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


organism: Rattus norvegicus

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

status: unverified

source: oed


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

mutation_type: substitution


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


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


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


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


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


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


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


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


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


organism: Homo sapiens


verification_status: verified

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

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

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

row_label: 2-Nitrobenzaldehyde / DD2

table_label: Table 3. Substrate specificity for carbonyl compounds

status: verified


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

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

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


substrate_name: Benzene dihydrodiol

substrate: Benzene dihydrodiol


substrate_name: Camphorquinone

kcat_over_km_display: Not reported

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

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

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

row_label: DD2 | Camphorquinone

substrate: Camphorquinone


substrate_name: Dimethylglyoxal

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

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

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

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

row_label: DD2 | Butane-2,3-dione

substrate: Dimethylglyoxal


substrate_name: m-Nitrobenzaldehyde

substrate: m-Nitrobenzaldehyde


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

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

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

row_label: DD2 | Pyridine-3-aldehyde


substrate_name: menadione

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

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

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

row_label: DD2 | Menadione

substrate: menadione


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


substrate_name: NAD+

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: p-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

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

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

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

row_label: AKR1C3 | 1-Acenaphthenol


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

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

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

row_label: AKR1C2 | 1-Acenaphthenol


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

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

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

row_label: AKR1C1 | 1-Acenaphthenol


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

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

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

row_label: AKR1C4 | Benzenedihydrodiol


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

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

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

row_label: AKR1C3 | Benzenedihydrodiol


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

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

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

row_label: AKR1C1 | Benzenedihydrodiol


enzyme_display_name: Farnesol dehydrogenase

organism: Aedes aegypti

substrate_name: (E,E) farnesol

source_db: uniprot

kcat_display: Not reported

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

enzyme: Farnesol dehydrogenase

substrate: (E,E) farnesol

source: uniprot


smiles: CCCCCCCCC(C)O

assay_conditions_summary: pH 10; buffer Stauffer; cofactor NADP+

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

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

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


substrate_name: geraniol (E)

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

substrate: geraniol (E)


substrate_name: citronellol

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

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

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

row_label: Citronellol

substrate: citronellol


substrate_name: octanol

smiles: CCCCCCCCO

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

raw_value_unit_evidence: KM raw_value=195 raw_unit=uM

row_label: Octanol

substrate: octanol


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

organism: Malus domestica

substrate_name: eriodictyol

assay_conditions_summary: cofactor NADPH

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

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

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

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

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

substrate: eriodictyol


substrate_name: dihydrokaempferol

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

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

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

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

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

substrate: dihydrokaempferol


substrate_name: dihydroquercetin

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

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

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

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

substrate: dihydroquercetin


substrate_name: testosterone

substrate: testosterone


source_db: brenda

sequence: MDSKYQCVK

wild_type_sequence: MDSKYQCVK

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

source: brenda


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


verification_status: corrected

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C2 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C2 (R): Km 26.0 uM; kcat 0.23 min^-1; kcat/Km 9 min^-1 mM^-1.

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

status: corrected


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C2; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C2: Km 6.26 uM; kcat 1.39 min^-1; kcat/Km 222 min^-1 mM^-1.


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

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

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


proof_lines: transformation of androstenedione into testosterone


enzyme_display_name: morphine 6-dehydrogenase

organism: Oryctolagus cuniculus

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

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

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

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

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

row_label: NAD+ / AKR1C26

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

enzyme: morphine 6-dehydrogenase


assay_conditions_summary: pH 7.4; buffer pH 7; cofactor NADH

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

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

row_label: NADH / AKR1C26

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


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

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

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

table_label: Results prose (page 7, right column)


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

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

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


substrate_name: codeine

assay_conditions_summary: cofactor NAD+

substrate: codeine


organism: Pyrus communis

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

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

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

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


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

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

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

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


enzyme_display_name: Aldo-keto reductase family 1 member C15

substrate_name: geranylgeranial

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

enzyme: Aldo-keto reductase family 1 member C15

substrate: geranylgeranial


enzyme_display_name: gluconate 2-dehydrogenase

organism: Gluconobacter oxydans

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

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

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

table_label: Springer Table 1

enzyme: gluconate 2-dehydrogenase


enzyme_display_name: flavanone 4-reductase

organism: Sinningia cardinalis

enzyme: flavanone 4-reductase


substrate_name: Prostaglandin E2; NAD+

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

sequence_source: multiple

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

unit: lgwedgeoneswedgeone

substrate: Prostaglandin E2; NAD+


substrate_name: NAD+; Prostaglandin E2

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+

substrate: NAD+; Prostaglandin E2


organism: Mus musculus

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


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


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


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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

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

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

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

row_label: Table 2, PGE2 block, row V186I

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


enzyme_display_name: Geraniol dehydrogenase

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

substrate_name: Unknown

km_display: Not reported

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

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

enzyme: Geraniol dehydrogenase

substrate: Unknown


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

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


substrate_name: NAD+; Pregnenolone

substrate: NAD+; Pregnenolone


enzyme_display_name: steroid Delta-isomerase

organism: Sus scrofa

substrate_name: NAD+; 7alpha-Hydroxycholesterol

enzyme: steroid Delta-isomerase

substrate: NAD+; 7alpha-Hydroxycholesterol


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

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


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

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


ki_unit: mM

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

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


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

proof_lines:
mutant H156Y, pH 7.4, 27°C
27°C, pH 7.4, H156Y mutant


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


organism: Mycobacterium tuberculosis


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


enzyme_display_name: 11beta-hydroxysteroid dehydrogenase

substrate_name: NAD+; Cortisol

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

assay_conditions_summary: pH 7.4; cofactor NAD+

source_databases_merged: sabio_rk skid uniprot

enzyme: 11beta-hydroxysteroid dehydrogenase

substrate: NAD+; Cortisol


organism: Cavia porcellus

substrate_name: H+; Cortisone; NADPH

substrate: H+; Cortisone; NADPH


organism: Mesocricetus auratus

substrate_name: 7alpha-Hydroxycholesterol; NADP+

assay_conditions_summary: cofactor NADP+

substrate: 7alpha-Hydroxycholesterol; NADP+


substrate_name: NADP+; Corticosterone

substrate: NADP+; Corticosterone


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

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

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

row_label: Recombinant protein / 7beta-hydroxycholesterol / Oxidation

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

enzyme: 11-beta-hydroxysteroid dehydrogenase 1


organism: Saimiri sciureus


enzyme_display_name: 20alpha-hydroxysteroid dehydrogenase

organism: Tetrahymena pyriformis

substrate_name: 17alpha-Hydroxyprogesterone; NADPH; H+

sequence: LAKTVPLNDGTNFPIFGG

wild_type_sequence: LAKTVPLNDGTNFPIFGG

enzyme: 20alpha-hydroxysteroid dehydrogenase

substrate: 17alpha-Hydroxyprogesterone; NADPH; H+


substrate_name: Progesterone; H+; NADPH

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

proof_lines: pH 6.5, temperature not specified in the publication

source_databases_merged: sabio_rk brenda uniprot

substrate: Progesterone; H+; NADPH


substrate_name: NADPH; H+; Progesterone

substrate: NADPH; H+; Progesterone


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


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

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


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

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

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

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


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

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

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


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

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


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

assay_conditions_summary: pH 7.4; buffer 0.1 M potassium phosphate

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

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


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

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

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


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

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

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


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

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


enzyme_display_name: sepiapterin reductase

substrate_name: NADPH; Sepiapterin; H+

enzyme: sepiapterin reductase

substrate: NADPH; Sepiapterin; H+


substrate_name: H+; Sepiapterin; NADPH

substrate: H+; Sepiapterin; NADPH


substrate_name: Sepiapterin; NADPH; H+

substrate: Sepiapterin; NADPH; H+


enzyme_display_name: Sepiapterin reductase

organism: Dictyostelium discoideum

enzyme: Sepiapterin reductase


enzyme_display_name: glycerol 2-dehydrogenase (NADP+)

organism: Trichoderma reesei

substrate_name: L-Glyceraldehyde; NADPH; H+

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

enzyme: glycerol 2-dehydrogenase (NADP+)

substrate: L-Glyceraldehyde; NADPH; H+


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

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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


enzyme_display_name: 3-hydroxybutyryl-CoA dehydrogenase

organism: Clostridium acetobutylicum

assay_conditions_summary: pH 7.5; cofactor CoA

enzyme: 3-hydroxybutyryl-CoA dehydrogenase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


enzyme_display_name: 7alpha-hydroxysteroid dehydrogenase

organism: Bacteroides fragilis

enzyme: 7alpha-hydroxysteroid dehydrogenase


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Homo sapiens

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

assay_conditions_summary: pH 9.3; cofactor CoA

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

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


enzyme_display_name: erythrulose reductase

organism: Gallus gallus

substrate_name: NADPH; D-Erythrulose; H+

enzyme: erythrulose reductase

substrate: NADPH; D-Erythrulose; H+


enzyme_display_name: 2-dehydropantoate 2-reductase

organism: Escherichia coli

substrate_name: 2-Dehydropantoate; H+; NADPH

enzyme: 2-dehydropantoate 2-reductase

substrate: 2-Dehydropantoate; H+; NADPH


organism: Thermococcus kodakarensis

substrate_name: D-pantoate

assay_conditions_summary: pH 6.4; 343.15 K; cofactor NADPH

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

source_databases_merged: brenda uniprot

substrate: D-pantoate


enzyme_display_name: UniProt A0A0J9X283

organism: Staphylococcus aureus

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt A0A0J9X283

source: skid


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

substrate_name: Unknown

substrate: Unknown


organism: Rattus norvegicus

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

assay_conditions_summary: cofactor NADH


substrate_name: NSDHL; NADH

substrate: NSDHL; NADH


organism: Saccharomyces cerevisiae

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

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


enzyme_display_name: D-xylose 1-dehydrogenase

organism: Arthrobacter nicotinovorans

substrate_name: NAD+; D-Xylose

enzyme: D-xylose 1-dehydrogenase

substrate: NAD+; D-Xylose


organism: Caulobacter vibrioides

substrate_name: D-Xylose; NAD+

substrate: D-Xylose; NAD+


enzyme_display_name: 12alpha-hydroxysteroid dehydrogenase

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

enzyme: 12alpha-hydroxysteroid dehydrogenase


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


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

organism: Sus scrofa

substrate_name: D-Xylose; NADP+

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

substrate: D-Xylose; NADP+


organism: Macaca fuscata

substrate_name: NADP+; D-Xylose

substrate: NADP+; D-Xylose


organism: Canis familiaris


organism: Oryctolagus cuniculus


organism: Trichoderma reesei


organism: Halobacterium volcanii


enzyme_display_name: geraniol dehydrogenase

organism: Ocimum basilicum

substrate_name: NADP+; Geraniol

enzyme: geraniol dehydrogenase

substrate: NADP+; Geraniol


enzyme_display_name: carbonyl reductase (NADPH)

substrate_name: 4-Nitroacetophenone; NADPH

enzyme: carbonyl reductase (NADPH)

substrate: 4-Nitroacetophenone; NADPH


organism: Homo sapiens

substrate_name: Menadione; NADPH; H+

assay_conditions_summary: pH 8.4; 298.15 K; cofactor NADPH

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

source_databases_merged: sabio_rk brenda skid

substrate: Menadione; NADPH; H+


organism: Candida magnoliae

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

assay_conditions_summary: cofactor NADPH


substrate_name: NADPH; H+; Menadione

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

substrate: NADPH; H+; Menadione


organism: Mus musculus

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

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


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

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


substrate_name: NADPH; S-Nitrosoglutathione; H+

substrate: NADPH; S-Nitrosoglutathione; H+


organism: Caenorhabditis elegans

substrate_name: NADPH; H+; Isatin

substrate: NADPH; H+; Isatin


organism: Mesocricetus auratus

substrate_name: Acetone; H+; NADH

substrate: Acetone; H+; NADH


enzyme_display_name: UniProt Q28960

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

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

source_databases_merged: skid uniprot

enzyme: UniProt Q28960


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

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

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

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

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


substrate_name: Unknown

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

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: Unknown


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

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

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


enzyme_display_name: prostaglandin-F synthase

organism: Bos taurus

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

proof_lines: prostaglandin D2 11-ketoreductase activity

enzyme: prostaglandin-F synthase

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


assay_conditions_summary: pH 7; buffer pH 7; cofactor NADPH

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

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

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

row_label: AKR1C1 / PQ

table_label: Table 1


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

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

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


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

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

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

row_label: AKR1C2 / PQ


substrate_name: Prostaglandin H2; H+; NADPH

substrate: Prostaglandin H2; H+; NADPH


substrate_name: NADPH; H+; Prostaglandin H2

substrate: NADPH; H+; Prostaglandin H2


organism: Trypanosoma brucei


substrate_name: prostaglandin PGH2

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

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

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

substrate: prostaglandin PGH2


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

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


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

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


substrate_name: prostaglandin PGD2

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

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

substrate: prostaglandin PGD2


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

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


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

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


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


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


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


enzyme_display_name: prostaglandin-E2 9-reductase

enzyme: prostaglandin-E2 9-reductase


enzyme_display_name: Carbonyl reductase [NADPH] 1

substrate_name: 9,1 O-phenanthrene-quinone

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

enzyme: Carbonyl reductase [NADPH] 1

substrate: 9,1 O-phenanthrene-quinone


organism: Escherichia coli


enzyme_display_name: Riboflavin biosynthesis protein PYRR, chloroplastic

organism: Zea mays

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


enzyme_display_name: cinnamyl-alcohol dehydrogenase

organism: Oryza sativa

substrate_name: H+; NADPH; Coniferaldehyde

assay_conditions_summary: pH 6.3; 303.15 K; cofactor NADPH

enzyme: cinnamyl-alcohol dehydrogenase

substrate: H+; NADPH; Coniferaldehyde


organism: Populus tremuloides

substrate_name: Sinapoyl aldehyde; H+; NADPH

substrate: Sinapoyl aldehyde; H+; NADPH


substrate_name: NADP+; Geraniol

substrate: NADP+; Geraniol


organism: Arabidopsis thaliana

substrate_name: H+; NADPH; 4-Hydroxycinnamyl aldehyde

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

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

substrate: H+; NADPH; 4-Hydroxycinnamyl aldehyde


substrate_name: NADPH; 4-Hydroxycinnamyl aldehyde; H+

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

substrate: NADPH; 4-Hydroxycinnamyl aldehyde; H+


substrate_name: H+; Sinapoyl aldehyde; NADPH

assay_conditions_summary: pH 6.25; buffer pH 6; cofactor NADPH

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

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

substrate: H+; Sinapoyl aldehyde; NADPH


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

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


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

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


substrate_name: NADPH; H+; Sinapoyl aldehyde

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

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

substrate: NADPH; H+; Sinapoyl aldehyde


substrate_name: NADPH; H+; Coniferaldehyde

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

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

substrate: NADPH; H+; Coniferaldehyde


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

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


organism: Oryza sativa Japonica Group

substrate_name: 4-coumaryl aldehyde

substrate: 4-coumaryl aldehyde


organism: Sorghum bicolor

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

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


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

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


enzyme_display_name: UniProt C5XC49

enzyme: UniProt C5XC49


enzyme_display_name: Cinnamyl alcohol dehydrogenase 1

organism: Medicago truncatula

substrate_name: Unknown

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

enzyme: Cinnamyl alcohol dehydrogenase 1

substrate: Unknown


organism: Sus scrofa


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

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

table_label: Table I


enzyme_display_name: aldose-6-phosphate reductase (NADPH)

organism: Malus domestica

assay_conditions_summary: pH 9

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

enzyme: aldose-6-phosphate reductase (NADPH)


organism: Prunus persica


organism: Clostridium sardiniense


organism: Collinsella aerofaciens

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


enzyme_display_name: 11-beta-hydroxysteroid dehydrogenase 1

organism: Homo sapiens

enzyme: 11-beta-hydroxysteroid dehydrogenase 1


organism: Mus musculus


organism: Rattus norvegicus


organism: Mesocricetus auratus


organism: Saimiri sciureus


enzyme_display_name: 7beta-hydroxysteroid dehydrogenase

organism: Mediterraneibacter gnavus

assay_conditions_summary: pH 6

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

enzyme: 7beta-hydroxysteroid dehydrogenase


enzyme_display_name: 1,3-propanediol dehydrogenase

organism: Clostridium butyricum

substrate_name: NAD+; 1,3-Propanediol

assay_conditions_summary: cofactor NAD+

enzyme: 1,3-propanediol dehydrogenase

substrate: NAD+; 1,3-Propanediol


enzyme_display_name: Uronate dehydrogenase

organism: Agrobacterium fabrum (strain C58 / ATCC 33970)

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

enzyme: Uronate dehydrogenase


enzyme_display_name: IMP dehydrogenase

substrate_name: H2O; NAD+; IMP

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

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

enzyme: IMP dehydrogenase

substrate: H2O; NAD+; IMP


organism: Streptococcus pyogenes

substrate_name: IMP; NAD+; H2O

substrate: IMP; NAD+; H2O


organism: Saccharomyces cerevisiae

substrate_name: NAD+; IMP; H2O

substrate: NAD+; IMP; H2O


substrate_name: H2O; IMP; NAD+

substrate: H2O; IMP; NAD+


organism: Tritrichomonas foetus


organism: Leishmania donovani


organism: Toxoplasma gondii


organism: Cryptosporidium parvum


organism: Candida albicans


organism: Borrelia burgdorferi

substrate_name: IMP; H2O; NAD+

substrate: IMP; H2O; NAD+


organism: Escherichia coli


organism: Pneumocystis carinii


organism: Vigna unguiculata


organism: Homo sapiens


organism: Eremothecium gossypii


organism: Babesia gibsoni


organism: Tritrichomonas suis

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


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


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


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


enzyme_display_name: tropinone reductase I

organism: Cochlearia officinalis

substrate_name: H+; NADPH; Tropinone

enzyme: tropinone reductase I

substrate: H+; NADPH; Tropinone


organism: Datura stramonium

substrate_name: NADPH; Tropinone

substrate: NADPH; Tropinone


organism: Mus musculus

substrate_name: NADP+; Pregnanediol

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

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

substrate: NADP+; Pregnanediol


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


enzyme_display_name: Aldo-keto reductase family 1 member C2

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

enzyme: Aldo-keto reductase family 1 member C2


enzyme_display_name: Aldo-keto reductase family 1 member C1

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

enzyme: Aldo-keto reductase family 1 member C1


enzyme_display_name: Retinol dehydrogenase 16

substrate_name: CRBP-all-trans-retinol

enzyme: Retinol dehydrogenase 16

substrate: CRBP-all-trans-retinol


enzyme_display_name: Aldo-keto reductase family 1 member C4

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

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: NADH tested with dihydrotestosterone

substrate: NADH tested with dihydrotestosterone


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

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


organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


enzyme_display_name: Retinol dehydrogenase 5

organism: Bos taurus

enzyme: Retinol dehydrogenase 5


organism: Macaca fuscata fuscata

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


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

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


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3


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


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

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


assay_conditions_summary: cofactor NADP+


substrate_name: Acenaphthen-1-ol; NADP+

substrate: Acenaphthen-1-ol; NADP+


assay_conditions_summary: pH 7

proof_lines: recombinant enzyme in intact COS-1 cells

proof_lines: pH 7.0, temperature not specified in the publication


enzyme_display_name: gluconate 2-dehydrogenase

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

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

enzyme: gluconate 2-dehydrogenase

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


organism: Gluconobacter oxydans


enzyme_display_name: Aldo-keto reductase family 1 member B15

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

assay_conditions_summary: cofactor CoA

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

enzyme: Aldo-keto reductase family 1 member B15


enzyme_display_name: Aldo-keto reductase family 1 member C15

enzyme: Aldo-keto reductase family 1 member C15


enzyme_display_name: morphine 6-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: trans-naphthalene dihydrodiol

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

proof_lines:
pH 7.4, 25°C
cosubstrate NAD+

enzyme: morphine 6-dehydrogenase

substrate: trans-naphthalene dihydrodiol


enzyme_display_name: dihydroflavonol 4-reductase

organism: Delphinium cardinale

substrate_name: dihydromyricetin

enzyme: dihydroflavonol 4-reductase

substrate: dihydromyricetin


substrate_name: dihydroquercetin

substrate: dihydroquercetin


substrate_name: dihydrokaempferol

substrate: dihydrokaempferol


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

organism: Pyrus communis

substrate_name: Unknown

substrate: Unknown


organism: Malus domestica

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


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


substrate_name: Phenanthrene quinone

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

substrate: Phenanthrene quinone


substrate_name: NADP+

substrate: NADP+


substrate_name: menadione

substrate: menadione


organism: [Clostridium] innocuum


substrate_name: 3-Ketoglycyrrhetic acid

substrate: 3-Ketoglycyrrhetic acid


substrate_name: NADPH

substrate: NADPH


organism: Torulaspora delbrueckii

substrate_name: Diethyl 2-methyl-3-oxosuccinate

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

substrate: Diethyl 2-methyl-3-oxosuccinate


substrate_name: Diethyl 2-methyl-3-hydroxysuccinate

substrate: Diethyl 2-methyl-3-hydroxysuccinate


substrate_name: prostaglandin I2

substrate: prostaglandin I2


enzyme_display_name: 8-oxocoformycin reductase

organism: Streptomyces antibioticus

enzyme: 8-oxocoformycin reductase


enzyme_display_name: tropinone reductase II

organism: Hyoscyamus niger

substrate_name: NADH

enzyme: tropinone reductase II

substrate: NADH


enzyme_display_name: hydroxyphenylpyruvate reductase

organism: Arabidopsis thaliana

substrate_name: phenylpyruvate

enzyme: hydroxyphenylpyruvate reductase

substrate: phenylpyruvate


organism: Wickerhamia fluorescens

substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


substrate_name: glyoxylate

substrate: glyoxylate


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH


substrate_name: hydroxyphenylpyruvate

substrate: hydroxyphenylpyruvate


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH


organism: Coleus scutellarioides


assay_conditions_summary: pH 7; cofactor NADPH


assay_conditions_summary: pH 7; cofactor NADH


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


organism: Alcaligenes sp.


substrate_name: testosterone

substrate: testosterone


substrate_name: NAD+

substrate: NAD+


organism: Ilyonectria destructans

assay_conditions_summary: pH 7; cofactor NAD+

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


assay_conditions_summary: pH 10

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


substrate_name: androstendione

substrate: androstendione


organism: Streptomyces exfoliatus


enzyme_display_name: 12beta-hydroxysteroid dehydrogenase

organism: Clostridium paraputrificum

enzyme: 12beta-hydroxysteroid dehydrogenase


assay_conditions_summary: cofactor NADPH


organism: Solanum tuberosum

substrate_name: Nortropinone

substrate: Nortropinone


substrate_name: tropinone

substrate: tropinone


enzyme_display_name: N-acetylhexosamine 1-dehydrogenase

organism: Pseudomonas sp.

substrate_name: N-acetyl-D-glucosamine

enzyme: N-acetylhexosamine 1-dehydrogenase

substrate: N-acetyl-D-glucosamine


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


organism: Przewalskia tangutica

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


organism: Brugmansia x candida


organism: Datura stramonium

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


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


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


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


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


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


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


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


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


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


enzyme_display_name: carveol dehydrogenase

organism: Rhodococcus erythropolis

enzyme: carveol dehydrogenase


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Homo sapiens

substrate_name: NAD

substrate: NAD


assay_conditions_summary: cofactor NADH


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

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

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

substrate: allopregnanolone


substrate_name: androsterone

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

row_label: ADT / NAD+ / 5alpha-Dione

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

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

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

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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

assay_conditions_summary: pH 9.3; cofactor CoA


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


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


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


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


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


organism: Rattus norvegicus


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


substrate_name: prostaglandin E1

substrate: prostaglandin E1


substrate_name: prostaglandin A1

substrate: prostaglandin A1


substrate_name: prostaglandin A2

substrate: prostaglandin A2


substrate_name: NAD in the presence of prostaglandin E1

substrate: NAD in the presence of prostaglandin E1


organism: Mentha piperita

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

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

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


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

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


assay_conditions_summary: pH 7.5; cofactor NAD+


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


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


enzyme_display_name: N-acylmannosamine 1-dehydrogenase

organism: Flavobacterium sp.

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

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

enzyme: N-acylmannosamine 1-dehydrogenase

substrate: NAD+


substrate_name: N-acetyl-D-mannosamine

substrate: N-acetyl-D-mannosamine


enzyme_display_name: Aldo-keto reductase family 1 member C3


substrate_name: progesterone

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


substrate_name: tetramyristoyl cardiolipin

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


substrate_name: prostaglandin H2

substrate: prostaglandin H2


substrate_name: prostaglandin E2

substrate: prostaglandin E2


organism: Mesocricetus auratus

substrate_name: NADH

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

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

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

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

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

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

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

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

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

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

row_label: AKR1C34 | NADP+

table_label: Table I. Kinetic constants for coenzymes

substrate: NADP+


substrate_name: nerol

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

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

substrate: nerol


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

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

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

row_label: R-Tetralol | AKR1C35

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


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

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

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

row_label: S-Tetralol | AKR1C35


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

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

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

row_label: S-1-Indanol | AKR1C35


substrate_name: trans-benzene dihydrodiol

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

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

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

row_label: trans-Benzene dihydrodiol | AKR1C35

substrate: trans-benzene dihydrodiol


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

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

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

row_label: 1-Acenaphthenol / AKR1C35

table_label: Table II


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

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

row_label: 2-Cyclohexen-1-ol / AKR1C35


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

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

row_label: beta-3-Hydroxyhexobarbital / AKR1C35


substrate_name: beta-ionol

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

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

row_label: beta-Ionol / AKR1C35

substrate: beta-ionol


substrate_name: cis-benzene dihydrodiol

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

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

row_label: cis-Benzene dihydrodiol / AKR1C35

substrate: cis-benzene dihydrodiol


substrate_name: farnesol

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

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

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

row_label: Farnesol / AKR1C35

substrate: farnesol


substrate_name: geraniol

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

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

row_label: Geraniol / AKR1C35

substrate: geraniol


substrate_name: geranylgeraniol

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

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

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

row_label: Geranylgeraniol / AKR1C35

substrate: geranylgeraniol


substrate_name: NAD+

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

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

row_label: NAD+ / AKR1C34

substrate: NAD+


organism: Hyoscyamus niger

substrate_name: NADPH

substrate: NADPH


substrate_name: tropinone

substrate: tropinone


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

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

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

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

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


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

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

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

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

row_label: TR-II / S148A


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

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

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

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


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

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

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

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