column_label: Table label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids. Row: 3,4-Didehydroretinol. Column group: ADH1B2. Cells: Km 24 ± 5 uM; kcat 5.3 ± 0.4 min^-1; kcat/Km 220 ± 50 mM^-1 min^-1. metric: kcat; raw value: 5.3 ± 0.4; raw unit: min^-1; normalized value: 0.088 s^(-1); metric: Km; raw value: 24 ± 5; raw unit: uM; normalized value: 0.024 mM; metric: kcat/Km; raw value: 220 ± 50; raw unit: mM^-1 min^-1; normalized value: 3.6666666666666665 s^-1 mM^-1; assay condition: 0.1 M sodium phosphate pH 7.5, 0.02% Tween 80, 2.4 mM NAD+, 25 C.

normalized_value_unit_evidence: metric: kcat; raw value: 5.3 ± 0.4; raw unit: min^-1; normalized value: 0.088 s^(-1); metric: Km; raw value: 24 ± 5; raw unit: uM; normalized value: 0.024 mM; metric: kcat/Km; raw value: 220 ± 50; raw unit: mM^-1 min^-1; normalized value: 3.6666666666666665 s^-1 mM^-1; The kcat normalization is stated at the export's stored precision; the independently printed efficiency converts exactly to the current stored efficiency.

raw_value_unit_evidence: Table 1 row 3,4-Didehydroretinol, ADH1B2 column: Km 24 ± 5 uM; kcat 5.3 ± 0.4 min^-1; kcat/Km 220 ± 50 mM^-1 min^-1.

row_label: 3,4-Didehydroretinol | ADH1B2


enzyme_display_name: alcohol dehydrogenase

organism: Homo sapiens

substrate_name: NADP+

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.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

data_origin: experimental

enzyme: alcohol dehydrogenase

substrate: NADP+

status: unverified

source: oed


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

substrate: NAD+


verification_status: corrected

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Human ADH1B2. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 16 +/- 4, kcat (min^-1) cell 3.4 +/- 0.1, kcat/Km (mM^-1 min^-1) cell 215 +/- 55. metric: Km; raw value: 16 +/- 4; raw unit: uM; normalized value: 0.016 mM; metric: kcat; raw value: 3.4 +/- 0.1; raw unit: min^-1; normalized value: 0.057 s^(-1); metric: kcat/Km; raw value: 215 +/- 55; raw unit: mM^-1 min^-1; normalized value: 3.5833333333333335 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 16 +/- 4 uM in the Human ADH1B2 column; 16 uM / 1000 = 0.016 mM, which is the catalog km exactly. kcat: printed cell 3.4 +/- 0.1 min^-1 in the Human ADH1B2 column; 3.4 min^-1 / 60 = 0.056666666666666664 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.057 s^-1, so the paper kcat field carries the catalog value 0.057 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 215 +/- 55 mM^-1 min^-1 in the Human ADH1B2 column; 215 mM^-1 min^-1 / 60 = 3.5833333333333335 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 3.5625 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.057 / 0.016). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 3.4 min^-1 / 0.016 mM = 212.5 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinal | Km (uM) | 15 +/- 3 | 16 +/- 4 | 21 +/- 3 | 26 +/- 7 | 28 +/- 3 | | kcat row: | 11-cis-retinal | kcat (min^-1) | 0.31 +/- 0.02 | 3.4 +/- 0.1 | 18 +/- 2 | 7.4 +/- 0.5 | 34 +/- 1 | | kcat/Km row: | 11-cis-retinal | kcat/Km (mM^-1 min^-1) | 21 +/- 4 | 215 +/- 55 | 860 +/- 155 | 285 +/- 80 | 1215 +/- 135 | | Human ADH1B2 column cells read: Km = 16 +/- 4 uM; kcat = 3.4 +/- 0.1 min^-1; kcat/Km = 215 +/- 55 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Human ADH1B2 | 11-cis-retinal

status: corrected


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 11-cis-retinol. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 28 +/- 5, kcat (min^-1) cell 190 +/- 20, kcat/Km (mM^-1 min^-1) cell 6790 +/- 1400. metric: Km; raw value: 28 +/- 5; raw unit: uM; normalized value: 0.028 mM; metric: kcat; raw value: 190 +/- 20; raw unit: min^-1; normalized value: 3.167 s^(-1); metric: kcat/Km; raw value: 6790 +/- 1400; raw unit: mM^-1 min^-1; normalized value: 113.16666666666667 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 28 +/- 5 uM in the Human ADH4 column; 28 uM / 1000 = 0.028 mM, which is the catalog km exactly. kcat: printed cell 190 +/- 20 min^-1 in the Human ADH4 column; 190 min^-1 / 60 = 3.1666666666666665 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 3.167 s^-1, so the paper kcat field carries the catalog value 3.167 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 6790 +/- 1400 mM^-1 min^-1 in the Human ADH4 column; 6790 mM^-1 min^-1 / 60 = 113.16666666666667 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 113.10714285714285 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (3.167 / 0.028). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 190 min^-1 / 0.028 mM = 6785.714285714285 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinol | Km (uM) | 35 +/- 7 | 18 +/- 4 | 28 +/- 5 | 34 +/- 9 | 23 +/- 6 | | kcat row: | 11-cis-retinol | kcat (min^-1) | 0.85 +/- 0.04 | 9.5 +/- 1.0 | 190 +/- 20 | 25 +/- 2 | 225 +/- 5 | | kcat/Km row: | 11-cis-retinol | kcat/Km (mM^-1 min^-1) | 24 +/- 5 | 530 +/- 55 | 6790 +/- 1400 | 735 +/- 205 | 9740 +/- 2550 | | Human ADH4 column cells read: Km = 28 +/- 5 uM; kcat = 190 +/- 20 min^-1; kcat/Km = 6790 +/- 1400 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Human ADH4 | 11-cis-retinol


sequence_source: UniProtKB:P00325 REST direct check on 2026-05-31; accession matched Homo sapiens human ADH1B

column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 9-cis-retinol. Enzyme column: Human ADH1B2. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 23 +/- 5, kcat (min^-1) cell 3.6 +/- 0.4, kcat/Km (mM^-1 min^-1) cell 160 +/- 40. metric: Km; raw value: 23 +/- 5; raw unit: uM; normalized value: 0.023 mM; metric: kcat; raw value: 3.6 +/- 0.4; raw unit: min^-1; normalized value: 0.06 s^(-1); metric: kcat/Km; raw value: 160 +/- 40; raw unit: mM^-1 min^-1; normalized value: 2.6666666666666665 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 23 +/- 5 uM in the Human ADH1B2 column; 23 uM / 1000 = 0.023 mM, which is the catalog km exactly. kcat: printed cell 3.6 +/- 0.4 min^-1 in the Human ADH1B2 column; 3.6 min^-1 / 60 = 0.06 s^-1, an exact terminating conversion, which is the catalog kcat exactly. kcat/Km: the paper prints an independent catalytic-efficiency cell 160 +/- 40 mM^-1 min^-1 in the Human ADH1B2 column; 160 mM^-1 min^-1 / 60 = 2.6666666666666665 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 2.608695652173913 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.06 / 0.023). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 3.6 min^-1 / 0.023 mM = 156.52173913043478 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 9-cis-retinol | Km (uM) | 11 +/- 3 | 23 +/- 5 | 36 +/- 4 | 8 +/- 1.1 | 21 +/- 3 | | kcat row: | 9-cis-retinol | kcat (min^-1) | 0.89 +/- 0.06 | 3.6 +/- 0.4 | 475 +/- 44 | 23 +/- 1 | 340 +/- 15 | | kcat/Km row: | 9-cis-retinol | kcat/Km (mM^-1 min^-1) | 81 +/- 23 | 160 +/- 40 | 13200 +/- 2020 | 2900 +/- 455 | 16100 +/- 2400 | | Human ADH1B2 column cells read: Km = 23 +/- 5 uM; kcat = 3.6 +/- 0.4 min^-1; kcat/Km = 160 +/- 40 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Human ADH1B2 | 9-cis-retinol


sequence_source: UniProtKB:P08319 REST direct check on 2026-05-31; accession matched Homo sapiens human ADH4

column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 7-cis-retinal. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 8 +/- 2, kcat (min^-1) cell 80 +/- 5, kcat/Km (mM^-1 min^-1) cell 10000 +/- 2610. metric: Km; raw value: 8 +/- 2; raw unit: uM; normalized value: 0.008 mM; metric: kcat; raw value: 80 +/- 5; raw unit: min^-1; normalized value: 1.333 s^(-1); metric: kcat/Km; raw value: 10000 +/- 2610; raw unit: mM^-1 min^-1; normalized value: 166.66666666666666 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 8 +/- 2 uM in the Human ADH4 column; 8 uM / 1000 = 0.008 mM, which is the catalog km exactly. kcat: printed cell 80 +/- 5 min^-1 in the Human ADH4 column; 80 min^-1 / 60 = 1.3333333333333333 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 1.333 s^-1, so the paper kcat field carries the catalog value 1.333 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 10000 +/- 2610 mM^-1 min^-1 in the Human ADH4 column; 10000 mM^-1 min^-1 / 60 = 166.66666666666666 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 166.625 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (1.333 / 0.008). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 80 min^-1 / 0.008 mM = 10000.0 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 7-cis-retinal | Km (uM) | ND | ND | 8 +/- 2 | ND | ND | | kcat row: | 7-cis-retinal | kcat (min^-1) | ND | ND | 80 +/- 5 | ND | ND | | kcat/Km row: | 7-cis-retinal | kcat/Km (mM^-1 min^-1) | ND | ND | 10000 +/- 2610 | ND | ND | | Human ADH4 column cells read: Km = 8 +/- 2 uM; kcat = 80 +/- 5 min^-1; kcat/Km = 10000 +/- 2610 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Human ADH4 | 7-cis-retinal


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 13-cis-retinol. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 26 +/- 3, kcat (min^-1) cell 0.76 +/- 0.02, kcat/Km (mM^-1 min^-1) cell 29 +/- 3. metric: Km; raw value: 26 +/- 3; raw unit: uM; normalized value: 0.026 mM; metric: kcat; raw value: 0.76 +/- 0.02; raw unit: min^-1; normalized value: 0.013 s^(-1); metric: kcat/Km; raw value: 29 +/- 3; raw unit: mM^-1 min^-1; normalized value: 0.48333333333333334 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 26 +/- 3 uM in the Human ADH4 column; 26 uM / 1000 = 0.026 mM, which is the catalog km exactly. kcat: printed cell 0.76 +/- 0.02 min^-1 in the Human ADH4 column; 0.76 min^-1 / 60 = 0.012666666666666666 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.013 s^-1, so the paper kcat field carries the catalog value 0.013 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 29 +/- 3 mM^-1 min^-1 in the Human ADH4 column; 29 mM^-1 min^-1 / 60 = 0.48333333333333334 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 0.5 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.013 / 0.026). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 0.76 min^-1 / 0.026 mM = 29.23076923076923 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 13-cis-retinol | Km (uM) | NA | NA | 26 +/- 3 | ND | ND | | kcat row: | 13-cis-retinol | kcat (min^-1) | NA | NA | 0.76 +/- 0.02 | ND | ND | | kcat/Km row: | 13-cis-retinol | kcat/Km (mM^-1 min^-1) | NA | NA | 29 +/- 3 | ND | ND | | Human ADH4 column cells read: Km = 26 +/- 3 uM; kcat = 0.76 +/- 0.02 min^-1; kcat/Km = 29 +/- 3 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Human ADH4 | 13-cis-retinol


verification_status: verified

column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 7-cis-retinol. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 27 +/- 3, kcat (min^-1) cell 425 +/- 15, kcat/Km (mM^-1 min^-1) cell 15740 +/- 1815. metric: Km; raw value: 27 +/- 3; raw unit: uM; normalized value: 0.027 mM; metric: kcat; raw value: 425 +/- 15; raw unit: min^-1; normalized value: 7.083 s^(-1); metric: kcat/Km; raw value: 15740 +/- 1815; raw unit: mM^-1 min^-1; normalized value: 262.3333333333333 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 27 +/- 3 uM in the Human ADH4 column; 27 uM / 1000 = 0.027 mM, which is the catalog km exactly. kcat: printed cell 425 +/- 15 min^-1 in the Human ADH4 column; 425 min^-1 / 60 = 7.083333333333333 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 7.083 s^-1, so the paper kcat field carries the catalog value 7.083 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 15740 +/- 1815 mM^-1 min^-1 in the Human ADH4 column; 15740 mM^-1 min^-1 / 60 = 262.3333333333333 s^-1 mM^-1, which is the catalog kcat_over_km 262.33333333333337 at export precision.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 7-cis-retinol | Km (uM) | ND | ND | 27 +/- 3 | ND | ND | | kcat row: | 7-cis-retinol | kcat (min^-1) | ND | ND | 425 +/- 15 | ND | ND | | kcat/Km row: | 7-cis-retinol | kcat/Km (mM^-1 min^-1) | ND | ND | 15740 +/- 1815 | ND | ND | | Human ADH4 column cells read: Km = 27 +/- 3 uM; kcat = 425 +/- 15 min^-1; kcat/Km = 15740 +/- 1815 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Human ADH4 | 7-cis-retinol

status: verified


sequence_source: UniProtKB reviewed accession P08319 (ADH4_HUMAN), fetched 2026-05-31

column_label: The literal 4-Hydroxy-retinol row and ADH4 column bind all three cells. The current quotient lies inside the converted printed interval [1738.3333333333333, 2795].

raw_value_unit_evidence: ADH4 cells: kcat 2050 ± 250 min^-1; Km 15 ± 3 uM; printed kcat/Km 136,000 ± 31,700 mM^-1 min^-1.

row_label: 4-Hydroxy-retinol | ADH4

table_label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids


substrate_name: all-trans-Dehydroretinal

sequence_source: UniProtKB reviewed accession P00325 (ADH1B_HUMAN), fetched 2026-05-31

column_label: Table label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids. Substrate block: 3,4-Didehydroretinal. Enzyme column: ADH1B2. Columns read: Km (uM) cell 25, kcat (min^-1) cell 13, kcat/Km (mM^-1 min^-1) cell 520. metric: kcat; raw value: 13; raw unit: min^-1; normalized value: 0.217 s^(-1); metric: Km; raw value: 25; raw unit: uM; normalized value: 0.025 mM; metric: kcat/Km; raw value: 520 ± 130; raw unit: mM^-1 min^-1; normalized value: 8.666666666666666 s^-1 mM^-1; explicit printed primary cell; assay condition: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH (0.77 mM for ADH4) for retinal reductions, at 25 C. Export row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: kcat raw 13 min^-1 -> 0.217 s^(-1); Km raw 25 uM -> 0.025 mM; explicit printed kcat/Km raw 520 ± 130 mM^-1 min^-1 -> 8.666666666666666 s^-1 mM^-1. Conversion: 520 mM^-1 min^-1 / 60 = 26/3 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence:
Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids | enzyme column header row: Substrate                                                              ADH1B1                      ADH1B2                 ADH4 | Km row: 3,4-Didehydroretinal              Km (lM)                              ND                             25 ± 6                   26 ± 6 | kcat row: kcat (min1)                                                        13 ± 1                   73 ± 5 | kcat/Km row: kcat/Km (mM1 min1)                                               520 ± 130               2800 ± 700 | ADH1B2 cells read: Km = 25 uM; kcat = 13 min^-1; kcat/Km = 520 mM^-1 min^-1 | table footnote: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH
(0.77 mM for ADH4) for retinal reductions, at 25 C. ND, not determined.

row_label: ADH1B2 | 3,4-Didehydroretinal

substrate: all-trans-Dehydroretinal


column_label: The literal 4-Oxo-retinal row and ADH4 column bind all three cells. The current quotient lies inside the converted printed interval.

raw_value_unit_evidence: ADH4 cells: kcat 1200 ± 140 min^-1; Km 17 ± 4 uM; printed kcat/Km 68,200 ± 18,000 mM^-1 min^-1.

row_label: 4-Oxo-retinal | ADH4


column_label: The literal 4-Oxo-retinal row and ADH1B2 column bind all three cells. The current quotient lies inside the converted printed interval.

raw_value_unit_evidence: ADH1B2 cells: kcat 470 ± 70 min^-1; Km 27 ± 5 uM; printed kcat/Km 17,480 ± 4200 mM^-1 min^-1.

row_label: 4-Oxo-retinal | ADH1B2


column_label: Table label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids. Substrate block: 3,4-Didehydroretinal. Enzyme column: ADH4. Columns read: Km (uM) cell 26, kcat (min^-1) cell 73, kcat/Km (mM^-1 min^-1) cell 2800. metric: kcat; raw value: 73; raw unit: min^-1; normalized value: 1.217 s^(-1); metric: Km; raw value: 26; raw unit: uM; normalized value: 0.026 mM; metric: kcat/Km; raw value: 2800 ± 700; raw unit: mM^-1 min^-1; normalized value: 46.666666666666664 s^-1 mM^-1; explicit printed primary cell; assay condition: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH (0.77 mM for ADH4) for retinal reductions, at 25 C. Export row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: kcat raw 73 min^-1 -> 1.217 s^(-1); Km raw 26 uM -> 0.026 mM; explicit printed kcat/Km raw 2800 ± 700 mM^-1 min^-1 -> 46.666666666666664 s^-1 mM^-1. Conversion: 2800 mM^-1 min^-1 / 60 = 140/3 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence:
Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids | enzyme column header row: Substrate                                                              ADH1B1                      ADH1B2                 ADH4 | Km row: 3,4-Didehydroretinal              Km (lM)                              ND                             25 ± 6                   26 ± 6 | kcat row: kcat (min1)                                                        13 ± 1                   73 ± 5 | kcat/Km row: kcat/Km (mM1 min1)                                               520 ± 130               2800 ± 700 | ADH4 cells read: Km = 26 uM; kcat = 73 min^-1; kcat/Km = 2800 mM^-1 min^-1 | table footnote: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH
(0.77 mM for ADH4) for retinal reductions, at 25 C. ND, not determined.

row_label: ADH4 | 3,4-Didehydroretinal


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: Cyclohexanol

kcat_over_km_display: Not reported

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

mutation_type: substitution

substrate: Cyclohexanol


sequence_source: UniProtKB REST P11766 reviewed canonical sequence

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row '5beta-cholan-3alpha,7alpha,12alpha,24-tetrol'; column 'Km (mM)' = 0.2; column 'kcat (min^-1)' = 55; column 'kcat/Km (mM^-1 min^-1)' = 279.

normalized_value_unit_evidence: Km: printed Table II cell 0.2 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.2 mM. kcat: printed Table II cell 55 min^-1; the printed turnover column is per MINUTE, so 55 / 60 = 0.916667 s^-1, which the export carries at its own three-decimal precision as 0.917 s^(-1); the exported value is 0.917 s^(-1). kcat/Km: printed Table II cell 279 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 279 / 60 = 4.65 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row '5beta-cholan-3alpha,7alpha,12alpha,24-tetrol': Km = 0.2 mM; kcat = 55 min^-1; printed kcat/Km = 279 mM^-1 min^-1.

table_label: Table II: Substrate Specificity of Human Liver chi chi-ADH (Biochemistry 1991, 30(23):5743-5749)


smiles: CCCCCCCCCCCCO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'n-dodecanol'; column 'Km (mM)' = 0.05; column 'kcat (min^-1)' = 18; column 'kcat/Km (mM^-1 min^-1)' = 310.

normalized_value_unit_evidence: Km: printed Table II cell 0.05 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.05 mM. kcat: printed Table II cell 18 min^-1; the printed turnover column is per MINUTE, so 18 / 60 = 0.3 s^-1; the exported value is 0.3 s^(-1). kcat/Km: printed Table II cell 310 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 310 / 60 = 5.166666666666667 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'n-dodecanol': Km = 0.05 mM; kcat = 18 min^-1; printed kcat/Km = 310 mM^-1 min^-1.

row_label: Table II, alcohol row 'n-dodecanol'


smiles: CCCC=CCO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'trans-2-hexene-1-ol'; column 'Km (mM)' = 0.9; column 'kcat (min^-1)' = 244; column 'kcat/Km (mM^-1 min^-1)' = 272.

normalized_value_unit_evidence: Km: printed Table II cell 0.9 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.9 mM. kcat: printed Table II cell 244 min^-1; the printed turnover column is per MINUTE, so 244 / 60 = 4.066667 s^-1, which the export carries at its own three-decimal precision as 4.067 s^(-1); the exported value is 4.067 s^(-1). kcat/Km: printed Table II cell 272 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 272 / 60 = 4.533333333333333 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'trans-2-hexene-1-ol': Km = 0.9 mM; kcat = 244 min^-1; printed kcat/Km = 272 mM^-1 min^-1.


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: OCCCCCCCCO


smiles: OCC=CCO


smiles: CCCCCCCCCCO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'n-decanol'; column 'Km (mM)' = 0.18; column 'kcat (min^-1)' = 40; column 'kcat/Km (mM^-1 min^-1)' = 150.

normalized_value_unit_evidence: Km: printed Table II cell 0.18 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.18 mM. kcat: printed Table II cell 40 min^-1; the printed turnover column is per MINUTE, so 40 / 60 = 0.666667 s^-1, which the export carries at its own three-decimal precision as 0.667 s^(-1); the exported value is 0.667 s^(-1). kcat/Km: printed Table II cell 150 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 150 / 60 = 2.5 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'n-decanol': Km = 0.18 mM; kcat = 40 min^-1; printed kcat/Km = 150 mM^-1 min^-1.

row_label: Table II, alcohol row 'n-decanol'


substrate_name: cinnamyl alcohol

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'cinnamyl alcohol'; column 'Km (mM)' = 0.44; column 'kcat (min^-1)' = 163; column 'kcat/Km (mM^-1 min^-1)' = 368.

normalized_value_unit_evidence: Km: printed Table II cell 0.44 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.44 mM. kcat: printed Table II cell 163 min^-1; the printed turnover column is per MINUTE, so 163 / 60 = 2.716667 s^-1, which the export carries at its own three-decimal precision as 2.717 s^(-1); the exported value is 2.717 s^(-1). kcat/Km: printed Table II cell 368 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 368 / 60 = 6.133333333333333 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'cinnamyl alcohol': Km = 0.44 mM; kcat = 163 min^-1; printed kcat/Km = 368 mM^-1 min^-1.

substrate: cinnamyl alcohol


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


substrate_name: Retinol

substrate: Retinol


sequence_source: UniProtKB reviewed accession P11766 (ADHX_HUMAN); direct REST exact-accession lookup fetched 2026-05-31

smiles: CCCCCCO


smiles: CCCCCCCCCCCCCCO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'n-tetradecanol'; column 'Km (mM)' = 0.006; column 'kcat (min^-1)' = 1; column 'kcat/Km (mM^-1 min^-1)' = 160.

normalized_value_unit_evidence: Km: printed Table II cell 0.006 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.006 mM. kcat: printed Table II cell 1 min^-1; the printed turnover column is per MINUTE, so 1 / 60 = 0.016667 s^-1, which the export carries at its own three-decimal precision as 0.017 s^(-1); the exported value is 0.017 s^(-1). kcat/Km: printed Table II cell 160 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 160 / 60 = 2.6666666666666665 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'n-tetradecanol': Km = 0.006 mM; kcat = 1 min^-1; printed kcat/Km = 160 mM^-1 min^-1.

row_label: Table II, alcohol row 'n-tetradecanol'


substrate_name: Prenol

smiles: CC(C)=CCO

substrate: Prenol


smiles: CCCCCCCCCO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'n-nonanol'; column 'Km (mM)' = 0.27; column 'kcat (min^-1)' = 53; column 'kcat/Km (mM^-1 min^-1)' = 201.

normalized_value_unit_evidence: Km: printed Table II cell 0.27 mM; the column is already in mM, so no unit conversion applies and the exported value is 0.27 mM. kcat: printed Table II cell 53 min^-1; the printed turnover column is per MINUTE, so 53 / 60 = 0.883333 s^-1, which the export carries at its own three-decimal precision as 0.883 s^(-1); the exported value is 0.883 s^(-1). kcat/Km: printed Table II cell 201 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 201 / 60 = 3.35 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'n-nonanol': Km = 0.27 mM; kcat = 53 min^-1; printed kcat/Km = 201 mM^-1 min^-1.

row_label: Table II, alcohol row 'n-nonanol'


sequence_source: UniProtKB reviewed accession P00326 (ADH1G_HUMAN); direct REST exact-accession lookup fetched 2026-05-31

smiles: CCCO


smiles: CCCCCCCCO


substrate_name: 12-Hydroxydodecanoic acid

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


sequence_source: UniProtKB reviewed accession P00325 (ADH1B_HUMAN); direct REST exact-accession lookup fetched 2026-05-31

smiles: CCCCO


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


sequence_source: UniProtKB:P00326 direct lookup 2026-05-31


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCO


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH4

substrate_name: all-trans-Retinal

sequence_source: UniProtKB reviewed P08319 (ADH4_HUMAN) direct REST lookup, 2026-05-31

substrate: all-trans-Retinal


enzyme: All-trans-retinol dehydrogenase [NAD(+)] ADH4


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH1B

sequence_source: UniProtKB reviewed P00325 (ADH1B_HUMAN) direct REST lookup, 2026-05-31


enzyme_display_name: Alcohol dehydrogenase class-3

sequence_source: UniProtKB reviewed P11766 (ADHX_HUMAN) direct REST lookup, 2026-05-31

smiles: OCCCCCCO

enzyme: Alcohol dehydrogenase class-3


substrate_name: farnesol

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

substrate: farnesol


substrate_name: Methylcrotyl alcohol

smiles: CC=CC(C)O

substrate: Methylcrotyl alcohol


smiles: CCC/C=C\CO

column_label: Table II (Substrate Specificity of Human Liver chi chi-ADH); alcohol row 'cis-2-hexene-1-ol'; column 'Km (mM)' = 2.9; column 'kcat (min^-1)' = 228; column 'kcat/Km (mM^-1 min^-1)' = 78.

normalized_value_unit_evidence: Km: printed Table II cell 2.9 mM; the column is already in mM, so no unit conversion applies and the exported value is 2.9 mM. kcat: printed Table II cell 228 min^-1; the printed turnover column is per MINUTE, so 228 / 60 = 3.8 s^-1; the exported value is 3.8 s^(-1). kcat/Km: printed Table II cell 78 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 78 / 60 = 1.3 s^(-1)*mM^(-1); this pass carries the printed efficiency cell in place of the quotient the export held for that field.

raw_value_unit_evidence: Table II, alcohol row 'cis-2-hexene-1-ol': Km = 2.9 mM; kcat = 228 min^-1; printed kcat/Km = 78 mM^-1 min^-1.


substrate_name: Glycol

smiles: OCCO

substrate: Glycol


sequence_source: UniProtKB:P00326 direct lookup, retrieved 2026-05-31

assay_conditions_summary: pH 10; 298.15 K; buffer 0.1 M glycine; cofactor NAD+

column_label: Table I (Km, uM) / Table II (kcat, min^-1) / Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row 'benzyl alcohol'; isoenzyme column (6) g1g1; Table I cell = 7; Table II cell = 127; Table III cell = 180.

normalized_value_unit_evidence: Km: printed Table I cell 7 uM; 7 / 1000 = 0.007 mM; the exported value is 0.008 mM. kcat: printed Table II cell 127 min^-1; the printed turnover column is per MINUTE, so 127 / 60 = 2.1166666666666667 s^(-1); the exported value is 2.117 s^(-1), which is that same number rounded to the export's three printed decimals. kcat/Km: printed Table III cell 180 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 180 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 300.0 s^(-1)*mM^(-1); the exported value is 264.625 s^(-1)*mM^(-1), which is the bare quotient of the export's own kcat and its Km.

raw_value_unit_evidence: Journal page 1860, substrate row 'benzyl alcohol', isoenzyme column (6) g1g1: Table I Km = 7 uM; Table II kcat = 127 min^-1; Table III kcat/Km = 180 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 180 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row 'benzyl alcohol', isoenzyme column (6) g1g1

table_label: Table I: Km Values (uM) for ADH Isoenzymes toward Various Alcohols; Table II: kcat Values (min^-1) for ADH Isoenzymes toward Various Alcohols; Table III: Human Class I ADH Isoenzymes: kcat/Km Values toward Various Alcohols, printed under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1)


smiles: CO


smiles: CCO


sequence_source: UniProtKB:P00326 reviewed canonical sequence, direct REST lookup on 2026-05-31

column_label: Table I row (c) ethylene glycol printed cells across isoenzyme columns (1) to (8): 50 000, a, 47 000, 32 000, 36 000, 57 000, 220 000, 13 000; the column (6) gamma1gamma1 cell is printed as 57 000 microM, that is 57000 microM. Table II row (c) ethylene glycol printed cells across isoenzyme columns (1) to (8): 72, a, 50, 66, 55, 85, 50, 7; the column (6) gamma1gamma1 cell is 85 min-1. Footnote a in both tables reads Not determined.

normalized_value_unit_evidence: Km 57000 microM divided by 1000 is 57.0 mM. kcat 85 min-1 divided by 60 is 1.4166666666666667 s^-1, carried in the export at three decimals as 1.417 s^-1. kcat/Km formed from those two printed cells is 0.02485964912280702 s^-1 mM^-1.

raw_value_unit_evidence: Table I ((c) ethylene glycol, isoenzyme column (6) gamma1gamma1): 57000 microM, printed with a thousands space as 57 000. Table II ((c) ethylene glycol, isoenzyme column (6) gamma1gamma1): 85 min-1.

row_label: (c) ethylene glycol

table_label: Table I: Km Values (microM) for ADH Isoenzymes toward Various Alcohols and Table II: kcat Values (min-1) for ADH Isoenzymes toward Various Alcohols


sequence_source: UniProtKB:P00325 canonical sequence (direct REST lookup)


sequence_source: UniProtKB:P00326 canonical sequence (direct REST lookup)

column_label: Table I (Km, uM), Table II (kcat, min^-1) and Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row '16-HHA'; isoenzyme column (6) g1g1; Table I cell = 26; Table II cell = 208; Table III cell = 80.

normalized_value_unit_evidence: Km: printed Table I cell 26 uM; 26 / 1000 = 0.026000000000000002 mM; the exported value is 0.026 mM. kcat: printed Table II cell 208 min^-1; the printed turnover column is per MINUTE, so 208 / 60 = 3.466666666666667 s^(-1); the exported value is 3.467 s^(-1). kcat/Km: printed Table III cell 80 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 80 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 133.33333333333334 s^(-1)*mM^(-1); the exported value is 133.34615384615387 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 1860, substrate row '16-HHA', isoenzyme column (6) g1g1: Table I Km = 26 uM; Table II kcat = 208 min^-1; Table III kcat/Km = 80 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 80 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row '16-HHA', isoenzyme column (6) g1g1


sequence_source: UniProtKB:P11766 direct REST lookup

smiles: CCCCCCCC=O


substrate_name: NADH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADPH

substrate: NADH


sequence_source: UniProtKB:P08319 direct REST lookup


sequence_source: UniProtKB:P08319 reviewed canonical sequence, direct lookup 2026-05-31


smiles: CC(C)O


assay_conditions_summary: pH 9; 298.15 K; cofactor NADH


sequence_source: UniProtKB P11766 canonical sequence with Y93F reconstructed after direct residue validation on 2026-05-31.

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


organism: Kluyveromyces lactis

substrate_name: Acetaldehyde

sequence_source: UniProtKB P49384 canonical sequence from direct UniProt REST check on 2026-05-31.

smiles: CC=O

substrate: Acetaldehyde


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

column_label: Table 1: Cofactor affinity of native and mutated KlADH III isoforms (Biochimie 2004, 86(9-10):705-712, journal page 709, PDF page 5); printed enzyme rows Wild-type, G225A, A274F and G225A-A274F, printed coenzyme column groups NAD, NADP, NADH and NADPH, each group carrying the metric column heads Km, kcat and kcat/Km, with the table footnote 'Km (mM); kcat (min-1); kcat/Km (min-1 mM-1)'. Table 1, enzyme row Wild-type, coenzyme column group NADPH; column Km (mM) = 0.21; column kcat (min^-1) = 1.70 x 10^3; column kcat/Km (min^-1 mM^-1) = 8.09 x 10^3. captured primary segment: Table 1, enzyme row Wild-type, coenzyme column group NADPH | construct Wild-type | substrate NADPH | condition pH 8.0, 25 C | Km 0.21 mM | kcat 1.70 x 10^3 min^-1 | kcat/Km 8.09 x 10^3 min^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 0.21 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.21 mM; the exported value is 0.21 mM. kcat: printed cell 1.70 x 10^3 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 1700 / 60 = 28.33333333 s^(-1), which the catalog carries rounded to three decimals as 28.333 s^(-1), the value this record keeps for kcat. kcat/Km: printed cell 8.09 x 10^3 under the column head kcat/Km (min^-1 mM^-1); 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 8090 / 60 = 134.83333333333334 s^(-1)*mM^(-1), the value this record carries for kcat_over_km. Quotient disclosure: the two printed component cells give 1700 / 0.21 = 8095.24 min^-1 mM^-1, which reads 8.10 x 10^3 at three significant figures, while the printed efficiency cell reads 8.09 x 10^3; the Methods derive catalytic efficiency from Vmax/Km [E], consistent with the printed cell being the article's own value computed from its fitted parameters.

raw_value_unit_evidence: Table 1, enzyme row Wild-type, coenzyme column group NADPH: Km = 0.21 mM; kcat = 1.70 x 10^3 min^-1; printed kcat/Km = 8.09 x 10^3 min^-1 mM^-1.

substrate: NADPH


sequence_source: UniProtKB REST P49384 canonical sequence, reviewed Swiss-Prot entry ADH3_KLULA, fetched 2026-05-31

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

column_label: Table 1: Cofactor affinity of native and mutated KlADH III isoforms (Biochimie 2004, 86(9-10):705-712, journal page 709, PDF page 5); printed enzyme rows Wild-type, G225A, A274F and G225A-A274F, printed coenzyme column groups NAD, NADP, NADH and NADPH, each group carrying the metric column heads Km, kcat and kcat/Km, with the table footnote 'Km (mM); kcat (min-1); kcat/Km (min-1 mM-1)'. Table 1, enzyme row Wild-type, coenzyme column group NADH; column Km (mM) = 0.025; column kcat (min^-1) = 6.0 x 10^4; column kcat/Km (min^-1 mM^-1) = 2.40 x 10^6. captured primary segment: Table 1, enzyme row Wild-type, coenzyme column group NADH | construct Wild-type | substrate NADH | condition pH 8.0, 25 C | Km 0.025 mM | kcat 6.0 x 10^4 min^-1 | kcat/Km 2.40 x 10^6 min^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 0.025 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 0.025 mM; the exported value is 0.025 mM. kcat: printed cell 6.0 x 10^4 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 60000 / 60 = 1000 s^(-1), an exact decimal; the exported value is 1000.0 s^(-1). kcat/Km: printed cell 2.40 x 10^6 under the column head kcat/Km (min^-1 mM^-1); 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 2400000 / 60 = 40000.0 s^(-1)*mM^(-1) for the printed cell. The exported value 40000.0 s^(-1)*mM^(-1) is the full-precision quotient 1000.0 / 0.025 of the same two printed cells; in the table's own unit that quotient is 60000 / 0.025 = 2400000.00 min^-1 mM^-1, which reads 2.40 x 10^6 at the three significant figures of the efficiency column, the printed cell.

raw_value_unit_evidence: Table 1, enzyme row Wild-type, coenzyme column group NADH: Km = 0.025 mM; kcat = 6.0 x 10^4 min^-1; printed kcat/Km = 2.40 x 10^6 min^-1 mM^-1.


organism: Macaca mulatta

smiles: CC(C)CCO

assay_conditions_summary: pH 7.3; 303.15 K; buffer 2 mM NAD+ (MmADHalpha) or 1 mM NAD+ (EqADH)". The; cofactor NAD+

column_label: Table III (journal page 12594); row `3-Methylbutanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 2.1; column `Km` (unit row `mM`) = 0.10. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 2.1 s^-1 -> 2.1 s^-1; catalog holds 2.1 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.10 mM -> 0.1 mM; catalog holds 0.1 mM; no conversion. kcat/Km: not printed; catalog 21.0 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `3-Methylbutanol`, MmADHalpha columns: V1 = 2.1 (unit row: s^-1); Km = 0.10 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `3-Methylbutanol`, MmADHalpha column group

table_label: Table III. Kinetic constants for primary, branched-chain, secondary alcohols


sequence_variant_note: Mutation signature G47R could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADH


sequence_variant_note: Mutation signature G47H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


assay_conditions_summary: pH 7.3; 303.15 K; buffer 2 mM NAD+ (MmADHalpha)". The; cofactor NAD+

column_label: Table III (journal page 12594); row `(S)-2-Butanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 1.4; column `Km` (unit row `mM`) = 1.4. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 1.4 s^-1 -> 1.4 s^-1; catalog holds 1.4 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 1.4 mM -> 1.4 mM; catalog holds 1.4 mM; no conversion. kcat/Km: not printed; catalog 1.0 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `(S)-2-Butanol`, MmADHalpha columns: V1 = 1.4 (unit row: s^-1); Km = 1.4 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `(S)-2-Butanol`, MmADHalpha column group


column_label: Table III (journal page 12594); row `(R)-2-Butanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 1.9; column `Km` (unit row `mM`) = 0.42. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 1.9 s^-1 -> 1.9 s^-1; catalog holds 1.9 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.42 mM -> 0.42 mM; catalog holds 0.42 mM; no conversion. kcat/Km: not printed; catalog 4.523809523809524 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `(R)-2-Butanol`, MmADHalpha columns: V1 = 1.9 (unit row: s^-1); Km = 0.42 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `(R)-2-Butanol`, MmADHalpha column group


substrate_name: NAD+

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+

substrate: NAD+


sequence_source: UniProtKB:P49384 canonical sequence; direct REST/FASTA lookup on 2026-05-31

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

column_label: Table 1: Cofactor affinity of native and mutated KlADH III isoforms (Biochimie 2004, 86(9-10):705-712, journal page 709, PDF page 5); printed enzyme rows Wild-type, G225A, A274F and G225A-A274F, printed coenzyme column groups NAD, NADP, NADH and NADPH, each group carrying the metric column heads Km, kcat and kcat/Km, with the table footnote 'Km (mM); kcat (min-1); kcat/Km (min-1 mM-1)'. Table 1, enzyme row Wild-type, coenzyme column group NADP; column Km (mM) = 2.64; column kcat (min^-1) = 1.16 x 10^3; column kcat/Km (min^-1 mM^-1) = 4.40 x 10^2. captured primary segment: Table 1, enzyme row Wild-type, coenzyme column group NADP | construct Wild-type | substrate NADP | condition pH 8.0, 25 C | Km 2.64 mM | kcat 1.16 x 10^3 min^-1 | kcat/Km 4.40 x 10^2 min^-1 mM^-1

normalized_value_unit_evidence: Km: printed cell 2.64 under the column head Km (mM); the column is already in mM, so no unit conversion applies and the paper value is 2.64 mM; the exported value is 2.64 mM. kcat: printed cell 1.16 x 10^3 under the column head kcat (min^-1); 1 min^-1 is 1/60 s^-1, so 1160 / 60 = 19.33333333 s^(-1), which the catalog carries rounded to three decimals as 19.333 s^(-1), the value this record keeps for kcat. kcat/Km: printed cell 4.40 x 10^2 under the column head kcat/Km (min^-1 mM^-1); 1 min^-1 mM^-1 is 1/60 s^-1 mM^-1, so 440 / 60 = 7.333333333333333 s^(-1)*mM^(-1), the value this record carries for kcat_over_km. Quotient disclosure: the two printed component cells give 1160 / 2.64 = 439.39 min^-1 mM^-1, which reads 4.39 x 10^2 at three significant figures, while the printed efficiency cell reads 4.40 x 10^2; the Methods derive catalytic efficiency from Vmax/Km [E], consistent with the printed cell being the article's own value computed from its fitted parameters.

raw_value_unit_evidence: Table 1, enzyme row Wild-type, coenzyme column group NADP: Km = 2.64 mM; kcat = 1.16 x 10^3 min^-1; printed kcat/Km = 4.40 x 10^2 min^-1 mM^-1.

substrate: NADP+


substrate_name: methanol

sequence_source: UniProtKB:P28469 FASTA

substrate: methanol


column_label: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); row Ethanol row under Primary alcohols; column V1 (s^-1), MmADHa = 1.1; column Km (mM), MmADHa = 15. Both cells are read from the same table row and the same enzyme column block (MmADHa) under one NAD+ condition. No kcat/Km column exists in Table III, so the ratio is derived as 1.1 s^-1 / 15 mM.

normalized_value_unit_evidence: V1 is printed in s^-1 in Table III, so kcat = 1.1 s^-1 with no unit conversion. Km is printed in mM in Table III, so Km = 15 mM with no unit conversion. Table III prints no kcat/Km cell, so kcat/Km is the quotient of this row's own two printed cells: 1.1 s^-1 / 15 mM = 0.07333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); Ethanol row under Primary alcohols; transcribed line: "Ethano! 7.8 0.80 1.1 15". Column V1 (s^-1), MmADHa raw value 1.1; column Km (mM), MmADHa raw value 15. Table III prints no kcat/Km column.

row_label: Ethanol row under Primary alcohols


column_label: Table III (journal page 12594); row `Pentanol`; column group `MmADHa`; column `V1` (printed unit row `s^-1`) = 1.8; column `Km` (printed unit row `mM`) = 0.045. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 1.8 s^-1 -> 1.8 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.045 mM -> 0.045 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 1.8 s^-1 / 0.045 mM = 40.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Pentanol`, MmADHa columns: V1 = 1.8 (printed unit row: s^-1); Km = 0.045 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

row_label: Table III row `Pentanol`, MmADHa column group


smiles: CCCO

column_label: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); row Propanol row under Primary alcohols; column V1 (s^-1), MmADHa = 1.4; column Km (mM), MmADHa = 2.0. Both cells are read from the same table row and the same enzyme column block (MmADHa) under one NAD+ condition. No kcat/Km column exists in Table III, so the ratio is derived as 1.4 s^-1 / 2.0 mM.

normalized_value_unit_evidence: V1 is printed in s^-1 in Table III, so kcat = 1.4 s^-1 with no unit conversion. Km is printed in mM in Table III, so Km = 2.0 mM with no unit conversion. Table III prints no kcat/Km cell, so kcat/Km is the quotient of this row's own two printed cells: 1.4 s^-1 / 2.0 mM = 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); Propanol row under Primary alcohols; transcribed line: "Propanol 8.2 0.39 1.4 2.0". Column V1 (s^-1), MmADHa raw value 1.4; column Km (mM), MmADHa raw value 2.0. Table III prints no kcat/Km column.

row_label: Propanol row under Primary alcohols


substrate_name: Cyclohexanol

column_label: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); row Cyclohexanol row under Secondary alcohols; column V1 (s^-1), MmADHa = 3.0; column Km (mM), MmADHa = 0.024. Both cells are read from the same table row and the same enzyme column block (MmADHa) under one NAD+ condition. No kcat/Km column exists in Table III, so the ratio is derived as 3.0 s^-1 / 0.024 mM.

normalized_value_unit_evidence: V1 is printed in s^-1 in Table III, so kcat = 3.0 s^-1 with no unit conversion. Km is printed in mM in Table III, so Km = 0.024 mM with no unit conversion. Table III prints no kcat/Km cell, so kcat/Km is the quotient of this row's own two printed cells: 3.0 s^-1 / 0.024 mM = 125.0 s^-1 mM^-1.

raw_value_unit_evidence: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); Cyclohexanol row under Secondary alcohols; transcribed line: "Cyclohexanol 6.1 1.1 3.0 0.024". Column V1 (s^-1), MmADHa raw value 3.0; column Km (mM), MmADHa raw value 0.024. Table III prints no kcat/Km column.

substrate: Cyclohexanol


organism: Mus musculus

sequence_source: UniProtKB:P00329 direct REST lookup, accessed 2026-05-31

smiles: CCCCCCO


substrate_name: Cyclohexanone

sequence_source: UniProtKB P28469 reviewed canonical FASTA, direct REST/FASTA check on 2026-05-31.

substrate: Cyclohexanone


column_label: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); row Hexanol row under Primary alcohols; column V1 (s^-1), MmADHa = 1.6; column Km (mM), MmADHa = 0.032. Both cells are read from the same table row and the same enzyme column block (MmADHa) under one NAD+ condition. No kcat/Km column exists in Table III, so the ratio is derived as 1.6 s^-1 / 0.032 mM.

normalized_value_unit_evidence: V1 is printed in s^-1 in Table III, so kcat = 1.6 s^-1 with no unit conversion. Km is printed in mM in Table III, so Km = 0.032 mM with no unit conversion. Table III prints no kcat/Km cell, so kcat/Km is the quotient of this row's own two printed cells: 1.6 s^-1 / 0.032 mM = 50.0 s^-1 mM^-1.

raw_value_unit_evidence: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); Hexanol row under Primary alcohols; transcribed line: "Hexano] 3.8 0.076 1.6 0.032". Column V1 (s^-1), MmADHa raw value 1.6; column Km (mM), MmADHa raw value 0.032. Table III prints no kcat/Km column.

row_label: Hexanol row under Primary alcohols


substrate_name: benzyl alcohol

column_label: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); row Benzyl alcohol row under Primary alcohols; column V1 (s^-1), MmADHa = 0.75; column Km (mM), MmADHa = 0.036. Both cells are read from the same table row and the same enzyme column block (MmADHa) under one NAD+ condition. No kcat/Km column exists in Table III, so the ratio is derived as 0.75 s^-1 / 0.036 mM.

normalized_value_unit_evidence: V1 is printed in s^-1 in Table III, so kcat = 0.75 s^-1 with no unit conversion. Km is printed in mM in Table III, so Km = 0.036 mM with no unit conversion. Table III prints no kcat/Km cell, so kcat/Km is the quotient of this row's own two printed cells: 0.75 s^-1 / 0.036 mM = 20.833333333333336 s^-1 mM^-1.

raw_value_unit_evidence: Table III: Kinetic constants for primary, branched-chain, secondary alcohols (journal page 12594); Benzyl alcohol row under Primary alcohols; transcribed line: "Benzyl alcohol 3.6 0.046 0.75 0.036". Column V1 (s^-1), MmADHa raw value 0.75; column Km (mM), MmADHa raw value 0.036. Table III prints no kcat/Km column.

substrate: benzyl alcohol


smiles: CCC(O)CC

column_label: Table III (journal page 12594); row `3-Pentanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 0.48; column `Km` (unit row `mM`) = 0.22. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 0.48 s^-1 -> 0.48 s^-1; catalog holds 0.48 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.22 mM -> 0.22 mM; catalog holds 0.22 mM; no conversion. kcat/Km: not printed; catalog 2.1818181818181817 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `3-Pentanol`, MmADHalpha columns: V1 = 0.48 (unit row: s^-1); Km = 0.22 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `3-Pentanol`, MmADHalpha column group


column_label: Table III (journal page 12594); row `2-Propanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 1.6; column `Km` (unit row `mM`) = 3.5. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 1.6 s^-1 -> 1.6 s^-1; catalog holds 1.6 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 3.5 mM -> 3.5 mM; catalog holds 3.5 mM; no conversion. kcat/Km: not printed; catalog 0.4571428571428572 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `2-Propanol`, MmADHalpha columns: V1 = 1.6 (unit row: s^-1); Km = 3.5 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `2-Propanol`, MmADHalpha column group


substrate_name: isobutanol

smiles: CC(C)CO

column_label: Table III (journal page 12594); row `2-Methylpropanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 0.62; column `Km` (unit row `mM`) = 1.2. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 0.62 s^-1 -> 0.62 s^-1; catalog holds 0.62 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 1.2 mM -> 1.2 mM; catalog holds 1.2 mM; no conversion. kcat/Km: not printed; catalog 0.5166666666666667 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `2-Methylpropanol`, MmADHalpha columns: V1 = 0.62 (unit row: s^-1); Km = 1.2 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `2-Methylpropanol`, MmADHalpha column group

substrate: isobutanol


smiles: CCCCO

assay_conditions_summary: pH 7.3; 303.15 K; buffer 2 mM NAD+". The; cofactor NAD+

column_label: Table III (journal page 12594); row `Butanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 2.2; column `Km` (unit row `mM`) = 0.19. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 2.2 s^-1 -> 2.2 s^-1; catalog holds 2.2 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.19 mM -> 0.19 mM; catalog holds 0.19 mM; no conversion. kcat/Km: not printed; catalog 11.578947368421053 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Butanol`, MmADHalpha columns: V1 = 2.2 (unit row: s^-1); Km = 0.19 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `Butanol`, MmADHalpha column group


sequence_variant_note: Resolved canonical sequence from Reconstructed mature-chain sequence from UniProtKB P28469 reviewed canonical sequence: UniProt marks initiator Met removed, mature chain is residues 2-375, and G47R was applied to mature residue 47. and applied mutation signature G47R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P11766 direct lookup; canonical FASTA for ADHX_HUMAN.

smiles: O=C(O)CCCCCCCCCCCO


sequence_source: Reconstructed from UniProtKB reviewed accession P11766 canonical sequence after direct lookup; Y93F mutation supported by PMID:7999766.


smiles: CCCCCCCCO


substrate_name: Ethanol

sequence_source: UniProtKB:Q9QYY9 FASTA

substrate: Ethanol


sequence_source: UniProtKB:P00329 FASTA

column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 11-cis-retinol. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 34 +/- 9, kcat (min^-1) cell 25 +/- 2, kcat/Km (mM^-1 min^-1) cell 735 +/- 205. metric: Km; raw value: 34 +/- 9; raw unit: uM; normalized value: 0.034 mM; metric: kcat; raw value: 25 +/- 2; raw unit: min^-1; normalized value: 0.417 s^(-1); metric: kcat/Km; raw value: 735 +/- 205; raw unit: mM^-1 min^-1; normalized value: 12.25 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 34 +/- 9 uM in the Mouse ADH1 column; 34 uM / 1000 = 0.034 mM, which is the catalog km exactly. kcat: printed cell 25 +/- 2 min^-1 in the Mouse ADH1 column; 25 min^-1 / 60 = 0.4166666666666667 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.417 s^-1, so the paper kcat field carries the catalog value 0.417 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 735 +/- 205 mM^-1 min^-1 in the Mouse ADH1 column; 735 mM^-1 min^-1 / 60 = 12.25 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 12.26470588235294 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.417 / 0.034). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 25 min^-1 / 0.034 mM = 735.2941176470588 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinol | Km (uM) | 35 +/- 7 | 18 +/- 4 | 28 +/- 5 | 34 +/- 9 | 23 +/- 6 | | kcat row: | 11-cis-retinol | kcat (min^-1) | 0.85 +/- 0.04 | 9.5 +/- 1.0 | 190 +/- 20 | 25 +/- 2 | 225 +/- 5 | | kcat/Km row: | 11-cis-retinol | kcat/Km (mM^-1 min^-1) | 24 +/- 5 | 530 +/- 55 | 6790 +/- 1400 | 735 +/- 205 | 9740 +/- 2550 | | Mouse ADH1 column cells read: Km = 34 +/- 9 uM; kcat = 25 +/- 2 min^-1; kcat/Km = 735 +/- 205 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH1 | 11-cis-retinol


substrate_name: Retinol

column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: all-trans-retinol. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 23 +/- 4, kcat (min^-1) cell 125 +/- 5, kcat/Km (mM^-1 min^-1) cell 5480 +/- 990. metric: Km; raw value: 23 +/- 4; raw unit: uM; normalized value: 0.023 mM; metric: kcat; raw value: 125 +/- 5; raw unit: min^-1; normalized value: 2.083 s^(-1); metric: kcat/Km; raw value: 5480 +/- 990; raw unit: mM^-1 min^-1; normalized value: 91.33333333333333 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 23 +/- 4 uM in the Mouse ADH4 column; 23 uM / 1000 = 0.023 mM, which is the catalog km exactly. kcat: printed cell 125 +/- 5 min^-1 in the Mouse ADH4 column; 125 min^-1 / 60 = 2.0833333333333335 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 2.083 s^-1, so the paper kcat field carries the catalog value 2.083 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 5480 +/- 990 mM^-1 min^-1 in the Mouse ADH4 column; 5480 mM^-1 min^-1 / 60 = 91.33333333333333 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 90.56521739130436 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (2.083 / 0.023). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 125 min^-1 / 0.023 mM = 5434.782608695652 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | all-trans-retinol | Km (uM) | 30 +/- 8 | 33 +/- 9 | 15 +/- 4 | 31 +/- 5 | 23 +/- 4 | | kcat row: | all-trans-retinol | kcat (min^-1) | 1.7 +/- 0.1 | 15 +/- 1 | 67 +/- 10 | 55 +/- 3 | 125 +/- 5 | | kcat/Km row: | all-trans-retinol | kcat/Km (mM^-1 min^-1) | 57 +/- 16 | 455 +/- 130 | 4500 +/- 1370 | 1775 +/- 300 | 5480 +/- 990 | | Mouse ADH4 column cells read: Km = 23 +/- 4 uM; kcat = 125 +/- 5 min^-1; kcat/Km = 5480 +/- 990 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH4 | all-trans-retinol

substrate: Retinol


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: all-trans-retinal. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 9.3 +/- 1.1, kcat (min^-1) cell 19 +/- 1, kcat/Km (mM^-1 min^-1) cell 2045 +/- 265. metric: Km; raw value: 9.3 +/- 1.1; raw unit: uM; normalized value: 0.0093 mM; metric: kcat; raw value: 19 +/- 1; raw unit: min^-1; normalized value: 0.317 s^(-1); metric: kcat/Km; raw value: 2045 +/- 265; raw unit: mM^-1 min^-1; normalized value: 34.083333333333336 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 9.3 +/- 1.1 uM in the Mouse ADH1 column; 9.3 uM / 1000 = 0.0093 mM, while the catalog stores km 0.009 mM. The conversion terminates, so this is a value disagreement and not an unavoidable rounding, and km is a corrected field. kcat: printed cell 19 +/- 1 min^-1 in the Mouse ADH1 column; 19 min^-1 / 60 = 0.31666666666666665 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.317 s^-1, so the paper kcat field carries the catalog value 0.317 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 2045 +/- 265 mM^-1 min^-1 in the Mouse ADH1 column; 2045 mM^-1 min^-1 / 60 = 34.083333333333336 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 35.22222222222223 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.317 / 0.009). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 19 min^-1 / 0.0093 mM = 2043.010752688172 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | all-trans-retinal | Km (uM) | 11 +/- 2 | 12 +/- 3 | 34 +/- 6 | 9.3 +/- 1.1 | 11 +/- 2 | | kcat row: | all-trans-retinal | kcat (min^-1) | 1.1 +/- 0.1 | 33 +/- 3 | 110 +/- 25 | 19 +/- 1 | 33 +/- 2 | | kcat/Km row: | all-trans-retinal | kcat/Km (mM^-1 min^-1) | 100 +/- 20 | 2750 +/- 730 | 3300 +/- 960 | 2045 +/- 265 | 3000 +/- 525 | | Mouse ADH1 column cells read: Km = 9.3 +/- 1.1 uM; kcat = 19 +/- 1 min^-1; kcat/Km = 2045 +/- 265 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Mouse ADH1 | all-trans-retinal


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 9-cis-retinal. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 15 +/- 2, kcat (min^-1) cell 190 +/- 5, kcat/Km (mM^-1 min^-1) cell 12800 +/- 1740. metric: Km; raw value: 15 +/- 2; raw unit: uM; normalized value: 0.015 mM; metric: kcat; raw value: 190 +/- 5; raw unit: min^-1; normalized value: 3.167 s^(-1); metric: kcat/Km; raw value: 12800 +/- 1740; raw unit: mM^-1 min^-1; normalized value: 213.33333333333334 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 15 +/- 2 uM in the Mouse ADH4 column; 15 uM / 1000 = 0.015 mM, which is the catalog km exactly. kcat: printed cell 190 +/- 5 min^-1 in the Mouse ADH4 column; 190 min^-1 / 60 = 3.1666666666666665 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 3.167 s^-1, so the paper kcat field carries the catalog value 3.167 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 12800 +/- 1740 mM^-1 min^-1 in the Mouse ADH4 column; 12800 mM^-1 min^-1 / 60 = 213.33333333333334 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 211.13333333333333 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (3.167 / 0.015). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 190 min^-1 / 0.015 mM = 12666.666666666666 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 9-cis-retinal | Km (uM) | 11 +/- 2 | 4.1 +/- 0.9 | 21 +/- 5 | 13 +/- 2 | 15 +/- 2 | | kcat row: | 9-cis-retinal | kcat (min^-1) | 1.8 +/- 0.2 | 2.7 +/- 0.1 | 190 +/- 25 | 17 +/- 1 | 190 +/- 5 | | kcat/Km row: | 9-cis-retinal | kcat/Km (mM^-1 min^-1) | 165 +/- 35 | 660 +/- 145 | 8980 +/- 2350 | 1310 +/- 215 | 12800 +/- 1740 | | Mouse ADH4 column cells read: Km = 15 +/- 2 uM; kcat = 190 +/- 5 min^-1; kcat/Km = 12800 +/- 1740 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Mouse ADH4 | 9-cis-retinal


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 26 +/- 7, kcat (min^-1) cell 7.4 +/- 0.5, kcat/Km (mM^-1 min^-1) cell 285 +/- 80. metric: Km; raw value: 26 +/- 7; raw unit: uM; normalized value: 0.026 mM; metric: kcat; raw value: 7.4 +/- 0.5; raw unit: min^-1; normalized value: 0.123 s^(-1); metric: kcat/Km; raw value: 285 +/- 80; raw unit: mM^-1 min^-1; normalized value: 4.75 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 26 +/- 7 uM in the Mouse ADH1 column; 26 uM / 1000 = 0.026 mM, which is the catalog km exactly. kcat: printed cell 7.4 +/- 0.5 min^-1 in the Mouse ADH1 column; 7.4 min^-1 / 60 = 0.12333333333333334 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.123 s^-1, so the paper kcat field carries the catalog value 0.123 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 285 +/- 80 mM^-1 min^-1 in the Mouse ADH1 column; 285 mM^-1 min^-1 / 60 = 4.75 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 4.730769230769231 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.123 / 0.026). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 7.4 min^-1 / 0.026 mM = 284.61538461538464 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinal | Km (uM) | 15 +/- 3 | 16 +/- 4 | 21 +/- 3 | 26 +/- 7 | 28 +/- 3 | | kcat row: | 11-cis-retinal | kcat (min^-1) | 0.31 +/- 0.02 | 3.4 +/- 0.1 | 18 +/- 2 | 7.4 +/- 0.5 | 34 +/- 1 | | kcat/Km row: | 11-cis-retinal | kcat/Km (mM^-1 min^-1) | 21 +/- 4 | 215 +/- 55 | 860 +/- 155 | 285 +/- 80 | 1215 +/- 135 | | Mouse ADH1 column cells read: Km = 26 +/- 7 uM; kcat = 7.4 +/- 0.5 min^-1; kcat/Km = 285 +/- 80 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Mouse ADH1 | 11-cis-retinal


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 11-cis-retinol. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 23 +/- 6, kcat (min^-1) cell 225 +/- 5, kcat/Km (mM^-1 min^-1) cell 9740 +/- 2550. metric: Km; raw value: 23 +/- 6; raw unit: uM; normalized value: 0.023 mM; metric: kcat; raw value: 225 +/- 5; raw unit: min^-1; normalized value: 3.75 s^(-1); metric: kcat/Km; raw value: 9740 +/- 2550; raw unit: mM^-1 min^-1; normalized value: 162.33333333333334 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 23 +/- 6 uM in the Mouse ADH4 column; 23 uM / 1000 = 0.023 mM, which is the catalog km exactly. kcat: printed cell 225 +/- 5 min^-1 in the Mouse ADH4 column; 225 min^-1 / 60 = 3.75 s^-1, an exact terminating conversion, which is the catalog kcat exactly. kcat/Km: the paper prints an independent catalytic-efficiency cell 9740 +/- 2550 mM^-1 min^-1 in the Mouse ADH4 column; 9740 mM^-1 min^-1 / 60 = 162.33333333333334 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 163.04347826086956 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (3.75 / 0.023). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 225 min^-1 / 0.023 mM = 9782.608695652174 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinol | Km (uM) | 35 +/- 7 | 18 +/- 4 | 28 +/- 5 | 34 +/- 9 | 23 +/- 6 | | kcat row: | 11-cis-retinol | kcat (min^-1) | 0.85 +/- 0.04 | 9.5 +/- 1.0 | 190 +/- 20 | 25 +/- 2 | 225 +/- 5 | | kcat/Km row: | 11-cis-retinol | kcat/Km (mM^-1 min^-1) | 24 +/- 5 | 530 +/- 55 | 6790 +/- 1400 | 735 +/- 205 | 9740 +/- 2550 | | Mouse ADH4 column cells read: Km = 23 +/- 6 uM; kcat = 225 +/- 5 min^-1; kcat/Km = 9740 +/- 2550 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH4 | 11-cis-retinol


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 28 +/- 3, kcat (min^-1) cell 34 +/- 1, kcat/Km (mM^-1 min^-1) cell 1215 +/- 135. metric: Km; raw value: 28 +/- 3; raw unit: uM; normalized value: 0.028 mM; metric: kcat; raw value: 34 +/- 1; raw unit: min^-1; normalized value: 0.567 s^(-1); metric: kcat/Km; raw value: 1215 +/- 135; raw unit: mM^-1 min^-1; normalized value: 20.25 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 28 +/- 3 uM in the Mouse ADH4 column; 28 uM / 1000 = 0.028 mM, which is the catalog km exactly. kcat: printed cell 34 +/- 1 min^-1 in the Mouse ADH4 column; 34 min^-1 / 60 = 0.5666666666666667 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.567 s^-1, so the paper kcat field carries the catalog value 0.567 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 1215 +/- 135 mM^-1 min^-1 in the Mouse ADH4 column; 1215 mM^-1 min^-1 / 60 = 20.25 s^-1 mM^-1, which is the catalog kcat_over_km 20.249999999999996 at export precision.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 11-cis-retinal | Km (uM) | 15 +/- 3 | 16 +/- 4 | 21 +/- 3 | 26 +/- 7 | 28 +/- 3 | | kcat row: | 11-cis-retinal | kcat (min^-1) | 0.31 +/- 0.02 | 3.4 +/- 0.1 | 18 +/- 2 | 7.4 +/- 0.5 | 34 +/- 1 | | kcat/Km row: | 11-cis-retinal | kcat/Km (mM^-1 min^-1) | 21 +/- 4 | 215 +/- 55 | 860 +/- 155 | 285 +/- 80 | 1215 +/- 135 | | Mouse ADH4 column cells read: Km = 28 +/- 3 uM; kcat = 34 +/- 1 min^-1; kcat/Km = 1215 +/- 135 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Mouse ADH4 | 11-cis-retinal


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 9-cis-retinol. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 8 +/- 1.1, kcat (min^-1) cell 23 +/- 1, kcat/Km (mM^-1 min^-1) cell 2900 +/- 455. metric: Km; raw value: 8 +/- 1.1; raw unit: uM; normalized value: 0.008 mM; metric: kcat; raw value: 23 +/- 1; raw unit: min^-1; normalized value: 0.383 s^(-1); metric: kcat/Km; raw value: 2900 +/- 455; raw unit: mM^-1 min^-1; normalized value: 48.333333333333336 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 8 +/- 1.1 uM in the Mouse ADH1 column; 8 uM / 1000 = 0.008 mM, which is the catalog km exactly. kcat: printed cell 23 +/- 1 min^-1 in the Mouse ADH1 column; 23 min^-1 / 60 = 0.38333333333333336 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.383 s^-1, so the paper kcat field carries the catalog value 0.383 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 2900 +/- 455 mM^-1 min^-1 in the Mouse ADH1 column; 2900 mM^-1 min^-1 / 60 = 48.333333333333336 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 47.875 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.383 / 0.008). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 23 min^-1 / 0.008 mM = 2875.0 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 9-cis-retinol | Km (uM) | 11 +/- 3 | 23 +/- 5 | 36 +/- 4 | 8 +/- 1.1 | 21 +/- 3 | | kcat row: | 9-cis-retinol | kcat (min^-1) | 0.89 +/- 0.06 | 3.6 +/- 0.4 | 475 +/- 44 | 23 +/- 1 | 340 +/- 15 | | kcat/Km row: | 9-cis-retinol | kcat/Km (mM^-1 min^-1) | 81 +/- 23 | 160 +/- 40 | 13200 +/- 2020 | 2900 +/- 455 | 16100 +/- 2400 | | Mouse ADH1 column cells read: Km = 8 +/- 1.1 uM; kcat = 23 +/- 1 min^-1; kcat/Km = 2900 +/- 455 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH1 | 9-cis-retinol


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: 9-cis-retinol. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 21 +/- 3, kcat (min^-1) cell 340 +/- 15, kcat/Km (mM^-1 min^-1) cell 16100 +/- 2400. metric: Km; raw value: 21 +/- 3; raw unit: uM; normalized value: 0.021 mM; metric: kcat; raw value: 340 +/- 15; raw unit: min^-1; normalized value: 5.667 s^(-1); metric: kcat/Km; raw value: 16100 +/- 2400; raw unit: mM^-1 min^-1; normalized value: 268.3333333333333 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 21 +/- 3 uM in the Mouse ADH4 column; 21 uM / 1000 = 0.021 mM, which is the catalog km exactly. kcat: printed cell 340 +/- 15 min^-1 in the Mouse ADH4 column; 340 min^-1 / 60 = 5.666666666666667 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 5.667 s^-1, so the paper kcat field carries the catalog value 5.667 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 16100 +/- 2400 mM^-1 min^-1 in the Mouse ADH4 column; 16100 mM^-1 min^-1 / 60 = 268.3333333333333 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 269.85714285714283 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (5.667 / 0.021). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 340 min^-1 / 0.021 mM = 16190.47619047619 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 9-cis-retinol | Km (uM) | 11 +/- 3 | 23 +/- 5 | 36 +/- 4 | 8 +/- 1.1 | 21 +/- 3 | | kcat row: | 9-cis-retinol | kcat (min^-1) | 0.89 +/- 0.06 | 3.6 +/- 0.4 | 475 +/- 44 | 23 +/- 1 | 340 +/- 15 | | kcat/Km row: | 9-cis-retinol | kcat/Km (mM^-1 min^-1) | 81 +/- 23 | 160 +/- 40 | 13200 +/- 2020 | 2900 +/- 455 | 16100 +/- 2400 | | Mouse ADH4 column cells read: Km = 21 +/- 3 uM; kcat = 340 +/- 15 min^-1; kcat/Km = 16100 +/- 2400 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH4 | 9-cis-retinol


column_label: Table label: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers. Substrate block: all-trans-retinol. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 2 block: Km (uM) cell 31 +/- 5, kcat (min^-1) cell 55 +/- 3, kcat/Km (mM^-1 min^-1) cell 1775 +/- 300. metric: Km; raw value: 31 +/- 5; raw unit: uM; normalized value: 0.031 mM; metric: kcat; raw value: 55 +/- 3; raw unit: min^-1; normalized value: 0.917 s^(-1); metric: kcat/Km; raw value: 1775 +/- 300; raw unit: mM^-1 min^-1; normalized value: 29.583333333333332 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 2.4 mM NAD+ (0.3 mM for mouse ADH1) for the retinol oxidations; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 31 +/- 5 uM in the Mouse ADH1 column; 31 uM / 1000 = 0.031 mM, which is the catalog km exactly. kcat: printed cell 55 +/- 3 min^-1 in the Mouse ADH1 column; 55 min^-1 / 60 = 0.9166666666666666 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.917 s^-1, so the paper kcat field carries the catalog value 0.917 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 1775 +/- 300 mM^-1 min^-1 in the Mouse ADH1 column; 1775 mM^-1 min^-1 / 60 = 29.583333333333332 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 29.580645161290324 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.917 / 0.031). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 55 min^-1 / 0.031 mM = 1774.1935483870968 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 2 Kinetic constants of alcohol dehydrogenases with retinol isomers | decoded plain-numeral Table 2 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | all-trans-retinol | Km (uM) | 30 +/- 8 | 33 +/- 9 | 15 +/- 4 | 31 +/- 5 | 23 +/- 4 | | kcat row: | all-trans-retinol | kcat (min^-1) | 1.7 +/- 0.1 | 15 +/- 1 | 67 +/- 10 | 55 +/- 3 | 125 +/- 5 | | kcat/Km row: | all-trans-retinol | kcat/Km (mM^-1 min^-1) | 57 +/- 16 | 455 +/- 130 | 4500 +/- 1370 | 1775 +/- 300 | 5480 +/- 990 | | Mouse ADH1 column cells read: Km = 31 +/- 5 uM; kcat = 55 +/- 3 min^-1; kcat/Km = 1775 +/- 300 mM^-1 min^-1 | table caption: Table 2. Kinetic constants of alcohol dehydrogenases with retinol isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 2.4 mM NAD+ (0.3 mM for mouse ADH1), at 25 C.

row_label: Mouse ADH1 | all-trans-retinol


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 9-cis-retinal. Enzyme column: Mouse ADH1. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 13 +/- 2, kcat (min^-1) cell 17 +/- 1, kcat/Km (mM^-1 min^-1) cell 1310 +/- 215. metric: Km; raw value: 13 +/- 2; raw unit: uM; normalized value: 0.013 mM; metric: kcat; raw value: 17 +/- 1; raw unit: min^-1; normalized value: 0.283 s^(-1); metric: kcat/Km; raw value: 1310 +/- 215; raw unit: mM^-1 min^-1; normalized value: 21.833333333333332 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 13 +/- 2 uM in the Mouse ADH1 column; 13 uM / 1000 = 0.013 mM, which is the catalog km exactly. kcat: printed cell 17 +/- 1 min^-1 in the Mouse ADH1 column; 17 min^-1 / 60 = 0.2833333333333333 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.283 s^-1, so the paper kcat field carries the catalog value 0.283 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 1310 +/- 215 mM^-1 min^-1 in the Mouse ADH1 column; 1310 mM^-1 min^-1 / 60 = 21.833333333333332 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 21.769230769230766 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.283 / 0.013). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 17 min^-1 / 0.013 mM = 1307.6923076923076 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 9-cis-retinal | Km (uM) | 11 +/- 2 | 4.1 +/- 0.9 | 21 +/- 5 | 13 +/- 2 | 15 +/- 2 | | kcat row: | 9-cis-retinal | kcat (min^-1) | 1.8 +/- 0.2 | 2.7 +/- 0.1 | 190 +/- 25 | 17 +/- 1 | 190 +/- 5 | | kcat/Km row: | 9-cis-retinal | kcat/Km (mM^-1 min^-1) | 165 +/- 35 | 660 +/- 145 | 8980 +/- 2350 | 1310 +/- 215 | 12800 +/- 1740 | | Mouse ADH1 column cells read: Km = 13 +/- 2 uM; kcat = 17 +/- 1 min^-1; kcat/Km = 1310 +/- 215 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Mouse ADH1 | 9-cis-retinal


organism: Mycobacterium sp.

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


substrate_name: Butanal

sequence_source: UniProtKB:W8VSK8 direct lookup on 2026-05-31

smiles: CCCC=O

substrate: Butanal


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Ogataea angusta

substrate_name: ethanol

sequence_source: UniProtKB:H9ZGN0 direct lookup on 2026-05-31

substrate: ethanol


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Pyrobaculum calidifontis

substrate_name: Glutaraldehyde

sequence_source: UniProtKB:A3MVR8 direct lookup on 2026-05-31

smiles: O=CCCCC=O

assay_conditions_summary: pH 6; 333.15 K; cofactor NADH

substrate: Glutaraldehyde


smiles: OCCCCO

assay_conditions_summary: pH 10; 333.15 K; cofactor NADH


organism: Rattus norvegicus

sequence_source: UniProtKB:P12711 direct lookup on 2026-05-31

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'Butanal'; isoenzyme column group ADH-3; Km (mM) cell = 0.09; kcat (min^-1) cell = 440; kcat/Km (mM^-1 min^-1) cell = 4900.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.09 mM; already in mM, no unit conversion applies; the exported value is 0.09 mM. kcat: printed Table 6 cell 440 min^-1; the printed turnover column is per MINUTE, so 440 / 60 = 7.333333333333333 s^(-1); the exported value is 7.333 s^(-1). kcat/Km: printed Table 6 cell 4900 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 4900 / 60 = 81.66666666666667 s^(-1)*mM^(-1); the exported value is 81.47777777777779 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'Butanal', isoenzyme column ADH-3: Km = 0.09 mM; kcat = 440 min^-1; kcat/Km = 4900 mM^-1 min^-1.

table_label: Table 6: Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5 (Eur. J. Biochem. 1987, 162(1): 179-189); printed column heads Substrate | ADH-1 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1) | ADH-2 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1) | ADH-3 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1)


sequence_source: UniProtKB:P06757 direct lookup on 2026-05-31

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row 'Cyclohexanol'; isoenzyme column group ADH-1; Km (mM) cell = 220; kcat (min^-1) cell = 105; kcat/Km (mM^-1 min^-1) cell = 0.5.

normalized_value_unit_evidence: Km: printed Table 5 cell 220 mM; already in mM, no unit conversion applies; the exported value is 220.0 mM. kcat: printed Table 5 cell 105 min^-1; the printed turnover column is per MINUTE, so 105 / 60 = 1.75 s^(-1); the exported value is 1.75 s^(-1). kcat/Km: printed Table 5 cell 0.5 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 0.5 / 60 = 0.008333333333333333 s^(-1)*mM^(-1); the exported value is 0.007954545454545454 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row 'Cyclohexanol', isoenzyme column ADH-1: Km = 220 mM; kcat = 105 min^-1; kcat/Km = 0.5 mM^-1 min^-1.

table_label: Table 5: Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0 (Eur. J. Biochem. 1987, 162(1): 179-189); printed column heads Substrate | ADH-1 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1) | ADH-2 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1) | ADH-3 (Km mM, kcat min^-1, kcat/Km mM^-1 min^-1)


sequence_source: UniProtKB reviewed accession P06757 FASTA, direct lookup on 2026-05-31

column_label: Table 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'Octanal'; isoenzyme column group ADH-1; Km (mM) cell = 0.3; kcat (min^-1) cell = 23400; kcat/Km (mM^-1 min^-1) cell = 78000.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.3 mM; already in mM, no unit conversion applies; the exported value is 0.3 mM. kcat: printed Table 6 cell 23400 min^-1; the printed turnover column is per MINUTE, so 23400 / 60 = 390.0 s^(-1); the exported value is 390.0 s^(-1). kcat/Km: printed Table 6 cell 78000 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 78000 / 60 = 1300.0 s^(-1)*mM^(-1); the exported value is 1300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'Octanal', isoenzyme column ADH-1: Km = 0.3 mM; kcat = 23400 min^-1; kcat/Km = 78000 mM^-1 min^-1.


sequence_source: UniProtKB reviewed accession P12711 FASTA, direct lookup on 2026-05-31


column_label: Table 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'Acetaldehyde'; isoenzyme column group ADH-3; Km (mM) cell = 0.17; kcat (min^-1) cell = 170; kcat/Km (mM^-1 min^-1) cell = 1000.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.17 mM; already in mM, no unit conversion applies; the exported value is 0.17 mM. kcat: printed Table 6 cell 170 min^-1; the printed turnover column is per MINUTE, so 170 / 60 = 2.8333333333333335 s^(-1); the exported value is 2.833 s^(-1). kcat/Km: printed Table 6 cell 1000 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 1000 / 60 = 16.666666666666668 s^(-1)*mM^(-1); the exported value is 16.66470588235294 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'Acetaldehyde', isoenzyme column ADH-3: Km = 0.17 mM; kcat = 170 min^-1; kcat/Km = 1000 mM^-1 min^-1.


substrate_name: 12-Hydroxydodecanoic acid

substrate: 12-Hydroxydodecanoic acid


smiles: CCCCCO