1 (PMID 15933031; PMCID PMC1151818)

enzyme: Glucose 1-dehydrogenase


substrate_name: D-glucose (at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 395 sec(-1) with D-glucose as substrate and NAD(+) cosubstrate (at pH 8.0 and 25 degrees Celsius).


assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl; cofactor NADP+

substrate: NAD(+) (at pH 8.0 and 25 degrees Celsius)


substrate: D-glucose (at pH 8.0 and 25 degrees Celsius)


substrate_name: NADP(+) (at pH 8.0 and 25 degrees Celsius)

column_label: PMCID PMC1151818 HTML Table 1; row Wild type; column Apparent Km (NADP+) (mM); raw value 0.033 mM; normalized value 0.033 mM.

normalized_value_unit_evidence: 0.033 mM is already normalized as 0.033 mM.

raw_value_unit_evidence: Table 1 reports Apparent Km (NADP+) = 0.033 mM for the wild-type enzyme.

row_label: Wild type glucose dehydrogenase / NADP+ apparent Km


organism: Taenia crassiceps

assay_conditions_summary: pH 7.8; cofactor NADP+

column_label: Springer PDF page 4 Table 2, Glucose 6-phosphate row, Turnover number (s^-1) column: 34.

raw_value_unit_evidence: kcat raw_value=34 raw_unit=s^-1

row_label: Glucose 6-phosphate


column_label: Springer abstract/prose reports Km 14+/-1.7 uM for glucose 6-phosphate.

normalized_value_unit_evidence: Km normalized_value=0.014 mM

raw_value_unit_evidence: Km raw_value=14+/-1.7 raw_unit=uM

row_label: glucose 6-phosphate

table_label: Abstract


substrate_name: NADP+

column_label: Springer PDF page 4 Table 2, NADP+ row, Turnover number (s^-1) column: 34.

substrate: NADP+


column_label: Springer abstract/prose reports Km 1.3+/-0.4 uM for NADP+.

normalized_value_unit_evidence: Km normalized_value=0.0013 mM

raw_value_unit_evidence: Km raw_value=1.3+/-0.4 raw_unit=uM


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


organism: Koliella antarctica

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


organism: Rattus norvegicus

substrate_name: Dehydrolithocholic acid

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: pH 7.4, 25°C, recombinant wild-type AKR1C17

substrate: Dehydrolithocholic acid


assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NAD+

column_label: Reduction-direction kinetic constants, decoded transcription, substrate row `5beta-pregnane-3,20-dione`: Km = 2.4 uM; kcat = 6.3 min^-1. The paper prints no kcat/Km value for this measurement.

normalized_value_unit_evidence: kcat: printed value 6.3 min^-1 -> 6.3 / 60 = 0.105 s^(-1); the catalog holds 0.105 s^(-1); the division by 60 is exact at the printed precision, with no rounding. Km: printed value 2.4 uM -> 2.4 / 1000 = 0.0024 mM; the catalog holds 0.0024 mM; the division by 1000 is exact, with no rounding. kcat/Km: the paper prints no kcat/Km value for the reduction direction; the catalog kcat_over_km 43.75 s^(-1)*mM^(-1) is the exact full-precision quotient of this measurement's own two values, 0.105 s^(-1) / 0.0024 mM, and is typed derived_same_measurement, not quoted.

raw_value_unit_evidence: Reduction-direction kinetic constants, decoded transcription, substrate row `5beta-pregnane-3,20-dione`: Km = 2.4 uM; kcat = 6.3 min^-1; no kcat/Km value is printed.

table_label: Results, 'Substrate specificity', journal page 125 (PDF page 4 of 8), reduction-direction kinetic constants stated in running prose


substrate_name: diacetyl

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

substrate: diacetyl


substrate_name: isatin

substrate: isatin


organism: Drosophila melanogaster

assay_conditions_summary: pH 8.2; cofactor NAD+


organism: Meyerozyma guilliermondii


assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADP+


row_label: Reduction-direction kinetic constants, decoded transcription, substrate row `5beta-pregnane-3,20-dione`


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


assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NADH


enzyme_display_name: Glucose 1-dehydrogenase 4

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: kcat is 420 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 462 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

enzyme: Glucose 1-dehydrogenase 4


enzyme_display_name: Glucose 1-dehydrogenase 1

proof_lines: kcat is 190 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 120 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

enzyme: Glucose 1-dehydrogenase 1


enzyme_display_name: Glucose 1-dehydrogenase 3

proof_lines: kcat is 430 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 802 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

enzyme: Glucose 1-dehydrogenase 3


enzyme_display_name: Glucose 1-dehydrogenase 2

proof_lines: kcat is 190 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 140 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

enzyme: Glucose 1-dehydrogenase 2


assay_conditions_summary: pH 8


substrate_name: NADP(+) (at pH 8.0)

substrate: NADP(+) (at pH 8.0)


assay_conditions_summary: pH 8; cofactor NADP+


assay_conditions_summary: pH 7.5; cofactor NADP+


proof_lines: mutant enzyme A117S/Q324H/M381I/V443I/S470I, pH 7.5, 30°C


proof_lines: mutant enzyme A117S/Q324H/V443I/S470I, pH 7.5, 30°C


organism: Pseudomonas sp. B-0831

substrate_name: cholate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K157A to reconstruct the assayed variant sequence.

substrate: cholate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S114A/Y153F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y153F with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S114A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


substrate_name: dehydrocholate

substrate: dehydrocholate


enzyme_display_name: mannitol-1-phosphate 5-dehydrogenase

organism: Acinetobacter baumannii

assay_conditions_summary: pH 7.5; cofactor NADPH

enzyme: mannitol-1-phosphate 5-dehydrogenase


substrate_name: NADH

assay_conditions_summary: pH 7.5; cofactor NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R609A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D16A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


substrate_name: androsterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S114A/Y155F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant S114A/Y155F

substrate: androsterone


sequence_variant_note: Mutation signature Y155F/K159A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F/K159A


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

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant S114A


proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant Y155F


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K159A to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant His-tagged mutant K159A


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

proof_lines: pH 9.0, 25°C, recombinant His-tagged wild-type

proof_lines: pH 10.4, 25°C, recombinant wild-type enzyme


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D249S with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10.2; buffer NAD+ and explicit CAPS; cofactor NAD+

proof_lines: mutant enzyme D249S, in 0.1 M CAPS buffer, at pH 10.2, at 25°C

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature D249A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D249A, in 0.1 M CAPS buffer, at pH 10.2, at 25°C


assay_conditions_summary: pH 10.2; buffer explicit CAPS; cofactor NAD+


assay_conditions_summary: pH 10.2; buffer explicit 0.1 M CAPS; cofactor NAD+


substrate_name: 2-deoxy-D-glucose 6-phosphate

substrate: 2-deoxy-D-glucose 6-phosphate


proof_lines:
pH 7.4, 80°C, recombinant enzyme
pH 7.8, 85°C, recombinant enzyme


assay_conditions_summary: pH 7.4; cofactor NADP+


substrate_name: glucose (at pH 6.0 and 37 degrees Celsius)

assay_conditions_summary: pH 6


substrate: glucose (at pH 6.0 and 37 degrees Celsius)


enzyme_display_name: UniProt P39485

substrate_name: D-glucose

source_db: skid

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

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

source_databases_merged: skid uniprot

enzyme: UniProt P39485

substrate: D-glucose

source: skid


enzyme_display_name: Name not preserved

organism: Trypanosoma cruzi

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: Name not preserved


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


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


proof_lines: wild type enzyme, in 0.1 M HEPES at pH 7.5

proof_lines: wild-type, pH 7.5, 25°C, steady-state kinetic study


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature S114A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S114A, in 0.1 M HEPES at pH 7.5


organism: Aspergillus aculeatus

column_label: Table 2 row Km G6P, column Values obtained; adjacent prose immediately below Table 2 for kcat and specificity constants.

raw_value_unit_evidence: Table 2 reports Km G6P 75 +/- 6 uM; adjacent prose reports turnover number kcat 83 sec^-1 and kcat/KmG6P 1.1 x 10^6 M^-1 s^-1.

row_label: Table 2 row Km G6P; adjacent prose for kcat and kcat/KmG6P

table_label: Table 2. Kinetic parameters of A. aculeatus glucose-6-phosphate dehydrogenase


column_label: Table 2 row Km NADP+, column Values obtained.

raw_value_unit_evidence: Table 2 reports Km NADP+ 6 +/- 1 uM.

row_label: Table 2 row Km NADP+


substrate_name: NADP(+) (at pH 8.0 and 25 degrees Celsius)

proof_lines: kcat is 395 sec(-1) with D-glucose as substrate and NAD(+) cosubstrate (at pH 8.0 and 25 degrees Celsius).


substrate_name: NAD(+) (at pH 8.0 and 25 degrees Celsius)


substrate_name: NADP+


organism: Digitalis lanata

column_label: Table 1, row NAD + Pregnenolone, column Km pQ3betaHSD (uM): 90 +/- 9; product Isoprogesterone + Progesterone.

row_label: NAD + Pregnenolone


assay_conditions_summary: pH 7.8; cofactor NADH

column_label: Table 1, row NADH + 5alpha-Pregnane-3,20-dione, column Km pQ3betaHSD (uM): 106 +/- 1; product 5alpha-Pregnan-3beta-ol-20-one.

row_label: NADH + 5alpha-Pregnane-3,20-dione


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)+]

organism: Thermoplasma acidophilum

assay_conditions_summary: pH 7; 328.15 K; cofactor NADP+

enzyme: glucose 1-dehydrogenase [NAD(P)+]


substrate_name: beta-D-glucose

assay_conditions_summary: pH 7

proof_lines: The KM value for NAD(+) is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.

substrate: beta-D-glucose


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: glucose

substrate: glucose


substrate_name: NADP(+)

substrate: NADP(+)


proof_lines:
nephridic enzyme
hepatic enzyme
0.0025 mM glucose 6-phosphate

substrate: NADP+


substrate_name: D-glucose 6-phosphate

proof_lines:
nephridic enzyme
hepatic enzyme
22°C, liver extralesional parenchyma

substrate: D-glucose 6-phosphate


organism: Eggerthella lenta

proof_lines: also in this range: 3alpha,7alpha-dihydroxy-5beta-cholanoyl glycine

proof_lines: also in this range: 3alpha,12alpha-dihydroxy-5beta-cholanoyl glycine


substrate_name: cholic acid

assay_conditions_summary: cofactor NAD+

substrate: cholic acid


organism: Comamonas testosteroni


substrate_name: 3-pyridinealdehyde adenine dinucleotide

substrate: 3-pyridinealdehyde adenine dinucleotide


organism: Macaca fuscata fuscata

substrate_name: (s)-tetralol

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

substrate: (s)-tetralol


organism: Homo sapiens

substrate_name: xylitol (at pH 10.0)

assay_conditions_summary: pH 10; cofactor NAD+

column_label: The copied official ACS PDF extract identifies Table III row xylitol and its exact kcat and Km cells; the target efficiency is the transparent quotient of those same-row central values, following packet 006 precedent.

raw_value_unit_evidence: Table III row xylitol: kcat 5.9 s^-1; Km 0.22 mM; kcat/Km derived transparently from those same-row central values.

row_label: xylitol

substrate: xylitol (at pH 10.0)


substrate_name: L-threitol (at pH 10.0)

column_label: The copied official ACS PDF extract identifies Table III row L-threitol and its exact kcat and Km cells; the target efficiency is the transparent quotient of those same-row central values, following packet 006 precedent.

raw_value_unit_evidence: Table III row L-threitol: kcat 5.3 s^-1; Km 2.7 mM; kcat/Km derived transparently from those same-row central values.

row_label: L-threitol

substrate: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

column_label: Table III: Steady-State Kinetic Parameters for Human Liver Sorbitol Dehydrogenase (Biochemistry 1988, volume 27, pages 1622-1628); printed column heads substrate | pH | kcat (s^-1) | Km (M). Table III, substrate row (2R,3R)-2,3-butanediol; column pH = 10.0; column kcat (s^-1) = 4.2; column Km (M) = 9.5 x 10^-3. Table III prints no kcat/Km column. captured primary segment: (2R,3R)-2,3-butanediol | pH 10.0 | kcat 4.2 s^-1 | Km 9.5 x 10^-3 M

normalized_value_unit_evidence: Km: printed Table III cell 9.5 x 10^-3 M under the column head 'Km (M)'; 1 M is 1000 mM, so 9.5 x 10^-3 x 1000 = 9.5 mM; the exported value is 9.5 mM. kcat: printed Table III cell 4.2 s^-1 under the column head 'kcat (s^-1)'; the printed unit is already the export unit, so no unit conversion applies; the exported value is 4.2 s^(-1). kcat/Km: Table III prints no kcat/Km column and the article prints no kcat/Km value for (2R,3R)-2,3-butanediol, so nothing is converted; the exported 0.4421052631578948 s^(-1)*mM^(-1) is carried unchanged and typed as the quotient of this row's own two confirmed printed components: 4.2 / 9.5 = 0.4421052631578948 s^-1 mM^-1.

raw_value_unit_evidence: Table III, substrate row (2R,3R)-2,3-butanediol: pH = 10.0; kcat = 4.2 s^-1; Km = 9.5 x 10^-3 M. Table III prints no kcat/Km column and the article prints no kcat/Km value for (2R,3R)-2,3-butanediol.

substrate: (2R,3R)-2,3-butanediol (at pH 10.0)


organism: Bos taurus

substrate_name: NADH (at pH 7.4)

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol oxidation (at pH 8.0). kcat is 24 sec(-1) f

substrate: NADH (at pH 7.4)


substrate_name: D-fructose (at pH 7.4)

substrate: D-fructose (at pH 7.4)


enzyme_display_name: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)

organism: Arabidopsis thaliana

substrate_name: pyruvate

proof_lines:
pH 7.0, 30°C, isozyme NADP-ME1
pH 7.0, 30°C, isozyme NADP-ME2
pH 7.0

substrate: pyruvate


substrate_name: (S)-malate

proof_lines:
pH 7.5, 30°C, isozyme NADP-ME1
pH 7.5, 30°C, isozyme NADP-ME4
pH 7.5

enzyme: malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)

substrate: (S)-malate


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


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


enzyme_display_name: UniProt P93819

substrate_name: oxaloacetate

sequence_source: multiple

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: kcat is 608 sec(-1) with oxaloacetate as substrate (PubMed:29194485). kcat is 677 sec(-1) with NADH as substrate (PubMed:29194485).

enzyme: UniProt P93819

substrate: oxaloacetate


substrate_name: NADH

substrate: NADH


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

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


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

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


enzyme_display_name: L-xylulose reductase

organism: Trichoderma reesei

substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: pH 7.0, 30°C, recombinant enzyme, with L-xylulose

enzyme: L-xylulose reductase

substrate: NADPH


assay_conditions_summary: pH 7.1; cofactor NADH

proof_lines: kcat is 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat i


organism: Rattus norvegicus

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 8 sec(-1) for sorbitol oxidation and 190 sec(-1) for D-fructose reduction.


organism: Ascaris suum

substrate_name: L-malate

proof_lines:
native and recombinant enzyme
native enzyme
recombinant enzyme

substrate: L-malate


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines:
pH 7.5, NADP-ME1
pH 7.5, NADP-ME4
pH 7.5, NADP-ME3

substrate: NADP+


enzyme_display_name: malate dehydrogenase (decarboxylating)

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: pH 6.4, temperature not specified in the publication, NAD-ME1

proof_lines: pH 6.5, temperature not specified in the publication, NAD-MEH

enzyme: malate dehydrogenase (decarboxylating)


substrate_name: NAD+

assay_conditions_summary: pH 6.4; cofactor NAD+

proof_lines: pH 6.6, temperature not specified in the publication, NAD-ME2

substrate: NAD+


organism: Halobacterium salinarum

substrate_name: beta-D-glucose

proof_lines:
reduction, reverse reaction
oxidation, forward reaction

substrate: beta-D-glucose


enzyme_display_name: UniProt Q8GQE7

organism: Burkholderia cepacia

enzyme: UniProt Q8GQE7


substrate_name: NADP(+)

proof_lines: The KM value for NAD(+) is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.

substrate: NADP(+)


organism: Taenia crassiceps

substrate_name: D-glucose 6-phosphate

assay_conditions_summary: pH 7.8; cofactor NADP+

substrate: D-glucose 6-phosphate


enzyme_display_name: UniProt P11413

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

enzyme: UniProt P11413


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


substrate_name: NADP

substrate: NADP


substrate_name: xylitol (at pH 10.0)

column_label: Table III; row label: xylitol; pH column: 10.0; metric: Km; raw value: 2.2 x 10^-4; raw unit: M; normalized value: 0.22; normalized unit: mM.

normalized_value_unit_evidence: Km 0.22 mM

raw_value_unit_evidence: Table III Km column reports 2.2 x 10^-4 M for xylitol at pH 10.0.

substrate: xylitol (at pH 10.0)


substrate_name: L-threitol (at pH 10.0)

column_label: Table III; row label: L-threitol; pH column: 10.0; metric: Km; raw value: 2.7 x 10^-3; raw unit: M; normalized value: 2.7; normalized unit: mM.

normalized_value_unit_evidence: Km 2.7 mM

raw_value_unit_evidence: Table III Km column reports 2.7 x 10^-3 M for L-threitol at pH 10.0.

substrate: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

column_label: Table III; row label: (2R,3R)-2,3-butanediol; pH column: 10.0; metric: Km; raw value: 9.5 x 10^-3; raw unit: M; normalized value: 9.5; normalized unit: mM.

normalized_value_unit_evidence: Km 9.5 mM

raw_value_unit_evidence: Table III Km column reports 9.5 x 10^-3 M for (2R,3R)-2,3-butanediol at pH 10.0.

substrate: (2R,3R)-2,3-butanediol (at pH 10.0)


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

organism: Gluconobacter oxydans (strain 621H)

substrate_name: NAD(+)

proof_lines: kcat is 44.1 sec(-1). Can use NAD or NADP in vitro, but primarily functions in a NADP-dependent manner in vivo.

enzyme: Glucose-6-phosphate 1-dehydrogenase

substrate: NAD(+)


substrate_name: androsterone

substrate: androsterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R1C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: also in this range: 5beta-dihydrotestosterone, rat epididymis


substrate_name: glycolithocholic acid

proof_lines: also in this range: 3alpha-hydroxy-5alpha-pregnan-20-one

substrate: glycolithocholic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K159A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


enzyme_display_name: Aldo-keto reductase family 1 member C2

enzyme: Aldo-keto reductase family 1 member C2


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


enzyme_display_name: 3-beta-hydroxysteroid dehydrogenase

organism: Mycolicibacterium neoaurum

substrate_name: testosterone

enzyme: 3-beta-hydroxysteroid dehydrogenase

substrate: testosterone


enzyme_display_name: L-iditol 2-dehydrogenase

substrate_name: D-ribulose (at pH 7.4)

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

proof_lines: kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol oxidation (at pH 8.0). kcat is 24 sec(-1) f

enzyme: L-iditol 2-dehydrogenase

substrate: D-ribulose (at pH 7.4)


enzyme_display_name: 3alpha-hydroxysteroid dehydrogenase

organism: Eggerthella lenta (strain ATCC 25559 / DSM 2243 / CCUG 17323 / JCM 9979 / KCTC 3265 / NCTC 11813 / VPI 0255 / 1899 B)

substrate_name: deoxycholate

column_label: PMC Table 1 row/column for Elen_0690, substrate DCA, cofactor NAD+ reports Km 1280 +/- 88 uM and kcat 291 +/- 7 min^-1.

raw_value_unit_evidence: Km raw_value=1280 +/- 88 uM raw_unit=uM

row_label: Elen_0690 / DCA / NAD+

table_label: PMC Table 1 Kinetic parameters for 3alpha- and 3beta-HSDHs

enzyme: 3alpha-hydroxysteroid dehydrogenase

substrate: deoxycholate


enzyme_display_name: L-gulonate 3-dehydrogenase

organism: Drosophila melanogaster

substrate_name: L-gulonate

assay_conditions_summary: pH 8.2; cofactor NAD+

proof_lines:
cofactor NAD+
cofactor NAD+, pH 8.2

enzyme: L-gulonate 3-dehydrogenase

substrate: L-gulonate


organism: Leuconostoc mesenteroides

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K343R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADP+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K343R; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 8.0 uM; kcat cell = 24 200 min^-1; kcat/Km NADP+ cell = 2030. captured primary segment: NADP+ | K343R G6PD, the site-directed K343R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 8.0 uM | Table 3 kcat 24 200 min^-1 | Table 3 kcat/Km NADP+ printed cell 2030 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K343R: Km NADP+ = 8.0 uM; kcat = 24 200 min^-1; kcat/Km NADP+ = 2030 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K343R

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature T14S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row T14S; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 22 700 min^-1; kcat/Km NADP+ cell = 1620. captured primary segment: NADP+ | T14S G6PD, the site-directed T14S single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 22 700 min^-1 | Table 3 kcat/Km NADP+ printed cell 1620 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row T14S: Km NADP+ = 14 uM; kcat = 22 700 min^-1; kcat/Km NADP+ = 1620 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row T14S


substrate_name: glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: glucose 6-phosphate


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.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature D374Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row D374Q; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 571 uM; kcat cell = 12 500 min^-1; kcat/Km NAD+ cell = 22. captured primary segment: NAD+ | D374Q G6PD, the site-directed D374Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 571 uM | Table 4 kcat 12 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 22 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row D374Q: Km NAD+ = 571 uM; kcat = 12 500 min^-1; kcat/Km NAD+ = 22 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row D374Q

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K182Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: K182Q mutational context in Leuconostoc mesenteroides G6PDH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K182R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row K182R; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 379 uM; kcat cell = 64 100 min^-1; kcat/Km NAD+ cell = 169. captured primary segment: NAD+ | K182R G6PD, the site-directed K182R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 379 uM | Table 4 kcat 64 100 min^-1 | Table 4 kcat/Km NAD+ printed cell 169 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K182R: Km NAD+ = 379 uM; kcat = 64 100 min^-1; kcat/Km NAD+ = 169 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K182R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K343Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row K343Q; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 503 uM; kcat cell = 51 000 min^-1; kcat/Km NAD+ cell = 101. captured primary segment: NAD+ | K343Q G6PD, the site-directed K343Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 503 uM | Table 4 kcat 51 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 101 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K343Q: Km NAD+ = 503 uM; kcat = 51 000 min^-1; kcat/Km NAD+ = 101 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K343Q


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row K343R; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 338 uM; kcat cell = 45 000 min^-1; kcat/Km NAD+ cell = 133. captured primary segment: NAD+ | K343R G6PD, the site-directed K343R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 338 uM | Table 4 kcat 45 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 133 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row K343R: Km NAD+ = 338 uM; kcat = 45 000 min^-1; kcat/Km NAD+ = 133 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row K343R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row P149G; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 1760 uM; kcat cell = 1 050 min^-1; kcat/Km NAD+ cell = 0.60. captured primary segment: NAD+ | P149G G6PD, the site-directed P149G single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 1760 uM | Table 4 kcat 1 050 min^-1 | Table 4 kcat/Km NAD+ printed cell 0.60 under the column head kcat/Km NAD+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 1760 uM; 1 uM = 1/1000 mM, so 1760 / 1000 = 1.76 mM; the export stores 1.76 mM. kcat: printed cell 1 050 min^-1; the printed turnover column is per MINUTE, so 1050 / 60 = 17.5 s^(-1); the export stores 17.5 s^(-1). kcat/Km: Printed kcat/Km NAD+ cell 0.60 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 0.60 x 16.666666666666668 = 10.0 s^(-1)*mM^(-1). The export stores 9.943181818181818 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row P149G: Km NAD+ = 1760 uM; kcat = 1 050 min^-1; kcat/Km NAD+ = 0.60 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row P149G


sequence_variant_note: Mutation signature P149V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Q47A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Q47A; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 234 uM; kcat cell = 34 600 min^-1; kcat/Km NAD+ cell = 148. captured primary segment: NAD+ | Q47A G6PD, the site-directed Q47A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 234 uM | Table 4 kcat 34 600 min^-1 | Table 4 kcat/Km NAD+ printed cell 148 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47A: Km NAD+ = 234 uM; kcat = 34 600 min^-1; kcat/Km NAD+ = 148 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Q47A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Q47E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Q47E; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 310 uM; kcat cell = 48 500 min^-1; kcat/Km NAD+ cell = 156. captured primary segment: NAD+ | Q47E G6PD, the site-directed Q47E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 310 uM | Table 4 kcat 48 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 156 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Q47E: Km NAD+ = 310 uM; kcat = 48 500 min^-1; kcat/Km NAD+ = 156 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Q47E


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature R46E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row R46E; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 986 uM; kcat cell = 39 500 min^-1; kcat/Km NAD+ cell = 40. captured primary segment: NAD+ | R46E G6PD, the site-directed R46E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 986 uM | Table 4 kcat 39 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 40 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row R46E: Km NAD+ = 986 uM; kcat = 39 500 min^-1; kcat/Km NAD+ = 40 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row R46E


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature T14A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row T14A; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 2340 uM; kcat cell = 48 500 min^-1; kcat/Km NAD+ cell = 21. captured primary segment: NAD+ | T14A G6PD, the site-directed T14A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 2340 uM | Table 4 kcat 48 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 21 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row T14A: Km NAD+ = 2340 uM; kcat = 48 500 min^-1; kcat/Km NAD+ = 21 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row T14A


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row T14S; Table 4, columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 199 uM; kcat cell = 35 000 min^-1; kcat/Km NAD+ cell = 176. captured primary segment: NAD+ | T14S G6PD, the site-directed T14S single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 199 uM | Table 4 kcat 35 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 176 under the column head kcat/Km NAD+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NAD+ cell 199 uM; 1 uM = 1/1000 mM, so 199 / 1000 = 0.199 mM; the export stores 0.199 mM, the same value. kcat: printed cell 35 000 min^-1; the printed turnover column is per MINUTE, so 35 000 / 60 = 583.3333333333334 s^(-1); the export stores 0.583 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NAD+ cell 176 under the column head kcat/Km NAD+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 176 x 16.666666666666668 = 2933.3333333333335 s^(-1)*mM^(-1). The export stores 2933.3333333333335 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row T14S: Km NAD+ = 199 uM; kcat = 35 000 min^-1; kcat/Km NAD+ = 176 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row T14S


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Y179F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Y179F; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 184 uM; kcat cell = 28 500 min^-1; kcat/Km NAD+ cell = 155. captured primary segment: NAD+ | Y179F G6PD, the site-directed Y179F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 184 uM | Table 4 kcat 28 500 min^-1 | Table 4 kcat/Km NAD+ printed cell 155 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Y179F: Km NAD+ = 184 uM; kcat = 28 500 min^-1; kcat/Km NAD+ = 155 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Y179F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature Y415F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 4, enzyme row Y415F; columns Km NAD+ (uM), kcat (min^-1) and kcat/Km NAD+ (min^-1 uM^-1); Km NAD+ cell = 116 uM; kcat cell = 19 000 min^-1; kcat/Km NAD+ cell = 164. captured primary segment: NAD+ | Y415F G6PD, the site-directed Y415F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 4 Km NAD+ 116 uM | Table 4 kcat 19 000 min^-1 | Table 4 kcat/Km NAD+ printed cell 164 under the column head kcat/Km NAD+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 4, enzyme row Y415F: Km NAD+ = 116 uM; kcat = 19 000 min^-1; kcat/Km NAD+ = 164 under the printed column head kcat/Km NAD+ (min^-1 uM^-1).

row_label: Table 4, enzyme row Y415F


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row D374Q; columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 13 uM; kcat cell = 4 510 min^-1; kcat/Km NADP+ cell = 346. captured primary segment: NADP+ | D374Q G6PD, the site-directed D374Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 13 uM | Table 3 kcat 4 510 min^-1 | Table 3 kcat/Km NADP+ printed cell 346 under the column head kcat/Km NADP+ (min^-1 uM^-1)

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row D374Q: Km NADP+ = 13 uM; kcat = 4 510 min^-1; kcat/Km NADP+ = 346 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row D374Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P11411 and applied mutation signature K182Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K182Q; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 6.5 uM; kcat cell = 18 500 min^-1; kcat/Km NADP+ cell = 2800. captured primary segment: NADP+ | K182Q G6PD, the site-directed K182Q single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 6.5 uM | Table 3 kcat 18 500 min^-1 | Table 3 kcat/Km NADP+ printed cell 2800 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 6.5 uM; 1 uM = 1/1000 mM, so 6.5 / 1000 = 0.0065 mM; the export stores 0.0065 mM, the same value. kcat: printed cell 18 500 min^-1; the printed turnover column is per MINUTE, so 18 500 / 60 = 308.3333333333333 s^(-1); the export stores 0.3 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 2800 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 2800 x 16.666666666666668 = 46666.66666666667 s^(-1)*mM^(-1). The export stores 46666.666666666664 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K182Q: Km NADP+ = 6.5 uM; kcat = 18 500 min^-1; kcat/Km NADP+ = 2800 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K182Q


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row K182R; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 15 uM; kcat cell = 35 100 min^-1; kcat/Km NADP+ cell = 2340. captured primary segment: NADP+ | K182R G6PD, the site-directed K182R single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 15 uM | Table 3 kcat 35 100 min^-1 | Table 3 kcat/Km NADP+ printed cell 2340 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 15 uM; 1 uM = 1/1000 mM, so 15 / 1000 = 0.015 mM; the export stores 0.015 mM, the same value. kcat: printed cell 35 100 min^-1; the printed turnover column is per MINUTE, so 35 100 / 60 = 585.0 s^(-1); the export stores 0.583 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 2340 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 2340 x 16.666666666666668 = 39000.0 s^(-1)*mM^(-1). The export stores 39000.0 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row K182R: Km NADP+ = 15 uM; kcat = 35 100 min^-1; kcat/Km NADP+ = 2340 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row K182R


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P11411 and applied mutation signature P149G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row label P149G; checked columns: kcat (min^-1), Km NADP+ (uM), kcat/Km NADP+ (min^-1 uM^-1); assay: NADP reaction; varied G6P and NADP+; pH/temperature as in PMID 11106479 primary kinetic table

raw_value_unit_evidence: Table 3 row P149G: kcat 512 min^-1; Km NADP+ 24 ± 1.4 uM; kcat/Km NADP+ 21 min^-1 uM^-1

table_label: Table 3


sequence_variant_note: Resolved canonical sequence from uniprotkb:P11411 and applied mutation signature P149V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row label P149V; checked columns: kcat (min^-1), Km NADP+ (uM), kcat/Km NADP+ (min^-1 uM^-1); assay: NADP reaction; varied G6P and NADP+; pH/temperature as in PMID 11106479 primary kinetic table

raw_value_unit_evidence: Table 3 row P149V: kcat 36 min^-1; Km NADP+ 18 ± 3.0 uM; kcat/Km NADP+ 2.0 min^-1 uM^-1


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Q47A (printed with footnote marker e: apparent kinetic values); Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 7.5 uM; kcat cell = 14 100 min^-1; kcat/Km NADP+ cell = 1880. captured primary segment: NADP+ | Q47A G6PD, the site-directed Q47A single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 7.5 uM | Table 3 kcat 14 100 min^-1 | Table 3 kcat/Km NADP+ printed cell 1880 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 7.5 uM; 1 uM = 1/1000 mM, so 7.5 / 1000 = 0.0075 mM; the export stores 0.0075 mM, the same value. kcat: printed cell 14 100 min^-1; the printed turnover column is per MINUTE, so 14 100 / 60 = 235.0 s^(-1); the export stores 0.233 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 1880 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 1880 x 16.666666666666668 = 31333.333333333336 s^(-1)*mM^(-1). The export stores 31333.333333333332 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Q47A (printed with footnote marker e: apparent kinetic values): Km NADP+ = 7.5 uM; kcat = 14 100 min^-1; kcat/Km NADP+ = 1880 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Q47E; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 84 uM; kcat cell = 33 100 min^-1; kcat/Km NADP+ cell = 394. captured primary segment: NADP+ | Q47E G6PD, the site-directed Q47E single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 84 uM | Table 3 kcat 33 100 min^-1 | Table 3 kcat/Km NADP+ printed cell 394 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 84 uM; 1 uM = 1/1000 mM, so 84 / 1000 = 0.084 mM; the export stores 0.084 mM, the same value. kcat: printed cell 33 100 min^-1; the printed turnover column is per MINUTE, so 33 100 / 60 = 551.6666666666666 s^(-1); the export stores 0.55 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 394 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 394 x 16.666666666666668 = 6566.666666666667 s^(-1)*mM^(-1). The export stores 6566.666666666667 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Q47E: Km NADP+ = 84 uM; kcat = 33 100 min^-1; kcat/Km NADP+ = 394 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Q47E


sequence_variant_note: Resolved canonical sequence from uniprotkb:P11411 and applied mutation signature R46E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3; row label R46Ee; checked columns: kcat (min^-1), Km NADP+ (uM), kcat/Km NADP+ (min^-1 uM^-1); assay: NADP reaction; varied G6P and NADP+; pH/temperature as in PMID 11106479 primary kinetic table

raw_value_unit_evidence: Table 3 row R46Ee: kcat 38 000 min^-1; Km NADP+ 21 000 ± 1 300 uM; kcat/Km NADP+ 1.8 min^-1 uM^-1


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


column_label: Table 3: Kinetic Constants for Mutant G6PDs, NADP Reaction, printed column heads enzyme | Km G6P (uM) | Km NADP+ (uM) | Ki NADP+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1 uM^-1) | kcat/Km NADP+ (min^-1 uM^-1); Table 4: Kinetic Constants for Mutant G6PDs, NAD Reaction, printed column heads enzyme | Km G6P (uM) | Km NAD+ (uM) | kcat (min^-1) | kcat/Km G6P (min^-1) | kcat/Km NAD+ (min^-1 uM^-1). Journal page 15016 (PDF page 5). Table 3, enzyme row Y179F; Table 3, columns Km NADP+ (uM), kcat (min^-1) and kcat/Km NADP+ (min^-1 uM^-1); Km NADP+ cell = 14 uM; kcat cell = 15 800 min^-1; kcat/Km NADP+ cell = 1130. captured primary segment: NADP+ | Y179F G6PD, the site-directed Y179F single-substitution mutant of recombinant Leuconostoc mesenteroides glucose 6-phosphate dehydrogenase expressed in Escherichia coli SU294 | Table 3 Km NADP+ 14 uM | Table 3 kcat 15 800 min^-1 | Table 3 kcat/Km NADP+ printed cell 1130 under the column head kcat/Km NADP+ (min^-1 uM^-1)

normalized_value_unit_evidence: Km: printed Km NADP+ cell 14 uM; 1 uM = 1/1000 mM, so 14 / 1000 = 0.014 mM; the export stores 0.014 mM, the same value. kcat: printed cell 15 800 min^-1; the printed turnover column is per MINUTE, so 15 800 / 60 = 263.3333333333333 s^(-1); the export stores 0.25 s^(-1), which is the same printed number with its thousands group dropped. kcat/Km: Printed kcat/Km NADP+ cell 1130 under the column head kcat/Km NADP+ (min^-1 uM^-1); 1 min^-1 uM^-1 = (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 1130 x 16.666666666666668 = 18833.333333333336 s^(-1)*mM^(-1). The export stores 18833.333333333332 s^(-1)*mM^(-1), the same value.

raw_value_unit_evidence: Journal page 15016, Table 3, enzyme row Y179F: Km NADP+ = 14 uM; kcat = 15 800 min^-1; kcat/Km NADP+ = 1130 under the printed column head kcat/Km NADP+ (min^-1 uM^-1).

row_label: Table 3, enzyme row Y179F


organism: Mesocricetus auratus

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

assay_conditions_summary: pH 7.4; 298.15 K; buffer pH 7; cofactor NAD+

column_label: Table III, row '17beta-Estradiol', AKR1C35 columns Km, kcat, kcat/Km. Authenticated official OUP full article preserves the Journal of Biochemistry Tables I-III; the complete article PDF rendered in Chrome. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 2.8 min^-1; kcat/Km 7.0 min^-1 uM^-1; Km 0.4 uM

row_label: 17beta-Estradiol / AKR1C35

table_label: Table III


column_label: Table II, row '1-Acenaphthenol', AKR1C34 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.3 min^-1; kcat/Km 0.057 min^-1 uM^-1; Km 23 uM

row_label: 1-Acenaphthenol / AKR1C34

table_label: Table II


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: PMID 26002966 / DOI 10.1093/jb/mvv057, Table II, row 2-Cyclohexen-1-ol / AKR1C34, columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table II 2-Cyclohexen-1-ol / AKR1C34: Km 26 uM; kcat 2.4 min^-1; kcat/Km 0.093 min^-1 uM^-1.

row_label: 2-Cyclohexen-1-ol / AKR1C34


column_label: Table III, row '3beta-Hydroxyprogesterone', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 3.4 min^-1; kcat/Km 3.8 min^-1 uM^-1; Km 0.9 uM

row_label: 3beta-Hydroxyprogesterone / AKR1C35


column_label: Table III, row '4-Androstene-3alpha,17beta-diol', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 2.6 min^-1; kcat/Km 0.33 min^-1 uM^-1; Km 8.1 uM


column_label: Table III, row '5alpha-Androstan-3beta-ol-17-one', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.6 min^-1; kcat/Km 0.64 min^-1 uM^-1; Km 2.5 uM


column_label: Table III, row '5alpha-DHT', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.3 min^-1; kcat/Km 0.17 min^-1 uM^-1; Km 7.6 uM

row_label: 5alpha-DHT / AKR1C35


column_label: Table III, row '5a-Pregnan-3b-ol-20-one', AKR1C35 column group, columns Km, kcat and kcat/Km. The AKR1C34 column group prints na for this substrate, so the AKR1C35 cells are the only kinetic constants the paper reports for it. The Table III footnote fixes the column units as Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 with 1.0 mM NAD+; normalizing the three printed cells gives Km 0.0039 mM, kcat 0.013 s^-1 and kcat/Km 3.333333333333333333333333333333333333333 s^-1 mM^-1, which decimal-match the exported row. Identity anchor: Table I assigns the coenzyme constants Km 2,400 uM NADP+ and 23 uM NAD+ to AKR1C35, and the exported A0A097ZMZ1 rows for NADP+ and NAD+ carry exactly those cells, so A0A097ZMZ1 is the AKR1C35 protein of this paper.

raw_value_unit_evidence: Table III row 5a-Pregnan-3b-ol-20-one, AKR1C35 column group: Km 3.9 uM; kcat 0.78 min^-1; kcat/Km 0.20 min^-1 uM^-1.

row_label: 5a-Pregnan-3b-ol-20-one | AKR1C35

table_label: Table III. Substrate specificity for hydroxysteroids


column_label: Table III, row '5-Androstene-3beta,17beta-diol', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.9 min^-1; kcat/Km 0.58 min^-1 uM^-1; Km 3.3 uM


column_label: Table III, row '5beta-Androstan-3beta-ol-17-one', AKR1C35 columns Km, kcat, kcat/Km. LookChem positioned full-text mirror preserves the Journal of Biochemistry article table text; OUP publisher HTML/PDF routes were Cloudflare/403 blocked. Table units are interpreted as Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1 for normalized CatLog mM / s^-1 / s^-1 mM^-1 values.

raw_value_unit_evidence: kcat 1.3 min^-1; kcat/Km 0.028 min^-1 uM^-1; Km 46 uM


substrate_name: dehydroepiandrosterone

column_label: Table III, row 'Dehydroepiandrosterone', AKR1C35 column group, columns Km, kcat and kcat/Km. Km 4.3 uM normalizes to 0.0043 mM and equals the exported km; kcat 0.60 min^-1 normalizes to 0.01 s^-1 and equals the exported kcat; the exported kcat_over_km 2.3255813953488373 s^-1 mM^-1 is the exact quotient of those same two printed cells. The row also prints its own kcat/Km cell 0.14 min^-1 uM^-1, which is that same quantity at the two-decimal precision the table prints, so it does not contradict the exported ratio. Captured paper table segment: Dehydroepiandrosterone                     4.3       0.60           0.14                             na

normalized_value_unit_evidence: Km 0.0043 mM; kcat 0.01 s^-1; kcat/Km 2.3255813953488373 s^-1 mM^-1 (derived quotient of this row's own printed cells: 0.01 s^-1 / 0.0043 mM).

raw_value_unit_evidence: Table III row Dehydroepiandrosterone, AKR1C35 column group: Km 4.3 uM; kcat 0.60 min^-1; kcat/Km 0.14 min^-1 uM^-1.

row_label: Dehydroepiandrosterone | AKR1C35

substrate: dehydroepiandrosterone


substrate_name: farnesol

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

column_label: Table II, row 'Farnesol', AKR1C34 column group, columns Km, kcat and kcat/Km. All three cells are read from that one printed row: Km 1.2 uM = 0.0012 mM, kcat 1.1 min^-1 = 0.018333333333333333 s^-1, and the row's own printed kcat/Km cell 0.85 min^-1 uM^-1 = 14.166666666666666 s^-1 mM^-1. The exported km 0.0012 mM matches the printed Km cell; the exported kcat 0.018 s^-1 is that printed kcat cell rounded, and the exported kcat_over_km 15.0 s^-1 mM^-1 is the quotient of the exported rounded cells rather than the paper's own printed ratio cell. Captured paper table segment: Farnesol                                  11               0.27        0.025              1.2            1.1             0.85

raw_value_unit_evidence: Table II row Farnesol, AKR1C34 column group: Km 1.2 uM; kcat 1.1 min^-1; kcat/Km 0.85 min^-1 uM^-1.

row_label: Farnesol | AKR1C34

table_label: Table II. Substrate specificity for non-steroidal alcohols

substrate: farnesol