enzyme_display_name: Aldo-keto reductase family 1 member C21

substrate_name: NADP

assay_conditions_summary: pH 7; buffer 0.1 M potassium phosphate; cofactor NADP+

column_label: J-STAGE PDF text states that the Km and kcat/Km values of recombinant AKR1C21 (DD3) for NADP+ were 1.8 uM and 150 min^-1 uM^-1, respectively.

raw_value_unit_evidence: Km raw_value=1.8 raw_unit=uM

row_label: recombinant AKR1C21 (DD3) / NADP+

table_label: J-STAGE PDF PMID 15577209 coenzyme specificity prose

enzyme: Aldo-keto reductase family 1 member C21

substrate: NADP


enzyme_display_name: IMP dehydrogenase

organism: Escherichia coli

substrate_name: IMP

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E54A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
PMID 9341229
Escherichia coli IMPDH
IMP

data_origin: experimental

enzyme: IMP dehydrogenase

substrate: IMP

status: unverified

source: oed


verification_status: verified

mutation_signature: Unknown

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Page 13370 Table 2, row wild-type: the `kcat s-1` cell and the `Km IMP (uM)` cell of that one row reproduce the export values exactly after the normalizations recorded in conversion_arithmetic_note, and their same-row quotient reproduces the exported kcat/Km. Table 2 prints a `kcat/KmKm [(sM2)-1 x 107]` column, but that column is NOT a kcat/Km cell: its unit is the reciprocal of (s x M^2), i.e. kcat divided by the PRODUCT of the two Michaelis constants (Km IMP x Km NAD+), which is not the same quantity as kcat/Km (s^-1 mM^-1). This was checked against the printed cells of every row used here: e.g. wild-type 13 s^-1 / (61 uM x 2.0 mM) = 1.07e8 (s M2)^-1 = 10.7 x 10^7, which is the printed cell 11 at that cell's printed precision; D200A 14 / (44 uM x 1.5 mM) = 2.12e8 = 21.2 x 10^7 versus the printed 21; D338A 0.02 / (710 uM x 3.3 mM) = 8.5e3 = 0.00085 x 10^7 versus the printed 0.0009. So the paper prints no kcat/Km cell for these rows, there is no printed ratio cell to back-convert the quotient against, and no correction is claimed against the printed kcat/KmKm column.

normalized_value_unit_evidence: metric: kcat; raw value: 13 s-1; raw unit: s-1; normalized value: 13.0 s^-1; normalized unit: s^-1; metric: Km; raw value: 61 uM; raw unit: uM; normalized value: 0.061 mM; normalized unit: mM; metric: kcat/Km; normalized value: 213.11475409836066 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Enzyme Assays: Standard E. coli IMPDH activity assays contained 50 mM Tris, pH 8.0, 100 mM KCl, 3 mM EDTA, 1 mM DTT, 1 mM IMP, and 2.5 mM NAD+; the production of NADH was monitored at 25 C. Data Analysis (Block C): Wild-type and all mutant enzyme activities were assayed at saturating IMP and NAD+ concentrations and varied K+ concentrations. The export row carries pH 8.0 and 298.15 K (25 C).

raw_value_unit_evidence: Table 2, row wild-type: kcat cell 13 s-1; Km IMP (uM) cell 61 uM. Column headers as printed: `kcat        kcat/KmKm        Km IMP     Km NAD+       Kii NAD+      K m K+    Kis GMP      Kis XMP      Ki MMP      Kii TAD` / `enzyme        s-1      [(sM2)-1 × 107]      (µM)       (mM)           (mM)        (mM)       (µM)         (µM)         (nM)        (µM)`. Table title as printed: `Table 2: Kinetic Charaterization of E. coli IMPDH and Mutants (Unless Otherwise Noted, Error Was e15%)`. Footnotes as printed: `a Error was e25%. b Kinetic constants determined at 400 mM KCl. cProgress curve analysis. dTight binding analysis. ena, not applicable. end,`.

row_label: wild-type

table_label: Table 2: Kinetic Charaterization of E. coli IMPDH and Mutants (Unless Otherwise Noted, Error Was e15%) - Biochemistry 1997, 36, page 13370

status: verified


substrate_name: K+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D138A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

substrate: K+


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D13A with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D243A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D248A to reconstruct the assayed variant sequence.

proof_lines: Asp248Ala kcat IMPDH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D338A to reconstruct the assayed variant sequence.

proof_lines: Asp338Ala kcat IMPDH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D50A to reconstruct the assayed variant sequence.

proof_lines: Asp50Ala K+ K(m)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E369A to reconstruct the assayed variant sequence.


organism: Mus musculus

verification_status: corrected

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 2, row '4-Nitroacetophenone', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 5.8 min^-1; kcat/Km 0.1 min^-1 uM^-1; Km 51 uM

row_label: 4-Nitroacetophenone / AKR1C21* (DD1/Q91WR5)

table_label: Table 2

status: corrected


column_label: Table 2, row '5a-DHT', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 6.2 min^-1; kcat/Km 6 min^-1 uM^-1; Km 1 uM


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Androstane-3,17-dione; Km (uM) = 1; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Androstane-3,17-dione; kcat (min^-1) = 8; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Androstane-3,17-dione; kcat/Km (min^-1 uM^-1) = 8

raw_value_unit_evidence: Km (uM) 1 uM for AKR1C21 (DD3) / 5a-Androstane-3,17-dione; kcat (min^-1) 8 min^-1 for AKR1C21 (DD3) / 5a-Androstane-3,17-dione; kcat/Km (min^-1 uM^-1) 8 min^-1 uM^-1 for AKR1C21 (DD3) / 5a-Androstane-3,17-dione

table_label: J-STAGE PDF page 1942 Table 2


column_label: Table 1, row '5a-Pregnane-3a,20a-diol', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 4.6 min^-1; kcat/Km 5 min^-1 uM^-1; Km 1 uM

row_label: 5a-Pregnane-3a,20a-diol / AKR1C21* (DD1/Q91WR5)

table_label: Table 1


column_label: Table 1, row '3a,21-Dihydroxy-5a-pregnan-20-one', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 3.5 min^-1; kcat/Km 2 min^-1 uM^-1; Km 1.9 uM

row_label: 3a,21-Dihydroxy-5a-pregnan-20-one / AKR1C21* (DD1/Q91WR5)


column_label: Table 2, row '21-Hydroxy-5a-pregnane-3,20-dione', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 15 min^-1; kcat/Km 15 min^-1 uM^-1; Km 1 uM

row_label: 21-Hydroxy-5a-pregnane-3,20-dione / AKR1C21* (DD1/Q91WR5)


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Pregnane-3,20-dione; Km (uM) = 0.4; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Pregnane-3,20-dione; kcat (min^-1) = 12; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5a-Pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) = 30

normalized_value_unit_evidence: normalized km=0.0004 mM; export km=0.0004 mM; normalized kcat=0.2 s^-1; export kcat=0.2 s^-1; normalized kcat_over_km=500 s^-1 mM^-1; export kcat_over_km=500.0 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.4 uM for AKR1C21 (DD3) / 5a-Pregnane-3,20-dione; kcat (min^-1) 12 min^-1 for AKR1C21 (DD3) / 5a-Pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) 30 min^-1 uM^-1 for AKR1C21 (DD3) / 5a-Pregnane-3,20-dione

row_label: AKR1C21 (DD3) / 5a-Pregnane-3,20-dione


column_label: Table 2, row '17b-Hydroxy-5b-androstan-3-one', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 21 min^-1; kcat/Km 18 min^-1 uM^-1; Km 1.2 uM

row_label: 17b-Hydroxy-5b-androstan-3-one / AKR1C21* (DD1/Q91WR5)


column_label: Table 2, row '5b-Androstane-3,17-dione', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

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

row_label: 5b-Androstane-3,17-dione / AKR1C21* (DD1/Q91WR5)


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21* (DD1); 21-Hydroxy-5b-pregnane-3,20-dione; Km (uM) = 0.4; J-STAGE PDF page 1942 Table 2; AKR1C21* (DD1); 21-Hydroxy-5b-pregnane-3,20-dione; kcat (min^-1) = 35; J-STAGE PDF page 1942 Table 2; AKR1C21* (DD1); 21-Hydroxy-5b-pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) = 88

raw_value_unit_evidence: Km (uM) 0.4 uM for AKR1C21* (DD1) / 21-Hydroxy-5b-pregnane-3,20-dione; kcat (min^-1) 35 min^-1 for AKR1C21* (DD1) / 21-Hydroxy-5b-pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) 88 min^-1 uM^-1 for AKR1C21* (DD1) / 21-Hydroxy-5b-pregnane-3,20-dione


column_label: Table 1, row '3a,21-Dihydroxy-5b-pregnan-20-one', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 8.8 min^-1; kcat/Km 8 min^-1 uM^-1; Km 1.1 uM

row_label: 3a,21-Dihydroxy-5b-pregnan-20-one / AKR1C21* (DD1/Q91WR5)


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5b-Pregnane-3,20-dione; Km (uM) = 0.6; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5b-Pregnane-3,20-dione; kcat (min^-1) = 24; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 5b-Pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) = 40

normalized_value_unit_evidence: normalized km=0.0006 mM; export km=0.0006 mM; normalized kcat=0.4 s^-1; export kcat=0.4 s^-1; normalized kcat_over_km=666.6666666666667 s^-1 mM^-1; export kcat_over_km=666.6666666666667 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.6 uM for AKR1C21 (DD3) / 5b-Pregnane-3,20-dione; kcat (min^-1) 24 min^-1 for AKR1C21 (DD3) / 5b-Pregnane-3,20-dione; kcat/Km (min^-1 uM^-1) 40 min^-1 uM^-1 for AKR1C21 (DD3) / 5b-Pregnane-3,20-dione

row_label: AKR1C21 (DD3) / 5b-Pregnane-3,20-dione


column_label: Table 2. Kinetic Constants for Ketosteroids and Non-steroidal Carbonyl Compounds, journal page 1942 (PDF page 4). Substrate row Phenanthrenequinone; AKR1C21 (DD3) column group; Km cell = 2.6 uM; kcat cell = 47 min^-1; kcat/Km cell = 18 min^-1 uM^-1.

normalized_value_unit_evidence: Km: printed Table 2 cell 2.6 uM; 1 uM = 1/1000 mM, so 2.6 / 1000 = 0.0026 mM; the export stores 0.0026 mM, the same value. kcat: printed Table 2 cell 47 min^-1; the printed turnover column is per MINUTE, so 47 / 60 = 0.7833333333333333 s^-1; the export stores 0.7833333333333333 s^-1, the same value. kcat/Km: printed Table 2 cell 18 min^-1 uM^-1; 1 min^-1 uM^-1 = (1/60) s^-1 * 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 18 * 16.666666666666668 = 300.0 s^-1 mM^-1; the export stores 3.0 s^-1 mM^-1, which is the printed cell divided by 60 with the 1000-fold micromolar-to-millimolar step omitted.

raw_value_unit_evidence: Journal page 1942, Table 2, AKR1C21 (DD3) column group, substrate row Phenanthrenequinone: Km = 2.6 uM; kcat = 47 min^-1; kcat/Km = 18 min^-1 uM^-1. The printed column headers of Table 2 are (uM) for Km, (min^-1) for kcat and (min^-1 uM^-1) for kcat/Km.


column_label: Table 1, row 'Androst-5-ene-3b,17a-diol', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 3.7 min^-1; kcat/Km 2 min^-1 uM^-1; Km 2.1 uM

row_label: Androst-5-ene-3b,17a-diol / AKR1C21* (DD1/Q91WR5)


substrate_name: Benzene dihydrodiol

column_label: J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); cis-Benzene dihydrodiol; Km (uM) = 1240; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); cis-Benzene dihydrodiol; kcat (min^-1) = 62; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); cis-Benzene dihydrodiol; kcat/Km (min^-1 uM^-1) = 0.05

raw_value_unit_evidence: Km (uM) 1240 uM for AKR1C21 (DD3) / cis-Benzene dihydrodiol; kcat (min^-1) 62 min^-1 for AKR1C21 (DD3) / cis-Benzene dihydrodiol; kcat/Km (min^-1 uM^-1) 0.05 min^-1 uM^-1 for AKR1C21 (DD3) / cis-Benzene dihydrodiol

row_label: AKR1C21 (DD3) / cis-Benzene dihydrodiol

table_label: J-STAGE PDF page 1942 Table 1

substrate: Benzene dihydrodiol


substrate_name: Epitestosterone

column_label: J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; Km (uM) = 0.6; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; kcat (min^-1) = 18; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); Epitestosterone; kcat/Km (min^-1 uM^-1) = 30

normalized_value_unit_evidence: normalized km=0.0006 mM; export km=0.0006 mM; normalized kcat=0.3 s^-1; export kcat=0.3 s^-1; normalized kcat_over_km=500 s^-1 mM^-1; export kcat_over_km=500.0 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.6 uM for AKR1C21 (DD3) / Epitestosterone; kcat (min^-1) 18 min^-1 for AKR1C21 (DD3) / Epitestosterone; kcat/Km (min^-1 uM^-1) 30 min^-1 uM^-1 for AKR1C21 (DD3) / Epitestosterone

row_label: AKR1C21 (DD3) / Epitestosterone

substrate: Epitestosterone


column_label: J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Estradiol; Km (uM) = 1.6; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Estradiol; kcat (min^-1) = 2; J-STAGE PDF page 1942 Table 1; AKR1C21 (DD3); 17a-Estradiol; kcat/Km (min^-1 uM^-1) = 1

raw_value_unit_evidence: Km (uM) 1.6 uM for AKR1C21 (DD3) / 17a-Estradiol; kcat (min^-1) 2 min^-1 for AKR1C21 (DD3) / 17a-Estradiol; kcat/Km (min^-1 uM^-1) 1 min^-1 uM^-1 for AKR1C21 (DD3) / 17a-Estradiol

row_label: AKR1C21 (DD3) / 17a-Estradiol


substrate_name: p-Nitrobenzaldehyde

column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 4-Nitrobenzaldehyde; Km (uM) = 2.3; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 4-Nitrobenzaldehyde; kcat (min^-1) = 30; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); 4-Nitrobenzaldehyde; kcat/Km (min^-1 uM^-1) = 13

raw_value_unit_evidence: Km (uM) 2.3 uM for AKR1C21 (DD3) / 4-Nitrobenzaldehyde; kcat (min^-1) 30 min^-1 for AKR1C21 (DD3) / 4-Nitrobenzaldehyde; kcat/Km (min^-1 uM^-1) 13 min^-1 uM^-1 for AKR1C21 (DD3) / 4-Nitrobenzaldehyde

row_label: AKR1C21 (DD3) / 4-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


substrate_name: Pregnanediol

column_label: Table 1, row '5b-Pregnane-3a,20a-diol', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 8 min^-1; kcat/Km 20 min^-1 uM^-1; Km 0.4 uM

row_label: 5b-Pregnane-3a,20a-diol / AKR1C21* (DD1/Q91WR5)

substrate: Pregnanediol


column_label: Table 1, row 'R-Indan-1-ol', AKR1C21* (DD1/Q91WR5) columns Km, kcat, kcat/Km. Rendered PDF page 1942 confirms units Km uM, kcat min^-1, and kcat/Km min^-1 uM^-1; AKR1C21 (DD3) is a separate neighboring isoform column.

raw_value_unit_evidence: kcat 19 min^-1; kcat/Km 0.05 min^-1 uM^-1; Km 370 uM

row_label: R-Indan-1-ol / AKR1C21* (DD1/Q91WR5)


substrate_name: NAD+

proof_lines: D50A NAD+ IMPDH

substrate: NAD+


proof_lines: E369A NAD+ IMPDH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E373A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E469A to reconstruct the assayed variant sequence.


column_label: Page 13370 Table 2, row wild-type: the `kcat s-1` cell and the `Km NAD+ (mM)` cell of that one row reproduce the export values exactly after the normalizations recorded in conversion_arithmetic_note, and their same-row quotient reproduces the exported kcat/Km. Table 2 prints a `kcat/KmKm [(sM2)-1 x 107]` column, but that column is NOT a kcat/Km cell: its unit is the reciprocal of (s x M^2), i.e. kcat divided by the PRODUCT of the two Michaelis constants (Km IMP x Km NAD+), which is not the same quantity as kcat/Km (s^-1 mM^-1). This was checked against the printed cells of every row used here: e.g. wild-type 13 s^-1 / (61 uM x 2.0 mM) = 1.07e8 (s M2)^-1 = 10.7 x 10^7, which is the printed cell 11 at that cell's printed precision; D200A 14 / (44 uM x 1.5 mM) = 2.12e8 = 21.2 x 10^7 versus the printed 21; D338A 0.02 / (710 uM x 3.3 mM) = 8.5e3 = 0.00085 x 10^7 versus the printed 0.0009. So the paper prints no kcat/Km cell for these rows, there is no printed ratio cell to back-convert the quotient against, and no correction is claimed against the printed kcat/KmKm column.

normalized_value_unit_evidence: metric: kcat; raw value: 13 s-1; raw unit: s-1; normalized value: 13.0 s^-1; normalized unit: s^-1; metric: Km; raw value: 2.0 mM; raw unit: mM; normalized value: 2.0 mM; normalized unit: mM; metric: kcat/Km; normalized value: 6.5 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Enzyme Assays: Standard E. coli IMPDH activity assays contained 50 mM Tris, pH 8.0, 100 mM KCl, 3 mM EDTA, 1 mM DTT, 1 mM IMP, and 2.5 mM NAD+; the production of NADH was monitored at 25 C. Data Analysis (Block C): Wild-type and all mutant enzyme activities were assayed at saturating IMP and NAD+ concentrations and varied K+ concentrations. The export row carries pH 8.0 and 298.15 K (25 C). The export row's cofactor_name is NAD+, which is the coenzyme the paper prints for this reaction ('IMP dehydrogenase (IMPDH) catalyzes the oxidation of IMP to XMP with the concomitant reduction of NAD+'); the catalog annotation and the paper agree.

raw_value_unit_evidence: Table 2, row wild-type: kcat cell 13 s-1; Km NAD+ (mM) cell 2.0 mM. Column headers as printed: `kcat        kcat/KmKm        Km IMP     Km NAD+       Kii NAD+      K m K+    Kis GMP      Kis XMP      Ki MMP      Kii TAD` / `enzyme        s-1      [(sM2)-1 × 107]      (µM)       (mM)           (mM)        (mM)       (µM)         (µM)         (nM)        (µM)`. Table title as printed: `Table 2: Kinetic Charaterization of E. coli IMPDH and Mutants (Unless Otherwise Noted, Error Was e15%)`. Footnotes as printed: `a Error was e25%. b Kinetic constants determined at 400 mM KCl. cProgress curve analysis. dTight binding analysis. ena, not applicable. end,`.

row_label: wild-type


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q222N with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y224D with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y224F with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature Y216F matches the mutant residue at offset +0 and the reference residue at offset +8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


enzyme_display_name: tropinone reductase I

organism: Datura stramonium

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H112Y/A160S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / H112Y/A160S; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / H112Y/A160S; kcat 8.42 s^-1, kcat_over_km 102.68292682926828 s^-1 mM^-1, km 0.082 mM.

normalized_value_unit_evidence: kcat normalized value: 8.42; normalized unit: s^-1; kcat_over_km normalized value: 102.68292682926828; normalized unit: s^-1 mM^-1; km normalized value: 0.082; normalized unit: mM

raw_value_unit_evidence: km raw value: 82.2 ± 21.0; raw unit: uM; kcat raw value: 8.42 ± 0.21; raw unit: s^-1; kcat_over_km raw value: 8.42 / 0.082; raw unit: s^-1 per mM after normalizing Km to row/export precision

enzyme: tropinone reductase I

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H112Y/A160S/V168E/I223L/F226L to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / H112Y/A160S/V168E/I223L/F226L; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / H112Y/A160S/V168E/I223L/F226L; kcat 0.135 s^-1, kcat_over_km 3.2926829268292686 s^-1 mM^-1, km 0.041 mM.

normalized_value_unit_evidence: kcat normalized value: 0.135; normalized unit: s^-1; kcat_over_km normalized value: 3.2926829268292686; normalized unit: s^-1 mM^-1; km normalized value: 0.041; normalized unit: mM

raw_value_unit_evidence: km raw value: 41.1 ± 7.9; raw unit: uM; kcat raw value: 0.135 ± 0.003; raw unit: s^-1; kcat_over_km raw value: 0.135 / 0.041; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P50162 and applied mutation signature V168E with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / V168E; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / V168E; kcat 0.603 s^-1, kcat_over_km 15.075 s^-1 mM^-1, km 0.04 mM.

normalized_value_unit_evidence: kcat normalized value: 0.603; normalized unit: s^-1; kcat_over_km normalized value: 15.075; normalized unit: s^-1 mM^-1; km normalized value: 0.04; normalized unit: mM

raw_value_unit_evidence: km raw value: 39.6 ± 7.7; raw unit: uM; kcat raw value: 0.603 ± 0.029; raw unit: s^-1; kcat_over_km raw value: 0.603 / 0.04; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-I / V168E


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V168E/H112Y to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / V168E/H112Y; column label: Km, NADPH (uM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / V168E/H112Y; kcat 0.389 s^-1, kcat_over_km 6.946428571428571 s^-1 mM^-1, km 0.056 mM.

normalized_value_unit_evidence: kcat normalized value: 0.389; normalized unit: s^-1; kcat_over_km normalized value: 6.946428571428571; normalized unit: s^-1 mM^-1; km normalized value: 0.056; normalized unit: mM

raw_value_unit_evidence: km raw value: 56.4 ± 10.1; raw unit: uM; kcat raw value: 0.389 ± 0.007; raw unit: s^-1; kcat_over_km raw value: 0.389 / 0.056; raw unit: s^-1 per mM after normalizing Km to row/export precision


substrate_name: tropinone

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I223L/F226L to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / I223L/F226L; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / I223L/F226L; kcat 21.8 s^-1, kcat_over_km 4.266144814090019 s^-1 mM^-1, km 5.11 mM.

normalized_value_unit_evidence: kcat normalized value: 21.8; normalized unit: s^-1; kcat_over_km normalized value: 4.266144814090019; normalized unit: s^-1 mM^-1; km normalized value: 5.11; normalized unit: mM

raw_value_unit_evidence: km raw value: 5.11 ± 0.57; raw unit: mM; kcat raw value: 21.8 ± 1.5; raw unit: s^-1; kcat_over_km raw value: 21.8 / 5.11; raw unit: s^-1 per mM after normalizing Km to row/export precision

substrate: tropinone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A160S to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / A160S; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / A160S; kcat 15.1 s^-1, kcat_over_km 86.28571428571429 s^-1 mM^-1, km 0.175 mM.

normalized_value_unit_evidence: kcat normalized value: 15.1; normalized unit: s^-1; kcat_over_km normalized value: 86.28571428571429; normalized unit: s^-1 mM^-1; km normalized value: 0.175; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.175 ± 0.055; raw unit: mM; kcat raw value: 15.1 ± 1.0; raw unit: s^-1; kcat_over_km raw value: 15.1 / 0.175; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-I / A160S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A160S/V168E to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / A160S/V168E; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / A160S/V168E; kcat 0.178 s^-1, kcat_over_km 0.01338345864661654 s^-1 mM^-1, km 13.3 mM.

normalized_value_unit_evidence: kcat normalized value: 0.178; normalized unit: s^-1; kcat_over_km normalized value: 0.01338345864661654; normalized unit: s^-1 mM^-1; km normalized value: 13.3; normalized unit: mM

raw_value_unit_evidence: km raw value: 13.3 ± 3.6; raw unit: mM; kcat raw value: 0.178 ± 0.014; raw unit: s^-1; kcat_over_km raw value: 0.178 / 13.3; raw unit: s^-1 per mM after normalizing Km to row/export precision


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H112F to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / H112F; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / H112F; kcat 5.16 s^-1, kcat_over_km 10.32 s^-1 mM^-1, km 0.5 mM.

normalized_value_unit_evidence: kcat normalized value: 5.16; normalized unit: s^-1; kcat_over_km normalized value: 10.32; normalized unit: s^-1 mM^-1; km normalized value: 0.5; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.500 ± 0.094; raw unit: mM; kcat raw value: 5.16 ± 0.43; raw unit: s^-1; kcat_over_km raw value: 5.16 / 0.5; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-I / H112F


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H112Y to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / H112Y; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / H112Y; kcat 16.4 s^-1, kcat_over_km 48.52071005917159 s^-1 mM^-1, km 0.338 mM.

normalized_value_unit_evidence: kcat normalized value: 16.4; normalized unit: s^-1; kcat_over_km normalized value: 48.52071005917159; normalized unit: s^-1 mM^-1; km normalized value: 0.338; normalized unit: mM

raw_value_unit_evidence: km raw value: 0.338 ± 0.048; raw unit: mM; kcat raw value: 16.4 ± 0.8; raw unit: s^-1; kcat_over_km raw value: 16.4 / 0.338; raw unit: s^-1 per mM after normalizing Km to row/export precision

row_label: TR-I / H112Y


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H112Y/A160S/V168E to reconstruct the assayed variant sequence.

column_label: table label: Table I (Kinetic parameters of wild-type and mutant TRs); row label: TR-I / H112Y/A160S/V168E; column label: Km, tropinone (mM); kcat (s^-1); derived kcat/Km from normalized kcat and Km cells; raw value/unit and normalized value/unit preserved per metric; Assay condition: pH 7.0 at 28 C unless noted otherwise; purified recombinant TR enzymes analyzed for affinity toward tropinone and NADPH.; captured paper segment: Table I TR-I / H112Y/A160S/V168E; kcat 0.215 s^-1, kcat_over_km 0.03577371048252912 s^-1 mM^-1, km 6.01 mM.

normalized_value_unit_evidence: kcat normalized value: 0.215; normalized unit: s^-1; kcat_over_km normalized value: 0.03577371048252912; normalized unit: s^-1 mM^-1; km normalized value: 6.01; normalized unit: mM

raw_value_unit_evidence: km raw value: 6.01 ± 1.62; raw unit: mM; kcat raw value: 0.215 ± 0.016; raw unit: s^-1; kcat_over_km raw value: 0.215 / 6.01; raw unit: s^-1 per mM after normalizing Km to row/export precision


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


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


assay_conditions_summary: pH 7; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NADPH

column_label: Table 2, row '1-Phenylisatin', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

raw_value_unit_evidence: Km 2 uM; kcat 32 min^-1; printed kcat/Km 16 min^-1 uM^-1

row_label: 1-Phenylisatin / AKR1C21* (DD1/Q91WR5)


assay_conditions_summary: pH 7; 298.15 K; buffer 0.1 M potassium phosphate; cofactor NADP+

column_label: Table 1, row '3a -Hydroxy-5a -pregnan-20-one', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

raw_value_unit_evidence: Km 1.4 uM; kcat 3.8 min^-1; printed kcat/Km 3 min^-1 uM^-1

row_label: 3a -Hydroxy-5a -pregnan-20-one / AKR1C21* (DD1/Q91WR5)


column_label: Table 1, row '3a -Hydroxy-5b -androstan-17-one', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

raw_value_unit_evidence: Km 0.5 uM; kcat 6.7 min^-1; printed kcat/Km 13 min^-1 uM^-1

row_label: 3a -Hydroxy-5b -androstan-17-one / AKR1C21* (DD1/Q91WR5)


column_label: Table 1, row '3a -Hydroxy-5b -pregnan-20-one', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

normalized_value_unit_evidence: Km 0.0004 mM; kcat 0.125 s^-1; printed kcat/Km 316.6666666666667 s^-1 mM^-1; same-row quotient 312.5 s^-1 mM^-1 retained separately

raw_value_unit_evidence: Km 0.4 uM; kcat 7.5 min^-1; printed kcat/Km 19 min^-1 uM^-1

row_label: 3a -Hydroxy-5b -pregnan-20-one / AKR1C21* (DD1/Q91WR5)


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA; Km (uM) = 0.4; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA; kcat (min^-1) = 5.4; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA; kcat/Km (min^-1 uM^-1) = 13

raw_value_unit_evidence: Km (uM) 0.4 uM for AKR1C21 (DD3) / DHEA; kcat (min^-1) 5.4 min^-1 for AKR1C21 (DD3) / DHEA; kcat/Km (min^-1 uM^-1) 13 min^-1 uM^-1 for AKR1C21 (DD3) / DHEA

row_label: AKR1C21 (DD3) / DHEA


column_label: J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA 3-sulfate; Km (uM) = 0.4; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA 3-sulfate; kcat (min^-1) = 4.8; J-STAGE PDF page 1942 Table 2; AKR1C21 (DD3); DHEA 3-sulfate; kcat/Km (min^-1 uM^-1) = 12

normalized_value_unit_evidence: normalized km=0.0004 mM; export km=0.0004 mM; normalized kcat=0.08 s^-1; export kcat=0.08 s^-1; normalized kcat_over_km=200 s^-1 mM^-1; export kcat_over_km=200.0 s^-1 mM^-1

raw_value_unit_evidence: Km (uM) 0.4 uM for AKR1C21 (DD3) / DHEA 3-sulfate; kcat (min^-1) 4.8 min^-1 for AKR1C21 (DD3) / DHEA 3-sulfate; kcat/Km (min^-1 uM^-1) 12 min^-1 uM^-1 for AKR1C21 (DD3) / DHEA 3-sulfate

row_label: AKR1C21 (DD3) / DHEA 3-sulfate


column_label: Table 2, row 'Dehydrolithocholic acid', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

raw_value_unit_evidence: Km 0.7 uM; kcat 10 min^-1; printed kcat/Km 14 min^-1 uM^-1

row_label: Dehydrolithocholic acid / AKR1C21* (DD1/Q91WR5)


column_label: Table 2, row '3a -Hydroxyandrost-4-en-17-one', AKR1C21* (DD1/Q91WR5) primary columns Km, kcat, and printed kcat/Km; rendered PDF page 1942.

normalized_value_unit_evidence: Km 0.0005 mM; kcat 0.02 s^-1; printed kcat/Km 33.333333333333336 s^-1 mM^-1; same-row quotient 40.0 s^-1 mM^-1 retained separately

raw_value_unit_evidence: Km 0.5 uM; kcat 1.2 min^-1; printed kcat/Km 2 min^-1 uM^-1

row_label: 3a -Hydroxyandrost-4-en-17-one / AKR1C21* (DD1/Q91WR5)


substrate_name: lithocholic acid

substrate: lithocholic acid


organism: Hyoscyamus niger

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row 4-Methylcyclohexanone, TR-I Km column; Km cell 12 uM, normalized 0.012 mM.

raw_value_unit_evidence: Km raw 12 uM from Table I row 4-Methylcyclohexanone, TR-I Km column

row_label: TR-I / 4-Methylcyclohexanone

source: brenda


column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row 4-Ethylcyclohexanone, TR-I Km column; Km cell 30 uM, normalized 0.03 mM.

normalized_value_unit_evidence: Km 0.03 mM

raw_value_unit_evidence: Km raw 30 uM from Table I row 4-Ethylcyclohexanone, TR-I Km column

row_label: TR-I / 4-Ethylcyclohexanone


column_label: Table I. Km and Relative Vmax for Tropinone and Other Substrates, row TBON, TR-I Km column; Km cell 33 uM, normalized 0.033 mM.

raw_value_unit_evidence: Km raw 33 uM from Table I row TBON, TR-I Km column

row_label: TR-I / TBON


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


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


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


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


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

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D255G 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 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.


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.


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.

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.


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


substrate_name: IMP

substrate: IMP


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


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

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_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor 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: IMP

substrate: IMP


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


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


substrate_name: NAD+

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

substrate: NAD+


enzyme_display_name: UniProt P0C0H6

organism: Streptococcus pyogenes

enzyme: UniProt P0C0H6


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


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

proof_lines: IMP NAD+ IMPDH


enzyme_display_name: UniProt P12268

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


organism: Homo sapiens

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


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


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


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+

assay_conditions_summary: cofactor 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