column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row 3-Methylcyclohexanone, TR-I Km column; Km cell 41 uM, normalized 0.041 mM.

raw_value_unit_evidence: Km raw 41 uM from Table I row 3-Methylcyclohexanone, TR-I Km column

row_label: TR-I / 3-Methylcyclohexanone


enzyme_display_name: tropinone reductase I

organism: Hyoscyamus niger

substrate_name: NADPH

source_db: brenda

verification_status: corrected

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: cofactor NADPH

column_label: Page 841 prose reports TR-I NADPH Km as 11.3 +/- 1.7 uM, normalized 0.0113 mM.

raw_value_unit_evidence: Km raw 11.3 +/- 1.7 uM from page 841 prose, TR-I NADPH cofactor Km

row_label: TR-I / NADPH

table_label: Page 841 prose; cofactor Km values

data_origin: experimental

enzyme: tropinone reductase I

substrate: NADPH

status: corrected

source: brenda


verification_status: verified

column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row N-Methyl-4-piperidone, TR-I Km column; Km cell 231 uM, normalized 0.231 mM.

raw_value_unit_evidence: Km raw 231 uM from Table I row N-Methyl-4-piperidone, TR-I Km column

row_label: TR-I / N-Methyl-4-piperidone

status: verified


substrate_name: tropinone

column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row Tropinone, TR-I Km column; Km cell 1010 uM, normalized 1.01 mM.

normalized_value_unit_evidence: Km 1.01 mM

raw_value_unit_evidence: Km raw 1010 uM from Table I row Tropinone, TR-I Km column

row_label: TR-I / Tropinone

substrate: tropinone


column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row 3-Quinuclidinone, TR-I Km column; Km cell 1810 uM, normalized 1.81 mM.

normalized_value_unit_evidence: Km 1.81 mM

raw_value_unit_evidence: Km raw 1810 uM from Table I row 3-Quinuclidinone, TR-I Km column

row_label: TR-I / 3-Quinuclidinone


substrate_name: Tropine

column_label: Page 841 prose reports TR-I tropine Km as 2600 +/- 130 uM, normalized 2.6 mM.

normalized_value_unit_evidence: Km 2.6 mM

raw_value_unit_evidence: Km raw 2600 +/- 130 uM from page 841 prose, TR-I tropine Km

row_label: TR-I / Tropine

table_label: Page 841 prose; TR-I tropinone and tropine Km values

substrate: Tropine


substrate_name: NADH

verification_status: unverified

assay_conditions_summary: cofactor NADH

substrate: NADH

status: unverified


enzyme_display_name: IMP dehydrogenase

organism: Homo sapiens

substrate_name: IMP

source_db: oed

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D255G to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row D255G; columns Km IMP (uM)=16.8 +/- 0.6 and kcat (s^-1)=0.35; kcat/Km locked from the same row for substrate IMP.

normalized_value_unit_evidence: kcat normalized_value=0.35 normalized_unit=s^-1; km normalized_value=0.0168 normalized_unit=mM; kcat_over_km normalized_value=20.833333333333332 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row D255G: Km IMP 16.8 +/- 0.6 uM; kcat 0.35 s^-1.

enzyme: IMP dehydrogenase

substrate: IMP

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G340E to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row G340E; columns Km IMP (uM)=7 +/- 3 and kcat (s^-1)=0.55; kcat/Km locked from the same row for substrate IMP.

normalized_value_unit_evidence: kcat normalized_value=0.55 normalized_unit=s^-1; km normalized_value=0.007 normalized_unit=mM; kcat_over_km normalized_value=78.57142857142857 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row G340E: Km IMP 7 +/- 3 uM; kcat 0.55 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M482I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row M482I; columns Km IMP (uM)=23 +/- 4 and kcat (s^-1)=0.40; kcat/Km locked from the same row for substrate IMP.

normalized_value_unit_evidence: kcat normalized_value=0.40 normalized_unit=s^-1; km normalized_value=0.023 normalized_unit=mM; kcat_over_km normalized_value=17.39130434782609 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row M482I: Km IMP 23 +/- 4 uM; kcat 0.40 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q277R to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row Q277R; columns Km IMP (uM)=80 +/- 17 and kcat (s^-1)=0.13; kcat/Km locked from the same row for substrate IMP.

normalized_value_unit_evidence: kcat normalized_value=0.13 normalized_unit=s^-1; km normalized_value=0.08 normalized_unit=mM; kcat_over_km normalized_value=1.625 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row Q277R: Km IMP 80 +/- 17 uM; kcat 0.13 s^-1.


kcat_over_km_origin: calculated


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A462T with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row A462T; columns Km NAD (uM)=37 +/- 7 and kcat (s^-1)=0.61; kcat/Km locked from the same row for substrate NAD+.

normalized_value_unit_evidence: kcat normalized_value=0.61 normalized_unit=s^-1; km normalized_value=0.037 normalized_unit=mM; kcat_over_km normalized_value=16.486486486486488 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row A462T: Km NAD 37 +/- 7 uM; kcat 0.61 s^-1.

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F456S/D470G to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row F456S/D470G; columns Km NAD (uM)=17 +/- 1 and kcat (s^-1)=0.17; kcat/Km locked from the same row for substrate NAD+.

normalized_value_unit_evidence: kcat normalized_value=0.17 normalized_unit=s^-1; km normalized_value=0.017 normalized_unit=mM; kcat_over_km normalized_value=10.0 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row F456S/D470G: Km NAD 17 +/- 1 uM; kcat 0.17 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L30F/Q277R to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row L30F/Q277R; columns Km NAD (uM)=180 +/- 13 and kcat (s^-1)=0.10; kcat/Km locked from the same row for substrate NAD+.

normalized_value_unit_evidence: kcat normalized_value=0.10 normalized_unit=s^-1; km normalized_value=0.18 normalized_unit=mM; kcat_over_km normalized_value=0.5555555555555556 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row L30F/Q277R: Km NAD 180 +/- 13 uM; kcat 0.10 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q277R/A462T to reconstruct the assayed variant sequence.

column_label: PMID 8995388 Table III. Ki for MPA inhibition and steady state kinetic parameters of wild type and mutant IMPDHs; row Q277R/A462T; columns Km NAD (uM)=320 +/- 30 and kcat (s^-1)=0.51; kcat/Km locked from the same row for substrate NAD+.

normalized_value_unit_evidence: kcat normalized_value=0.51 normalized_unit=s^-1; km normalized_value=0.32 normalized_unit=mM; kcat_over_km normalized_value=1.59375 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table III row Q277R/A462T: Km NAD 320 +/- 30 uM; kcat 0.51 s^-1.


organism: Cochlearia officinalis

proof_lines:
tropinone reductase
Cochlearia officinalis
tropinone reduction


enzyme_display_name: Tropinone reductase

source_db: uniprot

enzyme: Tropinone reductase

source: uniprot


substrate_name: nortropinone

proof_lines:
tropinone reductase
Cochlearia officinalis
broad substrate specificity

substrate: nortropinone


substrate_name: quinuclidinone

substrate: quinuclidinone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E120H with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.


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 '3alpha-Hydroxy-5beta-androstan-17-one'; column 'Substrate stereospecificity' = 3alpha, 5beta; column 'kcat (x 10^-3 s^-1)' = 125; column 'Km (uM)' = 36.4; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 34. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 125 with the column head x 10^-3 s^-1, so the cell reads 125 x 10^-3 s^-1; the paper value is 0.125 s^(-1); the exported value is 0.125 s^(-1). Km: printed Table 3 cell 36.4 uM; 1 uM is 0.001 mM, so 36.4 / 1000 = 0.0364 mM; the paper value is 0.0364 mM; the exported value is 0.036 mM. kcat/Km: printed Table 3 cell 34 with the column head x 10^2 M^-1 s^-1, so the cell reads 3400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3400 / 1000 = 3.4 s^-1 mM^-1; the paper value is 3.4 s^(-1)*mM^(-1); the exported value is 3.4722222222222223 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row '3alpha-Hydroxy-5beta-androstan-17-one': kcat = 125 s-1 under the column multiplier x 10^-3; Km = 36.4 uM; printed kcat/Km = 34 M-1 s-1 under the column multiplier x 10^2.


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 '3beta-Hydroxy-5beta-androstan-17-one'; column 'Substrate stereospecificity' = 3beta, 5beta; column 'kcat (x 10^-3 s^-1)' = 43; column 'Km (uM)' = 15.3; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 28. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 43 with the column head x 10^-3 s^-1, so the cell reads 43 x 10^-3 s^-1; the paper value is 0.043 s^(-1); the exported value is 0.043 s^(-1). Km: printed Table 3 cell 15.3 uM; 1 uM is 0.001 mM, so 15.3 / 1000 = 0.0153 mM; the paper value is 0.0153 mM; the exported value is 0.015 mM. kcat/Km: printed Table 3 cell 28 with the column head x 10^2 M^-1 s^-1, so the cell reads 2800 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2800 / 1000 = 2.8000000000000003 s^-1 mM^-1; the paper value is 2.8000000000000003 s^(-1)*mM^(-1); the exported value is 2.8666666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row '3beta-Hydroxy-5beta-androstan-17-one': kcat = 43 s-1 under the column multiplier x 10^-3; Km = 15.3 uM; printed kcat/Km = 28 M-1 s-1 under the column multiplier x 10^2.


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 'Androsterone'; column 'Substrate stereospecificity' = 3alpha, 5alpha; column 'kcat (x 10^-3 s^-1)' = 47; column 'Km (uM)' = 27.5; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 17. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 47 with the column head x 10^-3 s^-1, so the cell reads 47 x 10^-3 s^-1; the paper value is 0.047 s^(-1); the exported value is 0.047 s^(-1). Km: printed Table 3 cell 27.5 uM; 1 uM is 0.001 mM, so 27.5 / 1000 = 0.0275 mM; the paper value is 0.0275 mM; the exported value is 0.028 mM. kcat/Km: printed Table 3 cell 17 with the column head x 10^2 M^-1 s^-1, so the cell reads 1700 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1700 / 1000 = 1.7 s^-1 mM^-1; the paper value is 1.7 s^(-1)*mM^(-1); the exported value is 1.6785714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row 'Androsterone': kcat = 47 s-1 under the column multiplier x 10^-3; Km = 27.5 uM; printed kcat/Km = 17 M-1 s-1 under the column multiplier x 10^2.


assay_conditions_summary: pH 6; 310.15 K; buffer 1-ml systems containing 100 mM potassium phosphate; cofactor NADPH

column_label: Table 2: Kinetic constants for 3-ketosteroid reduction catalyzed by the E120H mutant and AKR1C2 (J. Biol. Chem. 2012, 287(20):16609-16622), enzyme block E120H, substrate row '5beta-DHT'; column 'Product specificity' = 3alpha (80%), 3beta (20%); column 'kcat (x 10^-3 s^-1)' = 26.8; column 'Km (uM)' = 1.5; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 180. Column 'Ki (uM)' = 47.1.

normalized_value_unit_evidence: kcat: printed Table 2 cell 26.8 with the column head x 10^-3 s^-1, so the cell reads 26.8 x 10^-3 s^-1; the paper value is 0.0268 s^(-1); the exported value is 0.027 s^(-1). Km: printed Table 2 cell 1.5 uM; 1 uM is 0.001 mM, so 1.5 / 1000 = 0.0015 mM; the paper value is 0.0015 mM; the exported value is 0.002 mM. kcat/Km: printed Table 2 cell 180 with the column head x 10^2 M^-1 s^-1, so the cell reads 18000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 18000 / 1000 = 18 s^-1 mM^-1; the paper value is 18 s^(-1)*mM^(-1); the exported value is 13.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme block E120H, substrate row '5beta-DHT': kcat = 26.8 s-1 under the column multiplier x 10^-3; Km = 1.5 uM; printed kcat/Km = 180 M-1 s-1 under the column multiplier x 10^2.


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 '17beta-Estradiol'; column 'Substrate stereospecificity' = 17beta; column 'kcat (x 10^-3 s^-1)' = 5.87; column 'Km (uM)' = 2.8; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 21. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.87 with the column head x 10^-3 s^-1, so the cell reads 5.87 x 10^-3 s^-1; the paper value is 0.00587 s^(-1); the exported value is 0.006 s^(-1). Km: printed Table 3 cell 2.8 uM; 1 uM is 0.001 mM, so 2.8 / 1000 = 0.0028 mM; the paper value is 0.0028 mM; the exported value is 0.003 mM. kcat/Km: printed Table 3 cell 21 with the column head x 10^2 M^-1 s^-1, so the cell reads 2100 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2100 / 1000 = 2.1 s^-1 mM^-1; the paper value is 2.1 s^(-1)*mM^(-1); the exported value is 2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row '17beta-Estradiol': kcat = 5.87 s-1 under the column multiplier x 10^-3; Km = 2.8 uM; printed kcat/Km = 21 M-1 s-1 under the column multiplier x 10^2.


substrate_name: testosterone

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 'Testosterone'; column 'Substrate stereospecificity' = 17beta; column 'kcat (x 10^-3 s^-1)' = 0.77; column 'Km (uM)' = 1.8; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 4.2. Column 'Ki (uM)' = 40.4.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.77 with the column head x 10^-3 s^-1, so the cell reads 0.77 x 10^-3 s^-1; the paper value is 0.00077 s^(-1); the exported value is 0.0008 s^(-1). Km: printed Table 3 cell 1.8 uM; 1 uM is 0.001 mM, so 1.8 / 1000 = 0.0018 mM; the paper value is 0.0018 mM; the exported value is 0.002 mM. kcat/Km: printed Table 3 cell 4.2 with the column head x 10^2 M^-1 s^-1, so the cell reads 420 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 420 / 1000 = 0.42 s^-1 mM^-1; the paper value is 0.42 s^(-1)*mM^(-1); the exported value is 0.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row 'Testosterone': kcat = 0.77 s-1 under the column multiplier x 10^-3; Km = 1.8 uM; printed kcat/Km = 4.2 M-1 s-1 under the column multiplier x 10^2.

substrate: testosterone


substrate_name: epiandrosterone

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 'epiA'; column 'Substrate stereospecificity' = 3beta, 5alpha; column 'kcat (x 10^-3 s^-1)' = 253; column 'Km (uM)' = 1.9; column 'kcat/Km (x 10^2 M^-1 s^-1)' = 1300. Column 'Ki (uM)' is empty for this row.

normalized_value_unit_evidence: kcat: printed Table 3 cell 253 with the column head x 10^-3 s^-1, so the cell reads 253 x 10^-3 s^-1; the paper value is 0.253 s^(-1); the exported value is 0.253 s^(-1). Km: printed Table 3 cell 1.9 uM; 1 uM is 0.001 mM, so 1.9 / 1000 = 0.0019 mM; the paper value is 0.0019 mM; the exported value is 0.002 mM. kcat/Km: printed Table 3 cell 1300 with the column head x 10^2 M^-1 s^-1, so the cell reads 130000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 130000 / 1000 = 130 s^-1 mM^-1; the paper value is 130 s^(-1)*mM^(-1); the exported value is 126.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme block E120H, substrate row 'epiA': kcat = 253 s-1 under the column multiplier x 10^-3; Km = 1.9 uM; printed kcat/Km = 1300 M-1 s-1 under the column multiplier x 10^2.

substrate: epiandrosterone


substrate_name: Nicotinamide guanine dinucleotide

substrate: Nicotinamide guanine dinucleotide


substrate_name: Nicotinamide hypoxanthine dinucleotide

substrate: Nicotinamide hypoxanthine dinucleotide


organism: Withania somnifera

substrate_name: NADP+

assay_conditions_summary: pH 6.7; 303.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 6.7; 303.15 K; buffer MES-NaOH; cofactor NADPH

column_label: Table 2; row NADPH; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=33.34 s^-1; Km paper=0.00043 mM; kcat/Km paper=77400 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row NADPH: Km 0.43 uM; kcat 33.34 s^-1; kcat/Km 7.74 x 10^7 M^-1 s^-1; dimer kcat 66.68 s^-1.

row_label: NADPH

table_label: Table 2. Kinetic parameters of Withania somnifera tropine forming tropinone reductase (WsTR-I) catalyzed reaction


substrate_name: N-methylpiperidine

substrate: N-methylpiperidine


assay_conditions_summary: pH 6.7; 303.15 K; buffer MES-NaOH; cofactor NADP+

column_label: Table 2; row Tropine; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=1.67 s^-1; Km paper=114.94 mM; kcat/Km paper=0.014 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row Tropine: Km 114.94 mM; kcat 1.67 s^-1; kcat/Km 0.14 x 10^2 M^-1 s^-1; dimer kcat 3.33 s^-1.

row_label: Tropine


column_label: Table 2; row Tropinone; columns Km, Kcat (Monomer, single active site), Kcat/Km (M^-1 s^-1), and Kcat (Dimer, single active site).

normalized_value_unit_evidence: kcat paper=9.51 s^-1; Km paper=1.27 mM; kcat/Km paper=7.49 s^-1 mM^-1

raw_value_unit_evidence: Table 2 row Tropinone: Km 1.27 mM; kcat 9.51 s^-1; kcat/Km 7.49 x 10^3 M^-1 s^-1; dimer kcat 19.03 s^-1.

row_label: Tropinone


enzyme_display_name: UniProt Q8T6T2

organism: Cryptosporidium parvum

source_db: skid

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

sequence_source: multiple

source_databases_merged: skid uniprot

enzyme: UniProt Q8T6T2

source: skid


substrate_name: 3-Acetylpyridine-adenine dinucleotide

substrate: 3-Acetylpyridine-adenine dinucleotide


enzyme_display_name: Inosine-5'-monophosphate dehydrogenase

substrate_name: Inosine 5'-phosphate

assay_conditions_summary: pH 8

column_label: Table I reports C. parvum IMPDH Km(IMP) 29 uM.

raw_value_unit_evidence: Km raw_value=29 uM raw_unit=uM

row_label: C. parvum IMPDH / Km(IMP)

table_label: Table I

enzyme: Inosine-5'-monophosphate dehydrogenase

substrate: Inosine 5'-phosphate


organism: Datura stramonium

assay_conditions_summary: cofactor NADP+


substrate_name: Scopine

substrate: Scopine


substrate_name: nortropine

substrate: nortropine


substrate_name: Nortropinone

substrate: Nortropinone


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: allopregnanolone

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table II; K_m (uM) block; Allopregnanolone row; raw K_m value 5.0 +/- 0.7 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for allopregnanolone = 5.0 +/- 0.7 uM.

row_label: Table II steroid-substrate K_m block; Allopregnanolone row

table_label: PMID 11294878, Table II: Kinetic constants for steroid substrates

substrate: allopregnanolone


column_label: Table II; K_m (uM) block; 3-alpha-Androstanediol row; raw K_m value 7.5 +/- 0.4 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for 3-alpha-androstanediol = 7.5 +/- 0.4 uM.

row_label: Table II steroid-substrate K_m block; 3-alpha-Androstanediol row

enzyme: Dehydrogenase/reductase SDR family member 9


substrate_name: dehydroepiandrosterone

column_label: Table II; K_m (uM) block; Dehydroepiandrosterone row; raw K_m value 14.0 +/- 1.0 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for dehydroepiandrosterone = 14.0 +/- 1.0 uM.

row_label: Table II steroid-substrate K_m block; Dehydroepiandrosterone row

substrate: dehydroepiandrosterone


substrate_name: androsterone

column_label: Table II; K_m (uM) block; Androsterone row; raw K_m value 24.0 +/- 1.0 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for androsterone = 24.0 +/- 1.0 uM.

row_label: Table II steroid-substrate K_m block; Androsterone row

substrate: androsterone


substrate_name: dihydrotestosterone

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table II; K_m (uM) block; Dihydrotestosterone row; raw K_m value 12.0 +/- 0.4 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for dihydrotestosterone = 12.0 +/- 0.4 uM.

row_label: Table II steroid-substrate K_m block; Dihydrotestosterone row

substrate: dihydrotestosterone


enzyme_display_name: Retinol dehydrogenase 16

enzyme: Retinol dehydrogenase 16


assay_conditions_summary: pH 7.3; cofactor NADH

column_label: JBC Table I, kinetic constants of RoDH-4 for steroid substrates; row Dihydrotestosterone; column Km (uM); raw Km 0.80 +/- 0.17 uM.

normalized_value_unit_evidence: Km normalized_value=0.0008 normalized_unit=mM from 0.80 +/- 0.17 uM.

raw_value_unit_evidence: JBC Table I, kinetic constants of RoDH-4 for steroid substrates row Dihydrotestosterone reports Km = 0.80 +/- 0.17 uM.

row_label: Dihydrotestosterone


substrate_name: NAD

assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: JBC Table II, apparent Km values of RoDH-4 for cofactors; row NAD+; column Km (uM); raw Km 0.13 +/- 0.01 uM.

normalized_value_unit_evidence: Km normalized_value=0.00013 normalized_unit=mM from 0.13 +/- 0.01 uM.

raw_value_unit_evidence: JBC Table II, apparent Km values of RoDH-4 for cofactors row NAD+ reports Km = 0.13 +/- 0.01 uM.

row_label: NAD+

substrate: NAD


substrate_name: NADP

assay_conditions_summary: pH 7.3; cofactor NADP+

column_label: JBC Table II, apparent Km values of RoDH-4 for cofactors; row NADP+; column Km (uM); raw Km 190 +/- 17 uM.

normalized_value_unit_evidence: Km normalized_value=0.19 normalized_unit=mM from 190 +/- 17 uM.

raw_value_unit_evidence: JBC Table II, apparent Km values of RoDH-4 for cofactors row NADP+ reports Km = 190 +/- 17 uM.

row_label: NADP+

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


organism: Candida albicans

substrate_name: IMP

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A251T to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat normalized_value=4.6 normalized_unit=s^-1; Km normalized_value=0.017 normalized_unit=mM; kcat/Km derived normalized_value=270.5882352941176 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.6 +/- 0.3 raw_unit=s^-1; Km(IMP) raw_value=17 +/- 3 raw_unit=uM

row_label: C. albicans IMPDH / A251T column; rows kcat and Km(IMP)

table_label: PMID 15665003 Table II

substrate: IMP


substrate_name: NAD+

normalized_value_unit_evidence: kcat normalized_value=4.6 normalized_unit=s^-1; Km normalized_value=0.6 normalized_unit=mM; kcat/Km derived normalized_value=7.666666666666666 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.6 +/- 0.3 raw_unit=s^-1; Km(NAD) raw_value=600 +/- 300 raw_unit=uM

row_label: C. albicans IMPDH / A251T column; rows kcat and Km(NAD)

substrate: NAD+


organism: Brugmansia arborea


substrate_name: Tropine

substrate: Tropine


substrate_name: tropinone

substrate: tropinone


km_display: Not reported

column_label: Table 1, D. stramonium TRI row, kcat column, 25.6 s^-1 with pH 7.0 printed in the cell.

raw_value_unit_evidence: Table 1 D. stramonium TRI row reports kcat 25.6 s^-1 at pH 7.0.

row_label: D. stramonium TRI

table_label: Table 1. Tropinone reductases from Solanaceae

source_databases_merged: brenda skid


column_label: Table 1, D. stramonium TRI row, Km tropinone column, 0.775 mM with pH 5.9 printed in the cell.

normalized_value_unit_evidence: tropinone Km=0.775 mM at pH 5.9.

raw_value_unit_evidence: Table 1 D. stramonium TRI row reports tropinone Km 0.775 mM at pH 5.9.


proof_lines:
pH 9.6, 22°C
Raw SKiD Env: Temp=22°C, pH=9.6


organism: Withania coagulans

substrate_name: NADP+

assay_conditions_summary: pH 6.6; 303.15 K; cofactor NADP+

column_label: Table 1, NADP+ row, kcat 2.94 s^-1, Km 208.33 uM, and kcat/Km 14000 M^-1 s^-1.

table_label: Table 1. Kinetic parameters of recombinant WcTR-I

substrate: NADP+


substrate_name: NADPH

assay_conditions_summary: pH 6.6; 303.15 K; cofactor NADPH

column_label: Table 1, NADPH row, kcat 6.76 s^-1, Km 126.582 uM, and kcat/Km 53000 M^-1 s^-1.

substrate: NADPH


column_label: ScienceDirect HTML Table 1 row Tropine has columns Km=26.31 mM, Kcat (s^-1)=1.87, and Kcat/Km (M^-1 s^-1)=71.

raw_value_unit_evidence: Tropine row reports Km=26.31 mM, Kcat=1.87 s^-1, Kcat/Km=71 M^-1 s^-1.

table_label: Table 1. Recombinant WcTRI kinetic parameters


column_label: ScienceDirect HTML Table 1 row Tropinone has columns Km=1.451 mM, Kcat (s^-1)=16.74, and Kcat/Km (M^-1 s^-1)=11530.

raw_value_unit_evidence: Tropinone row reports Km=1.451 mM, Kcat=16.74 s^-1, Kcat/Km=11530 M^-1 s^-1.


enzyme_display_name: (+)-neomenthol dehydrogenase

organism: Capsicum annuum

substrate_name: menthone

assay_conditions_summary: cofactor NADPH

enzyme: (+)-neomenthol dehydrogenase

substrate: menthone


substrate_name: neomenthol

substrate: neomenthol


organism: Leishmania donovani


substrate_name: Inosine 5'-phosphate

column_label: PubMed abstract prose; IMP / inosine 5-monophosphate prose in PubMed abstract; metric K(m)(app); PubMed abstract: LdIMPDH substrates IMP and NAD(+) with K(m)(app) values of 33 and 390 microM, respectively; IMP maps to 33 microM.

table_label: PubMed abstract prose

substrate: Inosine 5'-phosphate


substrate_name: NAD(+)

column_label: PubMed abstract prose; NAD(+) prose in PubMed abstract; metric K(m)(app); PubMed abstract: LdIMPDH substrates IMP and NAD(+) with K(m)(app) values of 33 and 390 microM, respectively; NAD(+) maps to 390 microM.

row_label: NAD(+) prose in PubMed abstract

substrate: NAD(+)


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus


enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


substrate_name: estradiol

substrate: estradiol


organism: Vigna unguiculata

column_label: PubMed abstract reports IMP Km = 9.1 X 10(-6) M at pH 8.8; this normalizes to 0.0091 mM.

raw_value_unit_evidence: Km raw_value=9.1 X 10(-6) M raw_unit=M

row_label: Prose segment: IMP Km

table_label: PubMed PMID 2857550 abstract


column_label: PubMed abstract reports K+ activation Km = 1.6 X 10(-3) M; this normalizes to 1.6 mM.

raw_value_unit_evidence: Km raw_value=1.6 X 10(-3) M raw_unit=M

row_label: Prose segment: K+ activation Km


substrate_name: 3-Acetylpyridine-adenine dinucleotide

substrate: 3-Acetylpyridine-adenine dinucleotide


substrate_name: thio-NAD+

substrate: thio-NAD+


organism: Escherichia coli (strain K12)


assay_conditions_summary: cofactor NAD+


enzyme_display_name: Trifunctional enzyme subunit alpha, mitochondrial

assay_conditions_summary: pH 8; buffer 50 mM TRIS-HCl; cofactor CoA

column_label: The full-text Results section states that alpha-TFP MLCL AT activity was determined in the presence of MLCL and varying concentrations of linoleoyl-CoA, oleoyl-CoA, or palmitoyl-CoA, and that Km was 18.1 uM, 51.8 uM, and 50.4 uM for linoleoyl-CoA, oleoyl-CoA, and palmitoyl-CoA, respectively. This row uses linoleoyl-CoA (Figure 2C), Km=18.1 uM, normalized to 0.0181 mM.

raw_value_unit_evidence: Km raw_value=18.1 raw_unit=uM

row_label: linoleoyl-CoA / C18:2 (Figure 2C)

table_label: PMC full-text Results paragraph linked to Figure 2C-E


column_label: The full-text Results section states that alpha-TFP MLCL AT activity was determined in the presence of MLCL and varying concentrations of linoleoyl-CoA, oleoyl-CoA, or palmitoyl-CoA, and that Km was 18.1 uM, 51.8 uM, and 50.4 uM for linoleoyl-CoA, oleoyl-CoA, and palmitoyl-CoA, respectively. This row uses oleoyl-CoA (Figure 2D), Km=51.8 uM, normalized to 0.0518 mM.

raw_value_unit_evidence: Km raw_value=51.8 raw_unit=uM

row_label: oleoyl-CoA / C18:1 (Figure 2D)

enzyme: Trifunctional enzyme subunit alpha, mitochondrial


substrate_name: hexadecanoyl-CoA

column_label: The full-text Results section states that alpha-TFP MLCL AT activity was determined in the presence of MLCL and varying concentrations of linoleoyl-CoA, oleoyl-CoA, or palmitoyl-CoA, and that Km was 18.1 uM, 51.8 uM, and 50.4 uM for linoleoyl-CoA, oleoyl-CoA, and palmitoyl-CoA, respectively. This row uses palmitoyl-CoA (Figure 2E), Km=50.4 uM, normalized to 0.0504 mM.

raw_value_unit_evidence: Km raw_value=50.4 raw_unit=uM

row_label: palmitoyl-CoA / C16:0 (Figure 2E)

substrate: hexadecanoyl-CoA


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Bos taurus

substrate_name: prostaglandin D2

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / prostaglandin D2; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS prostaglandin D2 Km raw_value=100 raw_unit=uM

row_label: PGFS / prostaglandin D2

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin D2


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 9,10-phenanthroquinone; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 9,10-phenanthroquinone Km raw_value=0.13 raw_unit=uM

row_label: PGFS / 9,10-phenanthroquinone


substrate_name: menadione

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

raw_value_unit_evidence: Table I PGFS menadione Km raw_value=13 raw_unit=uM

row_label: PGFS / menadione

substrate: menadione


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

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

row_label: PGFS / 4-nitrobenzaldehyde


organism: Babesia gibsoni

substrate_name: Inosine 5'-diphosphate

column_label: The abstract reports Km 8.18 +/- 0.878 uM for IMP, not inosine 5'-diphosphate / IDP.

normalized_value_unit_evidence: Km=0.00818 mM for IMP

row_label: rBgIMPDH IMP Km

substrate: Inosine 5'-diphosphate


assay_conditions_summary: pH 8; cofactor NAD+

column_label: The abstract reports Km 360.80 +/- 43.41 uM for NAD(+), respectively, after the IMP value.

normalized_value_unit_evidence: Km=0.36080 mM for NAD+

row_label: rBgIMPDH NAD+ Km


enzyme_display_name: UniProt P0C0H6

organism: Streptococcus pyogenes

substrate_name: IMP

enzyme: UniProt P0C0H6

substrate: IMP


substrate_name: NAD+

column_label: Abstract reports the Km for NAD (1180 microM) for Streptococcus pyogenes IMPDH.

raw_value_unit_evidence: Km raw_value=1180 microM raw_unit=microM

row_label: Streptococcus pyogenes IMP dehydrogenase / NAD

table_label: PubMed XML abstract PMID 10200156

substrate: NAD+


organism: Bacillus amyloliquefaciens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P166S/K481E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K481E with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 313.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P166S to reconstruct the assayed variant sequence.


organism: Tritrichomonas foetus

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines: IMP NAD+ IMPDH


enzyme_display_name: UniProt P12268

organism: Homo sapiens

enzyme: UniProt P12268


organism: Pneumocystis carinii

column_label: Abstract reports apparent Km for IMP of 21.7 +/- 0.3 microM and apparent Km for NAD of 314 +/- 84 microM.

raw_value_unit_evidence: Km raw_value=21.7 microM raw_unit=microM

row_label: Pneumocystis carinii IMP dehydrogenase expressed in Escherichia coli / IMP

table_label: PubMed XML abstract PMID 8980752


raw_value_unit_evidence: Km raw_value=314 microM raw_unit=microM

row_label: Pneumocystis carinii IMP dehydrogenase expressed in Escherichia coli / NAD


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: IMPDH IMP NAD+


organism: Toxoplasma gondii

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+


column_label: Table 1 reports K_m of NAD (uM) in the T. gondii column as 144 +/- 12; 144 uM equals 0.144 mM.

raw_value_unit_evidence: Km raw_value=144 +/- 12 raw_unit=uM

row_label: T. gondii column / K_m of NAD row

table_label: PMC Table 1 PMID 15917510 kinetics of TgIMPDH-F


organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31)

column_label: Steady State Kinetic Parameters section reports Km (IMP) = 29 +/- 8 uM; Figure 4A varies IMP at fixed NAD = 500 uM.

raw_value_unit_evidence: Km (IMP) raw_value=29 +/- 8 uM raw_unit=uM

row_label: B. burgdorferi IMPDH; IMP varied from 7 to 980 uM; NAD plots replotted against IMP concentration

table_label: JBC Steady State Kinetic Parameters text / Figure 4


column_label: Steady State Kinetic Parameters section reports Km (NAD) = 1100 +/- 160 uM; Figure 4B varies NAD at fixed IMP = 980 uM.

raw_value_unit_evidence: Km (NAD) raw_value=1100 +/- 160 uM raw_unit=uM

row_label: B. burgdorferi IMPDH; NAD varied from 125 to 5000 uM; IMP plots replotted against NAD concentration


organism: Anisodus luridus


column_label: Table 2; row SlTRI / Tropinone / pH 6.4; columns kcat (s^-1), Km (mM), and same-row kcat/Km quotient; raw kcat 0.98 +/- 0.096; raw Km 40.90 +/- 7.059.

row_label: SlTRI / Tropinone / pH 6.4

table_label: Table 2: The SlTRI enzymatic kinetics


organism: Artemisia annua

substrate_name: (-)-menthone

assay_conditions_summary: pH 7; 303.15 K; buffer 500 uM NADPH in; cofactor NADPH

column_label: Table 3, row (-)-Menthone, column kcat/Km (M^-1 s^-1); primary PDF page 7, journal page 1225.

row_label: (-)-Menthone

table_label: Table 3

substrate: (-)-menthone


substrate_name: (+)-neomenthol

assay_conditions_summary: pH 7; 303.15 K; buffer 500 uM NADP+ in; cofactor NADP+

column_label: Table 3, row (+)-Neomenthol, column kcat/Km (M^-1 s^-1); primary PDF page 7, journal page 1225.

row_label: (+)-Neomenthol

substrate: (+)-neomenthol


organism: Ovis aries

substrate_name: progesterone

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

column_label: Abstract reports progesterone kinetic characteristics of Km = 30.8 microM, which does not exactly equal the current row value 0.031 mM.

raw_value_unit_evidence: Km raw_value=30.8 microM raw_unit=microM

row_label: Ovine fetal blood 3 beta,20 alpha-hydroxysteroid oxidoreductase / progesterone

table_label: PubMed XML abstract PMID 3483295

substrate: progesterone


column_label: Abstract reports 5 alpha-dihydrotestosterone kinetic characteristics of Km = 74 microM and Vmax = 1.3 nmol min-1 (nmol enzyme)-1.

raw_value_unit_evidence: Km raw_value=74 microM raw_unit=microM

row_label: Ovine fetal blood 3 beta,20 alpha-hydroxysteroid oxidoreductase / 5 alpha-dihydrotestosterone


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

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


organism: Rattus norvegicus

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


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

organism: Mus musculus

substrate_name: estrone

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

substrate: estrone


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


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

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

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


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

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

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

row_label: DHT -> 3betaA-diol


organism: Schizosaccharomyces pombe

substrate_name: K+

proof_lines:
IMP dehydrogenase
Schizosaccharomyces pombe
allosteric enzymes

substrate: K+


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: inosine 5'-phosphate

proof_lines:
IMP
Km
0.02 mM

substrate: inosine 5'-phosphate


organism: Borrelia burgdorferi


organism: Hyoscyamus niger

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

column_label: Page 841 states respective Km values for NADPH, NADP+, and NADH were 11.3 +/- 1.7, 41.5 +/- 3.7, and >10,000 microM for TR-I.

raw_value_unit_evidence: Km raw_value=41.5 +/- 3.7 raw_unit=microM

row_label: TR-I / NADP+

table_label: PMC scanned page 841 prose/table text, Substrate and Cofactor Specificities

substrate: NADP+


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

substrate_name: dihydrotestosterone

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

raw_value_unit_evidence: Km raw_value=0.47 microM raw_unit=microM

row_label: Mouse expressed 3 beta HSD V / DHT

table_label: PubMed XML abstract PMID 7491113

substrate: dihydrotestosterone


proof_lines:
androsterone
3alpha-hydroxysterols
Michaelis-Menten kinetics


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

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

raw_value_unit_evidence: Km raw_value=2.2 raw_unit=microM for DHT

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

table_label: PubMed abstract PMID 7491113 with lead context PMID 8145763


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

substrate_name: dihydrotestosterone (in the presence of NADH)

column_label: Table I, DHT row, Km (uM) column: 2.1; footnote states NADH (1 mM) was used when DHT was the substrate.

raw_value_unit_evidence: Table I DHT row reports Km 2.1 uM.

row_label: DHT substrate row

table_label: Table I. Kinetic Constants for Human Skin 3B-HSD Activity Transfected in HeLa Cells


proof_lines: Differential recognition of the free versus bound retinol by human microsomal retinol/sterol dehydrogenases: characterization of the holo-CRBP dehydrogenase activity of RoDH-4

proof_lines: holo-CRBP is recognized as substrate by human microsomal short-chain dehydrogenase/reductase (SDR) RoDH-4


enzyme_display_name: tropinone reductase I

organism: Przewalskia tangutica

substrate_name: tropinone

substrate: tropinone


organism: Drosophila melanogaster

substrate_name: NADPH

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

substrate: NADPH


enzyme_display_name: carbonyl reductase (NADPH)

organism: Gallus gallus

substrate_name: H+; NADPH; Pyridine-4-aldehyde

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 NADPH

enzyme: carbonyl reductase (NADPH)

substrate: H+; NADPH; Pyridine-4-aldehyde


organism: Homo sapiens

substrate_name: Isatin; H+; NADPH

assay_conditions_summary: pH 8.4; 310.15 K; cofactor NADPH

proof_lines:
pH 8.4, 37°C
pH 7.4, 37°C, recombinant enzyme
pH 8.4, 25°C

substrate: Isatin; H+; NADPH


enzyme_display_name: UniProt P52895

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P52895


enzyme_display_name: gluconate 2-dehydrogenase

organism: Acetobacter ascendens

enzyme: gluconate 2-dehydrogenase


substrate_name: gluconate

substrate: gluconate


enzyme_display_name: morphine 6-dehydrogenase

organism: Pseudomonas putida

enzyme: morphine 6-dehydrogenase


organism: Mesocricetus auratus


proof_lines: slope effect, 0.025 mM androsterone, varying NADP+ concentrations

proof_lines: slope effect, 0.25 mM NADP+, varying androsterone concentrations

proof_lines: intercept effect, 0.25 mM NADP+, varying androsterone concentrations


substrate_name: glycochenodeoxycholic acid

substrate: glycochenodeoxycholic acid


substrate_name: lithocholic acid

substrate: lithocholic acid


substrate_name: glycolithocholic acid

substrate: glycolithocholic acid


substrate_name: Dehydrolithocholic acid

substrate: Dehydrolithocholic acid


enzyme_display_name: farnesol dehydrogenase (NADP+)

organism: Persicaria minor

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

enzyme: farnesol dehydrogenase (NADP+)


substrate_name: carveol

substrate: carveol


substrate_name: NAD+

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NAD+

substrate: NAD+


substrate_name: (S)-perillyl alcohol

substrate: (S)-perillyl alcohol


substrate_name: nerodilol

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

substrate: nerodilol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: geraniol

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

substrate: geraniol


substrate_name: NADP+

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

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


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines: cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant wild-type enzyme

proof_lines: cofactor NAD+, pH 7.0, 25°C, steroid oxidation, recombinant wild-type enzyme


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant wild-type enzyme

proof_lines: cofactor NADH, pH 7.0, 25°C, steroid reduction, recombinant wild-type enzyme


substrate_name: diacetyl

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

substrate: diacetyl


substrate_name: isatin

substrate: isatin


ki_unit: mM

assay_conditions_summary: cofactor NAD+


organism: Cavia porcellus

substrate_name: Morphine; NAD+

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

substrate: Morphine; NAD+


substrate_name: nalorphine

proof_lines:
cosubstrate NAD+
cosubstrate NADP+

substrate: nalorphine


substrate_name: codeine

proof_lines:
with NADP+
with NAD+

substrate: codeine


substrate_name: normorphine

substrate: normorphine


substrate_name: morphine

substrate: morphine


substrate_name: ethylmorphine

substrate: ethylmorphine


substrate_name: Dihydrocodeine

substrate: Dihydrocodeine


substrate_name: androsterone

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

proof_lines: steady-state, pH 8.0, 25°C, recombinant mutant W227A

substrate: androsterone


proof_lines: steady-state, pH 8.0, 25°C, recombinant mutant F118A


proof_lines: steady-state, pH 8.0, 25°C, recombinant mutant T226A


proof_lines: steady-state, pH 8.0, 25°C, recombinant wild-type enzyme


organism: Eggerthella sp. CAG:298

substrate_name: 3-oxo-deoxycholic acid

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: coenzyme: NADPH, pH 7.0, temperature not specified in the publication

substrate: 3-oxo-deoxycholic acid


substrate_name: deoxycholic acid

assay_conditions_summary: pH 10; cofactor NADP+

proof_lines: coenzyme: NADP+, pH 10, temperature not specified in the publication

proof_lines: coenzyme: NADP+, pH 7.0, temperature not specified in the publication

substrate: deoxycholic acid


substrate_name: 3-oxodeoxycholic acid

assay_conditions_summary: pH 6.5; cofactor NADPH

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

substrate: 3-oxodeoxycholic acid


substrate_name: isodeoxycholic acid

assay_conditions_summary: pH 9.5; cofactor NADP+

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

substrate: isodeoxycholic acid


substrate_name: NADH

substrate: NADH


substrate_name: NAD+

substrate: NAD+


proof_lines:
cloned human liver enzyme type I
cloned human liver enzyme type II
NAD(H), prostate


proof_lines: cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant mutant W227A


proof_lines: cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant mutant W227A


proof_lines: cofactor NADPH, pH 7.0, 25°C, steroid reduction, recombinant mutant R276M


proof_lines: cofactor NADP+, pH 7.0, 25°C, steroid oxidation, recombinant mutant R276M


organism: Comamonas testosteroni

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


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


proof_lines:
pH 9.0, 25°C, recombinant mutant K159A
pH 10.4, 25°C, recombinant mutant K159A


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

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


organism: Rattus norvegicus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


organism: Candida dubliniensis


enzyme_display_name: dihydroflavonol 4-reductase

organism: Fragaria x ananassa

substrate_name: dihydroquercetin

proof_lines: pH 6.3, temperature not specified in the publication

enzyme: dihydroflavonol 4-reductase

substrate: dihydroquercetin


substrate_name: dihydromyricetin

substrate: dihydromyricetin


substrate_name: dihydrokaempferol

substrate: dihydrokaempferol


organism: Persea americana


substrate_name: acetoacetyl-[acyl-carrier protein]

substrate: acetoacetyl-[acyl-carrier protein]


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Komagataella phaffii


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: naloxone

proof_lines:
cosubstrate NADPH
cosubstrate NADH

substrate: naloxone


organism: Ipomoea batatas

substrate_name: trans,trans-farnesol

substrate: trans,trans-farnesol


substrate_name: geraniol

substrate: geraniol


proof_lines:
pH 7.0, 25, reduction reaction
NADPH
NADH


substrate_name: androsterone

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines:
pH 7.0, 25, oxidation reaction
NAD+
NADP+

substrate: androsterone


organism: Saccharomyces cerevisiae

substrate_name: Benzyl 2-methyl-3-oxobutyrate

substrate: Benzyl 2-methyl-3-oxobutyrate


organism: Brevibacterium ketosoreductum


substrate_name: Prostaglandin

assay_conditions_summary: pH 6

proof_lines: competitive, for 9,10-phenanthrenequinone and 5alpha-androstane-3,17-dione reduction at pH 6.0

proof_lines: competitive for androstene oxidation at pH 7.0. IC50 is 0.003 mM at H 7.0, 0.045 at pH 9.0

substrate: Prostaglandin


proof_lines:
NAD(H), prostate
NADP(H), prostate
NAD(H), epididymis


organism: Aspergillus niger

substrate_name: L-Idonate

protein_accession_database: NCBI Protein

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

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Frontiers PDF page 7 Table 2; row GluD / L-idonate; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: GluD / L-idonate

table_label: Table 2 | Kinetic parameters of the purified GluD and GluE proteins

substrate: L-Idonate


assay_conditions_summary: pH 7

column_label: Frontiers PDF page 7 Table 2; row GluD / 2-keto-L-gulonate; columns Km (mM), kcat (s^-1), and kcat/Km (M^-1 s^-1).

row_label: GluD / 2-keto-L-gulonate


assay_conditions_summary: pH 8

proof_lines: pH 8.0, temperature not specified in the publication


organism: Plutella xylostella

substrate_name: Unknown

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

substrate: Unknown


organism: Manduca sexta

substrate_name: farnesol

substrate: farnesol


substrate_name: morphine

proof_lines: cosubstrate NAD+, in the male adult rats

proof_lines: cosubstrate NAD+, in the female adult rats

substrate: morphine


organism: Pseudomonas plecoglossicida

substrate_name: D-gluconate

substrate: D-gluconate


organism: Homo sapiens


organism: Pseudotsuga menziesii

substrate_name: (+)-dihydroquercetin

substrate: (+)-dihydroquercetin


organism: Cryptomeria japonica


sequence: MDSKYQCVK

wild_type_sequence: MDSKYQCVK

sequence_variant_note: Mutation signature R304L references residue 304, which is outside the resolved sequence length.


sequence_variant_note: Mutation signature R301L references residue 301, which is outside the resolved sequence length.


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

substrate: D,L-glyceraldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC(=O)C


substrate_name: farnesal

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

substrate: farnesal


substrate_name: NADPH

substrate: NADPH


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA

proof_lines: kcat is 454 sec(-1) with acetoacetyl-CoA as substrate. kcat is 169 sec(-1) with 3-hydroxybutanoyl-CoA as substrate. kcat is 319 sec(-1) with NADH as substrate. kcat is 83 sec(-1) with NAD(+) as substrate.

substrate: acetoacetyl-CoA


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NAD(+)

substrate: NAD(+)


organism: Ketogulonicigenium vulgare

proof_lines: recombinant His6-tagged enzyme, pH and temperature not specified in the publication


substrate_name: 2-keto-L-gluconic acid

substrate: 2-keto-L-gluconic acid


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


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


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


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


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


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


organism: Oryctolagus cuniculus


substrate_name: Dihydrocodeine

substrate: Dihydrocodeine


substrate_name: normorphine

substrate: normorphine


substrate_name: ethylmorphine

substrate: ethylmorphine


substrate_name: benzenedihydrodiol

substrate: benzenedihydrodiol


organism: Gluconobacter oxydans

proof_lines:
below 0.01 mM, pH 7.0, 25°C
kcat is 48.2 sec(-1).

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 7; cofactor NADH


proof_lines: recombinant enzyme in intact COS-1 cells


organism: Candida orthopsilosis

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


organism: Mesocricetus auratus

proof_lines: similar values of other 17beta-hydroxysteroids


substrate_name: testosterone

substrate: testosterone


substrate_name: morphine

substrate: morphine


enzyme_display_name: 2-ketogluconate reductase

organism: Gluconobacter oxydans (strain 621H)

enzyme: 2-ketogluconate reductase


substrate_name: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Pseudomonas putida

substrate_name: codeine

proof_lines:
with NADP+
cosubstrate NADP+

substrate: codeine


substrate_name: codeinone

substrate: codeinone


enzyme_display_name: Glyoxylate/hydroxypyruvate reductase B

organism: Escherichia coli (strain K12)

substrate_name: hydroxypyruvate (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADPH

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

enzyme: Glyoxylate/hydroxypyruvate reductase B

substrate: hydroxypyruvate (at pH 7.5)


substrate_name: glyoxylate (at pH 7.5)

substrate: glyoxylate (at pH 7.5)


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

column_label: Official ScienceDirect HTML Table 1 row Morphine, AKR1C26 columns Km=490 uM, kcat=3.1 min^-1, kcat/Km=0.006 min^-1 uM^-1; unit footnote Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

row_label: Morphine / AKR1C26

table_label: Table 1. Kinetic constants for NAD(P)+ and alcohols.


organism: Sporobolomyces salmonicolor

proof_lines: recombinant protein purified from E. coli


enzyme_display_name: Aldo-keto reductase family 1 member C15

organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; cofactor NADP+

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 4-Nitrobenzaldehyde Km 1.2 uM.

raw_value_unit_evidence: Km raw_value=1.2 raw_unit=uM

enzyme: Aldo-keto reductase family 1 member C15


substrate_name: benzaldehyde

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports Benzaldehyde Km 3.1 uM.

raw_value_unit_evidence: Km raw_value=3.1 raw_unit=uM

row_label: Benzaldehyde (Aromatic aldehydes)

substrate: benzaldehyde


column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports Pyridine-4-aldehyde Km 20 uM.

raw_value_unit_evidence: Km raw_value=20 raw_unit=uM


substrate_name: NADP(+)

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: Coenzyme specificity prose reports NADP+ Km 2.4 uM.

raw_value_unit_evidence: Km raw_value=2.4 raw_unit=uM

row_label: NADP+ (oxidation reaction with saturated S-tetralol)

table_label: Coenzyme specificity prose

substrate: NADP(+)


substrate_name: NAD(+)

column_label: Coenzyme specificity prose reports NAD+ Km 1430 uM.

raw_value_unit_evidence: Km raw_value=1430 raw_unit=uM

row_label: NAD+ (oxidation reaction with saturated S-tetralol)


column_label: Coenzyme specificity prose reports NADPH Km 0.6 uM.

raw_value_unit_evidence: Km raw_value=0.6 raw_unit=uM

row_label: NADPH (reverse reaction with saturated S-camphorquinone)

substrate: NADPH


substrate_name: NADH

column_label: Coenzyme specificity prose reports NADH Km 43 uM.

raw_value_unit_evidence: Km raw_value=43 raw_unit=uM

row_label: NADH (reverse reaction with saturated S-camphorquinone)

substrate: NADH


smiles: CCCCCCCCCC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 1-Decanal Km 0.3 uM.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=uM

row_label: 1-Decanal (Alkanals)


smiles: CCCCCCCCC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 1-Nonanal Km 0.9 uM.

raw_value_unit_evidence: Km raw_value=0.9 raw_unit=uM

row_label: 1-Nonanal (Alkanals)


smiles: CCCCCCCC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 1-Octanal Km 1.1 uM.

raw_value_unit_evidence: Km raw_value=1.1 raw_unit=uM

row_label: 1-Octanal (Alkanals)


column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 1-Hexanal Km 1.1 uM.

row_label: 1-Hexanal (Alkanals)


substrate_name: 4-methylpentanal (isocaproaldehyde)

smiles: CC(C)CCC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports Isocaproaldehyde Km 225 uM.

raw_value_unit_evidence: Km raw_value=225 raw_unit=uM

row_label: Isocaproaldehyde (Alkanals)

substrate: 4-methylpentanal (isocaproaldehyde)


substrate_name: all-trans-retinal

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports all-trans-Retinal Km 0.4 uM.

raw_value_unit_evidence: Km raw_value=0.4 raw_unit=uM

row_label: all-trans-Retinal (Alkenals)

substrate: all-trans-retinal


smiles: CCCCC=CC=CC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports trans-2,4-Nonadienal Km 3.5 uM.

raw_value_unit_evidence: Km raw_value=3.5 raw_unit=uM

row_label: trans-2,4-Nonadienal (Alkenals)


smiles: CCCCCCC=CC=O

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports trans-2-Nonenal Km 3.3 uM.

raw_value_unit_evidence: Km raw_value=3.3 raw_unit=uM

row_label: trans-2-Nonenal (Alkenals)


substrate_name: 4-hydroxy-2-nonenal (HNE)

column_label: Table 2. Substrate specificity for aromatic and aliphatic aldehydes reports 4-Hydroxynonenal Km 2.5 uM.

raw_value_unit_evidence: Km raw_value=2.5 raw_unit=uM

row_label: 4-Hydroxynonenal (Alkenals)

substrate: 4-hydroxy-2-nonenal (HNE)


column_label: Table 3. Substrate specificity for quinones and ketones reports 1,4-Naphthoquinone Km 2.7 uM.

raw_value_unit_evidence: Km raw_value=2.7 raw_unit=uM

row_label: 1,4-Naphthoquinone (Quinones)


substrate_name: 5-hydroxy-1,4-naphthoquinone (juglone)

column_label: Table 3. Substrate specificity for quinones and ketones reports 5-Hydroxy-1,4-naphthoquinone Km 14 uM.

raw_value_unit_evidence: Km raw_value=14 raw_unit=uM

row_label: 5-Hydroxy-1,4-naphthoquinone (Quinones)

substrate: 5-hydroxy-1,4-naphthoquinone (juglone)


column_label: Table 3. Substrate specificity for quinones and ketones reports 1-Indanone Km 22 uM.

raw_value_unit_evidence: Km raw_value=22 raw_unit=uM

row_label: 1-Indanone (Aromatic and alicyclic ketones)


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

column_label: Table 3. Substrate specificity for quinones and ketones reports 3-Hydroxy-2-butanone Km 22 uM.


smiles: CCCCCCCCCCO

column_label: Table 5. Kinetic constants for alcohols reports 1-Decanol Km 8.2 uM.

raw_value_unit_evidence: Km raw_value=8.2 raw_unit=uM

row_label: 1-Decanol (Aliphatic alcohols)

table_label: Table 5. Kinetic constants for alcohols


column_label: Table 6. Substrate specificity for steroids and monosaccharides reports 4-Androstene-3,17-dione Km 5.6 uM.

raw_value_unit_evidence: Km raw_value=5.6 raw_unit=uM

row_label: 4-Androstene-3,17-dione (Ketosteroids / reduction)


column_label: Table 6. Substrate specificity for steroids and monosaccharides reports 5alpha-Androstane-3alpha,17beta-diol Km 6.9 uM.

raw_value_unit_evidence: Km raw_value=6.9 raw_unit=uM

row_label: 5alpha-Androstane-3alpha,17beta-diol (Hydroxysteroids / oxidation)


column_label: Table 6. Substrate specificity for steroids and monosaccharides reports Testosterone Km 18 uM.

raw_value_unit_evidence: Km raw_value=18 raw_unit=uM

row_label: Testosterone (Hydroxysteroids / oxidation)


substrate_name: 1H-indole-2,3-dione (isatin)

substrate: 1H-indole-2,3-dione (isatin)


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


substrate_name: butane-2,3-dione (diacetyl)

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

substrate: butane-2,3-dione (diacetyl)


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: farnesol

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

proof_lines:
AKR1C15
broad substrate specificity
low Km values

substrate: farnesol


substrate_name: farnesal

substrate: farnesal


substrate_name: geranylgeraniol

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

substrate: geranylgeraniol


smiles: CCCCCCCCCO


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F118A to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
F118A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F129A to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
F129A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L54A to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
L54A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N306A to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
N306A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T226A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
T226A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T24A to reconstruct the assayed variant sequence.

proof_lines:
3alpha-HSD alanine-scan
T24A
wild type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y310A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature F118A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature F129A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature L54A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature N306A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature T226A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature T24A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature W227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from source_record and applied mutation signature Y310A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table 3, row 2-Nitrobenzaldehyde, DD2 columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 3 2-Nitrobenzaldehyde / DD2 reports kcat 3.2 min^-1 and Km 0.6 uM; kcat/Km is derived from those same-row same-column cells.

row_label: 2-Nitrobenzaldehyde / DD2

table_label: Table 3. Substrate specificity for carbonyl compounds


column_label: Table 3, row 5beta-Androstane-3,17-dione, DD2 columns kcat (min^-1) and Km (uM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 3 5beta-Androstane-3,17-dione / DD2 reports kcat 0.62 min^-1 and Km 0.3 uM; kcat/Km is derived from those same-row same-column cells.

row_label: 5beta-Androstane-3,17-dione / DD2


substrate_name: Benzene dihydrodiol

substrate: Benzene dihydrodiol


substrate_name: Camphorquinone

column_label: Table label: Table 3. Substrate specificity for carbonyl compounds. Row: Camphorquinone. Enzyme column group: DD2. Columns read: kcat. (min^-1) cell 1.4, Km (uM) cell 0.5. metric: kcat; raw value: 1.4; raw unit: min^-1; normalized value: 0.023 s^(-1); metric: Km; raw value: 0.5; raw unit: uM; normalized value: 0.0005 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 46.0 s^-1 mM^-1; assay condition: Kinetic constants were determined as described in Table 2. The activity was assayed in 0.1 M-potassium phosphate, pH 7.4, containing 0.1 mM-NADPH as a cofactor; catalytic constants were calculated by assuming an Mr value for DD2 of 37000. The DD2 cells of this row are printed without parentheses, so the Table 3 parenthesized-value note does not apply to them. Export row conditions: pH 7.4.

normalized_value_unit_evidence: DD2 columns of Table 3 row Camphorquinone: kcat 1.4 min^-1 = 1.4 / 60 = 0.023333333333333334 s^-1 (1 min^-1 = 1/60 s^-1), which at the export's stored precision of three decimal places is 0.023 s^(-1); the export stores 0.023, so the difference is printed precision only. Km 0.5 uM = 0.0005 mM (1 uM = 0.001 mM), an exact conversion. Table 3 prints no kcat/Km cell, so the exported ratio is the quotient of this same row's two DD2 cells at the export's stored precision: 0.023 s^-1 / 0.0005 mM = 46.0 s^-1 mM^-1. With the unrounded kcat conversion the same quotient is 0.023333333333333334 s^-1 / 0.0005 mM = 46.666666666666664 s^-1 mM^-1; the gap to the exported 46.0 is exactly the three-decimal rounding of the exported kcat, so the two agree at the export's stored precision.; the paper sets the header as k with a subscripted `cat.` and (min^-1)/(uM) with superscript and micro-sign typography, flattened to kcat. (min^-1) and Km (uM) in the transcription, and empty cells print as the en dash.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, page 744 | column header rows: DD2 DD4 / Substrate kcat. (min^-1) Km (uM) kcat. (min^-1) Km (uM) | row: Camphorquinone 1.4 0.5 8.1 0.6 | DD2 cells read: kcat. = 1.4 min^-1; Km = 0.5 uM. The DD4 cells of the same row read kcat. 8.1 min^-1 and Km 0.6 uM, and are not used here. Table 3 prints no kcat/Km or catalytic-efficiency column.

row_label: DD2 | Camphorquinone

substrate: Camphorquinone


substrate_name: Dimethylglyoxal

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

column_label: Table label: Table 3. Substrate specificity for carbonyl compounds. Row: Butane-2,3-dione. Enzyme column group: DD2. Columns read: kcat. (min^-1) cell 2.1, Km (uM) cell 3.3. metric: kcat; raw value: 2.1; raw unit: min^-1; normalized value: 0.035 s^(-1); metric: Km; raw value: 3.3; raw unit: uM; normalized value: 0.003 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 11.666666666666668 s^-1 mM^-1; assay condition: Kinetic constants were determined as described in Table 2. The activity was assayed in 0.1 M-potassium phosphate, pH 7.4, containing 0.1 mM-NADPH as a cofactor; catalytic constants were calculated by assuming an Mr value for DD2 of 37000. The DD2 cells of this row are printed without parentheses, so the Table 3 parenthesized-value note does not apply to them. Export row conditions: pH 7.4.

normalized_value_unit_evidence: DD2 columns of Table 3 row Butane-2,3-dione: kcat 2.1 min^-1 = 2.1 / 60 = 0.035 s^(-1) (1 min^-1 = 1/60 s^-1), an exact conversion that decimal-matches the exported kcat. Km 3.3 uM = 0.0033 mM (1 uM = 0.001 mM), which at the export's stored precision of three decimal places is 0.003 mM; the export stores 0.003, so the difference is printed precision only. Table 3 prints no kcat/Km cell, so the exported ratio is the quotient of this same row's two DD2 cells at the export's stored precision: 0.035 s^-1 / 0.003 mM = 11.666666666666668 s^-1 mM^-1. With the unrounded Km conversion the same quotient is 0.035 s^-1 / 0.0033 mM = 10.606060606060607 s^-1 mM^-1; the gap to the exported 11.666666666666668 is exactly the three-decimal rounding of the exported km, so the two agree at the export's stored precision.; the paper sets the header as k with a subscripted `cat.` and (min^-1)/(uM) with superscript and micro-sign typography, flattened to kcat. (min^-1) and Km (uM) in the transcription, and empty cells print as the en dash.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, page 744 | column header rows: DD2 DD4 / Substrate kcat. (min^-1) Km (uM) kcat. (min^-1) Km (uM) | row: Butane-2,3-dione 2.1 3.3 4.0 6.5 | DD2 cells read: kcat. = 2.1 min^-1; Km = 3.3 uM. The DD4 cells of the same row read kcat. 4.0 min^-1 and Km 6.5 uM, and are not used here. Table 3 prints no kcat/Km or catalytic-efficiency column.

row_label: DD2 | Butane-2,3-dione

substrate: Dimethylglyoxal


substrate_name: m-Nitrobenzaldehyde

substrate: m-Nitrobenzaldehyde


column_label: Table label: Table 3. Substrate specificity for carbonyl compounds. Row: Pyridine-3-aldehyde. Enzyme column group: DD2. Columns read: kcat. (min^-1) cell 1.9, Km (uM) cell 57. metric: kcat; raw value: 1.9; raw unit: min^-1; normalized value: 0.032 s^(-1); metric: Km; raw value: 57; raw unit: uM; normalized value: 0.057 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.5614035087719298 s^-1 mM^-1; assay condition: Kinetic constants were determined as described in Table 2. The activity was assayed in 0.1 M-potassium phosphate, pH 7.4, containing 0.1 mM-NADPH as a cofactor; catalytic constants were calculated by assuming an Mr value for DD2 of 37000. The DD2 cells of this row are printed without parentheses, so the Table 3 parenthesized-value note does not apply to them. Export row conditions: pH 7.4.

normalized_value_unit_evidence: DD2 columns of Table 3 row Pyridine-3-aldehyde: kcat 1.9 min^-1 = 1.9 / 60 = 0.03166666666666666 s^-1 (1 min^-1 = 1/60 s^-1), which at the export's stored precision of three decimal places is 0.032 s^(-1); the export stores 0.032, so the difference is printed precision only. Km 57 uM = 0.057 mM (1 uM = 0.001 mM), an exact conversion. Table 3 prints no kcat/Km cell, so the exported ratio is the quotient of this same row's two DD2 cells at the export's stored precision: 0.032 s^-1 / 0.057 mM = 0.5614035087719298 s^-1 mM^-1. With the unrounded kcat conversion the same quotient is 0.03166666666666666 s^-1 / 0.057 mM = 0.5555555555555556 s^-1 mM^-1; the gap to the exported 0.5614035087719298 is exactly the three-decimal rounding of the exported kcat, so the two agree at the export's stored precision.; the paper sets the header as k with a subscripted `cat.` and (min^-1)/(uM) with superscript and micro-sign typography, flattened to kcat. (min^-1) and Km (uM) in the transcription, and empty cells print as the en dash.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, page 744 | column header rows: DD2 DD4 / Substrate kcat. (min^-1) Km (uM) kcat. (min^-1) Km (uM) | row: Pyridine-3-aldehyde 1.9 57 10 330 | DD2 cells read: kcat. = 1.9 min^-1; Km = 57 uM. The DD4 cells of the same row read kcat. 10 min^-1 and Km 330 uM, and are not used here. Table 3 prints no kcat/Km or catalytic-efficiency column.

row_label: DD2 | Pyridine-3-aldehyde


substrate_name: menadione

column_label: Table label: Table 3. Substrate specificity for carbonyl compounds. Row: Menadione. Enzyme column group: DD2. Columns read: kcat. (min^-1) cell 1.5, Km (uM) cell 13. metric: kcat; raw value: 1.5; raw unit: min^-1; normalized value: 0.025 s^(-1); metric: Km; raw value: 13; raw unit: uM; normalized value: 0.013 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 1.9230769230769234 s^-1 mM^-1; assay condition: Kinetic constants were determined as described in Table 2. The activity was assayed in 0.1 M-potassium phosphate, pH 7.4, containing 0.1 mM-NADPH as a cofactor; catalytic constants were calculated by assuming an Mr value for DD2 of 37000. The DD2 cells of this row are printed without parentheses, so the Table 3 parenthesized-value note does not apply to them. Export row conditions: pH 7.4.

normalized_value_unit_evidence: DD2 columns of Table 3 row Menadione: kcat 1.5 min^-1 = 1.5 / 60 = 0.025 s^(-1) (1 min^-1 = 1/60 s^-1), an exact conversion that decimal-matches the exported kcat. Km 13 uM = 0.013 mM (1 uM = 0.001 mM), an exact conversion that decimal-matches the exported km. Table 3 prints no kcat/Km cell, so the exported ratio is the quotient of this same row's two DD2 cells at the export's stored precision: 0.025 s^-1 / 0.013 mM = 1.9230769230769234 s^-1 mM^-1. Both inputs are exact conversions of this row's own printed DD2 cells, so the quotient carries no rounding gap.; the paper sets the header as k with a subscripted `cat.` and (min^-1)/(uM) with superscript and micro-sign typography, flattened to kcat. (min^-1) and Km (uM) in the transcription, and empty cells print as the en dash.

raw_value_unit_evidence: Table 3. Substrate specificity for carbonyl compounds, page 744 | column header rows: DD2 DD4 / Substrate kcat. (min^-1) Km (uM) kcat. (min^-1) Km (uM) | row: Menadione 1.5 13 (3.1) – | DD2 cells read: kcat. = 1.5 min^-1; Km = 13 uM. The DD4 cells of the same row read kcat. (3.1) min^-1 and an empty Km cell, and are not used here. Table 3 prints no kcat/Km or catalytic-efficiency column.

row_label: DD2 | Menadione

substrate: menadione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y205F to reconstruct the assayed variant sequence.


substrate_name: NAD+

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: p-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C3. Row: 1-Acenaphthenol. Columns read: Km b (uM) cell 70, kcat (min^-1) cell 25, kcat /Km (min^-1 mM^-1) cell 360. The recombinant Km cell 70 uM normalizes to 0.07 mM and decimal-matches the exported km. The recombinant kcat cell 25 min^-1 normalizes to 0.417 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 5.957142857142856 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 360 min^-1 mM^-1: that cell is 6.0 s^-1 mM^-1, and the same-row quotient 5.957142857142856 s^-1 mM^-1 is 357.4285714285714 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 25; raw unit: min^-1; normalized value: 0.417 s^(-1); metric: Km; raw value: 70; raw unit: uM; normalized value: 0.07 mM; metric: kcat/Km; normalized value: 5.957142857142856 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C3; row 1-Acenaphthenol: Km cell 70 uM, kcat cell 25 min^-1, kcat/Km cell 360 min^-1 mM^-1. The recombinant values used here are 70 uM and 25 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C3 | 1-Acenaphthenol


column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C2. Row: 1-Acenaphthenol. Columns read: Km b (uM) cell 22 (56), kcat (min^-1) cell 35.1, kcat /Km (min^-1 mM^-1) cell 1600. The recombinant Km cell 22 uM normalizes to 0.022 mM and decimal-matches the exported km. The recombinant kcat cell 35.1 min^-1 normalizes to 0.585 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 26.59090909090909 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 1600 min^-1 mM^-1: that cell is 26.666666666666668 s^-1 mM^-1, and the same-row quotient 26.59090909090909 s^-1 mM^-1 is 1595.4545454545455 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 35.1; raw unit: min^-1; normalized value: 0.585 s^(-1); metric: Km; raw value: 22; raw unit: uM; normalized value: 0.022 mM; metric: kcat/Km; normalized value: 26.59090909090909 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C2; row 1-Acenaphthenol: Km cell 22 (56) uM, kcat cell 35.1 min^-1, kcat/Km cell 1600 min^-1 mM^-1. The recombinant values used here are 22 uM and 35.1 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C2 | 1-Acenaphthenol


column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C1. Row: 1-Acenaphthenol. Columns read: Km b (uM) cell 22 (26), kcat (min^-1) cell 29.4, kcat /Km (min^-1 mM^-1) cell 1300. The recombinant Km cell 22 uM normalizes to 0.022 mM and decimal-matches the exported km. The recombinant kcat cell 29.4 min^-1 normalizes to 0.49 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 22.272727272727273 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 1300 min^-1 mM^-1: that cell is 21.666666666666668 s^-1 mM^-1, and the same-row quotient 22.272727272727273 s^-1 mM^-1 is 1336.3636363636365 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 29.4; raw unit: min^-1; normalized value: 0.49 s^(-1); metric: Km; raw value: 22; raw unit: uM; normalized value: 0.022 mM; metric: kcat/Km; normalized value: 22.272727272727273 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C1; row 1-Acenaphthenol: Km cell 22 (26) uM, kcat cell 29.4 min^-1, kcat/Km cell 1300 min^-1 mM^-1. The recombinant values used here are 22 uM and 29.4 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C1 | 1-Acenaphthenol


column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C4. Row: Benzenedihydrodiol. Columns read: Km b (uM) cell 17 (24), kcat (min^-1) cell 2.0 (2.2), kcat /Km (min^-1 mM^-1) cell 120 (92). The recombinant Km cell 17 uM normalizes to 0.017 mM and decimal-matches the exported km. The recombinant kcat cell 2.0 min^-1 normalizes to 0.033 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 1.9411764705882353 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 120 min^-1 mM^-1: that cell is 2.0 s^-1 mM^-1, and the same-row quotient 1.9411764705882353 s^-1 mM^-1 is 116.47058823529412 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 2.0; raw unit: min^-1; normalized value: 0.033 s^(-1); metric: Km; raw value: 17; raw unit: uM; normalized value: 0.017 mM; metric: kcat/Km; normalized value: 1.9411764705882353 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C4; row Benzenedihydrodiol: Km cell 17 (24) uM, kcat cell 2.0 (2.2) min^-1, kcat/Km cell 120 (92) min^-1 mM^-1. The recombinant values used here are 17 uM and 2.0 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C4 | Benzenedihydrodiol


column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C3. Row: Benzenedihydrodiol. Columns read: Km b (uM) cell 320, kcat (min^-1) cell 0.9, kcat /Km (min^-1 mM^-1) cell 2.8. The recombinant Km cell 320 uM normalizes to 0.32 mM and decimal-matches the exported km. The recombinant kcat cell 0.9 min^-1 normalizes to 0.015 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 0.046875 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 2.8 min^-1 mM^-1: that cell is 0.04666666666666666 s^-1 mM^-1, and the same-row quotient 0.046875 s^-1 mM^-1 is 2.8125 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 0.9; raw unit: min^-1; normalized value: 0.015 s^(-1); metric: Km; raw value: 320; raw unit: uM; normalized value: 0.32 mM; metric: kcat/Km; normalized value: 0.046875 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C3; row Benzenedihydrodiol: Km cell 320 uM, kcat cell 0.9 min^-1, kcat/Km cell 2.8 min^-1 mM^-1. The recombinant values used here are 320 uM and 0.9 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C3 | Benzenedihydrodiol


column_label: Table label: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67). Enzyme block: AKR1C1. Row: Benzenedihydrodiol. Columns read: Km b (uM) cell 150 (580), kcat (min^-1) cell 2.9 (3.2), kcat /Km (min^-1 mM^-1) cell 19 (6). The recombinant Km cell 150 uM normalizes to 0.15 mM and decimal-matches the exported km. The recombinant kcat cell 2.9 min^-1 normalizes to 0.048 s^-1 at the export's stored precision and decimal-matches the exported kcat. The exported kcat_over_km 0.32 s^-1 mM^-1 is the same-row quotient of those two cells. Round-trip against the printed kcat/Km cell 19 min^-1 mM^-1: that cell is 0.31666666666666665 s^-1 mM^-1, and the same-row quotient 0.32 s^-1 mM^-1 is 19.2 min^-1 mM^-1, which agrees with the printed cell at the two significant figures the cell is printed to. The printed cell and the same-row quotient therefore do not disagree; the quotient is used because it carries the export's full stored precision.

normalized_value_unit_evidence: metric: kcat; raw value: 2.9; raw unit: min^-1; normalized value: 0.048 s^(-1); metric: Km; raw value: 150; raw unit: uM; normalized value: 0.15 mM; metric: kcat/Km; normalized value: 0.32 s^(-1)*mM^(-1); assay condition: 100 mM potassium phosphate (pH 7.4) and 2.3 mM NADP+ at 25 C.

raw_value_unit_evidence: Table 1 Comparison of steady-state kinetic parameters for recombinant AKR1C1-AKR1C4 with those obtained from the native enzymes purified from human liver (PMID 15026176, journal page 67); column headers: Enzyme | Substrate | Km b (uM) | kcat (min-1) | kcat /Km (min-1 mM-1); enzyme block AKR1C1; row Benzenedihydrodiol: Km cell 150 (580) uM, kcat cell 2.9 (3.2) min^-1, kcat/Km cell 19 (6) min^-1 mM^-1. The recombinant values used here are 150 uM and 2.9 min^-1. Table 1 footnote b: Native values in parenthesis were taken from Hara et al. (1990) and Deyashiki et al. (1992, 1994). The parenthesized numbers are therefore a different literature source and are NOT used as evidence here; only the non-parenthesized recombinant cell is quoted as this paper's value.

row_label: AKR1C1 | Benzenedihydrodiol


enzyme_display_name: Farnesol dehydrogenase

organism: Aedes aegypti

substrate_name: (E,E) farnesol

enzyme: Farnesol dehydrogenase

substrate: (E,E) farnesol


smiles: CCCCCCCCC(C)O

assay_conditions_summary: pH 10; buffer Stauffer; cofactor NADP+

column_label: Table 1 row 2-Decanol, KM column, value 184 +/- 6; footnote says KM is expressed in uM.

raw_value_unit_evidence: KM raw_value=184 raw_unit=uM raw_uncertainty=+/- 6 uM

table_label: PMID 19940247 PMC Table 1: Enzymatic activity of the recombinant AaSDR-1 for different substrates


substrate_name: geraniol (E)

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

substrate: geraniol (E)


substrate_name: citronellol

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

column_label: Table 1 row Citronellol, KM column, value 133 +/- 17; footnote says KM is expressed in uM.

raw_value_unit_evidence: KM raw_value=133 raw_unit=uM raw_uncertainty=+/- 17 uM

row_label: Citronellol

substrate: citronellol


substrate_name: octanol

smiles: CCCCCCCCO

column_label: Table 1 row Octanol, KM column, value 195; footnote says KM is expressed in uM.

raw_value_unit_evidence: KM raw_value=195 raw_unit=uM

row_label: Octanol

substrate: octanol


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

organism: Malus domestica

substrate_name: eriodictyol

assay_conditions_summary: cofactor NADPH

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

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

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

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

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

substrate: eriodictyol


substrate_name: dihydrokaempferol

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

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

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

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

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

substrate: dihydrokaempferol


substrate_name: dihydroquercetin

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

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

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

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

substrate: dihydroquercetin


substrate_name: testosterone

substrate: testosterone


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


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


assay_conditions_summary: pH 7; 298.15 K; 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-DHT reduction / AKR1C2 (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 / AKR1C2 (R): Km 26.0 uM; kcat 0.23 min^-1; kcat/Km 9 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C2 (R)


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 / 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 5alpha-Androstane-3,17-dione reduction / AKR1C2: Km 6.26 uM; kcat 1.39 min^-1; kcat/Km 222 min^-1 mM^-1.


assay_conditions_summary: pH 7; 298.15 K; 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 / 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.


proof_lines: transformation of androstenedione into testosterone


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

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

column_label: Official ScienceDirect HTML Table 1 row NAD+, AKR1C26 columns Km=4.0 uM, kcat=1.2 min^-1, kcat/Km=0.30 min^-1 uM^-1; unit footnote Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

normalized_value_unit_evidence: Km 0.004 mM; kcat 0.020 s^-1; kcat/Km 5.0 s^-1 mM^-1; exported values are Km 0.02 mM, kcat 0.004 s^-1, kcat/Km 0.2 s^-1 mM^-1

raw_value_unit_evidence: Km 4.0 uM; kcat 1.2 min^-1; kcat/Km 0.30 min^-1 uM^-1

row_label: NAD+ / AKR1C26


assay_conditions_summary: pH 7.4; buffer pH 7; cofactor NADH

column_label: Official ScienceDirect HTML Table 2 row NADH, AKR1C26 Km column = 3.3 uM; unit footnote Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Km 3.3 uM; kcat 7.4 min^-1; kcat/Km 2.2 min^-1 uM^-1

row_label: NADH / AKR1C26

table_label: Table 2. Kinetic constants for NADH and carbonyl compounds.


column_label: Page 7, right column, Results 'Identity of TBER2 with 3a-HSD': the single parenthetical for recombinant rat 3a-HSD; reduction of TBE (6-tert-butyl-2,3-epoxy-5-cyclohexene-1,4-dione) supplies both the Km and the kcat cell.

normalized_value_unit_evidence: Km 23 uM = 0.023 mM; kcat 24 min^-1 / 60 = 0.4 s^-1; kcat/Km = 0.4 s^-1 / 0.023 mM = 17.39130434782609 s^-1 mM^-1, derived only from this record's own two printed cells because the paper prints no ratio for this row.

raw_value_unit_evidence: Page-7 prose, recombinant rat 3a-HSD; reduction of TBE (6-tert-butyl-2,3-epoxy-5-cyclohexene-1,4-dione): Km 23 uM; kcat 24 min^-1. The paper prints no kcat/Km for this measurement.

table_label: Results prose (page 7, right column)


column_label: Page 7, right column, Results 'Identity of TBER2 with 3a-HSD': the single parenthetical for recombinant rat 3a-HSD; oxidation of trans-benzene dihydrodiol supplies both the Km and the kcat cell.

normalized_value_unit_evidence: Km 0.37 mM = 0.37 mM; kcat 3.6 min^-1 / 60 = 0.06 s^-1; kcat/Km = 0.06 s^-1 / 0.37 mM = 0.16216216216216217 s^-1 mM^-1, derived only from this record's own two printed cells because the paper prints no ratio for this row.

raw_value_unit_evidence: Page-7 prose, recombinant rat 3a-HSD; oxidation of trans-benzene dihydrodiol: Km 0.37 mM; kcat 3.6 min^-1. The paper prints no kcat/Km for this measurement.


substrate_name: codeine

assay_conditions_summary: cofactor NAD+

substrate: codeine


organism: Pyrus communis

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

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

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

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


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

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

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

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


substrate_name: geranylgeranial

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

substrate: geranylgeranial


column_label: Springer Table 1 Kinetic parameters: Gox0417 (2KGR), substrate 2KG, columns KM (mM), kcat (s^-1), kcat/KM (M^-1 s^-1).

normalized_value_unit_evidence: Km normalized_value=5.16 normalized_unit=mM; kcat normalized_value=48.2 normalized_unit=s^-1; explicit kcat/Km normalized_value=9.34 normalized_unit=s^-1 mM^-1. CatLog stores derived kcat/Km=9.34108527131783.

raw_value_unit_evidence: Table 1 row Gox0417 (2KGR), substrate 2KG, reports Km=5.16 mM, kcat=48.2 s^-1, kcat/KM=9.34 x 10^3 M^-1 s^-1.

table_label: Springer Table 1


enzyme_display_name: flavanone 4-reductase

organism: Sinningia cardinalis

enzyme: flavanone 4-reductase


organism: Homo sapiens

substrate_name: Prostaglandin E2; NAD+

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

unit: lgwedgeoneswedgeone

substrate: Prostaglandin E2; NAD+


substrate_name: NAD+; Prostaglandin E2

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: NAD+; Prostaglandin E2


organism: Mus musculus


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V186K with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V186A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.