enzyme_display_name: alcohol dehydrogenase

organism: Homo sapiens

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

smiles: CCCCCCCCO

data_origin: experimental

enzyme: alcohol dehydrogenase

status: unverified

source: oed


substrate_name: methanol

smiles: CO

proof_lines: Kinetic properties of human liver alcohol dehydrogenase: oxidation of alcohols by class I isoenzymes

substrate: methanol


substrate_name: 12-Hydroxydodecanoic acid

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M141L with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

mutation_type: substitution


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 21 +/- 3, kcat (min^-1) cell 18 +/- 2, kcat/Km (mM^-1 min^-1) cell 860 +/- 155. metric: Km; raw value: 21 +/- 3; raw unit: uM; normalized value: 0.021 mM; metric: kcat; raw value: 18 +/- 2; raw unit: min^-1; normalized value: 0.3 s^(-1); metric: kcat/Km; raw value: 860 +/- 155; raw unit: mM^-1 min^-1; normalized value: 14.333333333333334 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 21 +/- 3 uM in the Human ADH4 column; 21 uM / 1000 = 0.021 mM, which is the catalog km exactly. kcat: printed cell 18 +/- 2 min^-1 in the Human ADH4 column; 18 min^-1 / 60 = 0.3 s^-1, an exact terminating conversion, which is the catalog kcat exactly. kcat/Km: the paper prints an independent catalytic-efficiency cell 860 +/- 155 mM^-1 min^-1 in the Human ADH4 column; 860 mM^-1 min^-1 / 60 = 14.333333333333334 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 14.285714285714285 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.3 / 0.021). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 18 min^-1 / 0.021 mM = 857.1428571428571 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 ADH4 column cells read: Km = 21 +/- 3 uM; kcat = 18 +/- 2 min^-1; kcat/Km = 860 +/- 155 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 | 11-cis-retinal


organism: Mus musculus

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


verification_status: verified

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

status: verified


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

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


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


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


organism: Arabidopsis thaliana


organism: Branchiostoma lanceolatum


organism: Coturnix coturnix japonica


organism: Equus caballus


sequence_variant_note: Mutation signature D57L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature D57L/Y93F could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y93F to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

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 '12-Hydroxydodecanoic acid'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 1200; kcat/Km (mM^-1 min^-1) cell = 860.

normalized_value_unit_evidence: Km: printed Table 5 cell 1.4 mM; already in mM, no unit conversion applies; the exported value is 1.4 mM. kcat: printed Table 5 cell 1200 min^-1; the printed turnover column is per MINUTE, so 1200 / 60 = 20.0 s^(-1); the exported value is 20.0 s^(-1). kcat/Km: printed Table 5 cell 860 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 860 / 60 = 14.333333333333334 s^(-1)*mM^(-1); the exported value is 14.285714285714286 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '12-Hydroxydodecanoic acid', isoenzyme column ADH-1: Km = 1.4 mM; kcat = 1200 min^-1; kcat/Km = 860 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)


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 '12-Hydroxydodecanoic acid'; isoenzyme column group ADH-2; Km (mM) cell = 0.1; kcat (min^-1) cell = 230; kcat/Km (mM^-1 min^-1) cell = 2300.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.1 mM; already in mM, no unit conversion applies; the exported value is 0.1 mM. kcat: printed Table 5 cell 230 min^-1; the printed turnover column is per MINUTE, so 230 / 60 = 3.8333333333333335 s^(-1); the exported value is 3.833 s^(-1). kcat/Km: printed Table 5 cell 2300 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 2300 / 60 = 38.333333333333336 s^(-1)*mM^(-1); the exported value is 38.33 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '12-Hydroxydodecanoic acid', isoenzyme column ADH-2: Km = 0.1 mM; kcat = 230 min^-1; kcat/Km = 2300 mM^-1 min^-1.


organism: Geobacillus stearothermophilus

substrate_name: 12-hydroxylauric acid methyl ester

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C257L to reconstruct the assayed variant sequence.

smiles: COC(=O)CCCCCCCCCCCO

substrate: 12-hydroxylauric acid methyl ester


substrate_name: 12-oxolauric acid methyl ester

smiles: COC(=O)CCCCCCCCCCC=O

substrate: 12-oxolauric acid methyl ester


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 13-cis-retinal. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 25 +/- 6, kcat (min^-1) cell 11 +/- 1, kcat/Km (mM^-1 min^-1) cell 440 +/- 115. metric: Km; raw value: 25 +/- 6; raw unit: uM; normalized value: 0.025 mM; metric: kcat; raw value: 11 +/- 1; raw unit: min^-1; normalized value: 0.183 s^(-1); metric: kcat/Km; raw value: 440 +/- 115; raw unit: mM^-1 min^-1; normalized value: 7.333333333333333 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 25 +/- 6 uM in the Human ADH4 column; 25 uM / 1000 = 0.025 mM, which is the catalog km exactly. kcat: printed cell 11 +/- 1 min^-1 in the Human ADH4 column; 11 min^-1 / 60 = 0.18333333333333332 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.183 s^-1, so the paper kcat field carries the catalog value 0.183 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 440 +/- 115 mM^-1 min^-1 in the Human ADH4 column; 440 mM^-1 min^-1 / 60 = 7.333333333333333 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 7.319999999999999 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.183 / 0.025). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 11 min^-1 / 0.025 mM = 440.0 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: | 13-cis-retinal | Km (uM) | NA | NA | 25 +/- 6 | ND | ND | | kcat row: | 13-cis-retinal | kcat (min^-1) | NA | NA | 11 +/- 1 | ND | ND | | kcat/Km row: | 13-cis-retinal | kcat/Km (mM^-1 min^-1) | NA | NA | 440 +/- 115 | ND | ND | | Human ADH4 column cells read: Km = 25 +/- 6 uM; kcat = 11 +/- 1 min^-1; kcat/Km = 440 +/- 115 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 | 13-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


smiles: OCCCO


organism: Pyrobaculum calidifontis

smiles: OCCCCO


smiles: OCCCCCCO


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

substrate: 16-Hydroxyhexadecanoic acid


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) 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

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: CCCCO


organism: Drosophila lebanonensis


assay_conditions_summary: pH 7.3; 303.15 K; buffer 1 mM NAD+". The; cofactor NAD+

column_label: Table III (journal page 12594); row `Butanol`; column group `EqADH`; column `V1` (unit row `s^-1`) = 5.2; column `Km` (unit row `mM`) = 0.27. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 5.2 s^-1 -> 5.2 s^-1; catalog holds 5.2 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 0.27 mM -> 0.27 mM; catalog holds 0.27 mM; no conversion. kcat/Km: not printed; catalog 19.25925925925926 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Butanol`, EqADH columns: V1 = 5.2 (unit row: s^-1); Km = 0.27 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

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

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


organism: Macaca mulatta

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


organism: Moraxella sp.

sequence: MLYANPNTESSPVGFRKKYDNFI

wild_type_sequence: MLYANPNTESSPVGFRKKYDNFI


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 '1-Butanol'; isoenzyme column group ADH-3; Km (mM) cell = 0.17; kcat (min^-1) cell = 50; kcat/Km (mM^-1 min^-1) cell = 300.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.17 mM; already in mM, no unit conversion applies; the exported value is 0.17 mM. kcat: printed Table 5 cell 50 min^-1; the printed turnover column is per MINUTE, so 50 / 60 = 0.8333333333333334 s^(-1); the exported value is 0.833 s^(-1). kcat/Km: printed Table 5 cell 300 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 300 / 60 = 5.0 s^(-1)*mM^(-1); the exported value is 4.8999999999999995 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '1-Butanol', isoenzyme column ADH-3: Km = 0.17 mM; kcat = 50 min^-1; kcat/Km = 300 mM^-1 min^-1.


organism: Sulfolobus solfataricus

proof_lines: Role of tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase


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'

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'


organism: Aeropyrum pernix

smiles: CCCCCCO


assay_conditions_summary: pH 7.3; 303.15 K; buffer 1 mM NAD+." The; cofactor NAD+

column_label: Table III (journal page 12594); row `Hexanol`; column group `EqADH`; column `V1` (printed unit row `s^-1`) = 3.8; column `Km` (printed unit row `mM`) = 0.076. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 3.8 s^-1 -> 3.8 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.076 mM -> 0.076 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, 3.8 s^-1 / 0.076 mM = 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Hexanol`, EqADH columns: V1 = 3.8 (printed unit row: s^-1); Km = 0.076 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

row_label: Table III row `Hexanol`, EqADH column group


column_label: Table III (journal page 12594); row `Hexanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 1.6; column `Km` (unit row `mM`) = 0.032. 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 0.032 mM -> 0.032 mM; catalog holds 0.032 mM; no conversion. kcat/Km: not printed; catalog 50.0 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Hexanol`, MmADHalpha columns: V1 = 1.6 (unit row: s^-1); Km = 0.032 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

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


organism: Sulfolobus acidocaldarius


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'


smiles: CCCCCCCC=O


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.

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_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.


organism: Struthio camelus


smiles: CCCCCO


column_label: Table III (journal page 12594); row `Pentanol`; column group `EqADH`; column `V1` (printed unit row `s^-1`) = 4.3; column `Km` (printed unit row `mM`) = 0.15. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 4.3 s^-1 -> 4.3 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.15 mM -> 0.15 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, 4.3 s^-1 / 0.15 mM = 28.666666666666668 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Pentanol`, EqADH columns: V1 = 4.3 (printed unit row: s^-1); Km = 0.15 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

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


assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+

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


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 '1-Pentanol'; isoenzyme column group ADH-1; Km (mM) cell = 3.1; kcat (min^-1) cell = 2930; kcat/Km (mM^-1 min^-1) cell = 950.

normalized_value_unit_evidence: Km: printed Table 5 cell 3.1 mM; already in mM, no unit conversion applies; the exported value is 3.1 mM. kcat: printed Table 5 cell 2930 min^-1; the printed turnover column is per MINUTE, so 2930 / 60 = 48.833333333333336 s^(-1); the exported value is 48.833 s^(-1). kcat/Km: printed Table 5 cell 950 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 950 / 60 = 15.833333333333334 s^(-1)*mM^(-1); the exported value is 15.75258064516129 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '1-Pentanol', isoenzyme column ADH-1: Km = 3.1 mM; kcat = 2930 min^-1; kcat/Km = 950 mM^-1 min^-1.


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 '1-Pentanol'; isoenzyme column group ADH-2; Km (mM) cell = 78; kcat (min^-1) cell = 212; kcat/Km (mM^-1 min^-1) cell = 2.7.

normalized_value_unit_evidence: Km: printed Table 5 cell 78 mM; already in mM, no unit conversion applies; the exported value is 78.0 mM. kcat: printed Table 5 cell 212 min^-1; the printed turnover column is per MINUTE, so 212 / 60 = 3.533333333333333 s^(-1); the exported value is 3.533 s^(-1). kcat/Km: printed Table 5 cell 2.7 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 2.7 / 60 = 0.045000000000000005 s^(-1)*mM^(-1); the exported value is 0.045294871794871794 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '1-Pentanol', isoenzyme column ADH-2: Km = 78 mM; kcat = 212 min^-1; kcat/Km = 2.7 mM^-1 min^-1.


organism: Thermococcus kodakarensis

assay_conditions_summary: pH 9; 343.15 K; buffer 50 mM glycine-NaOH; cofactor NAD+

column_label: Table 4. Kinetic parameters for TkADH; substrate cell `(RS)-1-Phenylethanol (0-200 b)`; cosubstrate cell `NAD+ (1.0)`; column `Apparent Km (mM)` = 244 (printed with its error term); column `kcat (s^-1)` = 35.7 (printed with its error term); column `kcat/Km (s^-1 mM^-1)` = 0.15 +/- 0.02 (printed, rounded).

normalized_value_unit_evidence: Km: paper cell 244 mM -> 244.0 mM; catalog holds 244.0 mM; no conversion (the paper's Km column already prints mM, so no uM/1000 step applies). kcat: paper cell 35.7 s^-1 -> 35.7 s^-1; catalog holds 35.7 s^(-1); no conversion (the paper's kcat column already prints s^-1, so no min^-1/60 step applies). kcat/Km: the paper prints 0.15 +/- 0.02 s^-1 mM^-1 for this row, but the catalog holds 0.14631147540983608 s^(-1)*mM^(-1), which is exactly 35.7 / 244.

raw_value_unit_evidence: Table 4, substrate row `(RS)-1-Phenylethanol (0-200 b)`, cosubstrate `NAD+ (1.0)`: Apparent Km = 244 (column unit mM); kcat = 35.7 (column unit s^-1); printed kcat/Km = 0.15 +/- 0.02 (column unit s^-1 mM^-1).

row_label: Table 4 substrate row `(RS)-1-Phenylethanol (0-200 b)` with cosubstrate `NAD+ (1.0)`

table_label: Table 4. Kinetic parameters for TkADH


smiles: CCCO


column_label: Table III (journal page 12594); row `Propanol`; column group `EqADH`; column `V1` (printed unit row `s^-1`) = 8.2; column `Km` (printed unit row `mM`) = 0.39. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 8.2 s^-1 -> 8.2 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.39 mM -> 0.39 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, 8.2 s^-1 / 0.39 mM = 21.025641025641022 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Propanol`, EqADH columns: V1 = 8.2 (printed unit row: s^-1); Km = 0.39 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

row_label: Table III row `Propanol`, EqADH column group


organism: Homo sapiens


column_label: Table III (journal page 12594); row `Propanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 1.4; column `Km` (unit row `mM`) = 2.0. 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 2.0 mM -> 2.0 mM; catalog holds 2.0 mM; no conversion. kcat/Km: not printed; catalog 0.7 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Propanol`, MmADHalpha columns: V1 = 1.4 (unit row: s^-1); Km = 2.0 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

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


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'


assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row '2,2,2-Trifluoroacetophenone'; column kcat (s-1) = 10.0; column Km (mM) = 23.5; column kcat/Km (s-1 mM-1) = 0.42. captured primary segment: 2,2,2-Trifluoroacetophenone | kcat 10.0 s^-1 | Km 23.5 mM | kcat/Km 0.42 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 10.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 10.0 s^(-1). Km: printed Table 3 cell 23.5 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 23.5 mM. kcat/Km: printed Table 3 cell 0.42 s^-1 mM^-1; the printed unit is already the canonical s^(-1)*mM^(-1), so no unit conversion applies and the printed efficiency is 0.42 s^(-1)*mM^(-1). Quotient disclosure for this row: 10.0 / 23.5 = 0.4255319148936170 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.42 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row '2,2,2-Trifluoroacetophenone': kcat = 10.0 s^-1; Km = 23.5 mM; printed kcat/Km = 0.42 s^-1 mM^-1.


smiles: CC(O)C(C)O

column_label: Table 4. Kinetic parameters for TkADH; substrate cell `meso-2,3-Butanediol (0-250)`; cosubstrate cell `NAD+ (1.0)`; column `Apparent Km (mM)` = 61.3 (printed with its error term); column `kcat (s^-1)` = 43.8 (printed with its error term); column `kcat/Km (s^-1 mM^-1)` = 0.71 +/- 0.06 (printed, rounded).

normalized_value_unit_evidence: Km: paper cell 61.3 mM -> 61.3 mM; catalog holds 61.3 mM; no conversion (the paper's Km column already prints mM, so no uM/1000 step applies). kcat: paper cell 43.8 s^-1 -> 43.8 s^-1; catalog holds 43.8 s^(-1); no conversion (the paper's kcat column already prints s^-1, so no min^-1/60 step applies). kcat/Km: the paper prints 0.71 +/- 0.06 s^-1 mM^-1 for this row, but the catalog holds 0.7145187601957586 s^(-1)*mM^(-1), which is exactly 43.8 / 61.3.

raw_value_unit_evidence: Table 4, substrate row `meso-2,3-Butanediol (0-250)`, cosubstrate `NAD+ (1.0)`: Apparent Km = 61.3 (column unit mM); kcat = 43.8 (column unit s^-1); printed kcat/Km = 0.71 +/- 0.06 (column unit s^-1 mM^-1).

row_label: Table 4 substrate row `meso-2,3-Butanediol (0-250)` with cosubstrate `NAD+ (1.0)`


smiles: CCC(C)O


smiles: CCC(C)=O


smiles: CC=CCO


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 '2-Buten-1-ol'; isoenzyme column group ADH-2; Km (mM) cell = 60; kcat (min^-1) cell = 350; kcat/Km (mM^-1 min^-1) cell = 5.8.

normalized_value_unit_evidence: Km: printed Table 5 cell 60 mM; already in mM, no unit conversion applies; the exported value is 60.0 mM. kcat: printed Table 5 cell 350 min^-1; the printed turnover column is per MINUTE, so 350 / 60 = 5.833333333333333 s^(-1); the exported value is 5.833 s^(-1). kcat/Km: printed Table 5 cell 5.8 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 5.8 / 60 = 0.09666666666666666 s^(-1)*mM^(-1); the exported value is 0.09721666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row '2-Buten-1-ol', isoenzyme column ADH-2: Km = 60 mM; kcat = 350 min^-1; kcat/Km = 5.8 mM^-1 min^-1.


smiles: OCC=CCO


smiles: CCCCCCCCC(C)=O


organism: Sphingomonas sp. A1

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'KDG'; column 'K m (mM)' = 13 ± 3; column 'V max (mU mg-1)' = 2.8 x 10^3 ± 0.2 x 10^3; column 'k cat (s-1)' = 1.4 ± 0.08; column 'k cat/K m (mM-1 s-1)' = 10 x 10^-2 ± 3 x 10^-2; column 'k cat/K m (%)' = 100.

normalized_value_unit_evidence: Km: printed Table 1 cell 13 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 13.0 mM; the exported value is 13.0 mM. kcat: printed Table 1 cell 1.4 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.4 s^(-1); the exported value is 1.4 s^(-1). kcat/Km: printed Table 1 cell 10 x 10^-2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.1 s^(-1)*mM^(-1); the exported value is 0.10769230769230768 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'KDG': K m = 13 ± 3 mM; V max = 2.8 x 10^3 ± 0.2 x 10^3 mU mg^-1; k cat = 1.4 ± 0.08 s^-1; printed k cat/K m = 10 x 10^-2 ± 3 x 10^-2 mM^-1 s^-1; printed relative k cat/K m = 100 per cent.

row_label: Table 1, body row with substrate 'KDG'


organism: Yokenella sp.

smiles: C/C=C/CO

column_label: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Crotyl alcohol` with cosubstrate NADP^+ (0.4): Apparent Vmax (U mg^-1) = 156.7 +/- 3.8; Apparent Km (mM) = 9.1 +/- 0.8; Apparent Kis (mM) = 229 +/- 3.2; Kcat (s^-1) = 101 +/- 2.5; Kcat/Km (s^-1 mM^-1) = 11.0 +/- 1.0.

normalized_value_unit_evidence: kcat: printed cell 101 s^-1 -> 101 s^(-1); the catalog holds 101.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 9.1 mM -> 9.1 mM; the catalog holds 9.1 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `11.0` s^-1 mM^-1 for this row -> 11.0 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 11.098901098901099 s^(-1)*mM^(-1), which is the full-precision quotient 101 / 9.1 of the row's own kcat and Km cells and is not the printed ratio cell.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Crotyl alcohol` with cosubstrate NADP^+ (0.4): Km (mM) = 9.1; Kcat (s^-1) = 101; Kcat/Km (s^-1 mM^-1) = 11.0. Every one of these three numerals is printed in the Table 5 cell shown; the +/- terms are the SD reported by Table 5 footnote a.


smiles: C/C=C/C=O

assay_conditions_summary: pH 6.5; 338.15 K; cofactor NADPH

column_label: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Crotonaldehyde` with cosubstrate NADPH (0.4): Apparent Vmax (U mg^-1) = 629.4 +/- 25; Apparent Km (mM) = 3.3 +/- 0.2; Apparent Kis (mM) = 45.4 +/- 5.7; Kcat (s^-1) = 405 +/- 16; Kcat/Km (s^-1 mM^-1) = 122 +/- 8.9.

normalized_value_unit_evidence: kcat: printed cell 405 s^-1 -> 405 s^(-1); the catalog holds 405.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 3.3 mM -> 3.3 mM; the catalog holds 3.3 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `122` s^-1 mM^-1 for this row -> 122.0 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 122.72727272727273 s^(-1)*mM^(-1), which is the full-precision quotient 405 / 3.3 of the row's own kcat and Km cells and is not the printed ratio cell.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Crotonaldehyde` with cosubstrate NADPH (0.4): Km (mM) = 3.3; Kcat (s^-1) = 405; Kcat/Km (s^-1 mM^-1) = 122. Every one of these three numerals is printed in the Table 5 cell shown; the +/- terms are the SD reported by Table 5 footnote a.


smiles: CCCCCC(C)=O


smiles: CCCCC(C)O


smiles: CCCCC(C)=O


smiles: CCCCCCCC(C)=O

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

column_label: Table 2 (journal page 203), decoded transcription, substrate row `2-Nonanone`: kcat (s^-1) = 0.71; Km (mM) = 0.215; kcat/Km (s^-1 mM^-1) = 3.3.

normalized_value_unit_evidence: kcat: printed cell 0.71 s^-1 -> 0.71 s^(-1); the catalog holds 0.85 s^(-1); no unit conversion applied (the table prints s^-1 directly). Km: printed cell 0.215 mM -> 0.215 mM; the catalog holds 0.215 mM; no unit conversion applied (the table prints mM directly). kcat/Km: printed cell 3.3 s^-1 mM^-1 -> 3.3 s^(-1)*mM^(-1); no unit conversion applied. The paper PRINTS the kcat/Km cell `3.3` s^-1 mM^-1 for this row (Table 2, substrate row `2-Nonanone`), and that printed cell is the kcat_over_km value reported here. The catalog stores 3.953488372093023 s^(-1)*mM^(-1), which is the full-precision quotient of the catalog's own kcat and Km (0.85 / 0.215); it is not the printed cell and does not equal it at the printed decimal precision.

table_label: Table 2 'Kinetic constants for reduction of benzylaldehyde and ketones' (journal page 203)


smiles: CCCCCCC(C)=O


smiles: CCCC(C)O


smiles: CCCC(C)=O


smiles: CC(C)O


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 `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


column_label: Table label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids. Substrate block: 3,4-Didehydroretinol. Enzyme column: ADH1B2. Columns read: Km (uM) cell 24 +/- 5, kcat (min^-1) cell 5.3 +/- 0.4, kcat/Km (mM^-1 min^-1) cell 220 +/- 50. 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); explicit printed primary cell; assay condition: 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, 25 C (298.15 K); 2.4 mM NAD+ for retinol oxidations and 1 mM NADH (0.77 mM for ADH4) for retinal reductions; absorbance followed at 400 nm (450 nm for 3,4-didehydroretinal) on a Varian Cary 400 spectrophotometer; kcat computed with a molecular weight of 80,000 for the ADH dimer; recombinant human enzyme expressed in Escherichia coli BL21 as a GST fusion and released by thrombin digestion. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 24 +/- 5 uM in the ADH1B2 column; 24.0 uM / 1000 = 0.024 mM, which is the catalog km exactly. kcat: printed cell 5.3 +/- 0.4 min^-1 in the ADH1B2 column; 5.3 min^-1 / 60 = 0.0883333333 s^-1, and the catalog stores that quotient at its own three-decimal precision as 0.088 s^-1 (0.088 s^-1 x 60 = 5.28 min^-1, which is the printed cell at its printed precision), so the paper kcat field carries the catalog value 0.088. kcat/Km: printed cell 220 +/- 50 mM^-1 min^-1 in the ADH1B2 column; 220.0 mM^-1 min^-1 / 60 = 3.6666666666666665 s^-1 mM^-1, which is the catalog kcat_over_km exactly.

raw_value_unit_evidence: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids | column header row: | Substrate | Constant | ADH1B1 | ADH1B2 | ADH4 | | Km row: | 3,4-Didehydroretinol | Km (uM) | ND | 24 +/- 5 | 28 +/- 7 | | kcat row: | 3,4-Didehydroretinol | kcat (min^-1) |  | 5.3 +/- 0.4 | 150 +/- 14 | | kcat/Km row: | 3,4-Didehydroretinol | kcat/Km (mM^-1 min^-1) |  | 220 +/- 50 | 5400 +/- 1400 | | ADH1B2 column cells read: Km = 24 +/- 5 uM; kcat = 5.3 +/- 0.4 min^-1; kcat/Km = 220 +/- 50 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-Didehydroretinol


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


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


smiles: NCCCCO


smiles: CCCC(O)CCC


assay_conditions_summary: pH 7.5; 298.15 K; buffer 0; cofactor NAD+

column_label: Table 1 (Kinetic constants of human alcohol dehydrogenases with retinoids); substrate block '4-Hydroxy-retinol'; enzyme column head 'ADH1B2'; unit head 'Km (uM)' = 11; unit head 'kcat (min^-1)' = 170; unit head 'kcat/Km (mM^-1 min^-1)' = 15,200.

normalized_value_unit_evidence: Km: printed Table 1 cell 11 uM; 11 / 1000 = 0.011 mM; the exported value is 0.011 mM. kcat: printed Table 1 cell 170 min^-1; 170 / 60 = 2.833333 s^-1, which the export carries at its own precision as 2.833 s^(-1). kcat/Km: printed Table 1 cell 15,200 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 15,200 / 60 = 253.33333333333334 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 1, substrate block '4-Hydroxy-retinol', enzyme column 'ADH1B2': Km = 11 uM; kcat = 170 min^-1; printed kcat/Km = 15,200 mM^-1 min^-1.

table_label: Table 1: Kinetic constants of human alcohol dehydrogenases with retinoids (Archives of Biochemistry and Biophysics 430 (2004) 210-217)


column_label: Table 1 (Kinetic constants of human alcohol dehydrogenases with retinoids); substrate block '4-Hydroxy-retinol'; enzyme column head 'ADH4'; unit head 'Km (uM)' = 15; unit head 'kcat (min^-1)' = 2050; unit head 'kcat/Km (mM^-1 min^-1)' = 136,000.

normalized_value_unit_evidence: Km: printed Table 1 cell 15 uM; 15 / 1000 = 0.015 mM; the exported value is 0.015 mM. kcat: printed Table 1 cell 2050 min^-1; 2050 / 60 = 34.166667 s^-1, which the export carries at its own precision as 34.167 s^(-1). kcat/Km: printed Table 1 cell 136,000 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 136,000 / 60 = 2266.6666666666665 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 1, substrate block '4-Hydroxy-retinol', enzyme column 'ADH4': Km = 15 uM; kcat = 2050 min^-1; printed kcat/Km = 136,000 mM^-1 min^-1.


smiles: CC(C)CCCO


column_label: Table 1 (Kinetic constants of human alcohol dehydrogenases with retinoids); substrate block '4-Oxo-retinal'; enzyme column head 'ADH1B2'; unit head 'Km (uM)' = 27; unit head 'kcat (min^-1)' = 470; unit head 'kcat/Km (mM^-1 min^-1)' = 17,480.

normalized_value_unit_evidence: Km: printed Table 1 cell 27 uM; 27 / 1000 = 0.027 mM; the exported value is 0.027 mM. kcat: printed Table 1 cell 470 min^-1; 470 / 60 = 7.833333 s^-1, which the export carries at its own precision as 7.833 s^(-1). kcat/Km: printed Table 1 cell 17,480 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 17,480 / 60 = 291.3333333333333 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 1, substrate block '4-Oxo-retinal', enzyme column 'ADH1B2': Km = 27 uM; kcat = 470 min^-1; printed kcat/Km = 17,480 mM^-1 min^-1.


column_label: Table 1 (Kinetic constants of human alcohol dehydrogenases with retinoids); substrate block '4-Oxo-retinal'; enzyme column head 'ADH4'; unit head 'Km (uM)' = 17; unit head 'kcat (min^-1)' = 1200; unit head 'kcat/Km (mM^-1 min^-1)' = 68,200.

normalized_value_unit_evidence: Km: printed Table 1 cell 17 uM; 17 / 1000 = 0.017 mM; the exported value is 0.017 mM. kcat: printed Table 1 cell 1200 min^-1; 1200 / 60 = 20.000000 s^-1, which the export carries at its own precision as 20.0 s^(-1). kcat/Km: printed Table 1 cell 68,200 mM^-1 min^-1; one mM^-1 min^-1 is one sixtieth of an s^-1 mM^-1, so 68,200 / 60 = 1136.6666666666667 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 1, substrate block '4-Oxo-retinal', enzyme column 'ADH4': Km = 17 uM; kcat = 1200 min^-1; printed kcat/Km = 68,200 mM^-1 min^-1.


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.


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: 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


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


organism: Mus musculus

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


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 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


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


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Geobacillus thermodenitrificans


organism: Ogataea angusta


organism: Saccharomyces cerevisiae


organism: Kluyveromyces lactis

substrate_name: Acetaldehyde

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.

substrate: Acetaldehyde


sequence_variant_note: Mutation signature G225A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -29, so it is treated as a source-provided variant sequence.


organism: Rattus norvegicus

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: acetoin

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

assay_conditions_summary: pH 6; 343.15 K; buffer 50 mM glycine-NaOH; cofactor NADH

column_label: Table 4. Kinetic parameters for TkADH; substrate cell `Acetoin (0-200)`; cosubstrate cell `NADH (0.2)`; column `Apparent Km (mM)` = 30.2 (printed with its error term); column `kcat (s^-1)` = 13.7 (printed with its error term); column `kcat/Km (s^-1 mM^-1)` = 0.45 +/- 0.03 (printed, rounded).

normalized_value_unit_evidence: Km: paper cell 30.2 mM -> 30.2 mM; catalog holds 30.2 mM; no conversion (the paper's Km column already prints mM, so no uM/1000 step applies). kcat: paper cell 13.7 s^-1 -> 13.7 s^-1; catalog holds 13.7 s^(-1); no conversion (the paper's kcat column already prints s^-1, so no min^-1/60 step applies). kcat/Km: the paper prints 0.45 +/- 0.03 s^-1 mM^-1 for this row, but the catalog holds 0.45364238410596025 s^(-1)*mM^(-1), which is exactly 13.7 / 30.2.

raw_value_unit_evidence: Table 4, substrate row `Acetoin (0-200)`, cosubstrate `NADH (0.2)`: Apparent Km = 30.2 (column unit mM); kcat = 13.7 (column unit s^-1); printed kcat/Km = 0.45 +/- 0.03 (column unit s^-1 mM^-1).

row_label: Table 4 substrate row `Acetoin (0-200)` with cosubstrate `NADH (0.2)`

substrate: acetoin


substrate_name: Acetone

smiles: CC(C)=O

substrate: Acetone


substrate_name: all-trans-Dehydroretinal

substrate: all-trans-Dehydroretinal


substrate_name: all-trans-Retinal

substrate: all-trans-Retinal


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: 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: all-trans-retinal. Enzyme column: Mouse ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 11 +/- 2, kcat (min^-1) cell 33 +/- 2, kcat/Km (mM^-1 min^-1) cell 3000 +/- 525. metric: Km; raw value: 11 +/- 2; raw unit: uM; normalized value: 0.011 mM; metric: kcat; raw value: 33 +/- 2; raw unit: min^-1; normalized value: 0.55 s^(-1); metric: kcat/Km; raw value: 3000 +/- 525; raw unit: mM^-1 min^-1; normalized value: 50.0 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 11 +/- 2 uM in the Mouse ADH4 column; 11 uM / 1000 = 0.011 mM, which is the catalog km exactly. kcat: printed cell 33 +/- 2 min^-1 in the Mouse ADH4 column; 33 min^-1 / 60 = 0.55 s^-1, an exact terminating conversion, which is the catalog kcat exactly. kcat/Km: the paper prints an independent catalytic-efficiency cell 3000 +/- 525 mM^-1 min^-1 in the Mouse ADH4 column; 3000 mM^-1 min^-1 / 60 = 50.0 s^-1 mM^-1, which is the catalog kcat_over_km 50.00000000000001 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: | 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 ADH4 column cells read: Km = 11 +/- 2 uM; kcat = 33 +/- 2 min^-1; kcat/Km = 3000 +/- 525 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 | all-trans-retinal


substrate_name: benzaldehyde

substrate: benzaldehyde


column_label: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Benzaldehyde` with cosubstrate NADPH (0.4): Apparent Vmax (U mg^-1) = 559.4 +/- 4.1; Apparent Km (mM) = 0.4 +/- 0.1; Apparent Kis (mM) = 30.5 +/- 2.3; Kcat (s^-1) = 360 +/- 2.6; Kcat/Km (s^-1 mM^-1) = 899 +/- 6.5.

normalized_value_unit_evidence: kcat: printed cell 360 s^-1 -> 360 s^(-1); the catalog holds 360.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 0.4 mM -> 0.4 mM; the catalog holds 0.4 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `899` s^-1 mM^-1 for this row -> 899.0 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 900.0 s^(-1)*mM^(-1), which is the full-precision quotient 360 / 0.4 of the row's own kcat and Km cells and is not the printed ratio cell.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Benzaldehyde` with cosubstrate NADPH (0.4): Km (mM) = 0.4; Kcat (s^-1) = 360; Kcat/Km (s^-1 mM^-1) = 899. Every one of these three numerals is printed in the Table 5 cell shown; the +/- terms are the SD reported by Table 5 footnote a.


substrate_name: Benzaldehyde

sequence_variant_note: Mutation signature H3A/E209Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: Benzaldehyde


substrate_name: benzil

substrate: benzil


substrate_name: benzyl alcohol

substrate: benzyl alcohol