sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P51857 and applied mutation signature E120H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 310.15 K; buffer 1-ml systems containing 100 mM potassium phosphate; cofactor NAD+

column_label: Table 3: Kinetic constants for hydroxysteroid oxidation catalyzed by the E120H mutant and AKR1C2 (J. Biol. Chem. 2012, 287(20):16609-16622), enzyme block E120H, substrate row '5beta-DHT'; column 'Substrate stereospecificity' = 17beta; column 'kcat (x 10^-3 s^-1)' = 0.85; column 'Km (uM)' = 5.7; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 1.5. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.85 with the column head x 10^-3 s^-1, so the cell reads 0.85 x 10^-3 s^-1; the paper value is 0.00085 s^(-1); the exported value is 0.0008 s^(-1). Km: printed Table 3 cell 5.7 uM; 1 uM is 0.001 mM, so 5.7 / 1000 = 0.0057 mM; the paper value is 0.0057 mM; the exported value is 0.006 mM. kcat/Km: printed Table 3 cell 1.5 with the column head x 10^2 M^-1 s^-1, so the cell reads 150 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150 / 1000 = 0.15 s^-1 mM^-1; the paper value is 0.15 s^(-1)*mM^(-1); the exported value is 0.13333333333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row '5beta-DHT': kcat = 0.85 s-1 under the column multiplier x 10^-3; Km = 5.7 uM; printed kcat/Km = 1.5 M-1 s-1 under the column multiplier x 10^2.


organism: Homo sapiens

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

proof_lines:
AKR1D1 E120H
comparator kinetics
P52895

data_origin: experimental

status: unverified

source: oed


enzyme_display_name: Glucose 1-dehydrogenase

organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)

substrate_name: NADP(+) (at 70 degrees Celsius and pH 7)

source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: pH 7; cofactor NADP+

enzyme: Glucose 1-dehydrogenase

source: uniprot


organism: Aspergillus nidulans

substrate_name: NADP+

source_db: brenda

assay_conditions_summary: cofactor NADP+

substrate: NADP+

source: brenda


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

organism: Saccharolobus solfataricus

substrate_name: beta-D-glucose

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

substrate: beta-D-glucose


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

substrate_name: glucose 6-phosphate

enzyme: Glucose-6-phosphate 1-dehydrogenase

substrate: glucose 6-phosphate


organism: Rattus norvegicus

verification_status: corrected

column_label: Table 2; row 4-Androstene-3,17-dione; TBER1 Km/kcat/kcat/Km columns; raw 17 uM, 1.0 min^-1, 0.06 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 TBER1 cells: Km 17 uM; kcat 1.0 min^-1; kcat/Km 0.06 min^-1 uM^-1.

row_label: 4-Androstene-3,17-dione / TBER1

table_label: PMID 16788056 Table 2, steroid substrates

status: corrected


substrate_name: testosterone

column_label: Table 2; row Testosterone; TBER1 Km/kcat/kcat/Km columns; raw 25 uM, 16 min^-1, 0.62 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 TBER1 cells: Km 25 uM; kcat 16 min^-1; kcat/Km 0.62 min^-1 uM^-1.

row_label: Testosterone / TBER1

substrate: testosterone


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

organism: Priestia megaterium

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

mutation_type: substitution

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


assay_conditions_summary: cofactor NAD+


substrate_name: NAD+

substrate: NAD+


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

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

proof_lines:
wild type, coenzyme NADP+
wild type, coenzyme NAD+
wild-type enzyme, pH 8.0, 25°C


substrate_name: NAADP

substrate: NAADP


verification_status: verified

column_label: Table I column K m (unit microM) for row Rat RoDH1 - Testosterone gives 2.8

normalized_value_unit_evidence: Table I K m normalized_value=0.0028 normalized_unit=mM

raw_value_unit_evidence: Table I K m raw_value=2.8 raw_unit=microM

row_label: Rat RoDH1 / Testosterone / Androstenedione / Ox 17beta-HSD

table_label: Table I: Kinetic constants of steroid metabolizing enzymes

status: verified


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

proof_lines: apparent value, wild type enzyme, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


organism: Mesocricetus auratus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table I, row 'AKR1C35', AKR1C35 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 2.4 mM and kcat 0.15 s^-1; the kcat/Km entry is the quotient of those same two cells, 0.0625 s^-1 mM^-1, recorded as derived rather than transcribed. Conversion arithmetic, disclosed separately from the stored values: 9.0 min^-1 / 60 = 0.15 s^-1 exactly; 2,400 uM / 1000 = 2.4 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: 0.15 s^-1 / 2.4 mM = 0.0625 s^-1 mM^-1 = 9.0 min^-1 / 2,400 uM = 0.00375 min^-1 uM^-1, which rounds to the printed 0.0038 cell at its two-significant-figure precision.

normalized_value_unit_evidence: metric: kcat; raw value: 9.0 ± 2.0 min^-1; raw unit: min^-1; normalized value: 0.15 s^-1; metric: Km; raw value: 2,400 ± 530 uM; raw unit: uM; normalized value: 2.4 mM; metric: kcat/Km; raw value: derived from this row's own two printed cells; normalized value: 0.0625 s^-1 mM^-1; assay condition: Recombinant hamster AKR1C35; 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 AKR1C35 / NADP+: Km 2,400 ± 530 uM; kcat 9.0 ± 2.0 min^-1; kcat/Km 0.0038 min^-1 uM^-1.

row_label: AKR1C35 | NADP+

table_label: Table I. Kinetic constants for coenzymes


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T/V306G


proof_lines: pH and temperature not specified in the publication, mutant enzyme V306G


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T


proof_lines: pH and temperature not specified in the publication, mutant enzyme V306I


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192T/V306I


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


proof_lines: pH and temperature not specified in the publication, mutant enzyme I192V


km_display: Not reported

proof_lines: pH and temperature not specified in the publication, mutant enzyme 0.00184 I192T/V306G


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G261A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NAD+

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G261A; column pH 6.0 KM (mM); raw 4.1 x 10^2 +/- 35 mM; normalized Km=410 mM.

normalized_value_unit_evidence: Km=410 mM

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature A258F to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row A258F; column pH 6.0 KM (mM); raw 4.3 +/- 0.2 mM; normalized Km=4.3 mM.

normalized_value_unit_evidence: Km=4.3 mM


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row A258F; column pH 8.0 KM (mM); raw 9.8 +/- 1.0 mM; normalized Km=9.8 mM.

normalized_value_unit_evidence: Km=9.8 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G259A to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259A; column pH 6.0 KM (mM); raw 81 +/- 7.1 mM; normalized Km=81 mM.

normalized_value_unit_evidence: Km=81 mM


column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259A; column pH 8.0 KM (mM); raw 380 +/- 16 mM; normalized Km=380 mM.

normalized_value_unit_evidence: Km=380 mM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature ΔG261 to reconstruct the assayed variant sequence.

mutation_type: deletion

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row DeltaG261; column pH 6.0 KM (mM); raw 1.1 x 10^3 +/- 170 mM; normalized Km=1100 mM.

row_label: DeltaG261 / pH 6.0 KM


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G259V to reconstruct the assayed variant sequence.

column_label: Table 2. Kinetic parameters of BmGlcDH-III, -IV and its mutants at 37 C; row G259V; column pH 6.0 KM (mM); raw 1.4 x 10^3 +/- 96 mM; normalized Km=1400 mM.


assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprotkb:P39485 and applied mutation signature G261V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6


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


substrate_name: D-xylose

substrate: D-xylose


substrate_name: beta-D-galactose

proof_lines:
wild type enzyme, NADP+ as cofactor
wild type enzyme, NAD+ as cofactor

substrate: beta-D-galactose


enzyme_display_name: L-gulonate 3-dehydrogenase

organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column WTa Value; raw value 0.010 mM; normalized Km 0.01 mM; NAD+-linked activity; WT value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.01 mM

row_label: Km NAD+ (mM)

enzyme: L-gulonate 3-dehydrogenase


substrate_name: L-gulonate

column_label: Table 3; WT column; NAD-linked activity; Km L-gulonate row.

normalized_value_unit_evidence: Km paper=0.18 mM for NAD-linked WT; export=0.018 mM.

raw_value_unit_evidence: WT Km L-gulonate 0.18 mM; NADP-linked WT Km L-gulonate is 2.4 mM.

row_label: WT; NAD-linked activity; Km L-gulonate

table_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations

substrate: L-gulonate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q41N to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column Q41N Value; raw value 0.028 +/- 0.001 mM; normalized Km 0.028 mM; NAD+-linked activity; Q41N mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E97Q to reconstruct the assayed variant sequence.

column_label: Table 3 NAD+-linked activity, Km NAD+, mutant E97Q: 0.054 ± 0.06 mM.

row_label: NAD+-linked activity; Km NAD+; mutant E97Q


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36R/Q41N to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column D36R/Q41N Value; raw value 0.12 +/- 0.01 mM; normalized Km 0.12 mM; NADP+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 0.12 mM

row_label: Km NADP+ (mM)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D36R to reconstruct the assayed variant sequence.

column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column D36Ra Value; raw value 0.20 mM; normalized Km 0.2 mM; NADP+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.2 mM

raw_value_unit_evidence: Km 0.20 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column WTa Value; raw value 0.67 mM; normalized Km 0.67 mM; NADP+-linked activity; WT value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 0.67 mM

raw_value_unit_evidence: Km 0.67 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NADP+ (mM); column Q41N Value; raw value 0.86 +/- 0.13 mM; normalized Km 0.86 mM; NADP+-linked activity; Q41N mutant

normalized_value_unit_evidence: Km 0.86 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column D36Ra Value; raw value 1.3 mM; normalized Km 1.3 mM; NAD+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 1.3 mM

raw_value_unit_evidence: Km 1.3 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column Q41N Value; raw value 1.3 +/- 0.1 mM; normalized Km 1.3 mM; NAD+-linked activity; Q41N mutant

row_label: Km L-gulonate (mM)


column_label: Table 3 NAD+-linked activity, Km L-gulonate, mutant E97Q: 1.6 ± 0.1 mM.

row_label: NAD+-linked activity; Km L-gulonate; mutant E97Q


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km NAD+ (mM); column D36R/Q41N Value; raw value 2.6 +/- 0.4 mM; normalized Km 2.6 mM; NAD+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 2.6 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36R/Q41N Value; raw value 2.6 +/- 0.2 mM; normalized Km 2.6 mM; NADP+-linked activity; D36R/Q41N double mutant


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36R/Q41N Value; raw value 3.3 +/- 0.3 mM; normalized Km 3.3 mM; NAD+-linked activity; D36R/Q41N double mutant

normalized_value_unit_evidence: Km 3.3 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36Ra Value; raw value 14 mM; normalized Km 14.0 mM; NAD+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 14.0 mM

raw_value_unit_evidence: Km 14 mM


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column Q41N Value; raw value 14 +/- 1.2 mM; normalized Km 14.0 mM; NADP+-linked activity; Q41N mutant


column_label: Table 3. Alteration of kinetic parameters for coenzymes and L-gulonate by mutations; row Km L-gulonate (mM); column D36Ra Value; raw value 18 mM; normalized Km 18.0 mM; NADP+-linked activity; D36R value; footnote a says taken from Ishikura et al.5

normalized_value_unit_evidence: Km 18.0 mM

raw_value_unit_evidence: Km 18 mM


substrate_name: NADH

assay_conditions_summary: pH 8.5; cofactor NADH

proof_lines:
at pH 8.5, rabbit liver GDH
at pH 8.5, recombinant rabbit GDH

substrate: NADH


assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines:
at pH 8.5, recombinant rabbit GDH
at pH 8.5, rabbit liver GDH


proof_lines: mutant enzyme E157Q, NAD+-linked activity


assay_conditions_summary: pH 8.5; cofactor NADP+


substrate_name: L-threonate

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

substrate: L-threonate


proof_lines: mutant enzyme S124A, NAD+-linked activity


substrate_name: acetoacetate

substrate: acetoacetate


proof_lines: mutant enzyme D36R, NAD+-linked activity


proof_lines: mutant enzyme D36R, NADP+-linked activity


proof_lines: mutant enzyme E157Q, NADP+-linked activity


organism: Escherichia coli

assay_conditions_summary: pH 8.2; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADP+


proof_lines: mutant enzyme K18A/R50A, at pH 8.2 and 25°C


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
wild type enzyme, at pH 8.2 and 25°C
25°C, pH 8.0, wild-type strain K-10


organism: Sus scrofa


substrate_name: beta-keto-L-gulonate

assay_conditions_summary: pH 6.3; cofactor NADH

substrate: beta-keto-L-gulonate


substrate_name: L-Idonate

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

substrate: L-Idonate


organism: Corynebacterium sp.

assay_conditions_summary: pH 9.8; cofactor NAD+

proof_lines:
strain 93-1
pH 9.8
strain 150-1


proof_lines:
strain 93-1
strain 150-1


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: cellobiose

substrate: cellobiose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; buffer 50 mM Tris-HCl

proof_lines: apparent value, mutant enzyme Q252L, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme Q252L/E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E170K to reconstruct the assayed variant sequence.

proof_lines: apparent value, mutant enzyme E170K, in 50 mM Tris-HCl buffer (pH 8.0), at 25°C


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

column_label: PMCID PMC1151818 HTML Table 1; row Q252L; column Apparent Km (NAD+) (mM); raw value 0.15 mM; normalized value 0.15 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.15 mM is already normalized as 0.15 mM.

raw_value_unit_evidence: Table 1 row Q252L, column Apparent Km (NAD+) (mM): 0.15 mM.

row_label: Q252L glucose dehydrogenase

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


column_label: PMCID PMC1151818 HTML Table 1; row E170K; column Apparent Km (NAD+) (mM); raw value 0.22 mM; normalized value 0.22 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.22 mM is already normalized as 0.22 mM.

raw_value_unit_evidence: Table 1 row E170K, column Apparent Km (NAD+) (mM): 0.22 mM.

row_label: E170K glucose dehydrogenase


column_label: PMCID PMC1151818 HTML Table 1; row Q252L/E170K; column Apparent Km (NAD+) (mM); raw value 0.33 mM; normalized value 0.33 mM. Footnote a defines the pH 8.0, fixed 0.1 M glucose, and NAD+ concentration range.

normalized_value_unit_evidence: 0.33 mM is already normalized as 0.33 mM.

raw_value_unit_evidence: Table 1 row Q252L/E170K, column Apparent Km (NAD+) (mM): 0.33 mM.

row_label: Q252L/E170K glucose dehydrogenase


substrate_name: D-glucose 6-phosphate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454C to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with deamino-NADP+

substrate: D-glucose 6-phosphate


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

proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with NADP+

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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R454H to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 25°C, recombinant mutant R454H, with NADP+


substrate_name: NADP+

proof_lines: pH 8.0, 25°C, recombinant mutant R454H, with D-glucose 6-phosphate

substrate: NADP+


proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with D-glucose 6-phosphate


proof_lines: pH 8.0, 25°C, recombinant mutant R454C, with deoxy-D-glucose 6-phosphate


substrate_name: deamino-NADP+

substrate: deamino-NADP+


organism: Trypanosoma cruzi

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature L80G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADPH

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'L80G'; column 'KM G6P (uM)' = 74; column 'kcat (s^-1)' = 2.0; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.027.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.0 s^(-1). Km: printed Table 1 cell 74 uM; 74 / 1000 = 0.074 mM. kcat/Km: printed Table 1 cell 0.027 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.027 x 1000 = 27.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row L80G, G6P columns: KM G6P = 74 uM; kcat = 2.0 s^-1; printed kcat/KM G6P = 0.027 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row L80G, G6P columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q1WBU6 and applied mutation signature L80G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K83A'; column 'KM G6P (uM)' = 537; column 'kcat (s^-1)' = 2.8; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.005.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.8 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 2.8 s^(-1). Km: printed Table 1 cell 537 uM; 537 / 1000 = 0.537 mM. kcat/Km: printed Table 1 cell 0.005 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.005 x 1000 = 5.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K83A, G6P columns: KM G6P = 537 uM; kcat = 2.8 s^-1; printed kcat/KM G6P = 0.005 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K83A, G6P columns


assay_conditions_summary: pH 7.5; 298.15 K; buffer B (50 mM Tris pH 7; cofactor NADP+

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K83A'; column 'KM NADP+ (uM)' = 21; column 'kcat (s^-1)' = 3.0; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 0.14.

normalized_value_unit_evidence: kcat: printed Table 1 cell 3.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 3.0 s^(-1). Km: printed Table 1 cell 21 uM; 21 / 1000 = 0.021 mM. kcat/Km: printed Table 1 cell 0.14 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.14 x 1000 = 140.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K83A, NADP+ columns: KM NADP+ = 21 uM; kcat = 3.0 s^-1; printed kcat/KM NADP+ = 0.14 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K83A, NADP+ columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature R408A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'R408A'; column 'KM G6P (uM)' = 168; column 'kcat (s^-1)' = 15.0; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.089.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 15.0 s^(-1). Km: printed Table 1 cell 168 uM; 168 / 1000 = 0.168 mM. kcat/Km: printed Table 1 cell 0.089 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.089 x 1000 = 89.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row R408A, G6P columns: KM G6P = 168 uM; kcat = 15.0 s^-1; printed kcat/KM G6P = 0.089 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row R408A, G6P columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'R408A'; column 'KM NADP+ (uM)' = 17; column 'kcat (s^-1)' = 19; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 1.1.

normalized_value_unit_evidence: kcat: printed Table 1 cell 19 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 19.0 s^(-1). Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 1.1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.1 x 1000 = 1100.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row R408A, NADP+ columns: KM NADP+ = 17 uM; kcat = 19 s^-1; printed kcat/KM NADP+ = 1.1 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row R408A, NADP+ columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q1WBU6 and applied mutation signature K84A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K84A'; column 'KM G6P (uM)' = 618; column 'kcat (s^-1)' = 24.6; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.04.

normalized_value_unit_evidence: kcat: printed Table 1 cell 24.6 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 24.6 s^(-1). Km: printed Table 1 cell 618 uM; 618 / 1000 = 0.618 mM. kcat/Km: printed Table 1 cell 0.04 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.04 x 1000 = 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K84A, G6P columns: KM G6P = 618 uM; kcat = 24.6 s^-1; printed kcat/KM G6P = 0.04 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K84A, G6P columns


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

column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'WT'; column 'KM NADP+ (uM)' = 16; column 'kcat (s^-1)' = 52; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 3.2.

normalized_value_unit_evidence: kcat: printed Table 1 cell 52 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 52.0 s^(-1). Km: printed Table 1 cell 16 uM; 16 / 1000 = 0.016 mM. kcat/Km: printed Table 1 cell 3.2 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.2 x 1000 = 3200.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row WT, NADP+ columns: KM NADP+ = 16 uM; kcat = 52 s^-1; printed kcat/KM NADP+ = 3.2 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row WT, NADP+ columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'K84A'; column 'KM NADP+ (uM)' = 17; column 'kcat (s^-1)' = 58; column 'kcat/KM NADP+ (s^-1 uM^-1)' = 3.4.

normalized_value_unit_evidence: kcat: printed Table 1 cell 58 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 58.0 s^(-1). Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 3.4 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.4 x 1000 = 3400.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row K84A, NADP+ columns: KM NADP+ = 17 uM; kcat = 58 s^-1; printed kcat/KM NADP+ = 3.4 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row K84A, NADP+ columns


column_label: Table 1: Kinetic parameters of wildtype and point mutants of recombinant TcG6PDH with substrates and the inhibitor epiandrosterone (EA) (Molecules 2016, 21(3):368), row 'WT'; column 'KM G6P (uM)' = 77; column 'kcat (s^-1)' = 62; column 'kcat/KM G6P (s^-1 uM^-1)' = 0.8.

normalized_value_unit_evidence: kcat: printed Table 1 cell 62 s^-1; already in s^-1, no conversion (this paper prints no min^-1 kinetic cell); the paper value is 62.0 s^(-1). Km: printed Table 1 cell 77 uM; 77 / 1000 = 0.077 mM. kcat/Km: printed Table 1 cell 0.8 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.8 x 1000 = 800.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, row WT, G6P columns: KM G6P = 77 uM; kcat = 62 s^-1; printed kcat/KM G6P = 0.8 s^-1 uM^-1.

row_label: Table 1, TcG6PDH row WT, G6P columns


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q1WBU6 and applied mutation signature R408A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q1WBU6 and applied mutation signature K84A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q1WBU6 and applied mutation signature K83A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/K166R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: pH 7.0, 30°C, mutant enzyme Q252L/E170K/K166R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/S100P/K166R/K137R to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/K137R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/S100P to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/S100P/K166R to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/S100P/K166R/V72I to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme Q252L/E170K/S100P/K166R/V72I


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q252L/E170K/S100P/K166R/V72I/K137R to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: pH 7.4, reaction with 4-dionetestosterone


assay_conditions_summary: pH 7.4; cofactor NAD+


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

assay_conditions_summary: pH 7.4; cofactor NADP+


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: NAD+

proof_lines:
pH 7.4, reaction with testosterone
pH 7.4, reaction with estradiol

substrate: NAD+


substrate_name: testosterone

proof_lines:
pH 7.4, with NAD+ as cofactor
NADP+ as variable substrate

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G163S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G163D to reconstruct the assayed variant sequence.


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


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme, with D-glucose 6-phosphate


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


organism: Canis lupus familiaris

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines: pH 7.4, 37°C, with D-glucose 6-phosphate or 2-deoxy-D-glucose 6-phosphate


proof_lines: pH 7.4, 37°C, with NADP+ or deamino-NADP+


proof_lines: pH 7.4, 37°C, with D-glucose 6-phosphate


organism: Bacillus amyloliquefaciens

substrate_name: D-glucose

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

proof_lines: with NADP+ as cosubstrate,at pH 8.0 and 37°C

substrate: D-glucose


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


assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G488V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G488S to reconstruct the assayed variant sequence.


assay_conditions_summary: cofactor NADP+


organism: Lysinibacillus sphaericus

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


proof_lines:
with NADP+, pH 8.0, 25°C
with NAD+, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R393H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R393G to reconstruct the assayed variant sequence.


substrate_name: beta-D-glucose

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines:
pH 7.5, 37°C, coenzyme NAD+, 37°C
pH 10.0, 37°C, coenzyme NAD+
pH 7.5, 37°C, coenzyme NADP+

substrate: beta-D-glucose


proof_lines:
37°C, pH 7.5, coenzyme NADP+
pH 10.0, 37°C, coenzyme NADP+
pH 10.0


proof_lines: pH 7.5, 37°C, reaction with D-glucose-6-phosphate

proof_lines: pH 10.0, 37°C, reaction with beta-D-glucose


organism: Bacillus thuringiensis serovar kurstaki

assay_conditions_summary: pH 9; 328.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 328.15 K; cofactor NAD+


proof_lines: pH 7.6, temperature not specified in the publication

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor NADP+


proof_lines: substrate D-glucose 6-phosphate, pH 7.6, temperature not specified in the publication

proof_lines: substrate NADP+, pH 7.6, temperature not specified in the publication


organism: Bacillus subtilis

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


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADP+

proof_lines: pH 6.5, Km -value decreases with decreasing pH


substrate_name: D-glucosamine

substrate: D-glucosamine


organism: Bos taurus

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: isoform G6PD1, at pH 8.0, temperature not specified in the publication


assay_conditions_summary: cofactor NAD+


organism: Bacillus sp. (in: firmicutes)


organism: Ovis aries


organism: Arabidopsis thaliana


assay_conditions_summary: cofactor NADPH


organism: Nicotiana tabacum

proof_lines: G6PDH activity extracted from source leaves of wild-type tobacco Xanthi cultivars

proof_lines: G6PDH activity extracted from source leaves of wild-type tobacco SNN cultivars


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Staphylococcus aureus

substrate_name: isocitrate

enzyme: isocitrate dehydrogenase (NADP+)

substrate: isocitrate


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADP+

proof_lines:
pH 7.6, 25°C, leaf enzyme
pH 7.6, 25°C, root enzyme


substrate_name: D-isocitrate

substrate: D-isocitrate


substrate_name: D,L-isocitrate

substrate: D,L-isocitrate


substrate_name: DL-isocitrate

substrate: DL-isocitrate


organism: Thermus aquaticus

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

proof_lines:
25°C assay temperature
70°C assay temperature


organism: Archaeoglobus fulgidus


organism: Lathyrus oleraceus


enzyme_display_name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

organism: Enterococcus faecalis


enzyme: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)


proof_lines:
coenzyme NAD+
coenzyme NADP+


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADP+

proof_lines:
coenzyme NADP+
coenzyme NAD+
pH 9.5, 30°C, coenzyme NAD+


organism: Klebsiella pneumoniae

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

proof_lines: in 50 mM Tris-HCl buffer (pH 8.0), 20 mM MgCl2, at 25°C


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


organism: Priestia megaterium


organism: Phormidium sp.


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7.5; 338.15 K; cofactor NADP+

proof_lines: cosubstrate D-glucose, 65°C, pH not specified in the publication

proof_lines: cosubstrate D-glucose, 70°C, pH not specified in the publication


assay_conditions_summary: pH 7.5; 338.15 K; cofactor NAD+


organism: Nostoc sp.

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: pH 7.5, enzyme reduced with Nostoc sp. thioredoxin


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_exact_accession:P00350 and applied mutation signature Y378C to reconstruct the assayed variant sequence.

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

column_label: Table 2 reports Ec6PGDH NADP+ Km (uM) = 49 +/- 7.

raw_value_unit_evidence: Km raw_value=49 +/- 7 uM raw_unit=uM

row_label: Ec6PGDH row / NADP+ Km column

table_label: ScienceDirect PMID 19686854 Table 2


column_label: Table 2 reports Ec6PGDH 6PG Km (uM) = 93 +/- 1.

raw_value_unit_evidence: Km raw_value=93 +/- 1 uM raw_unit=uM

row_label: Ec6PGDH row / 6PG Km column


assay_conditions_summary: pH 9.5; 303.15 K; cofactor NAD+


proof_lines: pH 9.5, 30°C, reaction with D-glucose 6-phosphate


organism: Bacillus subtilis

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: 25°C, pH 8.0, high-level glucose-6-phosphate dehydrogenase strain DF82

proof_lines: pH 8.0, temperature not specified in the publication


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


enzyme_display_name: D-galactose 1-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: D-galactose

enzyme: D-galactose 1-dehydrogenase

substrate: D-galactose


assay_conditions_summary: cofactor NADP+


organism: Mus musculus

proof_lines: pH not specified in the publication, temperature not specified in the publication


substrate_name: D-glucose 6-phosphate

substrate: D-glucose 6-phosphate


organism: Hordeum vulgare

assay_conditions_summary: 298.15 K; cofactor NADP+

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

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


organism: Cavia porcellus

proof_lines: enzyme activity in microsomal fraction after centrifugation


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

organism: Curvularia lunata

substrate_name: NADPH

enzyme: 17beta-estradiol 17-dehydrogenase

substrate: NADPH


proof_lines: 25°C, pH 8.0, wild-type enzyme, cosubstrate: 4-estrene-3,17-dione


enzyme_display_name: mannitol 2-dehydrogenase

organism: Tetraselmis subcordiformis

substrate_name: D-mannitol

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

assay_conditions_summary: cofactor NADH

enzyme: mannitol 2-dehydrogenase

substrate: D-mannitol


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Homo sapiens

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 0.37 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one reduction (PubMed:10998348). kcat is 0.046 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one oxydation (PubMed:10998348).

enzyme: Aldo-keto reductase family 1 member C3


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


organism: Leuconostoc pseudomesenteroides

assay_conditions_summary: pH 8.6; cofactor NADH

column_label: The extracted paper text states the apparent Km for D-mannitol at 5 mM NAD+ is 12 mM and Table 4 lists D-mannitol Km as 12 mM, matching the expected row.

raw_value_unit_evidence: Km raw_value=12 raw_unit=mM

row_label: D-mannitol

table_label: Table 4 / purification properties paragraph


assay_conditions_summary: pH 5.4; cofactor NADH

column_label: The extracted paper text states the apparent Km for D-fructose at 200 uM NADH is 44 mM and Table 4 lists D-fructose Km as 44 mM, matching the expected row.

raw_value_unit_evidence: Km raw_value=44 raw_unit=mM

row_label: D-fructose


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table 1; row 2-Cyclohexen-1-ol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 7000 uM, 3.5 min^-1, 0.0005 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 7000 uM; kcat 3.5 min^-1; kcat/Km 0.0005 min^-1 uM^-1.

row_label: 2-Cyclohexen-1-ol / Rat 17HSD5

table_label: PMID 16788056 Table 1, non-steroidal substrates


substrate_name: Dimethylglyoxal

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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2,3-Butanedione; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 126 uM, kcat 16 min^-1, kcat/Km 0.13 min^-1 uM^-1.

raw_value_unit_evidence: Km 126 uM; kcat 16 min^-1; kcat/Km 0.13 min^-1 uM^-1

row_label: 2,3-Butanedione / Rat 17HSD5

substrate: Dimethylglyoxal


column_label: Table 2; row 17beta-Estradiol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 14 uM, 25 min^-1, 1.8 min^-1 uM^-1.

raw_value_unit_evidence: Table 2 Rat 17HSD5 cells: Km 14 uM; kcat 25 min^-1; kcat/Km 1.8 min^-1 uM^-1.

row_label: 17beta-Estradiol / Rat 17HSD5


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: p-Nitrobenzaldehyde

column_label: Table 1; row 4-Nitrobenzaldehyde; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 11 uM, 7.9 min^-1, 0.72 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 11 uM; kcat 7.9 min^-1; kcat/Km 0.72 min^-1 uM^-1.

row_label: 4-Nitrobenzaldehyde / Rat 17HSD5

substrate: p-Nitrobenzaldehyde


column_label: Table 1; row S-Indan-1-ol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 3080 uM, 6.8 min^-1, 0.002 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 3080 uM; kcat 6.8 min^-1; kcat/Km 0.002 min^-1 uM^-1.

row_label: S-Indan-1-ol / Rat 17HSD5


column_label: Table 1; row trans-Benzene dihydrodiol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw 2300 uM, 4.1 min^-1, 0.002 min^-1 uM^-1.

raw_value_unit_evidence: Table 1 Rat 17HSD5 cells: Km 2300 uM; kcat 4.1 min^-1; kcat/Km 0.002 min^-1 uM^-1.

row_label: trans-Benzene dihydrodiol / Rat 17HSD5


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: (3S)-3-hydroxybutanoyl-CoA (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 NAD+

column_label: Table 3; Drosophila species columns; row β-Hydroxybutyryl-CoA/NAD+; Km column

normalized_value_unit_evidence: Km=0.101 mM converted from 101 uM

raw_value_unit_evidence: Table 3 Drosophila β-Hydroxybutyryl-CoA/NAD+ Km 101 +/- 8 ×10^-6 M

row_label: β-Hydroxybutyryl-CoA/NAD+

table_label: Table 3

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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

column_label: Table 3; Drosophila species columns; row 5α-Pregnan-20β-ol-3-one; Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 3 Drosophila 5α-Pregnan-20β-ol-3-one Km 9 +/- 2 ×10^-6 M


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

column_label: Table 3; Drosophila species columns; row Isoursodeoxycholic acid; Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 3 Drosophila Isoursodeoxycholic acid Km 3 +/- 0.3 ×10^-6 M

row_label: Isoursodeoxycholic acid


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


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

organism: Clostridium kluyveri

substrate_name: succinic semialdehyde

sequence_source: multiple

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

assay_conditions_summary: pH 6.1; cofactor NADH

column_label: The official abstract states Km values for NADH and succinic semialdehyde were 150 +/- 20 uM and 560 +/- 80 uM, respectively.

raw_value_unit_evidence: Km raw_value=560 +/- 80 raw_unit=uM

row_label: succinic semialdehyde

table_label: Official ScienceDirect abstract kinetic summary for purified 4-hydroxybutanoate dehydrogenase

source_databases_merged: brenda uniprot

enzyme: 4-hydroxybutyrate dehydrogenase

substrate: succinic semialdehyde


substrate_name: NAD

assay_conditions_summary: pH 9.4; cofactor NAD+

column_label: The official abstract states that in the reverse direction the Km values were 670 +/- 80 uM and 55 +/- 16 mM for NAD and 4-hydroxybutanoate, respectively.

raw_value_unit_evidence: Km raw_value=670 +/- 80 raw_unit=uM

row_label: NAD

substrate: NAD


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 6, substrate `4-Androstene-3,17-dione`, Rat 17HSD5 column group: Km = 1.6 uM (normalized 0.0016 mM); kcat = 2.0 min-1 (normalized 0.03333333333333333 s^-1); kcat/Km = 1.3 min-1 uM-1 (normalized 21.666666666666668 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 2.0 min-1 / 60 = 0.03333333333333333 s^-1; the catalog holds 0.033 s^(-1). Km: printed cell 1.6 uM / 1000 = 0.0016 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 1.3 min-1 uM-1, which is 1.3 x 1000 / 60 = 21.666666666666668 s^-1 mM^-1; the catalog holds 16.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 6, substrate `4-Androstene-3,17-dione`, Rat 17HSD5 column group: Km = 1.6 uM; kcat = 2.0 min-1; kcat/Km = 1.3 min-1 uM-1.

table_label: Table 2 (journal page 1058) 'Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription


substrate_name: testosterone

column_label: PMID 16788056 Table 2, steroid substrates; row Testosterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 21 uM, kcat 21 min^-1, kcat/Km 1.0 min^-1 uM^-1.

raw_value_unit_evidence: Km 21 uM; kcat 21 min^-1; kcat/Km 1.0 min^-1 uM^-1

row_label: Testosterone / Rat 17HSD5

substrate: testosterone


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Saccharomyces cerevisiae

substrate_name: D,L-isocitrate

enzyme: isocitrate dehydrogenase (NAD+)


organism: Aspergillus niger

substrate_name: NADP+

substrate: NADP+


substrate_name: D-glucose 6-phosphate


substrate_name: Unknown

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: pH 8.0, temperature not specified in the publication, varied substrate: NADP+

proof_lines: 25°C, pH 8.0, competitive inhibition constant

proof_lines: pH 8.0, temperature not specified in the publication, varied substrate: glucose 6-phosphate, slope inhibition constant

substrate: Unknown


organism: Plasmodium falciparum

assay_conditions_summary: pH 7.5; cofactor NADP+

column_label: Figure 2B, NADP+ x-axis panel, in-panel label Km: 8.6 uM; Results paragraph P24 repeats the same NADP+ Km value.

normalized_value_unit_evidence: 8.6 uM = 0.0086 mM; matches package/export Km 0.0086 mM.

raw_value_unit_evidence: Figure 2B labels the Michaelis-Menten fit for NADP+ as Km: 8.6 uM; Results paragraph P24 states the NADP+ Km was 8.6 uM for the ChemBridge batch.

row_label: NADP+ co-substrate Km

table_label: PMC8765527 Figure 2B and Results paragraph P24


proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: estradiol 17beta-dehydrogenase

substrate_name: NADPH; H+; Estrone

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

proof_lines: pH 7.4, 37°C recombinant His-tagged enzyme

proof_lines: pH and temperature not specified in the publication

enzyme: estradiol 17beta-dehydrogenase

substrate: NADPH; H+; Estrone


organism: Bos taurus

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Pseudomonas sp.


organism: Mycobacterium tuberculosis

substrate_name: isocitrate

sequence_source: UniProt P9WKL1 inferred from PMID 23409873 and linked PDB 4HCX (ICDH-1 from Mycobacterium tuberculosis H37Rv / Rv3339c)

proof_lines: pH 7.5, temperature not specified in the publication, recombinant His-tagged enzyme

substrate: isocitrate


substrate: D,L-isocitrate


organism: Bacillus sp. (in: firmicutes)


enzyme_display_name: pyridoxine 4-dehydrogenase

organism: Schizosaccharomyces pombe

substrate_name: pyridoxal

assay_conditions_summary: cofactor NADPH

enzyme: pyridoxine 4-dehydrogenase

substrate: pyridoxal


sequence_variant_note: Resolved canonical sequence from uniprot:O93874 and applied mutation signature H111A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


organism: Sus scrofa

assay_conditions_summary: cofactor NADP+


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

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

assay_conditions_summary: pH 7; cofactor NADPH

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

normalized_value_unit_evidence: Km=0.0013 mM converted from 1.3 uM

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

table_label: Table 1


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

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

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

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

row_label: 17-Ketosteroids / DHEA

enzyme: Dehydrogenase/reductase SDR family member 11


substrate_name: DHEA sulfate (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.012 mM converted from 12 uM

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

row_label: 17-Ketosteroids / DHEA sulfate

substrate: DHEA sulfate (at 37 degrees Celsius)


substrate_name: dehydrolithocholic acid (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.0011 mM converted from 1.1 uM

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


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

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

normalized_value_unit_evidence: Km=0.0051 mM converted from 5.1 uM

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


substrate_name: taurodehydrocholic acid (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.044 mM converted from 44 uM

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


substrate_name: dehydrocholic acid (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.029 mM converted from 29 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Dehydrocholic acid Km 29 uM

row_label: 3-Ketosteroids / Dehydrocholic acid


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


substrate_name: Isatin

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, Rat 17HSD5 column group: Km = 2.1 uM (normalized 0.0021000000000000003 mM); kcat = 11 min-1 (normalized 0.18333333333333332 s^-1); kcat/Km = 5.2 min-1 uM-1 (normalized 86.66666666666667 s^-1 mM^-1).

raw_value_unit_evidence: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, Rat 17HSD5 column group: Km = 2.1 uM; kcat = 11 min-1; kcat/Km = 5.2 min-1 uM-1.

table_label: Table 1 (journal page 1058) 'Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription

substrate: Isatin


substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH


substrate_name: (3S)-3-hydroxybutanoyl-CoA (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: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)


substrate_name: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)


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


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

proof_lines:
17beta-HSD10
Drosophila melanogaster
hydroxyacyl-CoA dehydrogenase


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

assay_conditions_summary: pH 7; cofactor NADH


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


organism: Aspergillus fumigatus

substrate_name: D-mannitol

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

substrate: D-mannitol


substrate_name: D-Xylulose

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NAD+

column_label: Table label: Table 1: AfM2DH substrate rows. Row: AfM2DH | D-Xylulose. Enzyme column group: AfM2DH. Columns read: kcat (s^-1) cell 64, open-chain-corrected Km (mM) cell 1.7, corrected kcat/Km (s^-1 mM^-1) cell 39. metric: kcat; raw value: 64; raw unit: s^-1; normalized value: 64.0 s^(-1); metric: Km; raw value: 1.7; raw unit: mM; normalized value: 1.7 mM; metric: kcat/Km; raw value: 39 +/- 2; raw unit: s^-1 mM^-1; normalized value: 39 s^-1 mM^-1; explicit printed primary cell; assay condition: ketose reduction at pH 7.1, Km and kcat/Km corrected for the available open-chain form of the carbonyl substrate; companion Table 2 measurements at 25 C and pH 7.1. Export row conditions: pH 7.1; 298.15 K.

normalized_value_unit_evidence: kcat raw 64 s^-1 -> 64.0 s^(-1); Km raw 1.7 mM -> 1.7 mM; explicit printed kcat/Km raw 39 +/- 2 s^-1 mM^-1 -> 39 s^-1 mM^-1. Conversion: 39 s^-1 mM^-1 requires no unit conversion. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 1: AfM2DH substrate rows | row: D-Xylulose, ketose reduction at pH 7.1: kcat `64 +/- 1 s^-1`; open-chain-corrected Km `1.7 +/- 0.1 mM`; corrected kcat/Km `39 +/- 2 s^-1 mM^-1`. | AfM2DH cells read: kcat = 64 s^-1; open-chain-corrected Km = 1.7 mM; corrected kcat/Km = 39 s^-1 mM^-1

row_label: AfM2DH | D-Xylulose

table_label: Table 1: AfM2DH substrate rows

substrate: D-Xylulose


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus

substrate_name: all-trans-retinol

proof_lines:
mouse 17betaHSD9
retinol dehydrogenase activity

substrate: all-trans-retinol


organism: Pseudomonas fluorescens

substrate_name: D-arabitol

substrate: D-arabitol


proof_lines: mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C


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


organism: Gallus gallus

proof_lines:
in absence of bovine serum albumin
in presence of bovine serum albumin


organism: Homo sapiens

assay_conditions_summary: pH 7.4; 310.15 K; cofactor CoA

proof_lines: cosubstrate NADP+, secretory endometrium


substrate_name: testosterone


substrate_name: androsterone

substrate: androsterone


substrate_name: D-fructose

assay_conditions_summary: pH 10; buffer 50 mM glycine/NaOH

proof_lines:
in 50 mM glycine/NaOH buffer at pH 10.0
recombinant protein

substrate: D-fructose


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.


substrate_name: estrone

substrate: estrone


organism: Aeropyrum pernix

substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+


organism: Cavia porcellus


substrate: testosterone


enzyme_display_name: 2-hydroxy-3-oxopropionate reductase

organism: Mycosarcoma maydis

protein_accession_database: NCBI Protein

sequence_source: paper_backed_accession:EAK83762.1 (PMID:21305026; archived GenBank protein for UM02592/Tsr1)

assay_conditions_summary: pH 8.5; cofactor NADH

column_label: Prose immediately above Table 1 reports Km 0.19 +/- 0.03 mM for tartronic semialdehyde in the reduction reaction.

raw_value_unit_evidence: Km raw_value=0.19 raw_unit=mM

row_label: Tartronic semialdehyde

table_label: Table 1. Kinetic parameters of rTsr1.

enzyme: 2-hydroxy-3-oxopropionate reductase


assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Primary PMC HTML/JATS Table 1, Oxidation section, beta-NADP+ row, Km column = 0.30 +/- 0.04 uM.

normalized_value_unit_evidence: Normalized paper Km: 0.30 uM = 0.00030 mM, matching export Km 0.0003 mM.

raw_value_unit_evidence: Table 1 reports beta-NADP+ Km 0.30 +/- 0.04 uM.

row_label: Oxidation; beta-NADP+ row; Km column

table_label: Table 1. Kinetic parameters of rTsr1

substrate: NADP+


substrate_name: NADH

column_label: Primary PMC HTML/JATS Table 1, Reduction section, beta-NADH row, Km column = 14.29 +/- 3.1 uM.

normalized_value_unit_evidence: Normalized paper Km: 14.29 uM = 0.01429 mM; export has 0.0143 mM, matching by rounded value and within reported uncertainty.

raw_value_unit_evidence: Table 1 reports beta-NADH Km 14.29 +/- 3.1 uM.

row_label: Reduction; beta-NADH row; Km column

substrate: NADH


substrate_name: D-glycerate

column_label: Table 1 row D-Glycerate lists Km 17.7 +/- 2.3 mM.

raw_value_unit_evidence: Km raw_value=17.7 raw_unit=mM

row_label: D-Glycerate

substrate: D-glycerate


substrate_name: L-Glycerate

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

column_label: Table 1 row L-Glycerate lists Km 123.2 +/- 21.8 mM.

raw_value_unit_evidence: Km raw_value=123.2 raw_unit=mM

row_label: L-Glycerate

substrate: L-Glycerate


organism: Pseudomonas putida


organism: Rhodococcus sp. P14


organism: Thermotoga maritima

sequence_source: UniProt Q9WYD4 mapped from Thermotoga maritima TM_0298 / TM0298 named in PMID 18719905

assay_conditions_summary: pH 6.1; cofactor NADH

row_label: 60 C / pH 6.1 / NADH


substrate_name: NAD+

assay_conditions_summary: pH 8.3; cofactor NAD+

substrate: NAD+


substrate_name: NADPH

assay_conditions_summary: pH 6.1; cofactor NADPH

column_label: Table 1 row 80 C, pH 6.1, NADPH under Km (mM): 0.17 +/- 0.017.

row_label: 80 C / pH 6.1 / NADPH

substrate: NADPH


column_label: Table 1 row 80 C, pH 8.3, D-Mannitol under Km (mM): 5.51 +/- 0.74.

row_label: 80 C / pH 8.3 / D-Mannitol


assay_conditions_summary: pH 8.3; cofactor NADP+

column_label: Table 1 row 80 C, pH 8.3, NADP+ under Km (mM): 7.5 +/- 0.53.

normalized_value_unit_evidence: Km 7.5 mM.


organism: Levilactobacillus brevis

assay_conditions_summary: cofactor NADH


assay_conditions_summary: cofactor NAD+


organism: Absidia glauca


organism: Curvularia lunata

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: 25°C, pH 8.0, mutant enzyme Y49D, cosubstrate: 4-estrene-3,17-dione


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: 25°C, pH 8.0, mutant enzyme Y49D, cosubstrate: 4-estrene-17beta-ol-3-one


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


proof_lines: 25°C, pH 8.0, mutant enzyme H164W, cosubstrate: 4-estrene-3,17-dione


proof_lines: 25°C, pH 8.0, mutant enzyme H164G, cosubstrate: 4-estrene-3,17-dione


proof_lines: 25°C, pH 8.0, mutant enzyme H164W, cosubstrate: 4-estrene-17beta-ol-3-one


proof_lines: 25°C, pH 8.0, mutant enzyme H164G, cosubstrate: 4-estrene-17beta-ol-3-one


proof_lines: 25°C, pH 8.0, wild-type enzyme, cosubstrate: 4-estrene-17beta-ol-3-one


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H111A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; cofactor NADPH


proof_lines: 25°C, pH 8.0, wild-type enzyme, cosubstrate: 4-estrene-3,17-dione


organism: Leuconostoc mesenteroides


sequence_source: GenBank AY090766.1 CDS / protein AAM09029.1 linked from PMID 12226722 (Leuconostoc mesenteroides ATCC 9135 mdh)


organism: Bradyrhizobium japonicum


organism: Porphyromonas gingivalis

substrate_name: succinate semialdehyde

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: with NADH as cosubstrate, at pH 8.0 and 37°C

substrate: succinate semialdehyde


assay_conditions_summary: pH 9


proof_lines: pH and temperature not specified in the publication


organism: Tetraselmis subcordiformis


organism: Montipora capitata

assay_conditions_summary: cofactor NADP+


organism: Sus scrofa


organism: Fructilactobacillus sanfranciscensis


proof_lines:
isoenzyme 2
isoenzyme 1


assay_conditions_summary: cofactor NADPH


substrate_name: androstenedione

substrate: androstenedione


substrate_name: benzene dihydrodiol

proof_lines:
isoenzyme 1
isoenzyme 2

substrate: benzene dihydrodiol


organism: Canis lupus familiaris

substrate_name: Unknown

substrate: Unknown


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

column_label: Accepted manuscript page 14 states the kinetic constants for purified H6-17beta-HSD: Km, Vmax, kcat, and kcat/Km values are 18.9 uM, 12.5 umol/min/mg, 9.38 s^-1, and 4.96 x 10^5 s^-1 M^-1, respectively.

normalized_value_unit_evidence: Km normalized_value=0.0189 normalized_unit=mM; kcat normalized_value=9.38 normalized_unit=s^-1; kcat/Km normalized_value=496.29629629629636 normalized_unit=s^-1 mM^-1 from 9.38 / 0.0189.

raw_value_unit_evidence: Km raw_value=18.9 raw_unit=uM; kcat raw_value=9.38 raw_unit=s^-1; kcat/Km printed_value=4.96 x 10^5 printed_unit=s^-1 M^-1.

row_label: Purified H6-17beta-HSD from Rhodococcus sp. P14 with estradiol

table_label: Accepted manuscript page 14 kinetic-constant prose


organism: Thermotoga neapolitana

proof_lines:
pH 6.5, 90°C
at pH 6.5 and 90°C


organism: Homo sapiens

substrate_name: NAD

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

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: NAD


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: androsterone

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


enzyme_display_name: Aldo-keto reductase family 1 member C4

assay_conditions_summary: pH 7; cofactor NADP+

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

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

enzyme: Aldo-keto reductase family 1 member C4


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


assay_conditions_summary: pH 7; cofactor NADPH

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

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


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: testosterone (oxidation)

substrate: testosterone (oxidation)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: progesterone (reduction)

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

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

row_label: Progesterone reduction / AKR1C1

enzyme: Aldo-keto reductase family 1 member C1

substrate: progesterone (reduction)


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

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


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

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


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

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

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


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

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

row_label: Testosterone oxidation / AKR1C1 (R)


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

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


enzyme_display_name: Aldo-keto reductase family 1 member C2

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

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

enzyme: Aldo-keto reductase family 1 member C2


substrate_name: (s)-tetralol

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

substrate: (s)-tetralol


substrate_name: (s)-tetralol (oxidation)

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

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor CoA

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

enzyme: Aldo-keto reductase family 1 member B15

substrate: all-trans-retinal


substrate_name: D,L-glyceraldehyde

smiles: OCC(O)C=O

substrate: D,L-glyceraldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


smiles: CCCCC=CC=O


smiles: CCCCCC=CC(O)CC=O


smiles: CCCCCC=CC(=O)C


substrate_name: farnesal

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

substrate: farnesal


substrate_name: NADPH

substrate: NADPH


organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


enzyme_display_name: UniProt O93874

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt O93874

source: skid


substrate_name: NADP+

substrate: NADP+


substrate_name: NAD+

substrate: NAD+


substrate_name: NADH

substrate: NADH


organism: Aspergillus fumigatus

substrate_name: L-sorbitol

assay_conditions_summary: pH 10; buffer 100 mM glycine/NaOH

proof_lines: at 25°C, in 100 mM glycine/NaOH buffer pH 10.0

substrate: L-sorbitol


substrate_name: D-xylulose

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

column_label: Primary Wiley full article, Table 1, D-Xylulose row, kcat/Km column; caption supplies open-chain correction and pH 7.1.

normalized_value_unit_evidence: kcat 64 s^-1; Km 1.7 mM; explicit corrected kcat/Km 39 s^-1 mM^-1.

row_label: D-Xylulose

table_label: Table 1. Kinetic constants of AfM2DH for reactions with different polyol and ketose substrates

substrate: D-xylulose


substrate_name: D-fructose

assay_conditions_summary: pH 7.1; buffer 100 mM Tris/HCl; cofactor NADPH

column_label: Primary Wiley full article, Table 1, D-Fructose row, kcat/Km column; caption supplies open-chain correction and pH 7.1.

normalized_value_unit_evidence: kcat 86 s^-1; Km 0.60 mM; explicit corrected kcat/Km 140 s^-1 mM^-1.

row_label: D-Fructose

substrate: D-fructose


substrate_name: D-arabinitol

assay_conditions_summary: pH 10

column_label: Primary Wiley full article, Table 1, D-Arabinitol row, kcat/Km column; caption supplies polyol-oxidation pH 10.0.

normalized_value_unit_evidence: kcat 162 s^-1; Km 163 mM; explicit kcat/Km 0.99 s^-1 mM^-1.

row_label: D-Arabinitol

substrate: D-arabinitol


assay_conditions_summary: pH 7.1; buffer 100 mM Tris/HCl; cofactor NADH

column_label: Primary Wiley full article, Table 2, K_NADH row, AfM2DH column.

normalized_value_unit_evidence: Km NADH 0.015 mM.

raw_value_unit_evidence: Table 2 AfM2DH column, K_NADH row: 15 +/- 8 uM.

row_label: K_NADH; AfM2DH column

table_label: Table 2. Kinetic parameters of AfM1PDH and AfM2DH at 25 C and pH 7.1


assay_conditions_summary: pH 7.1; buffer 100 mM glycine/NaOH; cofactor NAD+

column_label: Primary Wiley full article, Table 2, K_NAD row, AfM2DH column.

normalized_value_unit_evidence: Km NAD+ 0.11 mM.

raw_value_unit_evidence: Table 2 AfM2DH column, K_NAD row: 0.11 +/- 0.02 mM.

row_label: K_NAD; AfM2DH column


organism: Escherichia coli

substrate_name: Succinic semialdehyde

assay_conditions_summary: pH 7.2; buffer 100 mM MOPS-KOH; cofactor NADH

proof_lines: in 100 mM MOPS-KOH buffer (pH 7.2), at 37°C

proof_lines: kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat is 548 sec(-1) with NADH as substrate.

substrate: Succinic semialdehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

assay_conditions_summary: pH 8.8; buffer 100 mM Tris-HCl; cofactor NADH

proof_lines: in 100 mM Tris-HCl buffer (pH 8.8), at 37°C

substrate: methylglyoxal


assay_conditions_summary: cofactor NADH


substrate_name: gamma-hydroxybutyrate

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

assay_conditions_summary: pH 8.8; 310.15 K; buffer 100 mM Tris-HCl

substrate: gamma-hydroxybutyrate


substrate_name: androsterone (tested with isoform 1 in the reductive reaction)

column_label: Table 2 row Androsterone under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 2.8 +/- 0.2 uM for Androsterone.

row_label: Reductive reactions; Androsterone

table_label: Table 2: Kinetic parameters of AKR1B15.1


substrate_name: delta-4-androstenedione (tested with isoform 1 in the reductive reaction)

column_label: PMC Table 3 columns Substrate, Km (uM), kcat (min^-1), and kcat/Km (uM^-1 min^-1); row Delta4-Androstenedione reports Km 1.9 +/- 0.2 uM.

raw_value_unit_evidence: Km raw_value=1.9 +/- 0.2 uM raw_unit=uM

row_label: Reductive reactions / Delta4-Androstenedione

table_label: PMC Table 3 Kinetic constants of AKR1B15.1


substrate_name: estrone (tested with isoform 1 in the reductive reaction)

column_label: Table 2 row Estrone under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 2.5 +/- 0.4 uM for Estrone.

row_label: Reductive reactions; Estrone


substrate_name: acetoacetyl-CoA (tested with isoform 1 in the reductive reaction)

column_label: Table 2 row Acetoacetyl-CoA under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 63.4 +/- 7.4 uM for Acetoacetyl-CoA.

row_label: Reductive reactions; Acetoacetyl-CoA


substrate_name: testosterone (tested with isoform 1 in the oxidative reaction)

column_label: Table 2 row Testosterone under Oxidative reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 7.1 +/- 1.5 uM for Testosterone.

row_label: Oxidative reactions; Testosterone


substrate_name: 17-beta-estradiol (tested with isoform 1 in the oxidative reaction)

column_label: Table 2 row 17beta-Estradiol under Oxidative reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 9.1 +/- 1.2 uM for 17beta-Estradiol.

row_label: Oxidative reactions; 17beta-Estradiol


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

assay_conditions_summary: pH 7; cofactor NADH

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


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)


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


organism: Macaca fuscata fuscata

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

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

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

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

table_label: Table 2


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

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

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

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


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


enzyme_display_name: 3-sulfolactaldehyde reductase

organism: Escherichia coli (strain K12)

enzyme: 3-sulfolactaldehyde reductase


substrate_name: NADH


organism: Leuconostoc pseudomesenteroides

substrate_name: D-mannitol

substrate: D-mannitol


substrate_name: D-fructose


organism: Cupriavidus necator

proof_lines: kcat is 8.4 sec(-1) with 4-hydroxybutanoate as substrate. kcat is 8.9 sec(-1) with NAD(+) as substrate.


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: UniProt Q9BPX1

enzyme: UniProt Q9BPX1


substrate_name: progesterone

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


enzyme_display_name: UniProt P14061

substrate_name: estrone

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

source_databases_merged: skid uniprot

enzyme: UniProt P14061

substrate: estrone


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

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


substrate_name: (s)-tetralol

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

substrate: (s)-tetralol


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


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

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


enzyme_display_name: Aldo-keto reductase family 1 member C3

substrate_name: prostaglandin H2

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin H2


enzyme_display_name: mannitol 2-dehydrogenase

organism: Eimeria tenella

enzyme: mannitol 2-dehydrogenase


enzyme_display_name: Pyridoxine 4-dehydrogenase

proof_lines: kcat is 0.11 sec(-1) for the Kemp eliminase activity towards 5-nitrobenzisoxazole.

enzyme: Pyridoxine 4-dehydrogenase


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 7, substrate `Estrone`, Rat 17HSD5 column group: Km = 11 uM (normalized 0.011 mM); kcat = 2.7 min-1 (normalized 0.045000000000000005 s^-1); kcat/Km = 0.25 min-1 uM-1 (normalized 4.166666666666667 s^-1 mM^-1).

enzyme: 17beta-estradiol 17-dehydrogenase


organism: Pseudomonas fluorescens

substrate_name: D-Arabitol

column_label: Table 2; row label WT; substrate D-Arabitol; checked column(s): km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm

row_label: WT

substrate: D-Arabitol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D230A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

column_label: Table 1; row label D230A; substrate D-mannitol; checked column(s): kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E133A to reconstruct the assayed variant sequence.

column_label: Table 1; row label E133A; substrate D-mannitol; checked column(s): kcat, kcat_over_km, km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E133Q to reconstruct the assayed variant sequence.

column_label: Table 1; row label E133Q; substrate D-mannitol; checked column(s): kcat, kcat_over_km, km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H303A to reconstruct the assayed variant sequence.

column_label: Table 1; row label H303A; substrate D-mannitol; checked column(s): kcat_over_km, km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature H303A/R373A/K381A to reconstruct the assayed variant sequence.

column_label: Table 1; row label H303A/R373A/K381A; substrate D-mannitol; checked column(s): kcat_over_km, km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature K381A to reconstruct the assayed variant sequence.

column_label: Table 1; row label K381A; substrate D-mannitol; checked column(s): kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature N191A to reconstruct the assayed variant sequence.

column_label: Table 1; row label N191A; substrate D-mannitol; checked column(s): kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature N300A to reconstruct the assayed variant sequence.

column_label: Table 1; row label N300A; substrate D-mannitol; checked column(s): kcat_over_km, km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N300D to reconstruct the assayed variant sequence.

column_label: Table 1; row label N300D; substrate D-mannitol; checked column(s): kcat, kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 2; row label D230A; substrate D-Arabitol; checked column(s): kcat, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 6, substrate `4-Chlorobenzaldehyde`, Rat 17HSD5 column group: Km = 263 uM (normalized 0.263 mM); kcat = 6.5 min-1 (normalized 0.10833333333333334 s^-1); kcat/Km = 0.02 min-1 uM-1 (normalized 0.33333333333333337 s^-1 mM^-1).


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 10, substrate `4-Nitroacetophenone`, Rat 17HSD5 column group: Km = 84 uM (normalized 0.084 mM); kcat = 8.3 min-1 (normalized 0.13833333333333334 s^-1); kcat/Km = 0.10 min-1 uM-1 (normalized 1.666666666666667 s^-1 mM^-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (A), printed row 2, substrate `5a-Dihydrotestosterone`, Rat 17HSD5 column group: Km = 28 uM (normalized 0.028 mM); kcat = 18 min-1 (normalized 0.3 s^-1); kcat/Km = 0.65 min-1 uM-1 (normalized 10.833333333333334 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 18 min-1 / 60 = 0.3 s^-1; the catalog holds 0.3 s^(-1). Km: printed cell 28 uM / 1000 = 0.028 mM; the catalog holds 0.028 mM. kcat/Km: the paper prints the cell 0.65 min-1 uM-1, which is 0.65 x 1000 / 60 = 10.833333333333334 s^-1 mM^-1; the catalog holds 10.714285714285714 s^(-1)*mM^(-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 5, substrate `5a-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 2.4 uM (normalized 0.0024 mM); kcat = 2.5 min-1 (normalized 0.041666666666666664 s^-1); kcat/Km = 1.1 min-1 uM-1 (normalized 18.333333333333332 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 2.5 min-1 / 60 = 0.041666666666666664 s^-1; the catalog holds 0.042 s^(-1). Km: printed cell 2.4 uM / 1000 = 0.0024 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 1.1 min-1 uM-1, which is 1.1 x 1000 / 60 = 18.333333333333332 s^-1 mM^-1; the catalog holds 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 5, substrate `5a-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 2.4 uM; kcat = 2.5 min-1; kcat/Km = 1.1 min-1 uM-1.


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (A), printed row 6, substrate `5a-Androstane-3a,17b-diol`, Rat 17HSD5 column group: Km = 19 uM (normalized 0.019 mM); kcat = 8.4 min-1 (normalized 0.14 s^-1); kcat/Km = 0.44 min-1 uM-1 (normalized 7.333333333333334 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 8.4 min-1 / 60 = 0.14 s^-1; the catalog holds 0.14 s^(-1). Km: printed cell 19 uM / 1000 = 0.019 mM; the catalog holds 0.019 mM. kcat/Km: the paper prints the cell 0.44 min-1 uM-1, which is 0.44 x 1000 / 60 = 7.333333333333334 s^-1 mM^-1; the catalog holds 7.36842105263158 s^(-1)*mM^(-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 2, substrate `5b-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 6.2 uM (normalized 0.0062 mM); kcat = 1.6 min-1 (normalized 0.02666666666666667 s^-1); kcat/Km = 0.25 min-1 uM-1 (normalized 4.166666666666667 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 1.6 min-1 / 60 = 0.02666666666666667 s^-1; the catalog holds 0.027 s^(-1). Km: printed cell 6.2 uM / 1000 = 0.0062 mM; the catalog holds 0.006 mM. kcat/Km: the paper prints the cell 0.25 min-1 uM-1, which is 0.25 x 1000 / 60 = 4.166666666666667 s^-1 mM^-1; the catalog holds 4.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 2, substrate `5b-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 6.2 uM; kcat = 1.6 min-1; kcat/Km = 0.25 min-1 uM-1.


column_label: table label: Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: TBE (Reduction section of Table 1); column label: Rat 17HSD5 Km (uM), Rat 17HSD5 kcat (min-1) and Rat 17HSD5 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the TBER1 column group and no cell is taken from any other row; raw value: Km 16 uM, kcat 9.2 min-1, kcat/Km 0.58 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.016 mM, kcat 0.153 s^-1, kcat/Km 9.5625 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined at pH 7.4 with NAD(H) for TBER1 and with NADP(H) for rat 17HSD5 as the coenzyme. This record reads the Rat 17HSD5 column group of this one row, so the coenzyme for these cells is NADP(H). Unit note: the CiteSeerX text layer renders the printed micro sign as m, so the transcribed footnote reads Km (mM) and kcat/Km (min-1 mM-1) Exported assay conditions: pH 7.4, 298.15 K; the exported row carries no cofactor annotation, so no cofactor record is contradicted.

normalized_value_unit_evidence: Km 16 uM divided by 1000 gives 0.016 mM at the export's stored precision; exported Km 0.016 mM. kcat 9.2 min-1 divided by 60 gives 0.153 s^-1 at the export's stored precision; exported kcat 0.153 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.153 s^-1 divided by 0.016 mM giving 9.5625 s^-1 mM^-1, and of nothing else; exported kcat/Km 9.5625 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Reduction section, row TBE, Rat 17HSD5 column group: Km 16 uM; kcat 9.2 min-1; kcat/Km 0.58 min-1 uM-1.

row_label: TBE


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 1, substrate `9,10-Phenanthrenequinone`, Rat 17HSD5 column group: Km = 0.5 uM (normalized 0.0005 mM); kcat = 18 min-1 (normalized 0.3 s^-1); kcat/Km = 36 min-1 uM-1 (normalized 600.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 18 min-1 / 60 = 0.3 s^-1; the catalog holds 0.3 s^(-1). Km: printed cell 0.5 uM / 1000 = 0.0005 mM; the catalog holds 0.0005 mM. kcat/Km: the paper prints the cell 36 min-1 uM-1, which is 36 x 1000 / 60 = 600.0 s^-1 mM^-1; the catalog holds 600.0 s^(-1)*mM^(-1).


substrate_name: 9alpha,11beta-Prostaglandin F2

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 7, substrate `9a,11b-PGF2`, Rat 17HSD5 column group: Km = 161 uM (normalized 0.161 mM); kcat = 1.8 min-1 (normalized 0.03 s^-1); kcat/Km = 0.01 min-1 uM-1 (normalized 0.16666666666666669 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 1.8 min-1 / 60 = 0.03 s^-1; the catalog holds 0.03 s^(-1). Km: printed cell 161 uM / 1000 = 0.161 mM; the catalog holds 0.161 mM. kcat/Km: the paper prints the cell 0.01 min-1 uM-1, which is 0.01 x 1000 / 60 = 0.16666666666666669 s^-1 mM^-1; the catalog holds 0.18633540372670807 s^(-1)*mM^(-1).

substrate: 9alpha,11beta-Prostaglandin F2


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 6, substrate `b-3-Hydroxyhexobarbital`, Rat 17HSD5 column group: Km = 840 uM (normalized 0.84 mM); kcat = 3.5 min-1 (normalized 0.058333333333333334 s^-1); kcat/Km = 0.004 min-1 uM-1 (normalized 0.06666666666666668 s^-1 mM^-1).


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: PMID 16788056 Table 2, steroid substrates; row 16-Ketoestrone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 0.7 uM, kcat 5.2 min^-1, kcat/Km 7.5 min^-1 uM^-1.

raw_value_unit_evidence: Km 0.7 uM; kcat 5.2 min^-1; kcat/Km 7.5 min^-1 uM^-1

row_label: 16-Ketoestrone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 17a-Hydroxyprogesterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 50 uM, kcat 6.2 min^-1, kcat/Km 0.12 min^-1 uM^-1.

raw_value_unit_evidence: Km 50 uM; kcat 6.2 min^-1; kcat/Km 0.12 min^-1 uM^-1

row_label: 17a-Hydroxyprogesterone / Rat 17HSD5


column_label: PMID 16788056 Table 1, non-steroidal substrates; row R-Camphorquinone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 1.6 uM, kcat 11 min^-1, kcat/Km 6.9 min^-1 uM^-1.

raw_value_unit_evidence: Km 1.6 uM; kcat 11 min^-1; kcat/Km 6.9 min^-1 uM^-1

row_label: R-Camphorquinone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Pregenen-20a-ol-3-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 24 uM, kcat 8.5 min^-1, kcat/Km 0.35 min^-1 uM^-1.

raw_value_unit_evidence: Km 24 uM; kcat 8.5 min^-1; kcat/Km 0.35 min^-1 uM^-1

row_label: 4-Pregenen-20a-ol-3-one / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 21-Dehydrocortisol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 2.8 uM, kcat 7.2 min^-1, kcat/Km 2.6 min^-1 uM^-1.

raw_value_unit_evidence: Km 2.8 uM; kcat 7.2 min^-1; kcat/Km 2.6 min^-1 uM^-1

row_label: 21-Dehydrocortisol / Rat 17HSD5


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

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2,3-Pentanedione; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 57 uM, kcat 8.8 min^-1, kcat/Km 0.15 min^-1 uM^-1.

raw_value_unit_evidence: Km 57 uM; kcat 8.8 min^-1; kcat/Km 0.15 min^-1 uM^-1

row_label: 2,3-Pentanedione / Rat 17HSD5


column_label: PMID 16788056 Table 1, non-steroidal substrates; row Acetylpyridine; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 266 uM, kcat 4.5 min^-1, kcat/Km 0.02 min^-1 uM^-1.

raw_value_unit_evidence: Km 266 uM; kcat 4.5 min^-1; kcat/Km 0.02 min^-1 uM^-1

row_label: Acetylpyridine / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 5b-Androstan-3a-ol-17-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 6.7 uM, kcat 1.3 min^-1, kcat/Km 0.20 min^-1 uM^-1.

raw_value_unit_evidence: Km 6.7 uM; kcat 1.3 min^-1; kcat/Km 0.20 min^-1 uM^-1

row_label: 5b-Androstan-3a-ol-17-one / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row Dehydroepiandrosterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 11 uM, kcat 5.0 min^-1, kcat/Km 0.45 min^-1 uM^-1.

raw_value_unit_evidence: Km 11 uM; kcat 5.0 min^-1; kcat/Km 0.45 min^-1 uM^-1

row_label: Dehydroepiandrosterone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Androsten-3a-ol-17-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 8.5 uM, kcat 1.9 min^-1, kcat/Km 0.22 min^-1 uM^-1.

raw_value_unit_evidence: Km 8.5 uM; kcat 1.9 min^-1; kcat/Km 0.22 min^-1 uM^-1

row_label: 4-Androsten-3a-ol-17-one / Rat 17HSD5


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

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

normalized_value_unit_evidence: Km=0.0052 mM converted from 5.2 uM

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


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

assay_conditions_summary: cofactor NADPH

column_label: Table 1 row 4-Androstene-3,17-dione; KM (uM) = 4.6; Vmax = 52 mU/mg; Vmax/KM = 11 mU/mg/uM.

raw_value_unit_evidence: KM column reports 4.6 uM.

table_label: Table 1. Substrate specificity for ketosteroids.


substrate_name: progesterone (at 37 degrees Celsius)

column_label: Table 1 row Progesterone; KM (uM) = 3.4; Vmax = 36 mU/mg; Vmax/KM = 11 mU/mg/uM.

raw_value_unit_evidence: KM column reports 3.4 uM.

row_label: Progesterone

substrate: progesterone (at 37 degrees Celsius)


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

column_label: Table 1 row 5-beta-Pregnane-3,20-dione; KM (uM) = 15; Vmax = 123 mU/mg; Vmax/KM = 8.2 mU/mg/uM.

raw_value_unit_evidence: KM column reports 15 uM.


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

assay_conditions_summary: cofactor NADP+

column_label: Table 2 row 17-beta-Estradiol; KM (uM) = 16; Vmax = 246 mU/mg; corresponding ketosteroid = Estrone.

raw_value_unit_evidence: KM column reports 16 uM.

table_label: Table 2. Substrate specificity for hydroxysteroids.