sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15428 and applied mutation signature V186I 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), 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

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


enzyme_display_name: Geraniol dehydrogenase

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

substrate_name: Unknown

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

km_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

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

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: Unknown

status: unverified

source: uniprot


organism: Homo sapiens

substrate_name: 3beta-Hydroxyandrost-5-en-17-one; NAD+

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

km_unit: mM

assay_conditions_summary: cofactor NAD+

substrate: 3beta-Hydroxyandrost-5-en-17-one; NAD+


organism: Mus musculus

substrate_name: NAD+; Pregnenolone

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

substrate: NAD+; Pregnenolone


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


enzyme_display_name: steroid Delta-isomerase

organism: Sus scrofa

substrate_name: NAD+; 7alpha-Hydroxycholesterol

enzyme: steroid Delta-isomerase

substrate: NAD+; 7alpha-Hydroxycholesterol


source_db: brenda

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.

mutation_type: substitution

proof_lines:
mutant R195R, pH 7.4, 27°C
pH 7.4, 27°C, mutant R195R

source: brenda


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.

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


ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M187T with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M187T, in 0.02 M potassium phosphate, pH 7.4, at 27°C


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


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.


organism: Mycobacterium tuberculosis


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


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

substrate_name: NAD+; Cortisol

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

sequence_source: multiple

assay_conditions_summary: pH 7.4; cofactor NAD+

source_databases_merged: sabio_rk skid uniprot

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: NAD+; Cortisol


organism: Cavia porcellus

substrate_name: H+; Cortisone; NADPH

assay_conditions_summary: cofactor NADPH

substrate: H+; Cortisone; NADPH


organism: Mesocricetus auratus

substrate_name: 7alpha-Hydroxycholesterol; NADP+

assay_conditions_summary: cofactor NADP+

substrate: 7alpha-Hydroxycholesterol; NADP+


organism: Rattus norvegicus

substrate_name: NADP+; Corticosterone

substrate: NADP+; Corticosterone


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

verification_status: verified

column_label: Table 2 row 7beta-hydroxycholesterol / Oxidation; Km (uM) column = 327.60 +/- 98.50.

raw_value_unit_evidence: Km raw_value=327.60 +/- 98.50 raw_unit=uM

row_label: Recombinant protein / 7beta-hydroxycholesterol / Oxidation

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

enzyme: 11-beta-hydroxysteroid dehydrogenase 1

status: verified


organism: Saimiri sciureus


enzyme_display_name: 20alpha-hydroxysteroid dehydrogenase

organism: Tetrahymena pyriformis

substrate_name: 17alpha-Hydroxyprogesterone; NADPH; H+

sequence: LAKTVPLNDGTNFPIFGG

wild_type_sequence: LAKTVPLNDGTNFPIFGG

enzyme: 20alpha-hydroxysteroid dehydrogenase

substrate: 17alpha-Hydroxyprogesterone; NADPH; H+


substrate_name: Progesterone; H+; NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: binding to NADPH-enzyme complex via ordered bi-bi-mechanism

proof_lines: pH 6.5, temperature not specified in the publication

source_databases_merged: sabio_rk brenda uniprot

substrate: Progesterone; H+; NADPH


substrate_name: NADPH; H+; Progesterone

substrate: NADPH; H+; Progesterone


organism: Oryctolagus cuniculus


proof_lines:
+/-1.6
NADP analog
pH 7.8, 23°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F311L with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant F311L, pH and temperature not specified in the publication


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

proof_lines: wild-type, 25°C, pH not specified in the publication

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

proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L308V to reconstruct the assayed variant sequence.

proof_lines: mutant L308V, pH and temperature not specified in the publication

proof_lines: mutant L308V, 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F311A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant F311A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L54V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; buffer 0.1 M potassium phosphate

proof_lines: mutant L54V, pH and temperature not specified in the publication

proof_lines: mutant enzyme L54V, in 0.1 M potassium phosphate buffer, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L306A to reconstruct the assayed variant sequence.

proof_lines: mutant L306A, pH and temperature not specified in the publication

proof_lines: mutant enzyme L306A, in 0.1 M potassium phosphate buffer, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L308A to reconstruct the assayed variant sequence.

proof_lines: mutant L308A, 25°C, pH not specified in the publication

proof_lines: mutant enzyme L308A, in 0.1 M potassium phosphate buffer, pH 7.4


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H222S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H222S, in 0.1 M potassium phosphate buffer, pH 7.4


enzyme_display_name: sepiapterin reductase

substrate_name: NADPH; Sepiapterin; H+

enzyme: sepiapterin reductase

substrate: NADPH; Sepiapterin; H+


substrate_name: H+; Sepiapterin; NADPH

substrate: H+; Sepiapterin; NADPH


substrate_name: Sepiapterin; NADPH; H+

substrate: Sepiapterin; NADPH; H+


enzyme_display_name: Sepiapterin reductase

organism: Dictyostelium discoideum

enzyme: Sepiapterin reductase


enzyme_display_name: glycerol 2-dehydrogenase (NADP+)

organism: Trichoderma reesei

substrate_name: L-Glyceraldehyde; NADPH; H+

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

enzyme: glycerol 2-dehydrogenase (NADP+)

substrate: L-Glyceraldehyde; NADPH; H+


enzyme_display_name: Glycerol 2-dehydrogenase (NADP(+))

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Glycerol 2-dehydrogenase (NADP(+))


enzyme_display_name: 3-hydroxybutyryl-CoA dehydrogenase

organism: Clostridium acetobutylicum

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.5; cofactor CoA

data_origin: experimental

enzyme: 3-hydroxybutyryl-CoA dehydrogenase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


enzyme_display_name: 7alpha-hydroxysteroid dehydrogenase

organism: Bacteroides fragilis

enzyme: 7alpha-hydroxysteroid dehydrogenase


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: erythrulose reductase

organism: Gallus gallus

substrate_name: NADPH; D-Erythrulose; H+

enzyme: erythrulose reductase

substrate: NADPH; D-Erythrulose; H+


enzyme_display_name: 2-dehydropantoate 2-reductase

organism: Escherichia coli

substrate_name: 2-Dehydropantoate; H+; NADPH

enzyme: 2-dehydropantoate 2-reductase

substrate: 2-Dehydropantoate; H+; NADPH


organism: Thermococcus kodakarensis

substrate_name: D-pantoate

assay_conditions_summary: pH 6.4; 343.15 K; cofactor NADPH

proof_lines: kcat is 23.1 sec(-1) toward ketopantoate (in the presence of NADH). kcat is 19.7 sec(-1) toward NADH. kcat is 2.22 sec(-1) toward NADPH.

source_databases_merged: brenda uniprot

substrate: D-pantoate


enzyme_display_name: UniProt A0A0J9X283

organism: Staphylococcus aureus

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A0A0J9X283

source: skid


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

substrate_name: Unknown

substrate: Unknown


substrate_name: O2; H+; NADH; 4,4-Dimethyl-5alpha-cholest-7-en-3beta-ol

assay_conditions_summary: cofactor NADH


organism: Homo sapiens

substrate_name: NSDHL; NADH

substrate: NSDHL; NADH


organism: Saccharomyces cerevisiae

proof_lines:
pH 7.5, 30°C
in vitro inhibition, pH 7.5, 30°C


enzyme_display_name: D-xylose 1-dehydrogenase

organism: Arthrobacter nicotinovorans

substrate_name: NAD+; D-Xylose

enzyme: D-xylose 1-dehydrogenase

substrate: NAD+; D-Xylose


organism: Caulobacter vibrioides

substrate_name: D-Xylose; NAD+

substrate: D-Xylose; NAD+


enzyme_display_name: 12alpha-hydroxysteroid dehydrogenase

organism: Clostridium sp. (strain ATCC 29733 / VPI C48-50)

enzyme: 12alpha-hydroxysteroid dehydrogenase


organism: Rattus norvegicus


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


enzyme_display_name: D-xylose 1-dehydrogenase (NADP+)

organism: Sus scrofa

substrate_name: D-Xylose; NADP+

enzyme: D-xylose 1-dehydrogenase (NADP+)

substrate: D-Xylose; NADP+


organism: Macaca fuscata

substrate_name: NADP+; D-Xylose

substrate: NADP+; D-Xylose


organism: Canis familiaris


organism: Oryctolagus cuniculus


organism: Trichoderma reesei


organism: Halobacterium volcanii


enzyme_display_name: geraniol dehydrogenase

organism: Ocimum basilicum

substrate_name: NADP+; Geraniol

enzyme: geraniol dehydrogenase

substrate: NADP+; Geraniol


enzyme_display_name: carbonyl reductase (NADPH)

substrate_name: 4-Nitroacetophenone; NADPH

enzyme: carbonyl reductase (NADPH)

substrate: 4-Nitroacetophenone; NADPH


substrate_name: Menadione; NADPH; H+

assay_conditions_summary: pH 8.4; 298.15 K; cofactor NADPH

proof_lines: CBR1 V88 with cofactor NADPH, with a fixed 0.4 mM daunorubicin concentration

source_databases_merged: sabio_rk brenda skid

substrate: Menadione; NADPH; H+


organism: Candida magnoliae

substrate_name: H+; Ethyl 4-chloro-3-oxobutanoate; NADPH


substrate_name: NADPH; H+; Menadione

proof_lines: kcat is 0.55 min(-1) with menadione as substrate (PubMed:18493841). kcat is 0.70 min(-1) with 4-benzoylpyridine as substrate (PubMed:18493841). kcat is 0.59 min(-1) with 4-nitorobenzaldehyde as substrate (PubMed:18493841).

substrate: NADPH; H+; Menadione


organism: Mus musculus

substrate_name: H+; Pyridine-3-aldehyde; NADPH

substrate: H+; Pyridine-3-aldehyde; NADPH


substrate_name: NADPH; 9,10-Phenanthroquinone; H+

substrate: NADPH; 9,10-Phenanthroquinone; H+


substrate_name: NADPH; S-Nitrosoglutathione; H+

substrate: NADPH; S-Nitrosoglutathione; H+


organism: Caenorhabditis elegans

substrate_name: NADPH; H+; Isatin

substrate: NADPH; H+; Isatin


organism: Mesocricetus auratus

substrate_name: Acetone; H+; NADH

substrate: Acetone; H+; NADH


enzyme_display_name: UniProt Q28960

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

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.

source_databases_merged: skid uniprot

enzyme: UniProt Q28960


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Homo sapiens

substrate_name: 5beta-Androstan-17b-ol-3-one (at pH7.4)

proof_lines: kcat is 3.4 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4) (PubMed:23128527). kcat is 11.8 min(-1) with 5beta-Androstan-17beta-ol-3-one as substrate (at pH7.4) (PubMed:23128527). kcat is 475 min(-1) with Isatin as substrate

proof_lines: kcat is 3.8 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4) (PubMed:18571493). kcat is 5 min(-1) with 5beta-Androstan-17beta-ol-3-one as substrate (at pH7.4) (PubMed:18571493). kcat is 4.6 min(-1) with 5beta-Androstane-3,17-d

substrate: 5beta-Androstan-17b-ol-3-one (at pH7.4)


substrate_name: Unknown

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: Unknown


substrate_name: R-(+)-1-Phenyl-1-butanol (at pH7.4)

proof_lines: kcat is 45 min(-1) with all-trans-Retinal as substrate (at pH7.4) (PubMed:12604222). kcat is 990 min(-1) with isatin as substrate (at pH6) (PubMed:12604222). kcat is 1180 min(-1) with 1-phenyl-1,2-propanedione as substrate (at pH6) (PubMed:

substrate: R-(+)-1-Phenyl-1-butanol (at pH7.4)


enzyme_display_name: prostaglandin-F synthase

organism: Bos taurus

substrate_name: H+; NADPH; 9,10-Phenanthroquinone

proof_lines: prostaglandin D2 11-ketoreductase activity

enzyme: prostaglandin-F synthase

substrate: H+; NADPH; 9,10-Phenanthroquinone


assay_conditions_summary: pH 7; buffer pH 7; cofactor NADPH

column_label: PMC Table 1 row AKR1C1 / PQ reports Km 0.73 +/- 0.2 uM and kcat 35 +/- 6.1 min^-1; methods identify PQ reduction with NADPH at pH 7.0 and 37 deg C.

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

raw_value_unit_evidence: kcat raw_value=35 raw_unit=min^-1; Km raw_value=0.73 raw_unit=uM

row_label: AKR1C1 / PQ

table_label: Table 1


substrate_name: 9,10-Phenanthroquinone; NADPH; H+

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

substrate: 9,10-Phenanthroquinone; NADPH; H+


column_label: PMC Table 1 row AKR1C2 / PQ reports Km 1.1 +/- 0.4 uM and kcat 110 +/- 18 min^-1; methods identify PQ reduction with NADPH at pH 7.0 and 37 deg C.

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

raw_value_unit_evidence: kcat raw_value=110 raw_unit=min^-1; Km raw_value=1.1 raw_unit=uM

row_label: AKR1C2 / PQ


substrate_name: Prostaglandin H2; H+; NADPH

substrate: Prostaglandin H2; H+; NADPH


substrate_name: NADPH; H+; Prostaglandin H2

substrate: NADPH; H+; Prostaglandin H2


organism: Trypanosoma brucei


substrate_name: prostaglandin PGH2

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

proof_lines: recombinant liver-type isozyme, mutant H170C, 37°C

proof_lines: recombinant liver-type isozyme mutant H170C, 37°C

substrate: prostaglandin PGH2


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

proof_lines: recombinant liver-type isozyme, mutants R91Q, R223L and N306Y, 37°C


proof_lines: recombinant liver-type isozyme, mutant R27E, 37°C

proof_lines: recombinant liver-type isozyme mutant R27E, 37°C


substrate_name: prostaglandin PGD2

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

proof_lines: recombinant wild-type liver-type isozyme, 37°C

substrate: prostaglandin PGD2


proof_lines: recombinant liver-type isozyme, mutant K225S, 37°C

proof_lines: recombinant liver-type isozyme mutant K225S, 37°C


proof_lines: recombinant liver-type isozyme, mutant S301R, 37°C

proof_lines: recombinant liver-type isozyme mutant S301R, 37°C


proof_lines: recombinant liver-type isozyme mutant N306Y, 37°C


proof_lines: recombinant liver-type isozyme mutant R91Q, 37°C


proof_lines: recombinant liver-type isozyme mutant R223L, 37°C


enzyme_display_name: prostaglandin-E2 9-reductase

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

enzyme: prostaglandin-E2 9-reductase


enzyme_display_name: Carbonyl reductase [NADPH] 1

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


organism: Escherichia coli


enzyme_display_name: Riboflavin biosynthesis protein PYRR, chloroplastic

organism: Zea mays

proof_lines: kcat is 5.0 sec(-1) with 2,5-diamino-6-hydroxy-4-(5-phospho-D-ribosylamino)pyrimidine as substrate. kcat is 9.39 sec(-1) with 5-amino-6-(5-phospho-D-ribosylamino)uracil as substrate.


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Oryza sativa

substrate_name: H+; NADPH; Coniferaldehyde

assay_conditions_summary: pH 6.3; 303.15 K; cofactor NADPH

enzyme: cinnamyl-alcohol dehydrogenase

substrate: H+; NADPH; Coniferaldehyde


organism: Populus tremuloides

substrate_name: Sinapoyl aldehyde; H+; NADPH

substrate: Sinapoyl aldehyde; H+; NADPH


substrate_name: NADP+; Geraniol

substrate: NADP+; Geraniol


organism: Arabidopsis thaliana

substrate_name: H+; NADPH; 4-Hydroxycinnamyl aldehyde

column_label: Table 2: Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8; row AtCAD4 / substrate 1 (p-coumaryl aldehyde / 4-hydroxycinnamyl aldehyde); Km 0.047 mM; Vmax 4.4e-05 mol s^-1 g^-1; kcat 3.44 s^-1; kcat/Km 74 s^-1 mM^-1.

raw_value_unit_evidence: Km 47 uM; Vmax 44.0 pKat/ug; kcat 3.44 sec^-1; kenz 74,000 M^-1 sec^-1

substrate: H+; NADPH; 4-Hydroxycinnamyl aldehyde


substrate_name: NADPH; 4-Hydroxycinnamyl aldehyde; H+

column_label: Table 2: Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8; row AtCAD5 / substrate 1 (p-coumaryl aldehyde / 4-hydroxycinnamyl aldehyde); Km 0.013 mM; Vmax 0.0001873 mol s^-1 g^-1; kcat 14.52 s^-1; kcat/Km 1091 s^-1 mM^-1.

substrate: NADPH; 4-Hydroxycinnamyl aldehyde; H+


substrate_name: H+; Sinapoyl aldehyde; NADPH

assay_conditions_summary: pH 6.25; buffer pH 6; cofactor NADPH

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

raw_value_unit_evidence: kcat=3.93 sec^-1; Vmax=48.1 pKat/ug; Km context=2161 uM

substrate: H+; Sinapoyl aldehyde; NADPH


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD2 / substrate 1 (p-coumaryl aldehyde / 4-hydroxycinnamyl aldehyde / 4-coumaraldehyde), columns Km (uM), Vmax (pKat/ug).

raw_value_unit_evidence: Km=114 uM; Vmax=3.3 pKat/ug; kcat context=0.27 sec^-1


column_label: Table 2: Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8; row AtCAD3 / substrate 1 (p-coumaryl aldehyde / 4-hydroxycinnamyl aldehyde); Km 0.292 mM; Vmax 2.01e-05 mol s^-1 g^-1; kcat 1.65 s^-1; kcat/Km 5.6 s^-1 mM^-1.

raw_value_unit_evidence: Km 292 uM; Vmax 20.1 pKat/ug; kcat 1.65 sec^-1; kenz 5,600 M^-1 sec^-1


substrate_name: NADPH; H+; Sinapoyl aldehyde

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD8 / substrate 5 (sinapyl aldehyde / sinapoyl aldehyde), columns kcat (sec^-1), Vmax (pKat/ug).

raw_value_unit_evidence: kcat=2.25 sec^-1; Vmax=28.9 pKat/ug; Km context=898 uM

substrate: NADPH; H+; Sinapoyl aldehyde


substrate_name: NADPH; H+; Coniferaldehyde

column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD8 / substrate 3 (coniferyl aldehyde / coniferaldehyde), columns Km (uM), Vmax (pKat/ug).

raw_value_unit_evidence: Km=141 uM; Vmax=5.6 pKat/ug; kcat context=0.44 sec^-1

substrate: NADPH; H+; Coniferaldehyde


column_label: PMID 14745009 Table 2. Kinetic parameters for CAD homologues AtCAD2-5, 7, and 8. row AtCAD8 / substrate 1 (p-coumaryl aldehyde / 4-hydroxycinnamyl aldehyde / 4-coumaraldehyde), columns Vmax (pKat/ug).

raw_value_unit_evidence: Vmax=20.4 pKat/ug; Km context=302 uM; kcat context=1.59 sec^-1


organism: Oryza sativa Japonica Group

substrate_name: 4-coumaryl aldehyde

substrate: 4-coumaryl aldehyde


organism: Sorghum bicolor

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

proof_lines: isoform CAD4 mutant L119W, at pH 6.5 and 30°C


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

proof_lines: isoform CAD4 mutant A278V, at pH 6.5 and 30°C


enzyme_display_name: UniProt C5XC49

enzyme: UniProt C5XC49


enzyme_display_name: Cinnamyl alcohol dehydrogenase 1

organism: Medicago truncatula

substrate_name: Unknown

proof_lines: kcat is 15.6 sec(-1) with coumaraldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 9.1 sec(-1) with coniferaldehyde as substrate (at pH 6.25 and 30 degrees Celsius) (PubMed:25217505). kcat is 10.2 sec(-1) w

enzyme: Cinnamyl alcohol dehydrogenase 1

substrate: Unknown


organism: Sus scrofa


column_label: Table I row 4,5-Benzo[a]pyrenequinone, Km column: 0.18 +/- 0.02 uM.

raw_value_unit_evidence: Table I reports 4,5-benzo[a]pyrenequinone Km 0.18 +/- 0.02 uM.

table_label: Table I


enzyme_display_name: aldose-6-phosphate reductase (NADPH)

organism: Malus domestica

assay_conditions_summary: pH 9

proof_lines:
C-term tagged enzyme
N-term tagged enzyme
pH 9.0

enzyme: aldose-6-phosphate reductase (NADPH)


organism: Prunus persica


organism: Clostridium sardiniense


organism: Collinsella aerofaciens

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


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

enzyme: 11-beta-hydroxysteroid dehydrogenase 1


organism: Mus musculus


organism: Rattus norvegicus


organism: Mesocricetus auratus


organism: Saimiri sciureus


enzyme_display_name: 7beta-hydroxysteroid dehydrogenase

organism: Mediterraneibacter gnavus

assay_conditions_summary: pH 6

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

enzyme: 7beta-hydroxysteroid dehydrogenase


enzyme_display_name: 1,3-propanediol dehydrogenase

organism: Clostridium butyricum

substrate_name: NAD+; 1,3-Propanediol

assay_conditions_summary: cofactor NAD+

enzyme: 1,3-propanediol dehydrogenase

substrate: NAD+; 1,3-Propanediol


enzyme_display_name: Uronate dehydrogenase

organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

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

enzyme: Uronate dehydrogenase


enzyme_display_name: IMP dehydrogenase

organism: Homo sapiens

substrate_name: H2O; NAD+; IMP

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
isoform IMPDH2, at pH 8.0 and 25°C
isoform IMPDH2, pH 8.0, 25°C

enzyme: IMP dehydrogenase

substrate: H2O; NAD+; IMP


organism: Streptococcus pyogenes

substrate_name: IMP; NAD+; H2O

substrate: IMP; NAD+; H2O


organism: Saccharomyces cerevisiae

substrate_name: NAD+; IMP; H2O

substrate: NAD+; IMP; H2O


substrate_name: H2O; IMP; NAD+

substrate: H2O; IMP; NAD+


organism: Tritrichomonas foetus


organism: Leishmania donovani


organism: Toxoplasma gondii


organism: Cryptosporidium parvum


organism: Candida albicans


organism: Borrelia burgdorferi

substrate_name: IMP; H2O; NAD+

substrate: IMP; H2O; NAD+


organism: Escherichia coli


organism: Pneumocystis carinii


organism: Vigna unguiculata


organism: Eremothecium gossypii


organism: Babesia gibsoni


organism: Tritrichomonas suis

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


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


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


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


enzyme_display_name: tropinone reductase I

organism: Cochlearia officinalis

substrate_name: H+; NADPH; Tropinone

assay_conditions_summary: cofactor NADPH

enzyme: tropinone reductase I

substrate: H+; NADPH; Tropinone


organism: Datura stramonium

substrate_name: NADPH; Tropinone

substrate: NADPH; Tropinone


organism: Mus musculus

substrate_name: NADP+; Pregnanediol

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

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

substrate: NADP+; Pregnanediol


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


enzyme_display_name: Aldo-keto reductase family 1 member C2

organism: Homo sapiens

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

enzyme: Aldo-keto reductase family 1 member C2


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: 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: 17-beta-hydroxysteroid dehydrogenase type 6

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


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

substrate_name: dehydroepiandrosterone (in the presence of NAD(+))


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


substrate_name: NADH; 3-Oxopalmitoyl-CoA; H+

substrate: NADH; 3-Oxopalmitoyl-CoA; H+


assay_conditions_summary: cofactor NADP+


substrate_name: Acenaphthen-1-ol; NADP+

substrate: Acenaphthen-1-ol; NADP+


sequence: MDSKYQCVK

wild_type_sequence: MDSKYQCVK

assay_conditions_summary: pH 7

proof_lines: recombinant enzyme in intact COS-1 cells

proof_lines: pH 7.0, temperature not specified in the publication


enzyme_display_name: gluconate 2-dehydrogenase

substrate_name: 2-Dehydro-D-gluconate; H+; NADPH

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

enzyme: gluconate 2-dehydrogenase

substrate: 2-Dehydro-D-gluconate; H+; NADPH


organism: Gluconobacter oxydans


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 C15

enzyme: Aldo-keto reductase family 1 member C15


enzyme_display_name: morphine 6-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: trans-naphthalene dihydrodiol

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

proof_lines:
pH 7.4, 25°C
cosubstrate NAD+

enzyme: morphine 6-dehydrogenase

substrate: trans-naphthalene dihydrodiol


enzyme_display_name: dihydroflavonol 4-reductase

organism: Delphinium cardinale

substrate_name: dihydromyricetin

enzyme: dihydroflavonol 4-reductase

substrate: dihydromyricetin


substrate_name: dihydroquercetin

substrate: dihydroquercetin


substrate_name: dihydrokaempferol

substrate: dihydrokaempferol


enzyme_display_name: Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase

organism: Pyrus communis

substrate_name: Unknown

substrate: Unknown


organism: Malus domestica

enzyme: Bifunctional dihydroflavonol 4-reductase/flavanone 4-reductase


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_name: Phenanthrene quinone

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

substrate: Phenanthrene quinone


substrate_name: NADP+

substrate: NADP+


substrate_name: menadione

substrate: menadione


organism: [Clostridium] innocuum


substrate_name: 3-Ketoglycyrrhetic acid

substrate: 3-Ketoglycyrrhetic acid


substrate_name: NADPH

substrate: NADPH


organism: Torulaspora delbrueckii

substrate_name: Diethyl 2-methyl-3-oxosuccinate

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

substrate: Diethyl 2-methyl-3-oxosuccinate


substrate_name: Diethyl 2-methyl-3-hydroxysuccinate

substrate: Diethyl 2-methyl-3-hydroxysuccinate


substrate_name: prostaglandin I2

substrate: prostaglandin I2


enzyme_display_name: 8-oxocoformycin reductase

organism: Streptomyces antibioticus

enzyme: 8-oxocoformycin reductase


enzyme_display_name: tropinone reductase II

organism: Hyoscyamus niger

substrate_name: NADH

enzyme: tropinone reductase II

substrate: NADH


enzyme_display_name: hydroxyphenylpyruvate reductase

organism: Arabidopsis thaliana

substrate_name: phenylpyruvate

source_db: oed

enzyme: hydroxyphenylpyruvate reductase

substrate: phenylpyruvate

source: oed


organism: Wickerhamia fluorescens

substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH


substrate_name: hydroxyphenylpyruvate

substrate: hydroxyphenylpyruvate


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH


organism: Coleus scutellarioides


assay_conditions_summary: pH 7; cofactor NADPH


assay_conditions_summary: pH 7; cofactor NADH


proof_lines:
pH 7, 30°C
pH 7.0, 30°C, recombinant enzyme


organism: Alcaligenes sp.


substrate_name: testosterone

substrate: testosterone


substrate_name: NAD+

substrate: NAD+


organism: Ilyonectria destructans

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines:
reduction of androstendione, pH 7.0
oxidation of testosterone, pH 10.0
oxidation of testosterone, pH 7.4


assay_conditions_summary: pH 10

proof_lines:
oxidation of testosterone, pH 10.0
oxidation of testosterone, pH 7.4


substrate_name: androstendione

substrate: androstendione


organism: Streptomyces exfoliatus


enzyme_display_name: 12beta-hydroxysteroid dehydrogenase

organism: Clostridium paraputrificum

enzyme: 12beta-hydroxysteroid dehydrogenase


organism: Solanum tuberosum

substrate_name: Nortropinone

substrate: Nortropinone


substrate_name: tropinone

substrate: tropinone


enzyme_display_name: N-acetylhexosamine 1-dehydrogenase

organism: Pseudomonas sp.

substrate_name: N-acetyl-D-glucosamine

enzyme: N-acetylhexosamine 1-dehydrogenase

substrate: N-acetyl-D-glucosamine


proof_lines: with N-acetyl-D-glucosamine as substrate


organism: Przewalskia tangutica

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


organism: Brugmansia x candida


organism: Datura stramonium

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S148A with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y100H/S148A/E156V/L210I/L213F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y100H/S148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L210I/L213F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S148A/E156V with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y100H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y100H/S148A/E156V to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E156V with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E156V/Y100H to reconstruct the assayed variant sequence.


enzyme_display_name: carveol dehydrogenase

organism: Rhodococcus erythropolis

enzyme: carveol dehydrogenase


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Homo sapiens

substrate_name: NAD

substrate: NAD


assay_conditions_summary: cofactor NADH


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

verification_status: corrected

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

column_label: Table I / Kinetic constants of 3(alpha->beta)-HSE; row: Allo-pregnanolone / NAD+ / Iso-pregnanolone; column: Km (uM); Table I reports Allo-pregnanolone with cofactor NAD+ and product Iso-pregnanolone: Km 3.0 uM. normalized to Km=0.003 mM.

substrate: allopregnanolone

status: corrected


substrate_name: androsterone

column_label: Table I / Kinetic constants of 3(alpha->beta)-HSE; row: ADT / NAD+ / 5alpha-Dione; column: Km (uM); Table I reports ADT with cofactor NAD+ and product 5alpha-Dione: Km 0.4 uM. normalized to Km=0.0004 mM.

row_label: ADT / NAD+ / 5alpha-Dione

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)

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


substrate_name: beta-hydroxybutyryl-CoA (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: isoursodeoxycholic acid (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: dehydrocorticosterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)


substrate_name: NAD (in the presence of beta-hydroxybutyryl-CoA, at pH 9.3 and 25 degrees Celsius)


organism: Rattus norvegicus


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


substrate_name: prostaglandin E1

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


organism: Mentha piperita

substrate_name: (-)-trans-carveol (at pH 7.5)

proof_lines: kcat is 0.02 sec(-1) with (-)-trans-carveol as substrate (at pH 7.5), kcat is 0.06 sec(-1) with (-)-trans-carveol as substrate (at pH 10), kcat is 0.002 sec(-1) with (-)-trans-isopiperitenol as substrate (at pH 7.5).

substrate: (-)-trans-carveol (at pH 7.5)


substrate_name: (-)-trans-isopiperitenol (at pH 7.5)

substrate: (-)-trans-isopiperitenol (at pH 7.5)


assay_conditions_summary: pH 7.5; cofactor NAD+


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


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


enzyme_display_name: N-acylmannosamine 1-dehydrogenase

organism: Flavobacterium sp.

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

proof_lines: value unchanged by cloning and expression in E. coli JM109

enzyme: N-acylmannosamine 1-dehydrogenase

substrate: NAD+


substrate_name: N-acetyl-D-mannosamine

substrate: N-acetyl-D-mannosamine


enzyme_display_name: Aldo-keto reductase family 1 member C3


substrate_name: progesterone

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


substrate_name: prostaglandin H2

substrate: prostaglandin H2


substrate_name: prostaglandin E2

substrate: prostaglandin E2


organism: Mesocricetus auratus

substrate_name: NADH

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

column_label: Table I (Kinetic constants for coenzymes), enzyme block 'AKR1C34', coenzyme row 'NADH'; column 'Km (uM)' = 13 with a standard deviation of 2; column 'kcat (min^-1)' = 10 with a standard deviation of 1; column 'kcat/Km (min^-1 uM^-1)' = 0.76. The AKR1C35 block of the same coenzyme row prints Km 17, kcat 6.2 and kcat/Km 0.36.

normalized_value_unit_evidence: Km: printed Table I cell 13 uM; 13 / 1000 = 0.013 mM, which is the exported value. kcat: printed Table I cell 10 min^-1; 10 / 60 = 0.16666666666666666 s^-1. kcat/Km: Printed kcat/Km cell 0.76 min^-1 uM^-1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.76 x 1000 / 60 = 12.666666666666668 s^-1 mM^-1. Closure disclosure: the quotient of this row's own printed component cells is 10 / 13 = 0.7692307692307693 min^-1 uM^-1, against the printed efficiency cell 0.76 carried at the precision of the printed column.

raw_value_unit_evidence: Table I, AKR1C34 enzyme block, coenzyme row 'NADH': Km = 13 uM; kcat = 10 min^-1; kcat/Km = 0.76 min^-1 uM^-1.

row_label: Table I, coenzyme row NADH of the AKR1C34 enzyme block

table_label: Table I: Kinetic constants for coenzymes (J. Biochem. 2015, 158(5):425-434)

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table I, row 'AKR1C34', AKR1C34 column group, columns Km, kcat and kcat/Km. The Table I column headers print Km, kcat and kcat/Km; the PDF glyph loss drops the Greek mu, so the columns are Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Every other AKR1C34/AKR1C35 row of Table I reproduces its own printed ratio under that reading. Normalizing the two printed primary cells gives Km 1.38 mM and kcat 0.0917 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.06644927536231884 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 5.5 min^-1 / 60 = 0.09166666666666666 s^-1, stated here at the exported row's stored precision as 0.0917 s^-1; 1,380 uM / 1000 = 1.38 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.0917 s^-1 / 1.38 mM = 0.06644927536231884 s^-1 mM^-1 = 5.5 min^-1 / 1,380 uM = 0.003985507246376812 min^-1 uM^-1, which rounds to the printed 0.004 cell at its one-significant-figure precision.

normalized_value_unit_evidence: metric: kcat; raw value: 5.5 ± 0.2 min^-1; raw unit: min^-1; normalized value: 0.0917 s^-1; metric: Km; raw value: 1,380 ± 450 uM; raw unit: uM; normalized value: 1.38 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.06644927536231884 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C34; coenzyme kinetic constants of Table I; 0.1 M potassium phosphate buffer, pH 7.4; 25 C; NADP+ varied as the coenzyme.

raw_value_unit_evidence: Table I row AKR1C34 / NADP+: Km 1,380 ± 450 uM; kcat 5.5 ± 0.2 min^-1; kcat/Km 0.004 min^-1 uM^-1.

row_label: AKR1C34 | NADP+

table_label: Table I. Kinetic constants for coenzymes

substrate: NADP+


substrate_name: nerol

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

proof_lines:
AKR1C35
NAD(+)-dependent
xenobiotic alicyclic alcohols

substrate: nerol


column_label: Table II, row 'R-Tetralol', AKR1C35 column group, columns Km, kcat and kcat/Km. The Table II footnote fixes the column units as Km, kcat (min^-1) and kcat/Km, with the same PDF glyph loss of the Greek mu, so Km is in uM and kcat/Km in min^-1 uM^-1, determined with 1.0 mM NAD+ as the coenzyme. Normalizing the two printed primary cells gives Km 0.095 mM and kcat 0.0075 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.07894736842105263 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 0.45 min^-1 / 60 = 0.0075 s^-1 exactly; 95 uM / 1000 = 0.095 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.0075 s^-1 / 0.095 mM = 0.07894736842105263 s^-1 mM^-1 = 0.45 min^-1 / 95 uM = 0.004736842105263158 min^-1 uM^-1, which rounds to the printed 0.005 cell at its one-significant-figure precision. The exported substrate name '(R)-1,2,3,4-tetrahydro-1-naphthol' is the systematic name of the printed row label 'R-Tetralol'; both printed cells of that row match the exported row.

normalized_value_unit_evidence: metric: kcat; raw value: 0.45 min^-1; raw unit: min^-1; normalized value: 0.0075 s^-1; metric: Km; raw value: 95 uM; raw unit: uM; normalized value: 0.095 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.07894736842105263 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; 0.1 M potassium phosphate buffer, pH 7.4; 1.0 mM NAD+ as the coenzyme; 25 C; oxidative dehydrogenase assay of Table II.

raw_value_unit_evidence: Table II row AKR1C35 / R-Tetralol: Km 95 uM; kcat 0.45 min^-1; kcat/Km 0.005 min^-1 uM^-1.

row_label: R-Tetralol | AKR1C35

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


column_label: Table II, row 'S-Tetralol', AKR1C35 column group, columns Km, kcat and kcat/Km. The Table II footnote fixes the column units as Km, kcat (min^-1) and kcat/Km, with the same PDF glyph loss of the Greek mu, so Km is in uM and kcat/Km in min^-1 uM^-1, determined with 1.0 mM NAD+ as the coenzyme. Normalizing the two printed primary cells gives Km 0.061 mM and kcat 0.105 s^-1; the kcat/Km entry is the quotient of those same two cells, 1.721311475409836 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 6.3 min^-1 / 60 = 0.105 s^-1 exactly; 61 uM / 1000 = 0.061 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.105 s^-1 / 0.061 mM = 1.721311475409836 s^-1 mM^-1 = 6.3 min^-1 / 61 uM = 0.10327868852459016 min^-1 uM^-1, which rounds to the printed 0.10 cell at its two-decimal precision. The exported substrate name '(S)-1,2,3,4-tetrahydro-1-naphthol' is the systematic name of the printed row label 'S-Tetralol'; both printed cells of that row match the exported row.

normalized_value_unit_evidence: metric: kcat; raw value: 6.3 min^-1; raw unit: min^-1; normalized value: 0.105 s^-1; metric: Km; raw value: 61 uM; raw unit: uM; normalized value: 0.061 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 1.721311475409836 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; 0.1 M potassium phosphate buffer, pH 7.4; 1.0 mM NAD+ as the coenzyme; 25 C; oxidative dehydrogenase assay of Table II.

raw_value_unit_evidence: Table II row AKR1C35 / S-Tetralol: Km 61 uM; kcat 6.3 min^-1; kcat/Km 0.10 min^-1 uM^-1.

row_label: S-Tetralol | AKR1C35


column_label: Table II, row 'S-1-Indanol', AKR1C35 column group, columns Km, kcat and kcat/Km. The Table II footnote fixes the column units as Km, kcat (min^-1) and kcat/Km, with the same PDF glyph loss of the Greek mu, so Km is in uM and kcat/Km in min^-1 uM^-1, determined with 1.0 mM NAD+ as the coenzyme. Normalizing the two printed primary cells gives Km 0.181 mM and kcat 0.1 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.5524861878453039 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 6.0 min^-1 / 60 = 0.1 s^-1 exactly; 181 uM / 1000 = 0.181 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.1 s^-1 / 0.181 mM = 0.5524861878453039 s^-1 mM^-1 = 6.0 min^-1 / 181 uM = 0.03314917127071823 min^-1 uM^-1, which rounds to the printed 0.033 cell at its three-decimal precision.

normalized_value_unit_evidence: metric: kcat; raw value: 6.0 min^-1; raw unit: min^-1; normalized value: 0.1 s^-1; metric: Km; raw value: 181 uM; raw unit: uM; normalized value: 0.181 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.5524861878453039 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; 0.1 M potassium phosphate buffer, pH 7.4; 1.0 mM NAD+ as the coenzyme; 25 C; oxidative dehydrogenase assay of Table II.

raw_value_unit_evidence: Table II row AKR1C35 / S-1-Indanol: Km 181 uM; kcat 6.0 min^-1; kcat/Km 0.033 min^-1 uM^-1.

row_label: S-1-Indanol | AKR1C35


substrate_name: trans-benzene dihydrodiol

column_label: Table II, row 'trans-Benzene dihydrodiol', AKR1C35 column group, columns Km, kcat and kcat/Km. The Table II footnote fixes the column units as Km, kcat (min^-1) and kcat/Km, with the same PDF glyph loss of the Greek mu, so Km is in uM and kcat/Km in min^-1 uM^-1, determined with 1.0 mM NAD+ as the coenzyme. Normalizing the two printed primary cells gives Km 1.0 mM and kcat 0.045 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.045 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 2.7 min^-1 / 60 = 0.045 s^-1 exactly; 1,000 uM / 1000 = 1.0 mM exactly; kcat/Km is not taken from the printed ratio cell but is the quotient of this row's own two printed cells, and it back-converts to the printed ratio cell: 0.045 s^-1 / 1.0 mM = 0.045 s^-1 mM^-1 = 2.7 min^-1 / 1,000 uM = 0.0027 min^-1 uM^-1, which rounds to the printed 0.003 cell at its one-significant-figure precision. The printed kcat and kcat/Km cells of this row carry an asterisk, which the Table II footnote assigns to an experimental-error band of 15-20% rather than to any change in the printed value; the cell value itself is 2.7.

normalized_value_unit_evidence: metric: kcat; raw value: 2.7* min^-1; raw unit: min^-1; normalized value: 0.045 s^-1; metric: Km; raw value: 1,000 uM; raw unit: uM; normalized value: 1.0 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.045 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; 0.1 M potassium phosphate buffer, pH 7.4; 1.0 mM NAD+ as the coenzyme; 25 C; oxidative dehydrogenase assay of Table II.

raw_value_unit_evidence: Table II row AKR1C35 / trans-Benzene dihydrodiol: Km 1,000 uM; kcat 2.7* min^-1; kcat/Km 0.003 min^-1 uM^-1.

row_label: trans-Benzene dihydrodiol | AKR1C35

substrate: trans-benzene dihydrodiol


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

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

raw_value_unit_evidence: kcat 17 min^-1; kcat/Km 0.11 min^-1 uM^-1; Km 148 uM

row_label: 1-Acenaphthenol / AKR1C35

table_label: Table II


column_label: PMID 26002966 / DOI 10.1093/jb/mvv057, Table II, row 2-Cyclohexen-1-ol / AKR1C35, columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table II 2-Cyclohexen-1-ol / AKR1C35: Km 569 uM; kcat 1.7 min^-1; kcat/Km 0.003 min^-1 uM^-1.

row_label: 2-Cyclohexen-1-ol / AKR1C35


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

raw_value_unit_evidence: kcat 5.8 min^-1; kcat/Km 0.45 min^-1 uM^-1; Km 13 uM

row_label: beta-3-Hydroxyhexobarbital / AKR1C35


substrate_name: beta-ionol

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

raw_value_unit_evidence: kcat 3.2 min^-1; kcat/Km 0.32 min^-1 uM^-1; Km 9.7 uM

row_label: beta-Ionol / AKR1C35

substrate: beta-ionol


substrate_name: cis-benzene dihydrodiol

column_label: PMID 26002966 / DOI 10.1093/jb/mvv057, Table II, row cis-Benzene dihydrodiol / AKR1C35, columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table II cis-Benzene dihydrodiol / AKR1C35: Km 630 uM; kcat 1.9 min^-1; kcat/Km 0.003 min^-1 uM^-1.

row_label: cis-Benzene dihydrodiol / AKR1C35

substrate: cis-benzene dihydrodiol


substrate_name: farnesol

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

column_label: PMID 26002966 / DOI 10.1093/jb/mvv057, Table II, row Farnesol / AKR1C35, columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table II Farnesol / AKR1C35: Km 11 uM; kcat 0.27 min^-1; kcat/Km 0.025 min^-1 uM^-1.

row_label: Farnesol / AKR1C35

substrate: farnesol


substrate_name: geraniol

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

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

row_label: Geraniol / AKR1C35

substrate: geraniol


substrate_name: geranylgeraniol

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

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

raw_value_unit_evidence: kcat 2.3 min^-1; kcat/Km 2.0 min^-1 uM^-1; Km 1.2 uM

row_label: Geranylgeraniol / AKR1C35

substrate: geranylgeraniol


substrate_name: NAD+

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

raw_value_unit_evidence: kcat 1.5 min^-1; kcat/Km 0.12 min^-1 uM^-1; Km 13 uM

row_label: NAD+ / AKR1C34

substrate: NAD+


organism: Hyoscyamus niger

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: tropinone

substrate: tropinone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E156V/Y100H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / E156V/Y100H; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / E156V/Y100H; kcat 1.02 s^-1, kcat_over_km 40.8 s^-1 mM^-1, km 0.025 mM.

normalized_value_unit_evidence: kcat normalized value: 1.02; normalized unit: s^-1; kcat_over_km normalized value: 40.8; normalized unit: s^-1 mM^-1; km normalized value: 0.025; normalized unit: mM

raw_value_unit_evidence: km raw value: 25.5 ± 2.0; raw unit: uM; kcat raw value: 1.02 ± 0.18; raw unit: s^-1; kcat_over_km raw value: 1.02 / 0.025; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50163 and applied mutation signature S148A with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / S148A; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / S148A; kcat 1.77 s^-1, kcat_over_km 885 s^-1 mM^-1, km 0.002 mM.

normalized_value_unit_evidence: kcat normalized value: 1.77; normalized unit: s^-1; kcat_over_km normalized value: 885; normalized unit: s^-1 mM^-1; km normalized value: 0.002; normalized unit: mM

raw_value_unit_evidence: km raw value: 1.72 ± 0.62; raw unit: uM; kcat raw value: 1.77 ± 0.07; raw unit: s^-1; kcat_over_km raw value: 1.77 / 0.002; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / S148A


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148A/E156V with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / S148A/E156V; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / S148A/E156V; kcat 2.52 s^-1, kcat_over_km 315 s^-1 mM^-1, km 0.008 mM.

normalized_value_unit_evidence: kcat normalized value: 2.52; normalized unit: s^-1; kcat_over_km normalized value: 315; normalized unit: s^-1 mM^-1; km normalized value: 0.008; normalized unit: mM

raw_value_unit_evidence: km raw value: 8.17 ± 1.10; raw unit: uM; kcat raw value: 2.52 ± 0.16; raw unit: s^-1; kcat_over_km raw value: 2.52 / 0.008; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y100H/S148A to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Y100H/S148A; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Y100H/S148A; kcat 4.58 s^-1, kcat_over_km 1145 s^-1 mM^-1, km 0.004 mM.

normalized_value_unit_evidence: kcat normalized value: 4.58; normalized unit: s^-1; kcat_over_km normalized value: 1145; normalized unit: s^-1 mM^-1; km normalized value: 0.004; normalized unit: mM

raw_value_unit_evidence: km raw value: 4.05 ± 1.64; raw unit: uM; kcat raw value: 4.58 ± 0.23; raw unit: s^-1; kcat_over_km raw value: 4.58 / 0.004; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y100H/S148A/E156V to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Y100H/S148A/E156V; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Y100H/S148A/E156V; kcat 4.86 s^-1, kcat_over_km 405 s^-1 mM^-1, km 0.012 mM.

normalized_value_unit_evidence: kcat normalized value: 4.86; normalized unit: s^-1; kcat_over_km normalized value: 405; normalized unit: s^-1 mM^-1; km normalized value: 0.012; normalized unit: mM

raw_value_unit_evidence: km raw value: 12.4 ± 1.4; raw unit: uM; kcat raw value: 4.86 ± 0.30; raw unit: s^-1; kcat_over_km raw value: 4.86 / 0.012; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50163 and applied mutation signature E156V with inferred residue-numbering offset -36 to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / E156V; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / E156V; kcat 1.11 s^-1, kcat_over_km 0.038675958188153316 s^-1 mM^-1, km 28.7 mM.

normalized_value_unit_evidence: kcat normalized value: 1.11; normalized unit: s^-1; kcat_over_km normalized value: 0.038675958188153316; normalized unit: s^-1 mM^-1; km normalized value: 28.7; normalized unit: mM

raw_value_unit_evidence: km raw value: 28.7 ± 4.44; raw unit: mM; kcat raw value: 1.11 ± 0.07; raw unit: s^-1; kcat_over_km raw value: 1.11 / 28.7; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / E156V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L210I/L213F to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / L210I/L213F; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / L210I/L213F; kcat 1.88 s^-1, kcat_over_km 41.77777777777778 s^-1 mM^-1, km 0.045 mM.

normalized_value_unit_evidence: kcat normalized value: 1.88; normalized unit: s^-1; kcat_over_km normalized value: 41.77777777777778; normalized unit: s^-1 mM^-1; km normalized value: 0.045; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.0448 ± 0.0072; raw unit: mM; kcat raw value: 1.88 ± 0.11; raw unit: s^-1; kcat_over_km raw value: 1.88 / 0.045; raw unit: s^-1 per mM after normalizing Km to row/export precision


column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Wild type; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Wild type; kcat 2.73 s^-1, kcat_over_km 56.875 s^-1 mM^-1, km 0.048 mM.

normalized_value_unit_evidence: kcat normalized value: 2.73; normalized unit: s^-1; kcat_over_km normalized value: 56.875; normalized unit: s^-1 mM^-1; km normalized value: 0.048; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.0476 ± 0.0122; raw unit: mM; kcat raw value: 2.73 ± 0.16; raw unit: s^-1; kcat_over_km raw value: 2.73 / 0.048; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / Wild type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y100H to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-II / Y100H; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-II / Y100H; kcat 6.84 s^-1, kcat_over_km 1.5 s^-1 mM^-1, km 4.56 mM.

normalized_value_unit_evidence: kcat normalized value: 6.84; normalized unit: s^-1; kcat_over_km normalized value: 1.5; normalized unit: s^-1 mM^-1; km normalized value: 4.56; normalized unit: mM

raw_value_unit_evidence: km raw value: 4.56 ± 0.23; raw unit: mM; kcat raw value: 6.84 ± 0.16; raw unit: s^-1; kcat_over_km raw value: 6.84 / 4.56; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-II / Y100H


enzyme_display_name: Tropinone reductase

organism: Cochlearia officinalis

assay_conditions_summary: pH 6.4; cofactor NADPH

column_label: Table 1; C. officinalis CoTR; row Tropinone; K_M (SD) (uM) column; raw 3290 (633) uM.

raw_value_unit_evidence: Table 1 Tropinone K_M cell: 3290 (633) uM

row_label: Tropinone

table_label: PMID 18221363 Table 1, C. officinalis CoTR kinetic properties

enzyme: Tropinone reductase


substrate_name: nortropinone

column_label: Table 1; C. officinalis CoTR; row Nortropinone; K_M (SD) (uM) column; raw 2002 (863) uM.

raw_value_unit_evidence: Table 1 Nortropinone K_M cell: 2002 (863) uM

row_label: Nortropinone

substrate: nortropinone


column_label: Table 1; C. officinalis CoTR; row TBON; K_M (SD) (uM) column; raw 42 (0 02) uM.

raw_value_unit_evidence: Table 1 TBON K_M cell: 42 (0 02) uM

row_label: TBON


substrate_name: quinuclidinone

column_label: Table 1; C. officinalis CoTR; row Quinuclidinone; K_M (SD) (uM) column; raw 2636 (338) uM.

raw_value_unit_evidence: Table 1 Quinuclidinone K_M cell: 2636 (338) uM

row_label: Quinuclidinone

substrate: quinuclidinone


column_label: Table 1; C. officinalis CoTR; row 3-methylcyclohexanone; K_M (SD) (uM) column; raw 13 (1.97) uM.

raw_value_unit_evidence: Table 1 3-methylcyclohexanone K_M cell: 13 (1.97) uM


column_label: Table 1; C. officinalis CoTR; row 4-methylcyclohexanone; K_M (SD) (uM) column; raw 15 (4.45) uM.

raw_value_unit_evidence: Table 1 4-methylcyclohexanone K_M cell: 15 (4.45) uM


organism: Wickerhamia fluorescens

substrate_name: glyoxylate

smiles: O=CC(=O)O

column_label: ScienceDirect full-text Table 2 row Glyoxylate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 18.9 mM; kcat 19 s^-1; kcat/Km 1.0052910052910053 s^-1*mM^-1 from the same row quotient 19/18.9; printed kcat/Km is rounded.

row_label: Glyoxylate / NADPH

table_label: Table 2. Kinetic properties of PPR isolated from W. fluorescens TK1

substrate: glyoxylate


substrate_name: hydroxyphenylpyruvate

column_label: ScienceDirect full-text Table 2 row Hydroxyphenylpyruvate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.64 mM; kcat 73 s^-1; kcat/Km 114.0625 s^-1*mM^-1 from the same row quotient 73/0.64; printed kcat/Km is rounded.

row_label: Hydroxyphenylpyruvate / NADPH

substrate: hydroxyphenylpyruvate


substrate_name: Hydroxypyruvate

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

column_label: ScienceDirect full-text Table 2 row Hydroxypyruvate with fixed substrate NADPH gives all three metric columns.

row_label: Hydroxypyruvate / NADPH

substrate: Hydroxypyruvate


substrate_name: NADH

column_label: ScienceDirect full-text Table 2 row NADH with fixed substrate PPA gives all three metric columns.

row_label: NADH / PPA

substrate: NADH


column_label: ScienceDirect full-text Table 2 row NADPH with fixed substrate PPA gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.01 mM; kcat 121 s^-1; kcat/Km 12100 s^-1*mM^-1 from the same row quotient 121/0.010; printed kcat/Km is rounded.

row_label: NADPH / PPA


substrate_name: phenylpyruvate

column_label: ScienceDirect full-text Table 2 row Phenylpyruvate with fixed substrate NADPH gives Km and kcat directly and a rounded kcat/Km column.

normalized_value_unit_evidence: Km 0.4 mM; kcat 150 s^-1; kcat/Km 375 s^-1*mM^-1 from the same row quotient 150/0.40; printed kcat/Km is rounded.

row_label: Phenylpyruvate / NADPH

substrate: phenylpyruvate


organism: Bos taurus

substrate_name: prostaglandin D2

proof_lines:
prostaglandin D2
Bos taurus
prostaglandin F synthase

substrate: prostaglandin D2


proof_lines:
9,10-phenanthroquinone
Bos taurus
prostaglandin F synthase


substrate_name: menadione

proof_lines:
menadione
Bos taurus
prostaglandin F synthase

substrate: menadione


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 4-nitrobenzaldehyde; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 4-nitrobenzaldehyde Km raw_value=8.3 raw_unit=uM

row_label: PGFS / 4-nitrobenzaldehyde


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 2

substrate_name: estradiol

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table I, row Estradiol -> Estrone; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00021 mM converted from 0.21 uM.

raw_value_unit_evidence: Table I reports Estradiol -> Estrone; NAD+ Km=0.21 +/- 0.04 uM.

row_label: Estradiol -> Estrone; NAD+

table_label: Table I: Characterization in vitro of human 17beta-HSD type 2 expressed in transfected 293 cells

substrate: estradiol


substrate_name: testosterone

column_label: Table I, row Testosterone -> Androstenedione; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00039 mM converted from 0.39 uM.

raw_value_unit_evidence: Table I reports Testosterone -> Androstenedione; NAD+ Km=0.39 +/- 0.09 uM.

row_label: Testosterone -> Androstenedione; NAD+

enzyme: 17-beta-hydroxysteroid dehydrogenase type 2

substrate: testosterone


substrate_name: dihydrotestosterone

column_label: Table III row Dihydrotestosterone / cofactor NAD / Km app column = 0.25 +/- 0.11 uM.

row_label: Dihydrotestosterone row; cofactor NAD

table_label: Table III. Kinetic constants of substrates in the oxidation reaction with purified reconstituted His6-tagged 17beta-HSD2

substrate: dihydrotestosterone


column_label: Table III row 20alpha-Dihydroprogesterone P / cofactor NAD / Km app column = 0.53 +/- 0.22 uM.

row_label: 20alpha-Dihydroprogesterone P row; cofactor NAD


substrate_name: androstenedione

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table I, row Androstenedione -> Testosterone; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00263 mM converted from 2.63 uM.

raw_value_unit_evidence: Table I reports Androstenedione -> Testosterone; NADH Km=2.63 +/- 0.20 uM.

row_label: Androstenedione -> Testosterone; NADH

substrate: androstenedione


substrate_name: estrone

column_label: Table I, row Estrone -> Estradiol; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00078 mM converted from 0.78 uM.

raw_value_unit_evidence: Table I reports Estrone -> Estradiol; NADH Km=0.78 +/- 0.08 uM.

row_label: Estrone -> Estradiol; NADH

substrate: estrone


enzyme_display_name: (3R)-3-hydroxyacyl-CoA dehydrogenase

organism: Mus musculus

assay_conditions_summary: buffer 50 mM Hepes

column_label: Results prose tied to Fig. 5; substrate row estradiol/E2; metric label Km; raw unit uM; Fig. 5A Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.110 uM / 1000 = 0.000110 mM; required UniProt Km row value is 0.00011 mM.

raw_value_unit_evidence: Results prose / Fig. 5A: estradiol Km = 0.110 +/- 0.02 uM.

row_label: estradiol (E2), Fig. 5A

table_label: Results prose and Fig. 5

enzyme: (3R)-3-hydroxyacyl-CoA dehydrogenase


column_label: Results prose tied to Fig. 5; substrate row testosterone/T; metric label Km; raw unit uM; Fig. 5B Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.422 uM / 1000 = 0.000422 mM; required UniProt Km row value is 0.000422 mM.

raw_value_unit_evidence: Results prose / Fig. 5B: testosterone Km = 0.422 +/- 0.063 uM.

row_label: testosterone (T), Fig. 5B


assay_conditions_summary: buffer potassium phosphate; cofactor NADPH

column_label: Results prose tied to Fig. 5; substrate row estrone/E1; metric label Km; raw unit uM; Fig. 5D Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.368 uM / 1000 = 0.000368 mM; required UniProt Km row value is 0.000368 mM.

raw_value_unit_evidence: Results prose / Fig. 5D: estrone Km = 0.368 +/- 0.063 uM.

row_label: estrone (E1), Fig. 5D


column_label: Results prose tied to Fig. 5; substrate row dihydrotestosterone/DHT; metric label Km; raw unit uM; Fig. 5C Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.360 uM / 1000 = 0.000360 mM; required UniProt Km row value is 0.00036 mM.

raw_value_unit_evidence: Results prose / Fig. 5C: dihydrotestosterone Km = 0.360 +/- 0.04 uM.

row_label: dihydrotestosterone (DHT), Fig. 5C


assay_conditions_summary: pH 9; buffer 0.25 ml CHES; cofactor NAD+

column_label: Official OUP Table 5; row 3alpha-Adiolb; column K0.5 (uM); raw value 1.4; normalized km 0.0014 mM

normalized_value_unit_evidence: K0.5=0.0014 mM for km field; raw 1.4 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row 3alpha-Adiolb; column K0.5 (uM); raw cell 1.4 uM.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


substrate_name: androsterone

column_label: Official OUP Table 5; row Androsterone; column K0.5 (uM); raw value 1.3; normalized km 0.0013 mM

normalized_value_unit_evidence: K0.5=0.0013 mM for km field; raw 1.3 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Androsterone; column K0.5 (uM); raw cell 1.3 uM.

row_label: Androsterone

substrate: androsterone


substrate_name: all-trans-retinol

column_label: Official OUP Table 5; row All-trans-retinol; column K0.5 (uM); raw value 3.2; normalized km 0.0032 mM

normalized_value_unit_evidence: K0.5=0.0032 mM for km field; raw 3.2 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row All-trans-retinol; column K0.5 (uM); raw cell 3.2 uM.

row_label: All-trans-retinol

substrate: all-trans-retinol


column_label: Official OUP Table 5; row Estradiol; column K0.5 (uM); raw value 1.5; normalized km 0.0015 mM

normalized_value_unit_evidence: K0.5=0.0015 mM for km field; raw 1.5 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Estradiol; column K0.5 (uM); raw cell 1.5 uM.

row_label: Estradiol


organism: Atropa belladonna

substrate_name: NADPH

substrate: NADPH


substrate_name: tropinone

substrate: tropinone


organism: Malus domestica

substrate_name: eriodictyol

column_label: Table 2 reports Malus cv. 'Weirouge' substrate ERI (eriodictyol), Km (μM) = 3.9; normalized Km = 0.0039 mM.

normalized_value_unit_evidence: Km=0.0039 mM after μM to mM conversion from Table 2 3.9 μM.

raw_value_unit_evidence: 3.9 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / ERI (eriodictyol) / Km (μM) column

table_label: Table 2 / Overview of kinetic data obtained with the heterologously expressed DFR enzymes from Malus domestica cv. 'Weirouge' and Pyrus communis cv. 'Pyrodwarf'

substrate: eriodictyol


substrate_name: dihydrokaempferol

column_label: Table 2 reports Malus cv. 'Weirouge' substrate DHK (dihydrokaempferol), Km (μM) = 34.0; normalized Km = 0.034 mM.

normalized_value_unit_evidence: Km=0.034 mM after μM to mM conversion from Table 2 34.0 μM.

raw_value_unit_evidence: 34.0 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / DHK (dihydrokaempferol) / Km (μM) column

substrate: dihydrokaempferol


substrate_name: dihydroquercetin

column_label: Table 2 reports Malus cv. 'Weirouge' substrate DHQ (dihydroquercetin), Km (μM) = 26.0; normalized Km = 0.026 mM.

normalized_value_unit_evidence: Km=0.026 mM after μM to mM conversion from Table 2 26.0 μM.

raw_value_unit_evidence: 26.0 μM in Table 2 Km (μM) column

row_label: Malus cv. 'Weirouge' / DHQ (dihydroquercetin) / Km (μM) column

substrate: dihydroquercetin


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 3; row 5alpha-Dihydrotestosterone oxidation / AKR1C3; columns Km (microM), kcat (min^-1), kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3 reports 5alpha-dihydrotestosterone oxidation / AKR1C3: Km=11.9 +/- 4.4 microM, kcat=0.046 min^-1, kcat/Km=3.8 min^-1 mM^-1.

table_label: Table 3


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2; row 5alpha-Androstane-3,17-dione reduction / AKR1C3; columns kcat (min^-1), kcat/Km (min^-1 mM^-1), and Km (microM).

normalized_value_unit_evidence: Converted: kcat=0.28/60=0.004667 s^-1; Km=0.005 mM; kcat/Km=56/60=0.9333 s^-1 mM^-1. Export values 0.005 and 1.0 are supported by rounded table conversion.

raw_value_unit_evidence: Table 2 reports 5alpha-androstane-3,17-dione reduction / AKR1C3: Km=5.00 +/- 0.86 microM, kcat=0.28 min^-1, kcat/Km=56 min^-1 mM^-1.

table_label: Table 2


proof_lines:
3alpha-hydroxy-5alpha-androstan-17-one
androsterone
KM 8.96 uM


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

column_label: Abstract reports apparent values of Km of 8.3 microM and Vmax of 2.8 nmoles/mg.min in the oxidation of 15-HETE.

raw_value_unit_evidence: Km raw_value=8.3 microM raw_unit=microM

row_label: Mouse liver microsomal 15-HETE dehydrogenase / 15-HETE

table_label: PubMed XML abstract PMID 3052453


substrate_name: NAD+

column_label: Results prose reports that at 200 microM 15-HETE the apparent Michaelis constant for NAD was 60 microM.

raw_value_unit_evidence: Km raw_value=60 microM raw_unit=microM

row_label: Mouse liver microsomal 15-HETE dehydrogenase / NAD cosubstrate

table_label: Results prose, journal page 527 (PDF page 4)

substrate: NAD+


organism: Pyrus communis

column_label: Table 2 reports Pyrus cv. 'Pyrodwarf' substrate ERI (eriodictyol), Km (μM) = 3.8; normalized Km = 0.0038 mM.

normalized_value_unit_evidence: Km=0.0038 mM after μM to mM conversion from Table 2 3.8 μM.

raw_value_unit_evidence: 3.8 μM in Table 2 Km (μM) column

row_label: Pyrus cv. 'Pyrodwarf' / ERI (eriodictyol) / Km (μM) column


column_label: Table 2 reports Pyrus cv. 'Pyrodwarf' substrate DHQ (dihydroquercetin), Km (μM) = 3.0; normalized Km = 0.003 mM.

normalized_value_unit_evidence: Km=0.003 mM after μM to mM conversion from Table 2 3.0 μM.

raw_value_unit_evidence: 3.0 μM in Table 2 Km (μM) column

row_label: Pyrus cv. 'Pyrodwarf' / DHQ (dihydroquercetin) / Km (μM) column


proof_lines:
tropinone reductase II
tropinone
Datura stramonium

source_databases_merged: brenda skid


proof_lines:
tropinone reductase II
kinetic characterisation
Datura stramonium


substrate_name: NAD

column_label: The abstract reports the Km of NAD being 110+/-10 microM and that of NADP 9600+/-100 microM using estradiol as substrate.

raw_value_unit_evidence: Km raw_value=110 microM raw_unit=microM

row_label: Prose segment: NAD Km

table_label: PubMed PMID 11940569 abstract

substrate: NAD


substrate_name: NADP

raw_value_unit_evidence: Km raw_value=9600 microM raw_unit=microM

row_label: Prose segment: NADP Km

substrate: NADP


substrate_name: N-glycolyl-D-mannosamine

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

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Abstract reports apparent Km values for N-acetyl- and N-glycolyl-D-mannosamine and NAD+ were 1.0, 13.3, and 0.41 mM, respectively.

raw_value_unit_evidence: Km raw_value=13.3 mM raw_unit=mM

row_label: N-acyl-D-mannosamine dehydrogenase / N-glycolyl-D-mannosamine

table_label: PubMed XML abstract PMID 3240988

substrate: N-glycolyl-D-mannosamine


assay_conditions_summary: pH 7.5; 288.15 K; cofactor NADPH

proof_lines: two crystal structures of enzyme-substrate complexes prior to reaction initiation


organism: Przewalskia tangutica


smiles: CCCCCC(=O)/C=C/C=O


substrate_name: Tropinone; H+; NADPH

assay_conditions_summary: cofactor NADP+

substrate: Tropinone; H+; NADPH


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


substrate_name: Unknown

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

substrate: Unknown


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: Vmax was measured using transfected cell lysates.


enzyme_display_name: cyclohexanol dehydrogenase

organism: Pseudomonas sp.

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

enzyme: cyclohexanol dehydrogenase


substrate_name: Cyclohexanol

substrate: Cyclohexanol


organism: Nocardia sp.

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

assay_conditions_summary: cofactor NAD+


enzyme_display_name: methanol dehydrogenase

organism: Lysinibacillus xylanilyticus

substrate_name: n-Propanol

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

smiles: CCCO

enzyme: methanol dehydrogenase

substrate: n-Propanol


enzyme_display_name: tetrahydroxynaphthalene reductase

organism: Pyricularia oryzae

enzyme: tetrahydroxynaphthalene reductase


substrate_name: Scytalone

substrate: Scytalone


organism: Bacillus methanolicus

substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: salutaridine reductase (NADPH)

organism: Papaver somniferum

substrate_name: salutaridine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M271A to reconstruct the assayed variant sequence.

enzyme: salutaridine reductase (NADPH)

substrate: salutaridine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L185A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N272A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature T182A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; 303.15 K; cofactor NADPH

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'T182A'; column 'Km (uM)' = 4.1; column 'Kim (uM)' = 58 uM; column 'Vmax/opt (nkat mg^-1)' = 3.43; column 'kcat (s^-1)' = 0.126; column 'kcat/Km (s^-1 mM^-1)' = 32.4; column 'Km NADPH (uM)' = 21.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 4.1 uM; 1 uM is 0.001 mM, so 4.1 / 1000 = 0.0040999999999999995 mM; the exported value is 0.0041 mM. kcat: printed Table 1 cell 0.126 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.126 s^(-1); the exported value is 0.126 s^(-1). kcat/Km: printed Table 1 cell 32.4 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 32.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'T182A': Km = 4.1 uM; kcat = 0.126 s^-1; printed kcat/Km = 32.4 s^-1 mM^-1.

row_label: Table 1, version row 'T182A'

table_label: Table 1: Apparent kinetic parameters for SalR and its mutated versions (J. Biol. Chem. 2009, volume 284, number 39, pages 26758-26767)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature L266A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'L266A'; column 'Km (uM)' = 49.4; column 'Kim (uM)' = ND; column 'Vmax/opt (nkat mg^-1)' = 13.68; column 'kcat (s^-1)' = 0.501; column 'kcat/Km (s^-1 mM^-1)' = 10.2; column 'Km NADPH (uM)' = 15.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 49.4 uM; 1 uM is 0.001 mM, so 49.4 / 1000 = 0.0494 mM; the exported value is 0.0494 mM. kcat: printed Table 1 cell 0.501 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.501 s^(-1); the exported value is 0.501 s^(-1). kcat/Km: printed Table 1 cell 10.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 10.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'L266A': Km = 49.4 uM; kcat = 0.501 s^-1; printed kcat/Km = 10.2 s^-1 mM^-1.

row_label: Table 1, version row 'L266A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature D107A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'D107A'; column 'Km (uM)' = 14.8; column 'Kim (uM)' = 436 uM; column 'Vmax/opt (nkat mg^-1)' = 16.61; column 'kcat (s^-1)' = 0.610; column 'kcat/Km (s^-1 mM^-1)' = 41.7; column 'Km NADPH (uM)' = 30.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 14.8 uM; 1 uM is 0.001 mM, so 14.8 / 1000 = 0.0148 mM; the exported value is 0.0148 mM. kcat: printed Table 1 cell 0.610 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.61 s^(-1); the exported value is 0.61 s^(-1). kcat/Km: printed Table 1 cell 41.7 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 41.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'D107A': Km = 14.8 uM; kcat = 0.610 s^-1; printed kcat/Km = 41.7 s^-1 mM^-1.

row_label: Table 1, version row 'D107A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature K186V to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'K186V'; column 'Km (uM)' = 7.8; column 'Kim (uM)' = 18 uM; column 'Vmax/opt (nkat mg^-1)' = 27.23; column 'kcat (s^-1)' = 0.998; column 'kcat/Km (s^-1 mM^-1)' = 149.3; column 'Km NADPH (uM)' = 3.4.

normalized_value_unit_evidence: Km: printed Table 1 cell 7.8 uM; 1 uM is 0.001 mM, so 7.8 / 1000 = 0.0078 mM; the exported value is 0.0078 mM. kcat: printed Table 1 cell 0.998 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 0.998 s^(-1); the exported value is 0.998 s^(-1). kcat/Km: printed Table 1 cell 149.3 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 149.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'K186V': Km = 7.8 uM; kcat = 0.998 s^-1; printed kcat/Km = 149.3 s^-1 mM^-1.

row_label: Table 1, version row 'K186V'


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

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'SalR-WT'; column 'Km (uM)' = 2.1; column 'Kim (uM)' = 184 uM; column 'Vmax/opt (nkat mg^-1)' = 35.61; column 'kcat (s^-1)' = 1.306; column 'kcat/Km (s^-1 mM^-1)' = 661.7; column 'Km NADPH (uM)' = 3.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.1 uM; 1 uM is 0.001 mM, so 2.1 / 1000 = 0.0021000000000000003 mM; the exported value is 0.0021 mM. kcat: printed Table 1 cell 1.306 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 1.306 s^(-1); the exported value is 1.306 s^(-1). kcat/Km: printed Table 1 cell 661.7 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 661.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'SalR-WT': Km = 2.1 uM; kcat = 1.306 s^-1; printed kcat/Km = 661.7 s^-1 mM^-1.

row_label: Table 1, version row 'SalR-WT'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature S181A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'S181A'; column 'Km (uM)' = 5.0; column 'Kim (uM)' = 199 uM; column 'Vmax/opt (nkat mg^-1)' = 52.75; column 'kcat (s^-1)' = 1.933; column 'kcat/Km (s^-1 mM^-1)' = 430.3; column 'Km NADPH (uM)' = 4.5.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.0 uM; 1 uM is 0.001 mM, so 5.0 / 1000 = 0.005 mM; the exported value is 0.005 mM. kcat: printed Table 1 cell 1.933 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 1.933 s^(-1); the exported value is 1.933 s^(-1). kcat/Km: printed Table 1 cell 430.3 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 430.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'S181A': Km = 5.0 uM; kcat = 1.933 s^-1; printed kcat/Km = 430.3 s^-1 mM^-1.

row_label: Table 1, version row 'S181A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature F104A/I275A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'F104A/I275A'; column 'Km (uM)' = 408.6; column 'Kim (uM)' = ND; column 'Vmax/opt (nkat mg^-1)' = 66.85; column 'kcat (s^-1)' = 2.450; column 'kcat/Km (s^-1 mM^-1)' = 5.9; column 'Km NADPH (uM)' = 43.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 408.6 uM; 1 uM is 0.001 mM, so 408.6 / 1000 = 0.4086 mM; the exported value is 0.4086 mM. kcat: printed Table 1 cell 2.450 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.45 s^(-1); the exported value is 2.45 s^(-1). kcat/Km: printed Table 1 cell 5.9 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 5.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'F104A/I275A': Km = 408.6 uM; kcat = 2.450 s^-1; printed kcat/Km = 5.9 s^-1 mM^-1.

row_label: Table 1, version row 'F104A/I275A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature V106A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'V106A'; column 'Km (uM)' = 8.9; column 'Kim (uM)' = 283 uM; column 'Vmax/opt (nkat mg^-1)' = 67.13; column 'kcat (s^-1)' = 2.458; column 'kcat/Km (s^-1 mM^-1)' = 295.4; column 'Km NADPH (uM)' = 7.0.

normalized_value_unit_evidence: Km: printed Table 1 cell 8.9 uM; 1 uM is 0.001 mM, so 8.9 / 1000 = 0.0089 mM; the exported value is 0.0089 mM. kcat: printed Table 1 cell 2.458 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.458 s^(-1); the exported value is 2.458 s^(-1). kcat/Km: printed Table 1 cell 295.4 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 295.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'V106A': Km = 8.9 uM; kcat = 2.458 s^-1; printed kcat/Km = 295.4 s^-1 mM^-1.

row_label: Table 1, version row 'V106A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature F104A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'F104A'; column 'Km (uM)' = 31.8; column 'Kim (uM)' = 466 uM; column 'Vmax/opt (nkat mg^-1)' = 74.38; column 'kcat (s^-1)' = 2.727; column 'kcat/Km (s^-1 mM^-1)' = 86.2; column 'Km NADPH (uM)' = 9.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 31.8 uM; 1 uM is 0.001 mM, so 31.8 / 1000 = 0.0318 mM; the exported value is 0.0318 mM. kcat: printed Table 1 cell 2.727 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 2.727 s^(-1); the exported value is 2.727 s^(-1). kcat/Km: printed Table 1 cell 86.2 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 86.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'F104A': Km = 31.8 uM; kcat = 2.727 s^-1; printed kcat/Km = 86.2 s^-1 mM^-1.

row_label: Table 1, version row 'F104A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q071N0 and applied mutation signature I275A to reconstruct the assayed variant sequence.

column_label: Table 1 (Apparent kinetic parameters for SalR and its mutated versions), version row 'I275A'; column 'Km (uM)' = 33.1; column 'Kim (uM)' = 1249 uM; column 'Vmax/opt (nkat mg^-1)' = 87.03; column 'kcat (s^-1)' = 3.188; column 'kcat/Km (s^-1 mM^-1)' = 98.0; column 'Km NADPH (uM)' = 21.1.

normalized_value_unit_evidence: Km: printed Table 1 cell 33.1 uM; 1 uM is 0.001 mM, so 33.1 / 1000 = 0.033100000000000004 mM; the exported value is 0.0331 mM. kcat: printed Table 1 cell 3.188 s^-1; the printed unit is already the canonical s^(-1), so no unit conversion applies and the paper-side value is 3.188 s^(-1); the exported value is 3.188 s^(-1). kcat/Km: printed Table 1 cell 98.0 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper-side value is 98.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, version row 'I275A': Km = 33.1 uM; kcat = 3.188 s^-1; printed kcat/Km = 98.0 s^-1 mM^-1.

row_label: Table 1, version row 'I275A'


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K186V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S181A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V106A to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L266A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M271A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I275A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T182A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L185A to reconstruct the assayed variant sequence.