enzyme_display_name: Probable NADP-dependent mannitol dehydrogenase

organism: Yarrowia lipolytica (strain CLIB 122 / E 150)

smiles: CCCCCC(C)O

proof_lines: kcat is 3.17 sec(-1) with rac-2-heptanol as substrate and 6.15 sec(-1) for NADP(+). kcat is 5.42 sec(-1) for ribulose.


substrate_name: ribulose

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

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

data_origin: experimental

enzyme: Probable NADP-dependent mannitol dehydrogenase

substrate: ribulose

status: unverified

source: uniprot


substrate_name: NADP(+)

substrate: NADP(+)


enzyme_display_name: mannitol 2-dehydrogenase (NADP+)

organism: Agaricus bisporus

substrate_name: D-mannitol

source_db: brenda

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

assay_conditions_summary: pH 9

proof_lines: kcat is 2.20 sec(-1) for mannitol. kcat is 7.31 sec(-1) for fructose.

source_databases_merged: brenda uniprot

enzyme: mannitol 2-dehydrogenase (NADP+)

substrate: D-mannitol

source: brenda


substrate_name: D-fructose

substrate: D-fructose


organism: Pseudomonas aeruginosa

substrate_name: NADP(+) (refolded enzyme)

proof_lines: kcat is 110 min(-1) with UDP-GlcNAc as substrate. kcat is 0.69 min(-1) with UDP-GalNAc as substrate. kcat is 110 min(-1) with NAD(+) as substrate. kcat is 0.71 min(-1) with NADP(+) as substrate (PubMed:18065759). kcat is 5.5 min(-1) with UD

substrate: NADP(+) (refolded enzyme)


organism: Cladosporium herbarum

substrate_name: NADP+

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

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+

proof_lines: plusminus 0.007 mM, pH 7.5, room temperature

substrate: NADP+


substrate_name: NADPH

sequence_source: multiple

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADPH

proof_lines: plusminus 0.01 mM, pH 7.5, room temperature

substrate: NADPH


proof_lines: plusminus 5 mM, pH 7.5, room temperature


proof_lines: plusminus 20 mM, pH 7.5, room temperature


organism: Salmonella typhi

substrate_name: UDP-GlcNAc

substrate: UDP-GlcNAc


substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

substrate: NAD(+)


enzyme_display_name: dTDP-4-dehydrorhamnose reductase

organism: Acanthamoeba polyphaga Mimivirus

enzyme: dTDP-4-dehydrorhamnose reductase


enzyme_display_name: ribitol-5-phosphate 2-dehydrogenase

organism: Lactiplantibacillus plantarum

assay_conditions_summary: cofactor NADP+

proof_lines:
ribitol-5-phosphate 2-dehydrogenase
Lactiplantibacillus plantarum
NADP+

enzyme: ribitol-5-phosphate 2-dehydrogenase


substrate_name: D-ribulose 5-phosphate

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

proof_lines:
ribitol-5-phosphate 2-dehydrogenase
Lactiplantibacillus plantarum
D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


organism: Salmonella typhimurium

source_db: oed

source: oed


substrate_name: NADH

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH


enzyme_display_name: GDP-mannose 6-dehydrogenase

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

substrate_name: GDP-D-mannose

enzyme: GDP-mannose 6-dehydrogenase

substrate: GDP-D-mannose


organism: Arabidopsis thaliana

verification_status: verified

assay_conditions_summary: pH 8.5; cofactor NADPH

column_label: The abstract reports apparent Km values of 90 microm for NADPH and 16.9 microm for dTDP-4-keto-6-deoxy-Glc.

raw_value_unit_evidence: Km raw_value=90 microm raw_unit=microM

row_label: Prose segment: NADPH Km

table_label: PubMed PMID 15020741 abstract

status: verified


raw_value_unit_evidence: Km raw_value=16.9 microm raw_unit=microM

row_label: Prose segment: dTDP-4-keto-6-deoxy-Glc Km


organism: Aneurinibacillus thermoaerophilus

column_label: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes; block 'DSM 10155 RmlD'; substrate row 'NADH'; column 'Km (mM)' = 0.012 +/- 0.0017; column 'kcat (s-1)' = 1.5 +/- 6.6; the table has no kcat/Km column.

normalized_value_unit_evidence: Km: paper cell 0.012 mM; the column is already mM, so normalized Km = 0.012 mM. kcat: paper cell 1.5 s-1; the column is already s^(-1), so normalized kcat = 1.5 s^(-1). kcat/Km: not printed anywhere in the paper; the full-precision quotient of the row's own cells is 1.5 / 0.012 = 125.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4. Apparent kinetic constants for dTDP-l-rhamnose biosynthetic enzymes, block 'DSM 10155 RmlD', substrate row 'NADH': Km = 0.012 +/- 0.0017 mM; kcat = 1.5 +/- 6.6 s-1; no kcat/Km cell is printed.

row_label: Table 4, block 'DSM 10155 RmlD', substrate row 'NADH'


enzyme_display_name: NADP-dependent mannitol dehydrogenase

organism: Alternaria alternata

assay_conditions_summary: cofactor NADPH

enzyme: NADP-dependent mannitol dehydrogenase


organism: Davidiella tassiana

substrate_name: NADP(+) (at pH 7.5)

assay_conditions_summary: pH 7.5; buffer pH 7; cofactor NADP+

column_label: Results/Figure 4 text reports Michaelis-Menten constants for d-fructose, d-mannitol, NADPH, and NADP+ as 1.17 M, 0.23 M, 53 microM, and 67 microM, respectively.

raw_value_unit_evidence: Km raw_value=67 +/- 7 microM raw_unit=microM

row_label: Natural C. herbarum MtDH / NADP+ reverse reaction

table_label: JBC full text PMID 16608840 Results / Figure 4 Michaelis-Menten kinetics

substrate: NADP(+) (at pH 7.5)


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)

substrate_name: dTDP-6-deoxy-L-mannose (at pH 6.5)

substrate: dTDP-6-deoxy-L-mannose (at pH 6.5)


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Pseudomonas sp. 'mevalonii'

substrate_name: mevalonate

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

smiles: CC(CCO)(CC(=O)[O-])O

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: mevalonate


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

organism: Oryza sativa Japonica Group

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: pH and temperature not specified in the publication

enzyme: ketol-acid reductoisomerase (NADP+)

substrate: Unknown


organism: Oryza sativa

proof_lines: pH 8.0, 30°C, recombinant enzyme, versus hydroxypyruvate

proof_lines: pH 8.0, 30°C, recombinant enzyme, competitive mode


enzyme_display_name: phosphoglycerate dehydrogenase

organism: Escherichia coli

proof_lines:
apparent
Km at pH 7.5 is lower than at pH 8.8

enzyme: phosphoglycerate dehydrogenase


substrate_name: DL-mevalonate

smiles: CC(CCO)(CC(=O)O)O

substrate: DL-mevalonate


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Streptomyces sp.

substrate_name: coniferyl alcohol

proof_lines:
recombinant enzyme, pH 8.5, 30°C
pH 8.0, 30°C
native enzyme, pH 8.5, 30°C

enzyme: aryl-alcohol dehydrogenase

substrate: coniferyl alcohol


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7; buffer pH 7.0

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication


organism: Homo sapiens

proof_lines: pH 7.1, 25°C, wild-type enzyme from fibroblasts

proof_lines: pH 7.1, 25°C, recombinant FLAG-tagged wild-type enzyme from HEK-293 cells


enzyme_display_name: glyoxylate reductase (NADP+)

organism: Zea mays

substrate_name: NADH; Glyoxylate; H+

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

assay_conditions_summary: cofactor NADH

enzyme: glyoxylate reductase (NADP+)

substrate: NADH; Glyoxylate; H+


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Sorghum bicolor

substrate_name: Oxaloacetate; H+; NADPH

enzyme: malate dehydrogenase (NADP+)

substrate: Oxaloacetate; H+; NADPH


enzyme_display_name: L-threonine 3-dehydrogenase

organism: Capra hircus

substrate_name: NAD+; L-Threonine

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

enzyme: L-threonine 3-dehydrogenase

substrate: NAD+; L-Threonine


organism: Dictyostelium discoideum

substrate_name: Sepiapterin; NADPH; H+

substrate: Sepiapterin; NADPH; H+


organism: Streptomyces exfoliatus


enzyme_display_name: Aldo-keto reductase family 1 member C4

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

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: NADH tested with dihydrotestosterone

substrate: NADH tested with dihydrotestosterone


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3


enzyme_display_name: Aldo-keto reductase family 1 member C1

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


enzyme_display_name: Retinol dehydrogenase 16

substrate_name: CRBP-all-trans-retinol

enzyme: Retinol dehydrogenase 16

substrate: CRBP-all-trans-retinol


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: 5-alpha-pregnan-20-beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

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


organism: Drosophila melanogaster

substrate_name: NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at pH 9.3 and 25 degrees Celsius)


organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


enzyme_display_name: Retinol dehydrogenase 5

organism: Bos taurus

enzyme: Retinol dehydrogenase 5


organism: Mus musculus


organism: Macaca fuscata fuscata

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


enzyme_display_name: Aldo-keto reductase family 1 member B1

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1


enzyme_display_name: Aldo-keto reductase family 1 member B10

substrate_name: GS-acrolein

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

enzyme: Aldo-keto reductase family 1 member B10

substrate: GS-acrolein


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: 3-alpha,17-beta-androstandiol (tested with isoform 1 in the oxidative reaction)

assay_conditions_summary: cofactor CoA

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

enzyme: Aldo-keto reductase family 1 member B15


enzyme_display_name: Aldo-keto reductase family 1 member A1

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1


enzyme_display_name: Carbonyl reductase [NADPH] 1

organism: Sus scrofa

substrate_name: 9,1 O-phenanthrene-quinone

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

enzyme: Carbonyl reductase [NADPH] 1

substrate: 9,1 O-phenanthrene-quinone


enzyme_display_name: glycerol dehydrogenase (NADP+)

organism: Trichoderma reesei

substrate_name: H+; NADPH; Dihydroxyacetone

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

enzyme: glycerol dehydrogenase (NADP+)

substrate: H+; NADPH; Dihydroxyacetone


enzyme_display_name: Glycerol dehydrogenase

organism: Escherichia coli (strain K12)

proof_lines: The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation).

enzyme: Glycerol dehydrogenase


enzyme_display_name: (S,S)-butanediol dehydrogenase

organism: Corynebacterium glutamicum

substrate_name: L-acetoin

proof_lines:
pH 6.0
Dixon plot
pH 8.0, 37°C

enzyme: (S,S)-butanediol dehydrogenase

substrate: L-acetoin


enzyme_display_name: glyoxylate reductase (NADP+)

substrate_name: H+; NADPH; 3-Hydroxypyruvate

enzyme: glyoxylate reductase (NADP+)

substrate: H+; NADPH; 3-Hydroxypyruvate


substrate_name: Glyoxylate; H+; NADH

substrate: Glyoxylate; H+; NADH


organism: Saccharomyces cerevisiae

substrate_name: NADPH; H+; Glyoxylate

substrate: NADPH; H+; Glyoxylate


organism: Escherichia coli

substrate_name: NADPH; Glyoxylate; H+

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

proof_lines: The catalytic efficiency is better for glyoxylate than hydroxypyruvate with NADPH as electron donor.

substrate: NADPH; Glyoxylate; H+


substrate_name: H+; NADPH; Glyoxylate

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: The catalytic efficiency is better for hydroxypyruvate than glyoxylate with NADPH as electron donor.

substrate: H+; NADPH; Glyoxylate


organism: Spinacia oleracea

substrate_name: Glyoxylate; H+; NADPH

substrate: Glyoxylate; H+; NADPH


organism: Arabidopsis thaliana


organism: Thermus thermophilus

substrate_name: NADH

assay_conditions_summary: pH 6.7; cofactor NADH

proof_lines: pH 6.7, 45°C, substrate glyoxylate, purified recombinant enzyme

proof_lines: with glyoxylate as substrate, pH 6.7, 45°C

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 6.7; cofactor NADPH

substrate: NADPH


substrate_name: glyoxylate

proof_lines: pH 6.7, 45°C, cofactor NADPH, purified recombinant enzyme

proof_lines: pH 6.7, 45°C, cofactor NADH, purified recombinant enzyme

substrate: glyoxylate


organism: Vitis vinifera

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: hydroxypyruvate reductase

substrate_name: 3-Hydroxypyruvate; NADH; H+

enzyme: hydroxypyruvate reductase

substrate: 3-Hydroxypyruvate; NADH; H+


substrate_name: NADPH; H+; 3-Hydroxypyruvate

substrate: NADPH; H+; 3-Hydroxypyruvate


substrate_name: 3-Hydroxypyruvate; NADPH; H+

substrate: 3-Hydroxypyruvate; NADPH; H+


organism: Hyphomicrobium methylovorum

substrate_name: NADH; 3-Hydroxypyruvate; H+

substrate: NADH; 3-Hydroxypyruvate; H+


organism: Blautia hydrogenotrophica

substrate_name: NAD+; Glycerate

substrate: NAD+; Glycerate


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Methanocaldococcus jannaschii

substrate_name: NADPH; Oxaloacetate

enzyme: malate dehydrogenase (NADP+)

substrate: NADPH; Oxaloacetate


organism: Methanothermus fervidus


organism: Sorghum bicolor

substrate_name: Oxaloacetate; NADPH; H+

substrate: Oxaloacetate; NADPH; H+


organism: Pisum sativum

substrate_name: H+; NADPH; Oxaloacetate

substrate: H+; NADPH; Oxaloacetate


organism: Zea mays

substrate_name: NADPH; Oxaloacetate; H+

substrate: NADPH; Oxaloacetate; H+


substrate_name: NADP+; L-Malate

substrate: NADP+; L-Malate


organism: Glycine max


substrate_name: D-Malate; NAD+

substrate: D-Malate; NAD+


enzyme_display_name: Tartrate dehydrogenase/decarboxylase

organism: Pseudomonas putida

substrate_name: NAD(+) (for (+)-tartrate oxidation)

enzyme: Tartrate dehydrogenase/decarboxylase

substrate: NAD(+) (for (+)-tartrate oxidation)


enzyme_display_name: 3-isopropylmalate dehydrogenase

substrate_name: 3-Isopropylmalate; NAD+

enzyme: 3-isopropylmalate dehydrogenase

substrate: 3-Isopropylmalate; NAD+


organism: Sulfurisphaera tokodaii

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

assay_conditions_summary: pH 8

proof_lines:
pH 8.0
Raw SKiD Env: Temp=-----, pH=8

source_databases_merged: brenda skid


enzyme_display_name: 3-isopropylmalate dehydrogenase 2, chloroplastic

proof_lines: kcat is 373 min(-1) with 3-isopropylmalate as substrate (at pH 7.5) (PubMed:20840499, PubMed:21697089). kcat is 274 min(-1) with 3-isopropylmalate as substrate (at pH 7.5 and 25 degrees Celsius) (PubMed:27137927). kcat is 1 min(-1) with 3-(


enzyme_display_name: 3-isopropylmalate dehydrogenase 1, chloroplastic

proof_lines: kcat is 37 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 51 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


enzyme_display_name: 3-isopropylmalate dehydrogenase 3, chloroplastic

proof_lines: kcat is 543 min(-1) with 3-isopropylmalate as substrate (PubMed:20840499, PubMed:21697089). kcat is 1 min(-1) with 3-(2'-methylthio)ethylmalate as substrate (PubMed:21697089).


enzyme_display_name: ketol-acid reductoisomerase

substrate_name: H+; 3-Hydroxypyruvate; NADPH

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: kcat is 7.2 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 3.1 min(-1) for reductoisomerase activity with NADPH as substrate (PubMed:9015391). kcat is 0.11 min(-1) for reductoisomerase activity with

enzyme: ketol-acid reductoisomerase

substrate: H+; 3-Hydroxypyruvate; NADPH


enzyme_display_name: ketol-acid reductoisomerase (NADP+)

organism: Corynebacterium glutamicum

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

enzyme: ketol-acid reductoisomerase (NADP+)


organism: Streptomyces viridifaciens

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


organism: Streptomyces avermitilis


organism: Streptomyces ambofaciens


organism: Spinacia oleracea

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NADPH

proof_lines: pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-acetolactate as fixed substrate

proof_lines: pH 8.2, 30°C, NADPH as variable substrate, 0.2 mM (2S)-2-aceto-2-hydroxybutanoate as fixed substrate

proof_lines: pH 8.2, 30°C, (2S)-2-acetolactate as variable substrate, 0.250 mM NADPH as fixed substrate


enzyme_display_name: Ketol-acid reductoisomerase (NADP(+))

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature S2A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: kcat is 12.5 sec(-1) for reductoisomerase activity with HP as substrate. kcat is 1.4 sec(-1) for reductoisomerase activity with S2AL as substrate.

enzyme: Ketol-acid reductoisomerase (NADP(+))


enzyme_display_name: homoisocitrate dehydrogenase

organism: Thermus thermophilus

substrate_name: Homoisocitrate; NAD+

assay_conditions_summary: cofactor NAD+

enzyme: homoisocitrate dehydrogenase

substrate: Homoisocitrate; NAD+


organism: Saccharomyces cerevisiae

substrate_name: (2R,3S)-3-(4-pentenyl)malic acid

proof_lines: oxidate decarboxylation of homoisocitrate

substrate: (2R,3S)-3-(4-pentenyl)malic acid


enzyme_display_name: Homoisocitrate dehydrogenase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

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

enzyme: Homoisocitrate dehydrogenase


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Pseudomonas mevalonii

substrate_name: NAD+; Coenzyme A; Mevalonate

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: NAD+; Coenzyme A; Mevalonate


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Lactobacillus plantarum

substrate_name: Benzyl alcohol; NAD+

enzyme: aryl-alcohol dehydrogenase

substrate: Benzyl alcohol; NAD+


enzyme_display_name: aryl-alcohol dehydrogenase (NADP+)

organism: Phanerodontia chrysosporium

substrate_name: Unknown

enzyme: aryl-alcohol dehydrogenase (NADP+)

substrate: Unknown


enzyme_display_name: aryl-alcohol dehydrogenase (NADP(+))

organism: Ralstonia sp.

substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N15G/G37D/R38V/R39S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NADP+

enzyme: aryl-alcohol dehydrogenase (NADP(+))

substrate: NADP+


enzyme_display_name: tartrate dehydrogenase

organism: Sus scrofa

substrate_name: meso-Tartrate; NAD+

enzyme: tartrate dehydrogenase

substrate: meso-Tartrate; NAD+


substrate_name: NAD+; meso-Tartrate

substrate: NAD+; meso-Tartrate


substrate_name: isopropylmalate

substrate: isopropylmalate


organism: Escherichia coli

substrate_name: sn-glycerol 3-phosphate

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

substrate: sn-glycerol 3-phosphate


proof_lines: pH 7.4, 23°C, wild-type and feedback-resistant mutant enzyme

proof_lines: pH 7.4, 23°C, wild-type enzyme and feedback-resistant mutant enzyme


substrate_name: NAD(P)+

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: pH 7.4, 23°C, feedback-resistant mutant enzyme

substrate: NAD(P)+


organism: Escherichia coli (strain K12)

proof_lines: Essentially identical kinetic constants are found when NADH and NAD(+) are substituted for NADPH and NADP(+), respectively.


enzyme_display_name: phosphoglycerate dehydrogenase

substrate_name: 3-Phospho-D-glycerate; NAD+

proof_lines: kcat is 0.55 sec(-1) for 3-phospho-D-glycerate oxidation. kcat is 27.8 sec(-1) for 3-phosphonooxypyruvate reduction. kcat is 33.3 sec(-1) for 2-oxoglutarate reduction. kcat is 0.71 sec(-1) for (R)-2-hydroxyglutarate oxidation. kcat is 0.25

enzyme: phosphoglycerate dehydrogenase

substrate: 3-Phospho-D-glycerate; NAD+


organism: Arabidopsis thaliana

substrate_name: H+; 3-Phosphohydroxypyruvate; NADH

substrate: H+; 3-Phosphohydroxypyruvate; NADH


organism: Homo sapiens

substrate_name: NADH; H+; 3-Phosphohydroxypyruvate

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

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: kcat is 4.5 min(-1) for 3-phosphoglycerate oxidation. kcat is 10.6 min(-1) for oxaloacetate reduction. kcat is 4.7 min(-1) for 2-oxoglutarate reduction.

source_databases_merged: sabio_rk skid uniprot

substrate: NADH; H+; 3-Phosphohydroxypyruvate


substrate_name: NAD+; 3-Phospho-D-glycerate

substrate: NAD+; 3-Phospho-D-glycerate


assay_conditions_summary: pH 7.1; cofactor NAD+


organism: Streptomyces coelicolor

assay_conditions_summary: pH 7; buffer 50 mM MOPS

proof_lines: in 50 mM MOPS buffer, pH 7.0, temperature not specified in the publication

proof_lines: in 200 mM KPO4 buffer, pH 7.0, temperature not specified in the publication


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D463A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


organism: Sulfurisphaera tokodaii

assay_conditions_summary: cofactor NADPH

proof_lines: value of phosphate against 3-phosphohydroxypyruvate


substrate_name: Acetoacetyl-CoA; H+; NADPH

assay_conditions_summary: cofactor NADP+

substrate: Acetoacetyl-CoA; H+; NADPH


organism: Persea americana

substrate_name: acetoacetyl-[acyl-carrier protein]

substrate: acetoacetyl-[acyl-carrier protein]


enzyme_display_name: Fatty acid synthase

organism: Rattus norvegicus

enzyme: Fatty acid synthase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: beta-ketododecanoyl-CoA (at 25 degrees Celsius and at pH 7.0)

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 4.3 sec(-1) with beta-ketododecanoyl-CoA as substrate. kcat is 3.5 sec(-1) with beta-ketooctanoyl-CoA as substrate. kcat is 1.9 sec(-1) with acetoacetyl-CoA as substrate. kcat is 2.6 sec(-1) with NADPH as substrate (PubMed:11932442)


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

substrate_name: beta-keto-octanoyl-CoA

proof_lines: kcat is 1.14 sec(-1) with acetoacetyl-CoA as substrate. kcat is 5.72 sec(-1) with beta-keto-octanoyl-CoA as substrate.

substrate: beta-keto-octanoyl-CoA


enzyme_display_name: acylglycerone-phosphate reductase

organism: Mus musculus

substrate_name: 1-O-Hexadecyl glycerone phosphate; NADPH; H+

smiles: CCCCCCCCCCCCCCCCOCC(=O)COP(O)(O)=O

enzyme: acylglycerone-phosphate reductase


substrate_name: NADPH; H+; 1-O-Hexadecyl glycerone phosphate


organism: Saccharomyces cerevisiae

substrate_name: 1-O-Hexadecyl glycerone phosphate; NADPH


organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: C18-3-oxosphinganine (at pH 6.9)

proof_lines: kcat is 64 min(-1) with C18-3-oxosphinganine as substrate (PubMed:16431155). kcat is 19 min(-1) with C12-3-oxosphinganine as substrate (PubMed:16431155). kcat is 13 min(-1) with C11-3-oxosphinganine as substrate (PubMed:16431155). kcat is 5

substrate: C18-3-oxosphinganine (at pH 6.9)


enzyme_display_name: L-threonine 3-dehydrogenase

substrate_name: NAD+; L-Threonine

enzyme: L-threonine 3-dehydrogenase

substrate: NAD+; L-Threonine


organism: Flavobacterium frigidimaris

substrate_name: L-Threonine; NAD+

substrate: L-Threonine; NAD+


organism: Pyrococcus horikoshii


organism: Cytophaga sp.

substrate_name: Unknown

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines:
substrate NAD+, pH 9.0, 30°C
substrate L-threonine, pH 9.0, 30°C

substrate: Unknown


substrate_name: L-threonine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R180K to reconstruct the assayed variant sequence.

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

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T237A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S133A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M333A to reconstruct the assayed variant sequence.


organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)


enzyme_display_name: Dehydrogenase/reductase SDR family member 6

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 19 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.


proof_lines: kcat is 14 sec(-1) for the NADH-dependent reduction of 4-oxo-L-proline. kcat is 0.02 sec(-1) for the NAD(+)-dependent oxidation of (R)-3-hydroxybutanoate.

enzyme: Dehydrogenase/reductase SDR family member 6


enzyme_display_name: retinol dehydrogenase

substrate_name: NADPH; H+; all-trans-Retinal

verification_status: corrected

assay_conditions_summary: pH 7.4; cofactor NADP+

column_label: PMID 14674758 Table 2, Kinetic Constants of the Membrane-Bound Wild-Type RalR1 and Purified RalR1-His6; row all-trans-retinal determined with NADPH; purified RalR1-His6 columns apparent Km=0.12 +/- 0.1 uM and apparent Vmax=506 +/- 13 nmol/min/mg. Results prose converts Vmax with a 35.4 kDa subunit mass to kcat=18 min^-1.

normalized_value_unit_evidence: kcat normalized_value=0.3 normalized_unit=s^-1; km normalized_value=0.00012 normalized_unit=mM; vmax normalized_value=0.000008433333333333333 normalized_unit=mol*s^-1*g^-1.

raw_value_unit_evidence: Table 2 purified RalR1-His6 row all-trans-retinal with NADPH: apparent Km 0.12 +/- 0.1 uM; apparent Vmax 506 +/- 13 nmol/min/mg. Results prose: kcat 18 min^-1.

row_label: all-trans-retinal determined with NADPH / purified RalR1-His6

table_label: Table 2. Kinetic Constants of the Membrane-Bound Wild-Type RalR1 and Purified RalR1-His6

enzyme: retinol dehydrogenase

substrate: NADPH; H+; all-trans-Retinal

status: corrected


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

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


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: NADH tested with dihydrotestosterone

substrate: NADH tested with dihydrotestosterone


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH7

substrate_name: 12-OH-dodecanoic acid (with 0.1 M sodium phosphate at pH 7.5)

smiles: OCCCCCCCCCCCC(=O)O

assay_conditions_summary: pH 7.5; buffer only


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase 13

enzyme: 17-beta-hydroxysteroid dehydrogenase 13


proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


enzyme_display_name: pyridoxal 4-dehydrogenase

organism: Microbacterium luteolum

substrate_name: NAD+; Pyridoxal

enzyme: pyridoxal 4-dehydrogenase

substrate: NAD+; Pyridoxal


enzyme_display_name: carnitine 3-dehydrogenase

organism: Rhizobium sp. (Cicer)

substrate_name: NAD+; L-Carnitine

enzyme: carnitine 3-dehydrogenase

substrate: NAD+; L-Carnitine


organism: Xanthomonas translucens

substrate_name: L-Carnitine; NAD+

substrate: L-Carnitine; NAD+


enzyme_display_name: L-carnitine dehydrogenase

organism: Pseudomonas sp

substrate_name: L-carnithine

proof_lines: Part of the values are for the recombinant protein expressed in E.coli (PubMed:20530902). Other values are for the wild-type protein (Ref.2).

enzyme: L-carnitine dehydrogenase

substrate: L-carnithine


enzyme_display_name: Aromatic 2-oxoacid reductase

organism: Clostridium sporogenes (strain ATCC 15579)

substrate_name: phenyllactate

enzyme: Aromatic 2-oxoacid reductase

substrate: phenyllactate


enzyme_display_name: indanol dehydrogenase

organism: Homo sapiens

substrate_name: Indan-1-ol; NADP+

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: indanol dehydrogenase

substrate: Indan-1-ol; NADP+


substrate_name: NADP+; Indan-1-ol

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

substrate: NADP+; Indan-1-ol


enzyme_display_name: D-arabinose 1-dehydrogenase

substrate_name: NAD+; D-Arabinose

enzyme: D-arabinose 1-dehydrogenase

substrate: NAD+; D-Arabinose


enzyme_display_name: glucose 1-dehydrogenase (NADP+)

organism: Halobacterium volcanii

substrate_name: D-Glucose; NADP+

enzyme: glucose 1-dehydrogenase (NADP+)

substrate: D-Glucose; NADP+


enzyme_display_name: Glucose 1-dehydrogenase

organism: Gluconobacter oxydans (strain 621H)

proof_lines: kcat is 84.8 sec(-1) with glucose as substrate. kcat is 106 sec(-1) with mannose as substrate.

enzyme: Glucose 1-dehydrogenase


organism: Saccharolobus solfataricus

substrate_name: D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8)


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

organism: Azospirillum brasilense

substrate_name: L-arabinose (in the presence of NAD(+), at 30 degrees Celsius and pH 9.0)

assay_conditions_summary: pH 9

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))


enzyme_display_name: UniProt Q5SLC4

organism: Thermus thermophilus HB8

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q5SLC4

source: skid


enzyme_display_name: L-fucose dehydrogenase

substrate_name: L-fuctose

proof_lines: kcat is 14.00 sec(-1) with L-fucose as substrate. kcat is 16.89 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat is 0.0003 sec(-1) with beta-estradiol as substrate. kcat is 0.00028sec(-1) with androst-5-en-3beta,17beta-diol as subst

enzyme: L-fucose dehydrogenase

substrate: L-fuctose


enzyme_display_name: D-threo-aldose 1-dehydrogenase

substrate_name: Unknown

enzyme: D-threo-aldose 1-dehydrogenase


organism: Rattus norvegicus

proof_lines: kcat is 0.13 sec(-1) with L-fucose as substrate. kcat is 0.15 sec(-1) with NAD(+) as substrate.


organism: Oryctolagus cuniculus

proof_lines: kcat is 7.00 sec(-1) with L-fucose as substrate. kcat is 7.00 sec(-1) with NAD(+) as substrate (PubMed:38944119). kcat/KM=4878 min(-1) mM(-1) for L-fuctose (PubMed:38944119).


enzyme_display_name: GDP-mannose 6-dehydrogenase

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

enzyme: GDP-mannose 6-dehydrogenase


enzyme_display_name: dTDP-4-dehydrorhamnose reductase

organism: Salmonella typhimurium

enzyme: dTDP-4-dehydrorhamnose reductase


organism: Aneurinibacillus thermoaerophilus


organism: Pseudomonas aeruginosa

substrate_name: UDP-GlcNAc (refolded enzyme, in the presence of NAD(+))

proof_lines: kcat is 110 min(-1) with UDP-GlcNAc as substrate. kcat is 0.69 min(-1) with UDP-GalNAc as substrate. kcat is 110 min(-1) with NAD(+) as substrate. kcat is 0.71 min(-1) with NADP(+) as substrate (PubMed:18065759). kcat is 5.5 min(-1) with UD


substrate_name: UDP-D-GlcNAc

substrate: UDP-D-GlcNAc


enzyme_display_name: mannitol 2-dehydrogenase (NADP+)

organism: Alternaria alternata

substrate_name: H+; D-Fructose; NADPH

enzyme: mannitol 2-dehydrogenase (NADP+)

substrate: H+; D-Fructose; NADPH


enzyme_display_name: UniProt P28845

enzyme: UniProt P28845


substrate_name: dehydroepiandrosterone

proof_lines: wild-type, presence of 2-mercatoethanol pH 7.4

substrate: dehydroepiandrosterone


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

substrate: NAD+


organism: Solanum lycopersicum

substrate_name: pregnenolone

substrate: pregnenolone


substrate_name: dehydrotomatidine

substrate: dehydrotomatidine


organism: Digitalis lanata

substrate_name: NADH

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+


organism: Rhinella arenarum


organism: Bufo gargarizans


proof_lines:
NAD+ as cofactor
pH 7.8, 30°C


enzyme_display_name: 16alpha-hydroxysteroid dehydrogenase

organism: Rattus sp.

substrate_name: NADPH

enzyme: 16alpha-hydroxysteroid dehydrogenase

substrate: NADPH


organism: Cricetinae

proof_lines:
type I
type II


enzyme_display_name: perillyl-alcohol dehydrogenase

organism: Acinetobacter calcoaceticus

substrate_name: perillyl alcohol

enzyme: perillyl-alcohol dehydrogenase

substrate: perillyl alcohol


organism: Pseudomonas sp.

assay_conditions_summary: pH 8.6; cofactor NAD+


organism: Homo sapiens

proof_lines:
wild-type 3beta-HSD1, pH 7.4, 27°C
wild-type 3beta-HSD2, pH 7.4, 27°C
pH 7.4, 27°C, wild-tpye 3beta-HSD1


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

substrate_name: cortisol

proof_lines: pH 7.5, 22°C, recombinant wild-type isozyme 11beta-HSD1 oxidized with K3Fe(CN)6

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: cortisol


organism: Comamonas testosteroni


organism: Clarias gariepinus


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C72S with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant C72S, presence of 2-mercatoethanol pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C83A with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant C83A, presence of 2-mercatoethanol pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C72F with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant C72F, presence of 2-mercatoethanol pH 7.4


enzyme_display_name: Geraniol dehydrogenase

organism: Castellaniella defragrans (strain DSM 12143 / CCUG 39792 / 65Phen)

substrate_name: geraniol

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

proof_lines: The values given here are for the native GeDH, the values for the recombinant protein can be found in another article (PubMed:22286981).

enzyme: Geraniol dehydrogenase

substrate: geraniol


substrate_name: (S)-perillyl alcohol

substrate: (S)-perillyl alcohol


substrate_name: citronellol

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

substrate: citronellol


substrate_name: cumic alcohol

substrate: cumic alcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


proof_lines: pH 7.4, 27°C, chimeric R195P-1 mutant of the enzyme (3beta-HSD1)


assay_conditions_summary: pH 7.4; cofactor NADH


substrate_name: prostaglandin E1

proof_lines: kcat is 8.6 min(-1) with (11R)-hydroxy-(5Z,8Z,12E,14Z)-eicosatetraenoate and (5Z,8Z,11Z,13E,15S)-hydroxyeicosatetraenoate as substrates.

substrate: prostaglandin E1


substrate_name: prostaglandin A1

substrate: prostaglandin A1


substrate_name: prostaglandin A2

substrate: prostaglandin A2


substrate_name: NAD in the presence of prostaglandin E1

substrate: NAD in the presence of prostaglandin E1


substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P195R to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


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


substrate_name: NAD+

substrate: NAD+


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; 300.15 K; cofactor NADH


organism: Mesocricetus auratus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: PMID 14973125 Table I, Reduction of 7-ketocholesterol, Hamster row, Km (nM) = 384 +/- 44.

normalized_value_unit_evidence: Km normalized_value=0.000384 mM; exported 0.00038 mM is rounded from the printed nM cell.

raw_value_unit_evidence: Table I row Reduction of 7-ketocholesterol / Hamster, Km column: 384 +/- 44 nM.

table_label: Table I. Oxidation and reduction by lysates from HEK-293 cells expressing recombinant 11beta-HSD1


column_label: PMID 14973125 Table I, Reduction of 11-dehydrocorticosterone, Hamster row, Km (nM) = 396 +/- 82.

normalized_value_unit_evidence: Km normalized_value=0.000396 mM; exported 0.0004 mM is rounded from the printed nM cell.

raw_value_unit_evidence: Table I row Reduction of 11-dehydrocorticosterone / Hamster, Km column: 396 +/- 82 nM.


proof_lines: 37°C, pH 7.4, in HEK-293 lysates expressing 11beta-HSD1


substrate_name: corticosterone

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

normalized_value_unit_evidence: Km normalized_value=0.000321 mM.

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

row_label: Oxidation of corticosterone / Hamster

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

substrate: corticosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q240R with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q240R


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD1 mutant Q105M

proof_lines: pH 7.4, 27°C, recombinant isozyme 3beta-HSD2 mutant Q105M


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature R240Q to reconstruct the assayed variant sequence.

column_label: Table 3 (Cofactor kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes), enzyme row R240Q2, 3β-HSD NAD+ column group; column Km uM = 37.2; column kcat min^-1 = 11.2; column kcat/Km min^-1 uM^-1 = 0.30.

raw_value_unit_evidence: Table 3, enzyme row R240Q2, 3β-HSD NAD+ column group: Km = 37.2 uM; kcat = 11.2 min^-1; printed kcat/Km = 0.30 min^-1 uM^-1.

table_label: Table 3: Cofactor kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes (J Biol Chem 2005, 280(22):21321-21328)


column_label: Table 2 (Substrate kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes), enzyme row R240Q2, 3β-HSD1 column group; column Km uM = 32.7; column kcat min^-1 = 13.0; column kcat/Km min^-1 uM^-1 = 0.40.

raw_value_unit_evidence: Table 2, enzyme row R240Q2, 3β-HSD1 column group: Km = 32.7 uM; kcat = 13.0 min^-1; printed kcat/Km = 0.40 min^-1 uM^-1.

table_label: Table 2: Substrate kinetics for the 3β-HSD and isomerase activities of the purified mutant and wild-type enzymes (J Biol Chem 2005, 280(22):21321-21328)


smiles: CCCCCC=CC=CC(CC=CCC=CCCCC(=O)[O-])O


smiles: CCCCCC(C=CC=CCC=CCC=CCCCC(=O)[O-])O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186K'; column 'Km (uM)' = 22; column 'kcat (s^-1)' = 35; column 'kcat/Km (M^-1 s^-1)' = 1.6 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 22 uM; 22 / 1000 = 0.022 mM. kcat: printed Table 2 cell 35 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 35 s^(-1). kcat/Km: printed Table 2 cell 1.6 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.6 x 10^6 / 1000 = 1600 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186K: the Km (uM) cell prints 22, the kcat (s^-1) cell prints 35, and the kcat/Km (M^-1 s^-1) cell prints 1.6 x 10^6.

row_label: Table 2, NAD+ block, row V186K

table_label: Table 2: Km, kcat, and kcat/Km values for 15-PGDH mutants (Archives of Biochemistry and Biophysics 433 (2005) 447-453)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186A'; column 'Km (uM)' = 24; column 'kcat (s^-1)' = 70; column 'kcat/Km (M^-1 s^-1)' = 2.9 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 24 uM; 24 / 1000 = 0.024 mM. kcat: printed Table 2 cell 70 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 70 s^(-1). kcat/Km: printed Table 2 cell 2.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.9 x 10^6 / 1000 = 2900 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186A: the Km (uM) cell prints 24, the kcat (s^-1) cell prints 70, and the kcat/Km (M^-1 s^-1) cell prints 2.9 x 10^6.

row_label: Table 2, NAD+ block, row V186A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186I to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'V186I'; column 'Km (uM)' = 272; column 'kcat (s^-1)' = 247; column 'kcat/Km (M^-1 s^-1)' = 0.9 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 272 uM; 272 / 1000 = 0.272 mM. kcat: printed Table 2 cell 247 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 247 s^(-1). kcat/Km: printed Table 2 cell 0.9 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.9 x 10^6 / 1000 = 900 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row V186I: the Km (uM) cell prints 272, the kcat (s^-1) cell prints 247, and the kcat/Km (M^-1 s^-1) cell prints 0.9 x 10^6.

row_label: Table 2, NAD+ block, row V186I


enzyme_display_name: Alcohol dehydrogenase 2

organism: Tanacetum cinerariifolium

substrate_name: trans-chrysanthemol

proof_lines: kcat is 0.75 sec(-1) with trans-chrysanthemol as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.64 sec(-1) with NAD(+) as substrate (in the presence of trans-chrysanthemol) (PubMed:29122986).

enzyme: Alcohol dehydrogenase 2

substrate: trans-chrysanthemol


substrate_name: NAD(+)

substrate: NAD(+)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195P with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S123A to reconstruct the assayed variant sequence.


substrate_name: prostaglandin E2

substrate: prostaglandin E2


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H156Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

proof_lines:
mutant H156Y, pH 7.4, 27°C
27°C, pH 7.4, H156Y mutant 3beta-HSD1
pH 7.4, 27°C, recombinant mutant H156Y


organism: Cavia porcellus

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 expressed in Escherichia coli


substrate_name: cortisone

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 measured in intact COS cells transfected with 11beta-HSD1

proof_lines: 37°C, pH 7.4, recombinant 11beta-HSD1 expressed in Pichia pastoris

substrate: cortisone


proof_lines:
27°C, pH 7.4, H156Y mutant 3beta-HSD1
27°C, pH 7.4, H156Y mutant


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

organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

assay_conditions_summary: cofactor NADPH

column_label: Abstract reports with NADPH the type I isoform has Km value 1.18 microM for DHT.

raw_value_unit_evidence: Km raw_value=1.18 microM raw_unit=microM

row_label: Rat type I 3 beta-HSD / dihydrotestosterone with NADPH

table_label: PubMed XML abstract PMID 1537836


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines: cosubstrate dehydroepiandrosterone, pH 8.5, 37°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17A'; column 'Km (uM)' = 555; column 'kcat (s^-1)' = 129; column 'kcat/Km (M^-1 s^-1)' = 0.2 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 555 uM; 555 / 1000 = 0.555 mM. kcat: printed Table 2 cell 129 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 129 s^(-1). kcat/Km: printed Table 2 cell 0.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.2 x 10^6 / 1000 = 200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17A: the Km (uM) cell prints 555, the kcat (s^-1) cell prints 129, and the kcat/Km (M^-1 s^-1) cell prints 0.2 x 10^6.

row_label: Table 2, NAD+ block, row I17A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17L to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17L'; column 'Km (uM)' = 59; column 'kcat (s^-1)' = 165; column 'kcat/Km (M^-1 s^-1)' = 2.8 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 59 uM; 59 / 1000 = 0.059 mM. kcat: printed Table 2 cell 165 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 165 s^(-1). kcat/Km: printed Table 2 cell 2.8 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.8 x 10^6 / 1000 = 2800 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17L: the Km (uM) cell prints 59, the kcat (s^-1) cell prints 165, and the kcat/Km (M^-1 s^-1) cell prints 2.8 x 10^6.

row_label: Table 2, NAD+ block, row I17L


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature I17V to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'I17V'; column 'Km (uM)' = 98; column 'kcat (s^-1)' = 110; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 98 uM; 98 / 1000 = 0.098 mM. kcat: printed Table 2 cell 110 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 110 s^(-1). kcat/Km: printed Table 2 cell 1.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^6 / 1000 = 1100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row I17V: the Km (uM) cell prints 98, the kcat (s^-1) cell prints 110, and the kcat/Km (M^-1 s^-1) cell prints 1.1 x 10^6.

row_label: Table 2, NAD+ block, row I17V


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature N91A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'N91A'; column 'Km (uM)' = 719; column 'kcat (s^-1)' = 91; column 'kcat/Km (M^-1 s^-1)' = 0.1 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 719 uM; 719 / 1000 = 0.719 mM. kcat: printed Table 2 cell 91 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 91 s^(-1). kcat/Km: printed Table 2 cell 0.1 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.1 x 10^6 / 1000 = 100 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row N91A: the Km (uM) cell prints 719, the kcat (s^-1) cell prints 91, and the kcat/Km (M^-1 s^-1) cell prints 0.1 x 10^6.

row_label: Table 2, NAD+ block, row N91A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature N91D to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'N91D'; column 'Km (uM)' = 32; column 'kcat (s^-1)' = 42; column 'kcat/Km (M^-1 s^-1)' = 1.3 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 32 uM; 32 / 1000 = 0.032 mM. kcat: printed Table 2 cell 42 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 42 s^(-1). kcat/Km: printed Table 2 cell 1.3 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^6 / 1000 = 1300 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row N91D: the Km (uM) cell prints 32, the kcat (s^-1) cell prints 42, and the kcat/Km (M^-1 s^-1) cell prints 1.3 x 10^6.

row_label: Table 2, NAD+ block, row N91D


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), NAD+ substrate block, row 'Wild type'; column 'Km (uM)' = 38; column 'kcat (s^-1)' = 47; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^6.

normalized_value_unit_evidence: Km: printed Table 2 cell 38 uM; 38 / 1000 = 0.038 mM. kcat: printed Table 2 cell 47 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 47 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^6 / 1000 = 1200 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, NAD+ block, row Wild type: the Km (uM) cell prints 38, the kcat (s^-1) cell prints 47, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^6.

row_label: Table 2, NAD+ block, row Wild type


substrate_name: Prostaglandin E2

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17A'; column 'Km (uM)' = 11.0; column 'kcat (s^-1)' = 127; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.0 uM; 11.0 / 1000 = 0.011 mM. kcat: printed Table 2 cell 127 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 127 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17A: the Km (uM) cell prints 11.0, the kcat (s^-1) cell prints 127, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row I17A

substrate: Prostaglandin E2


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D241N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D265N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36A/K37R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NADP+

column_label: PMID 12832414 Table IV. Comparison of substrate kinetics of purified D36A/K37R and wild-type 3beta-HSD and isomerase activities using NAD(H) and NADP(H) as cofactor; row D36A/K37R / DHEA / NADP+ / 3beta-HSD; columns Km (uM), Kcat (min^-1); same-row normalized tuple kcat=0.01833333333333333333333333333 s^-1, Km=0.0048 mM, kcat/Km=3.819444444444444444444444444 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.01833333333333333333333333333 normalized_unit=s^-1; Km normalized_value=0.0048 normalized_unit=mM; kcat/Km normalized_value=3.819444444444444444444444444 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table IV row DHEA, cofactor NADP+, activity 3beta-HSD, D36A/K37R columns: Km 4.8 uM; Kcat 1.1 min^-1.

row_label: D36A/K37R / DHEA / NADP+ / 3beta-HSD


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


substrate_name: NADP+

column_label: PMID 12832414 Table III. Comparison of NAD(H) and NADP(H) cofactor kinetics for the 3beta-HSD and isomerase activities of the purified D36A/K37R and wild-type enzymes; row D36A/K37R / NADP+ / 3beta-HSD; columns Km (uM), Kcat (min^-1); same-row normalized tuple kcat=0.02166666666666666666666666667 s^-1, Km=0.0206 mM, kcat/Km=1.051779935275080906148867314 s^-1*mM^-1.

normalized_value_unit_evidence: kcat normalized_value=0.02166666666666666666666666667 normalized_unit=s^-1; Km normalized_value=0.0206 normalized_unit=mM; kcat/Km normalized_value=1.051779935275080906148867314 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row D36A/K37R, cofactor NADP+, activity 3beta-HSD: Km 20.6 uM; Kcat 1.3 min^-1.

row_label: D36A/K37R / NADP+ / 3beta-HSD

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148E with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148H with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q148N with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


enzyme_display_name: sorbitol-6-phosphate 2-dehydrogenase

organism: Erwinia amylovora

substrate_name: D-fructose 6-phosphate

assay_conditions_summary: pH 9; cofactor NADH

column_label: Primary Table 3 row d-Fructose 6-phosphate has columns Km [mM], kcat [s^-1], and kcat/Km with values 2.0 +/- 0.4, 0.56, and 0.28.

raw_value_unit_evidence: Table 3 row d-Fructose 6-phosphate: Km [mM] 2.0 +/- 0.4; kcat [s^-1] 0.56; kcat/Km column 0.28 with table header rendered as uM^-1 s^-1

row_label: d-Fructose 6-phosphate

table_label: ScienceDirect full text Table 3, Kinetic parameters for SrlD (Mw = 28.13 KDa)

enzyme: sorbitol-6-phosphate 2-dehydrogenase

substrate: D-fructose 6-phosphate


substrate_name: D-sorbitol 6-phosphate

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Primary Table 3 row d-Sorbitol 6-phosphate has columns Km [mM], kcat [s^-1], and kcat/Km with values 9.0 +/- 1.3, 5.6, and 0.62.

raw_value_unit_evidence: Table 3 row d-Sorbitol 6-phosphate: Km [mM] 9.0 +/- 1.3; kcat [s^-1] 5.6; kcat/Km column 0.62 with table header rendered as uM^-1 s^-1

row_label: d-Sorbitol 6-phosphate

substrate: D-sorbitol 6-phosphate


substrate_name: NADH

column_label: Primary Table 3 row NADH has Km [mM] value 0.048 +/- 0.006.

raw_value_unit_evidence: Table 3 row NADH, column Km [mM]: 0.048 +/- 0.006

row_label: NADH

substrate: NADH


assay_conditions_summary: pH 9; cofactor NADP+

column_label: Primary Table 3 row NAD+ has Km [mM] value 1.6 +/- 0.2*; footnote marks Kmapp.

normalized_value_unit_evidence: Km 1.6 mM

raw_value_unit_evidence: Table 3 row NAD+, column Km [mM]: 1.6 +/- 0.2*; footnote * Kmapp

row_label: NAD+


assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+

column_label: Primary Table 3 row d-Sorbitol 6-phosphate has kcat/Km value 0.62; Km 9.0 mM and kcat 5.6 s^-1 provide the same precise expected ratio.

raw_value_unit_evidence: Table 3 row d-Sorbitol 6-phosphate, kcat/Km column: 0.62 with table header rendered as uM^-1 s^-1


substrate_name: D-Fructose 6-phosphate

assay_conditions_summary: pH 9; 295.15 K; cofactor NADH

column_label: Primary Table 3 row d-Fructose 6-phosphate has kcat/Km value 0.28; Km 2.0 mM and kcat 0.56 s^-1 match the same expected ratio.

raw_value_unit_evidence: Table 3 row d-Fructose 6-phosphate, kcat/Km column: 0.28 with table header rendered as uM^-1 s^-1

substrate: D-Fructose 6-phosphate


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17L'; column 'Km (uM)' = 11.8; column 'kcat (s^-1)' = 210; column 'kcat/Km (M^-1 s^-1)' = 1.8 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.8 uM; 11.8 / 1000 = 0.0118 mM. kcat: printed Table 2 cell 210 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 210 s^(-1). kcat/Km: printed Table 2 cell 1.8 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.8 x 10^7 / 1000 = 18000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17L: the Km (uM) cell prints 11.8, the kcat (s^-1) cell prints 210, and the kcat/Km (M^-1 s^-1) cell prints 1.8 x 10^7.

row_label: Table 2, PGE2 block, row I17L


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'I17V'; column 'Km (uM)' = 11.2; column 'kcat (s^-1)' = 143; column 'kcat/Km (M^-1 s^-1)' = 1.3 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 11.2 uM; 11.2 / 1000 = 0.0112 mM. kcat: printed Table 2 cell 143 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 143 s^(-1). kcat/Km: printed Table 2 cell 1.3 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^7 / 1000 = 13000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row I17V: the Km (uM) cell prints 11.2, the kcat (s^-1) cell prints 143, and the kcat/Km (M^-1 s^-1) cell prints 1.3 x 10^7.

row_label: Table 2, PGE2 block, row I17V


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'N91A'; column 'Km (uM)' = 6.1; column 'kcat (s^-1)' = 73; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 6.1 uM; 6.1 / 1000 = 0.0061 mM. kcat: printed Table 2 cell 73 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 73 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row N91A: the Km (uM) cell prints 6.1, the kcat (s^-1) cell prints 73, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row N91A


column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'N91D'; column 'Km (uM)' = 2.6; column 'kcat (s^-1)' = 45; column 'kcat/Km (M^-1 s^-1)' = 1.7 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.6 uM; 2.6 / 1000 = 0.0026 mM. kcat: printed Table 2 cell 45 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 45 s^(-1). kcat/Km: printed Table 2 cell 1.7 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^7 / 1000 = 17000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row N91D: the Km (uM) cell prints 2.6, the kcat (s^-1) cell prints 45, and the kcat/Km (M^-1 s^-1) cell prints 1.7 x 10^7.

row_label: Table 2, PGE2 block, row N91D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186A to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186A'; column 'Km (uM)' = 4.5; column 'kcat (s^-1)' = 78; column 'kcat/Km (M^-1 s^-1)' = 1.7 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 4.5 uM; 4.5 / 1000 = 0.0045 mM. kcat: printed Table 2 cell 78 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 78 s^(-1). kcat/Km: printed Table 2 cell 1.7 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.7 x 10^7 / 1000 = 17000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186A: the Km (uM) cell prints 4.5, the kcat (s^-1) cell prints 78, and the kcat/Km (M^-1 s^-1) cell prints 1.7 x 10^7.

row_label: Table 2, PGE2 block, row V186A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186I to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186I'; column 'Km (uM)' = 21.8; column 'kcat (s^-1)' = 262; column 'kcat/Km (M^-1 s^-1)' = 1.2 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 21.8 uM; 21.8 / 1000 = 0.0218 mM. kcat: printed Table 2 cell 262 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 262 s^(-1). kcat/Km: printed Table 2 cell 1.2 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^7 / 1000 = 12000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186I: the Km (uM) cell prints 21.8, the kcat (s^-1) cell prints 262, and the kcat/Km (M^-1 s^-1) cell prints 1.2 x 10^7.

row_label: Table 2, PGE2 block, row V186I


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186K to reconstruct the assayed variant sequence.

column_label: Table 2 (Km, kcat, and kcat/Km values for 15-PGDH mutants), PGE2 substrate block, row 'V186K'; column 'Km (uM)' = 3.5; column 'kcat (s^-1)' = 37; column 'kcat/Km (M^-1 s^-1)' = 1.1 x 10^7.

normalized_value_unit_evidence: Km: printed Table 2 cell 3.5 uM; 3.5 / 1000 = 0.0035 mM. kcat: printed Table 2 cell 37 s^-1; already in s^-1, so no unit conversion applies and the canonical value is 37 s^(-1). kcat/Km: printed Table 2 cell 1.1 x 10^7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.1 x 10^7 / 1000 = 11000 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, PGE2 block, row V186K: the Km (uM) cell prints 3.5, the kcat (s^-1) cell prints 37, and the kcat/Km (M^-1 s^-1) cell prints 1.1 x 10^7.

row_label: Table 2, PGE2 block, row V186K


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195P with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R195R with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature D61N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 300.15 K; buffer 0.02 M potassium phosphate; cofactor NADH

column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row D61N, NADH Isomerase2 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NADH Isomerase2 block; Km cell = 7.2 uM; kcat cell = 46.1 min^-1; kcat/Km cell = 6.4.

raw_value_unit_evidence: Table 6, enzyme row D61N, NADH Isomerase2 block: Km = 7.2 uM; kcat = 46.1 min^-1; kcat/Km = 6.4 under the printed column head kcat/Km min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P26439 and applied mutation signature E192A to reconstruct the assayed variant sequence.

column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row E192A, NADH Isomerase2 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NADH Isomerase2 block; Km cell = 2.5 uM; kcat cell = 18.8 min^-1; kcat/Km cell = 7.5.

raw_value_unit_evidence: Table 6, enzyme row E192A, NADH Isomerase2 block: Km = 2.5 uM; kcat = 18.8 min^-1; kcat/Km = 7.5 under the printed column head kcat/Km min^-1 uM^-1.


organism: Klebsiella aerogenes

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

assay_conditions_summary: pH 7.1; buffer pH 7; cofactor NADH

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (DPNH) = 1.8 x 10^-4 M; DPNH is historical NADH label; normalized to 0.18 mM.

normalized_value_unit_evidence: Km=0.18 mM after M -> mM conversion

raw_value_unit_evidence: Km=1.8 x 10^-4 M (paper unit M)

row_label: K_m (DPNH)

table_label: Table VIII: Michaelis-Menten constants of reactants in D-sorbitol 6-phosphate and D-mannitol 1-phosphate dehydrogenases


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

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (DPN) = 4.2 x 10^-4 M; DPN is historical NAD+ label; normalized to 0.42 mM.

normalized_value_unit_evidence: Km=0.42 mM after M -> mM conversion

raw_value_unit_evidence: Km=4.2 x 10^-4 M (paper unit M)

row_label: K_m (DPN)


substrate_name: sorbitol 6-phosphate

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

assay_conditions_summary: pH 9; buffer pH 9

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (D-sorbitol 6-phosphate) = 6.25 x 10^-3 M; normalized to 6.25 mM.

normalized_value_unit_evidence: Km=6.25 mM after M -> mM conversion

raw_value_unit_evidence: Km=6.25 x 10^-3 M (paper unit M)

row_label: K_m (D-sorbitol 6-phosphate)

substrate: sorbitol 6-phosphate


assay_conditions_summary: pH 7.1; buffer pH 7

column_label: Table VIII, D-sorbitol 6-phosphate dehydrogenase column, row K_m (D-fructose 6-phosphate) = 1.05 x 10^-2 M; normalized to 10.5 mM.

normalized_value_unit_evidence: Km=10.5 mM after M -> mM conversion

raw_value_unit_evidence: Km=1.05 x 10^-2 M (paper unit M)

row_label: K_m (D-fructose 6-phosphate)


column_label: Table 5 (substrate kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the 3beta-HSD1 substrate block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the Isomerase2 substrate block. Table 5, enzyme row D61N, 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the 3beta-HSD1 block; Km cell = 4.7 uM; kcat cell = 2.8 min^-1; kcat/Km cell = 0.60.

raw_value_unit_evidence: Table 5, enzyme row D61N, 3beta-HSD1 block: Km = 4.7 uM; kcat = 2.8 min^-1; kcat/Km = 0.60 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 5 (substrate kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the 3beta-HSD1 substrate block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the Isomerase2 substrate block. Table 5, enzyme row E192A, 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the 3beta-HSD1 block; Km cell = 30.4 uM; kcat cell = 1.8 min^-1; kcat/Km cell = 0.06.

raw_value_unit_evidence: Table 5, enzyme row E192A, 3beta-HSD1 block: Km = 30.4 uM; kcat = 1.8 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row D61N, NAD 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NAD 3beta-HSD1 block; Km cell = 64.3 uM; kcat cell = 3.7 min^-1; kcat/Km cell = 0.06.

raw_value_unit_evidence: Table 6, enzyme row D61N, NAD 3beta-HSD1 block: Km = 64.3 uM; kcat = 3.7 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km min^-1 uM^-1.


column_label: Table 6 (cofactor kinetics for the 3beta-HSD and isomerase activities of the purified mutant and wild-type enzymes), printed column heads Purified Enzyme | Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NAD 3beta-HSD1 block and Km uM | kcat min^-1 | kcat/Km min^-1 uM^-1 under the NADH Isomerase2 block. Table 6, enzyme row E192A, NAD 3beta-HSD1 block; columns Km uM, kcat min^-1 and kcat/Km min^-1 uM^-1 of the NAD 3beta-HSD1 block; Km cell = 35.1 uM; kcat cell = 1.6 min^-1; kcat/Km cell = 0.05.

raw_value_unit_evidence: Table 6, enzyme row E192A, NAD 3beta-HSD1 block: Km = 35.1 uM; kcat = 1.6 min^-1; kcat/Km = 0.05 under the printed column head kcat/Km min^-1 uM^-1.


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

enzyme: 11-beta-hydroxysteroid dehydrogenase 1


column_label: PMID 14973125 Table II, Reduction of 7-ketocholesterol, Rat row, Km (nM) = 776 +/- 154.

normalized_value_unit_evidence: Km normalized_value=0.000776 mM.

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

row_label: Reduction of 7-ketocholesterol / Rat


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+

proof_lines:
Bbg-3βHSD
dehydroepiandrosterone
Bufo gargarizans


substrate_name: pregnenolone

proof_lines:
Bbg-3βHSD
pregnenolone
Bufo gargarizans

substrate: pregnenolone


proof_lines:
kcat could not be accurately determined
pregnenolone


proof_lines:
second-order rate constants (kcat/Km)
dehydroepiandrosterone


organism: Mus musculus

column_label: Table 2 reports 7-Ketocholesterol / Reduction Km = 1269 +/- 282 uM.

raw_value_unit_evidence: Km raw_value=1269 uM raw_unit=uM

row_label: Recombinant protein / 7-Ketocholesterol / Reduction

table_label: PMC3694296 Table 2


assay_conditions_summary: cofactor NADP+

column_label: Table 2 reports Corticosterone / Oxidation Km = 1.78 +/- 0.56 uM.

raw_value_unit_evidence: Km raw_value=1.78 uM raw_unit=uM

row_label: Recombinant protein / Corticosterone / Oxidation


substrate_name: cortisol

substrate: cortisol


substrate_name: Cortisol

assay_conditions_summary: pH 9.2; 310.15 K; cofactor NADP+

column_label: Table II; Human row; cortisol columns Km, kcat, kcat/Km

row_label: Human; enzyme s, delta_tm; cortisol columns

table_label: Table II

substrate: Cortisol


assay_conditions_summary: pH 6; 310.15 K; cofactor NADPH

column_label: Table II; Human row; cortisone columns Km, kcat, kcat/Km

normalized_value_unit_evidence: Km 0.0008 mM; kcat 0.027 s^-1 after rounding; paper kcat_over_km 25.0 s^-1 mM^-1

row_label: Human; enzyme s, delta_tm; cortisone columns


substrate_name: dehydroepiandrosterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H156Y with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

substrate: dehydroepiandrosterone


organism: Saimiri sciureus


column_label: Table II; Guinea pig row; cortisone columns Km, kcat, kcat/Km

row_label: Guinea pig; enzyme s, delta_tm; cortisone columns


substrate_name: corticosterone

column_label: Table IV row 1F, Oxidation column group, Km column = 163 +/- 18 nM for corticosterone oxidation.

raw_value_unit_evidence: Km raw_value=163 raw_unit=nM

row_label: 1F; oxidation of corticosterone

table_label: Table IV


column_label: Table IV row 1F, Oxoreduction column group, Km column = 594 +/- 127 nM for 11-dehydrocorticosterone reduction.

raw_value_unit_evidence: Km raw_value=594 raw_unit=nM

row_label: 1F; oxoreduction of 11-dehydrocorticosterone


substrate_name: dihydrotestosterone (in the presence of NADH)

assay_conditions_summary: cofactor NADH

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


proof_lines:
11-oxygenated steroids
substrate efficiencies
Km values


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Q105M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2


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

row_label: Reduction of 7-ketocholesterol / Human

column_label: Km

metric: Km

raw_unit: nM

normalized_unit: mM

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


assay_conditions_summary: pH 6; cofactor NADPH

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

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

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

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


column_label: PDF p.624 states 11beta-HSD1 catalysed reduction of 7-oxoLCA with apparent Km=980 +/- 210 nM.

normalized_value_unit_evidence: 980 nM converts to 0.00098 mM.

raw_value_unit_evidence: Results text reports apparent Km of 980 +/- 210 nM for 7-oxoLCA.

row_label: Human 11beta-HSD1 / 7-oxoLCA reduction

table_label: Biochemical Journal PDF p.624 Results / Figure 4 kinetic text


enzyme_display_name: UniProt A7A7R9

organism: Bifidobacterium adolescentis

assay_conditions_summary: pH 5

enzyme: UniProt A7A7R9


enzyme_display_name: 20alpha-hydroxysteroid dehydrogenase

organism: Tetrahymena thermophila

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

enzyme: 20alpha-hydroxysteroid dehydrogenase


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


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


substrate_name: ethyl acetoacetate

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

substrate: ethyl acetoacetate


substrate_name: acetoacetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetoacetyl-CoA


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


substrate_name: ethyl 4-chloroacetoacetate

smiles: CCOC(=O)CC(=O)CCl

substrate: ethyl 4-chloroacetoacetate


substrate_name: isatin

substrate: isatin


substrate_name: methyl acetoacetate

smiles: CC(=O)CC(=O)OC

substrate: methyl acetoacetate


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


substrate_name: ethyl 3-oxovalerate

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

substrate: ethyl 3-oxovalerate


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


substrate_name: acetoin

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

substrate: acetoin


substrate_name: ethyl benzoylacetate

substrate: ethyl benzoylacetate


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: D-Lactaldehyde

smiles: CC(C=O)O

substrate: D-Lactaldehyde


substrate_name: DL-glyceraldehyde 3-phosphate

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

substrate: DL-glyceraldehyde 3-phosphate


substrate_name: (S)-ethyl 3-hydroxybutyrate

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

substrate: (S)-ethyl 3-hydroxybutyrate


substrate_name: n-octyl acetoacetate

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

substrate: n-octyl acetoacetate


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: n-hexyl acetoacetate

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

substrate: n-hexyl acetoacetate


substrate_name: n-butyl acetoacetate

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

substrate: n-butyl acetoacetate


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


substrate_name: benzyl acetoacetate

substrate: benzyl acetoacetate


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


substrate_name: NADP+

substrate: NADP+


substrate_name: ethyl 2-methylacetoacetate

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

substrate: ethyl 2-methylacetoacetate


substrate_name: (S)-methyl 3-hydroxybutyrate

smiles: CC(CC(=O)OC)O

substrate: (S)-methyl 3-hydroxybutyrate


smiles: CC(C(C)O)O


enzyme_display_name: estradiol 17alpha-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: Epitestosterone

enzyme: estradiol 17alpha-dehydrogenase

substrate: Epitestosterone


substrate_name: 17alpha-estradiol 3-glucuronide

substrate: 17alpha-estradiol 3-glucuronide


organism: Chlorobaculum tepidum


substrate_name: sepiapterin

substrate: sepiapterin


substrate_name: diacetyl

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

substrate: diacetyl


organism: Eubacterium sp.


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


enzyme_display_name: ureidoglycolate dehydrogenase [NAD(P)+]

organism: Arthrobacter allantoicus

enzyme: ureidoglycolate dehydrogenase [NAD(P)+]


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: (R,S)-ureidoglycolate

substrate: (R,S)-ureidoglycolate


organism: Sus scrofa

assay_conditions_summary: 277.15 K; cofactor NADPH

proof_lines: 10 mM cysteine, at 4°C until activity decreases to half of the initial value


substrate_name: NADH

assay_conditions_summary: 277.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: 21-hydroxysteroid dehydrogenase (NAD+)

organism: Ovis aries aries

proof_lines:
NAD dehydrogenase I
NAD dehydrogenase II

enzyme: 21-hydroxysteroid dehydrogenase (NAD+)


enzyme_display_name: 21-hydroxysteroid dehydrogenase (NADP+)

enzyme: 21-hydroxysteroid dehydrogenase (NADP+)


organism: Gallus gallus


organism: Equus caballus


proof_lines:
isozyme HSD-I
isozyme HSD-II


organism: Bos taurus


organism: Ovis aries

substrate_name: NADH; 21-Dehydrocortisone; H+

substrate: NADH; 21-Dehydrocortisone; H+


substrate_name: 21-Dehydrocortisone; H+; NADPH

substrate: 21-Dehydrocortisone; H+; NADPH


organism: Rattus norvegicus

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


substrate_name: D,L-glyceraldehyde

assay_conditions_summary: pH 6; 298.15 K; buffer and the printed 25 C; cofactor NADPH

column_label: Table 3 (Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates) prints a substrate column, a cofactor column and three numeric columns whose printed heads are kcat (min^-1), Km (uM) and kcat/Km (min^-1 uM^-1) in that order. The cited cell set is Table 3, substrate row D,L-Glyceraldehyde, cofactor NADPH: kcat (min^-1) = 12.9; Km (uM) = 120000; kcat/Km (min^-1 uM^-1) = 0.00011. The printed uncertainty of that row is kcat 12.9 +/- 0.3; the Km cell and the efficiency cell are printed with no uncertainty.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.9 min^-1; 12.9 / 60 = 0.215 s^(-1), and the catalog carries 0.215 s^(-1). Km: printed Table 3 cell 120000 uM; 120000 / 1000 = 120.0 mM, and the catalog carries 120.0 mM. kcat/Km: printed Table 3 cell 0.00011 min^-1 uM^-1; 1 min^-1 uM^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 0.00011 x 16.666666666666668 = 0.0018333333333333335 s^(-1)*mM^(-1). The catalog carries the full-precision quotient of the two printed component cells, 0.215 / 120.0 = 0.0017916666666666667 s^(-1)*mM^(-1), and that quotient written to the five decimal places the printed efficiency column uses is 0.00011 min^-1 uM^-1, the printed cell itself, so the printed cell corroborates the held quotient at the paper's own precision.

raw_value_unit_evidence: Table 3, substrate row D,L-Glyceraldehyde, cofactor NADPH: kcat cell 12.9 in the column headed kcat, printed unit min^-1; Km cell 120000 in the column headed Km, printed unit uM; kcat/Km cell 0.00011 in the column headed kcat/Km, printed unit min^-1 uM^-1.

table_label: Table 3: Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates (Biochem. J. 1999, 341(Pt 3):853-859)

substrate: D,L-glyceraldehyde


assay_conditions_summary: pH 7.8; 298.15 K; buffer and the printed 25 C; cofactor NADP+

column_label: Table 3 (Kinetic constants of 20alpha-HSD for endogenous steroids and aldose reductase substrates) prints a substrate column, a cofactor column and three numeric columns whose printed heads are kcat (min^-1), Km (uM) and kcat/Km (min^-1 uM^-1) in that order. The cited cell set is Table 3, substrate row 20alpha-OH-5alpha-pregnan-3-one (CNS steroid), cofactor NADP+: kcat (min^-1) = 47.1; Km (uM) = 13.8; kcat/Km (min^-1 uM^-1) = 3.4. The printed uncertainties of that row are kcat 47.1 +/- 4.3 and Km 13.8 +/- 3.5; the efficiency cell is printed with no uncertainty, and the Results paragraph of the paper prints the same efficiency again in words as 3.4 min^-1 uM^-1 for 20alpha-hydroxy-5alpha-pregnan-3-one.

normalized_value_unit_evidence: kcat: printed Table 3 cell 47.1 min^-1; 47.1 / 60 = 0.785 s^(-1), the value the catalog already carries. Km: printed Table 3 cell 13.8 uM; 13.8 / 1000 = 0.0138 mM, and the catalog carries 0.013 mM, so the paper cell supplies 0.0138 mM. kcat/Km: printed Table 3 cell 3.4 min^-1 uM^-1; 1 min^-1 uM^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 3.4 x 16.666666666666668 = 56.66666666666667 s^(-1)*mM^(-1), which the paper prints as its own efficiency cell and which this record adopts in place of the held 60.38461538461539 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 20alpha-OH-5alpha-pregnan-3-one (CNS steroid), cofactor NADP+: kcat cell 47.1 in the column headed kcat, printed unit min^-1; Km cell 13.8 in the column headed Km, printed unit uM; kcat/Km cell 3.4 in the column headed kcat/Km, printed unit min^-1 uM^-1.


substrate_name: NADPH

assay_conditions_summary: pH 6.8; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 6.8; cofactor NADP+


substrate_name: progesterone

substrate: progesterone


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature S157A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.4; buffer 50 mM phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row S157A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 3.2 uM; kcat cell = 0.92 min^-1; kcat/Km cell = 0.29 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | S157A hSPR, the site-directed S157A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 3.2 uM | Table 5 kcat Redox 0.92 min^-1 | Table 5 kcat/Km Redox printed cell 0.29 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 3.2 uM; 1 uM is 1/1000 mM, so 3.2 / 1000 = 0.0032 mM; the export stores 0.0032 mM. kcat: printed kcat Redox cell 0.92 min^-1; the printed turnover column is per MINUTE, so 0.92 / 60 = 0.015333333333333334 s^(-1); the export stores 0.0048 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.29 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.29 x 16.666666666666668 = 4.833333333333333 s^-1 mM^-1; the export stores 1.4999999999999998 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row S157A, Redox columns: Km = 3.2 uM; kcat = 0.92 min^-1; kcat/Km = 0.29 under the printed column head kcat/Km Redox (min^-1 uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature N99A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.4; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row N99A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 94.1 uM; kcat cell = 3.3 min^-1; kcat/Km cell = 0.04 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | N99A hSPR, the site-directed N99A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 94.1 uM | Table 5 kcat SPR 3.3 min^-1 | Table 5 kcat/Km SPR printed cell 0.04 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 94.1 uM; 1 uM is 1/1000 mM, so 94.1 / 1000 = 0.0941 mM; the export stores 0.094 mM. kcat: printed kcat SPR cell 3.3 min^-1; the printed turnover column is per MINUTE, so 3.3 / 60 = 0.05499999999999999 s^(-1); the export stores 0.0053 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.04 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.04 x 16.666666666666668 = 0.6666666666666667 s^-1 mM^-1; the export stores 0.05638297872340425 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row N99A, SPR columns: Km = 94.1 uM; kcat = 3.3 min^-1; kcat/Km = 0.04 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row N99A, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row S157A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 50.3 uM; kcat cell = 3.5 min^-1; kcat/Km cell = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | S157A hSPR, the site-directed S157A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 50.3 uM | Table 5 kcat SPR 3.5 min^-1 | Table 5 kcat/Km SPR printed cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row S157A, SPR columns: Km = 50.3 uM; kcat = 3.5 min^-1; kcat/Km = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row S157A, SPR columns


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature Δ257 to reconstruct the assayed variant sequence.

mutation_type: deletion


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature K174L to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row K174L; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 27.7 uM; kcat cell = 1.79 min^-1; kcat/Km cell = 0.06 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | K174L hSPR, the site-directed K174L single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 27.7 uM | Table 5 kcat Redox 1.79 min^-1 | Table 5 kcat/Km Redox printed cell 0.06 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 27.7 uM; 1 uM is 1/1000 mM, so 27.7 / 1000 = 0.0277 mM; the export stores 0.027 mM. kcat: printed kcat Redox cell 1.79 min^-1; the printed turnover column is per MINUTE, so 1.79 / 60 = 0.029833333333333333 s^(-1); the export stores 0.027 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.06 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.06 x 16.666666666666668 = 1.0 s^-1 mM^-1; the export stores 1.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row K174L, Redox columns: Km = 27.7 uM; kcat = 1.79 min^-1; kcat/Km = 0.06 under the printed column head kcat/Km Redox (min^-1 uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature G18D to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row G18D; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 464.1 uM; kcat cell = 2.90 min^-1; kcat/Km cell = 0.01 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | G18D hSPR, the site-directed G18D single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 464.1 uM | Table 5 kcat Redox 2.90 min^-1 | Table 5 kcat/Km Redox printed cell 0.01 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 464.1 uM; 1 uM is 1/1000 mM, so 464.1 / 1000 = 0.4641 mM; the export stores 0.464 mM. kcat: printed kcat Redox cell 2.90 min^-1; the printed turnover column is per MINUTE, so 2.90 / 60 = 0.04833333333333333 s^(-1); the export stores 0.048 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.01 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.01 x 16.666666666666668 = 0.16666666666666669 s^-1 mM^-1; the export stores 0.10344827586206896 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row G18D, Redox columns: Km = 464.1 uM; kcat = 2.90 min^-1; kcat/Km = 0.01 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row G18D, Redox columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature R42G to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row R42G; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 45.7 uM; kcat cell = 3.2 min^-1; kcat/Km cell = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | R42G hSPR, the site-directed R42G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 45.7 uM | Table 5 kcat SPR 3.2 min^-1 | Table 5 kcat/Km SPR printed cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 45.7 uM; 1 uM is 1/1000 mM, so 45.7 / 1000 = 0.0457 mM; the export stores 0.045 mM. kcat: printed kcat SPR cell 3.2 min^-1; the printed turnover column is per MINUTE, so 3.2 / 60 = 0.05333333333333334 s^(-1); the export stores 0.053 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.07 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.07 x 16.666666666666668 = 1.166666666666667 s^-1 mM^-1; the export stores 1.1777777777777778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row R42G, SPR columns: Km = 45.7 uM; kcat = 3.2 min^-1; kcat/Km = 0.07 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row R42G, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row K174L; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 169.8 uM; kcat cell = 5.4 min^-1; kcat/Km cell = 0.03 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | K174L hSPR, the site-directed K174L single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 169.8 uM | Table 5 kcat SPR 5.4 min^-1 | Table 5 kcat/Km SPR printed cell 0.03 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 169.8 uM; 1 uM is 1/1000 mM, so 169.8 / 1000 = 0.1698 mM; the export stores 0.169 mM. kcat: printed kcat SPR cell 5.4 min^-1; the printed turnover column is per MINUTE, so 5.4 / 60 = 0.09000000000000001 s^(-1); the export stores 0.09 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.03 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.03 x 16.666666666666668 = 0.5 s^-1 mM^-1; the export stores 0.5325443786982248 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row K174L, SPR columns: Km = 169.8 uM; kcat = 5.4 min^-1; kcat/Km = 0.03 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row K174L, SPR columns