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


enzyme_display_name: alcohol dehydrogenase

organism: Mus musculus

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB:Q9QYY9 FASTA

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

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

data_origin: experimental

enzyme: alcohol dehydrogenase

status: corrected

source: oed


verification_status: unverified

kcat_over_km_origin: calculated

smiles: CCCCCCO

status: unverified


sequence_source: UniProtKB:P00329 FASTA

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


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: 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


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


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: Retinol

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

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

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

row_label: Mouse ADH1 | all-trans-retinol

substrate: Retinol


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


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

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

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

row_label: Mouse ADH1 | 9-cis-retinal


organism: Mycobacterium sp.

substrate_name: NAD+

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

substrate: NAD+


smiles: CCCCO


substrate_name: Butanal

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

smiles: CCCC=O

substrate: Butanal


substrate_name: NADH

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

substrate: NADH


organism: Ogataea angusta

substrate_name: ethanol

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

substrate: ethanol


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Pyrobaculum calidifontis

substrate_name: Glutaraldehyde

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

smiles: O=CCCCC=O

assay_conditions_summary: pH 6; 333.15 K; cofactor NADH

substrate: Glutaraldehyde


smiles: OCCCCO

assay_conditions_summary: pH 10; 333.15 K; cofactor NADH


organism: Rattus norvegicus

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

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

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

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

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


substrate_name: Cyclohexanol

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

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

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

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

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

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

substrate: Cyclohexanol


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

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.


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

smiles: CCCCCCCCO


substrate_name: Acetaldehyde

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: Acetaldehyde


substrate_name: 12-Hydroxydodecanoic acid

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


smiles: CCCCCO


sequence_source: UniProtKB reviewed accession P12711

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.


substrate_name: m-Nitrobenzaldehyde

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 'm-Nitrobenzaldehyde'; isoenzyme column group ADH-3; Km (mM) cell = 0.06; kcat (min^-1) cell = 260; kcat/Km (mM^-1 min^-1) cell = 4300.

normalized_value_unit_evidence: Km: printed Table 6 cell 0.06 mM; already in mM, no unit conversion applies; the exported value is 0.06 mM. kcat: printed Table 6 cell 260 min^-1; the printed turnover column is per MINUTE, so 260 / 60 = 4.333333333333333 s^(-1); the exported value is 4.333 s^(-1). kcat/Km: printed Table 6 cell 4300 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 4300 / 60 = 71.66666666666667 s^(-1)*mM^(-1); the exported value is 72.21666666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'm-Nitrobenzaldehyde', isoenzyme column ADH-3: Km = 0.06 mM; kcat = 260 min^-1; kcat/Km = 4300 mM^-1 min^-1.

substrate: m-Nitrobenzaldehyde


sequence_source: UniProtKB reviewed accession P06757

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.


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 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'Butanal'; isoenzyme column group ADH-1; Km (mM) cell = 3.0; kcat (min^-1) cell = 9360; kcat/Km (mM^-1 min^-1) cell = 3120.

normalized_value_unit_evidence: Km: printed Table 6 cell 3.0 mM; already in mM, no unit conversion applies; the exported value is 3.0 mM. kcat: printed Table 6 cell 9360 min^-1; the printed turnover column is per MINUTE, so 9360 / 60 = 156.0 s^(-1); the exported value is 156.0 s^(-1). kcat/Km: printed Table 6 cell 3120 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 3120 / 60 = 52.0 s^(-1)*mM^(-1); the exported value is 52.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'Butanal', isoenzyme column ADH-1: Km = 3.0 mM; kcat = 9360 min^-1; kcat/Km = 3120 mM^-1 min^-1.


smiles: CC=CCO


substrate_name: methanol

smiles: CO

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 'Methanol'; isoenzyme column group ADH-3; Km (mM) cell = 380; kcat (min^-1) cell = 12; kcat/Km (mM^-1 min^-1) cell = 0.03.

normalized_value_unit_evidence: Km: printed Table 5 cell 380 mM; already in mM, no unit conversion applies; the exported value is 380.0 mM. kcat: printed Table 5 cell 12 min^-1; the printed turnover column is per MINUTE, so 12 / 60 = 0.2 s^(-1); the exported value is 0.2 s^(-1). kcat/Km: printed Table 5 cell 0.03 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 0.03 / 60 = 0.0005 s^(-1)*mM^(-1); the exported value is 0.0005263157894736842 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row 'Methanol', isoenzyme column ADH-3: Km = 380 mM; kcat = 12 min^-1; kcat/Km = 0.03 mM^-1 min^-1.

substrate: methanol


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 'm-Nitrobenzaldehyde'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 58800; kcat/Km (mM^-1 min^-1) cell = 42000.

normalized_value_unit_evidence: Km: printed Table 6 cell 1.4 mM; already in mM, no unit conversion applies; the exported value is 1.4 mM. kcat: printed Table 6 cell 58800 min^-1; the printed turnover column is per MINUTE, so 58800 / 60 = 980.0 s^(-1); the exported value is 980.0 s^(-1). kcat/Km: printed Table 6 cell 42000 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 42000 / 60 = 700.0 s^(-1)*mM^(-1); the exported value is 700.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 186, Table 6, substrate row 'm-Nitrobenzaldehyde', isoenzyme column ADH-1: Km = 1.4 mM; kcat = 58800 min^-1; kcat/Km = 42000 mM^-1 min^-1.


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB:P28625 REST lookup 2026-05-31


substrate_name: furfural

substrate: furfural


organism: Sphingomonas sp. A1

substrate_name: D-mannonate

sequence_source: UniProtKB:A0A075B5H4 REST lookup 2026-05-31

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-mannonate'; column 'K m (mM)' = 14 ± 1; column 'V max (mU mg-1)' = 1.1 x 10^3 ± 0.2 x 10^3; column 'k cat (s-1)' = 5.3 x 10^-1 ± 0.1 x 10^-1; column 'k cat/K m (mM-1 s-1)' = 3.8 x 10^-2 ± 0.4 x 10^-2; column 'k cat/K m (%)' = 37.

normalized_value_unit_evidence: Km: printed Table 1 cell 14 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 14.0 mM; the exported value is 14.0 mM. kcat: printed Table 1 cell 5.3 x 10^-1 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 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 1 cell 3.8 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 0.038 s^(-1)*mM^(-1); the exported value is 0.03785714285714286 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-mannonate': K m = 14 ± 1 mM; V max = 1.1 x 10^3 ± 0.2 x 10^3 mU mg^-1; k cat = 5.3 x 10^-1 ± 0.1 x 10^-1 s^-1; printed k cat/K m = 3.8 x 10^-2 ± 0.4 x 10^-2 mM^-1 s^-1; printed relative k cat/K m = 37 per cent.

row_label: Table 1, body row with substrate 'd-mannonate'

substrate: D-mannonate


substrate_name: D-sorbitol

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-sorbitol'; column 'K m (mM)' = 3.5 x 10^2 ± 0.1 x 10^2; column 'V max (mU mg-1)' = 11 ± 0.2; column 'k cat (s-1)' = 5.2 x 10^-3 ± 0.09 x 10^-3; column 'k cat/K m (mM-1 s-1)' = 1.5 x 10^-5 ± 0.08 x 10^-5; column 'k cat/K m (%)' = 0.01.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.5 x 10^2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 350.0 mM; the exported value is 350.0 mM. kcat: printed Table 1 cell 5.2 x 10^-3 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 0.0052 s^(-1); the exported value is 0.0052 s^(-1). kcat/Km: printed Table 1 cell 1.5 x 10^-5 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 0.000015 s^(-1)*mM^(-1); the exported value is 0.000014857142857142857 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-sorbitol': K m = 3.5 x 10^2 ± 0.1 x 10^2 mM; V max = 11 ± 0.2 mU mg^-1; k cat = 5.2 x 10^-3 ± 0.09 x 10^-3 s^-1; printed k cat/K m = 1.5 x 10^-5 ± 0.08 x 10^-5 mM^-1 s^-1; printed relative k cat/K m = 0.01 per cent.

row_label: Table 1, body row with substrate 'd-sorbitol'

substrate: D-sorbitol


substrate_name: D-altronate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-altronate'; column 'K m (mM)' = 24 ± 4; column 'V max (mU mg-1)' = 3.9 x 10^2 ± 0.2 x 10^2; column 'k cat (s-1)' = 1.9 x 10^-1 ± 0.08 x 10^-1; column 'k cat/K m (mM-1 s-1)' = 8.0 x 10^-3 ± 2 x 10^-3; column 'k cat/K m (%)' = 8.

normalized_value_unit_evidence: Km: printed Table 1 cell 24 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 24.0 mM; the exported value is 24.0 mM. kcat: printed Table 1 cell 1.9 x 10^-1 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 0.19 s^(-1); the exported value is 0.19 s^(-1). kcat/Km: printed Table 1 cell 8.0 x 10^-3 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 0.008 s^(-1)*mM^(-1); the exported value is 0.007916666666666667 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-altronate': K m = 24 ± 4 mM; V max = 3.9 x 10^2 ± 0.2 x 10^2 mU mg^-1; k cat = 1.9 x 10^-1 ± 0.08 x 10^-1 s^-1; printed k cat/K m = 8.0 x 10^-3 ± 2 x 10^-3 mM^-1 s^-1; printed relative k cat/K m = 8 per cent.

row_label: Table 1, body row with substrate 'd-altronate'

substrate: D-altronate


substrate_name: D-Arabitol

substrate: D-Arabitol


substrate_name: D-Gluconate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-gluconate'; column 'K m (mM)' = 12 ± 1; column 'V max (mU mg-1)' = 2.0 x 10^3 ± 0.6 x 10^3; column 'k cat (s-1)' = 9.8 x 10^-1 ± 0.3 x 10^-1; column 'k cat/K m (mM-1 s-1)' = 8.2 x 10^-2 ± 0.9 x 10^-2; column 'k cat/K m (%)' = 79.

normalized_value_unit_evidence: Km: printed Table 1 cell 12 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 12.0 mM; the exported value is 12.0 mM. kcat: printed Table 1 cell 9.8 x 10^-1 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 0.98 s^(-1); the exported value is 0.98 s^(-1). kcat/Km: printed Table 1 cell 8.2 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 0.082 s^(-1)*mM^(-1); the exported value is 0.08166666666666667 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-gluconate': K m = 12 ± 1 mM; V max = 2.0 x 10^3 ± 0.6 x 10^3 mU mg^-1; k cat = 9.8 x 10^-1 ± 0.3 x 10^-1 s^-1; printed k cat/K m = 8.2 x 10^-2 ± 0.9 x 10^-2 mM^-1 s^-1; printed relative k cat/K m = 79 per cent.

row_label: Table 1, body row with substrate 'd-gluconate'

substrate: D-Gluconate


substrate_name: D-allonate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-allonate'; column 'K m (mM)' = 16 ± 2; column 'V max (mU mg-1)' = 3.6 x 10^2 ± 0.1 x 10^2; column 'k cat (s-1)' = 1.8 x 10^-1 ± 0.05 x 10^-1; column 'k cat/K m (mM-1 s-1)' = 1.1 x 10^-2 ± 0.2 x 10^-2; column 'k cat/K m (%)' = 10.

normalized_value_unit_evidence: Km: printed Table 1 cell 16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 16.0 mM; the exported value is 16.0 mM. kcat: printed Table 1 cell 1.8 x 10^-1 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 0.18 s^(-1); the exported value is 0.18 s^(-1). kcat/Km: printed Table 1 cell 1.1 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 0.011 s^(-1)*mM^(-1); the exported value is 0.01125 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-allonate': K m = 16 ± 2 mM; V max = 3.6 x 10^2 ± 0.1 x 10^2 mU mg^-1; k cat = 1.8 x 10^-1 ± 0.05 x 10^-1 s^-1; printed k cat/K m = 1.1 x 10^-2 ± 0.2 x 10^-2 mM^-1 s^-1; printed relative k cat/K m = 10 per cent.

row_label: Table 1, body row with substrate 'd-allonate'

substrate: D-allonate


sequence_source: UniProtKB reviewed accession P06757 (ADH1_RAT) REST/FASTA direct check on 2026-05-31


substrate_name: benzyl alcohol

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 'Benzyl alcohol'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 5380; kcat/Km (mM^-1 min^-1) cell = 3900.

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 5380 min^-1; the printed turnover column is per MINUTE, so 5380 / 60 = 89.66666666666667 s^(-1); the exported value is 89.667 s^(-1). kcat/Km: printed Table 5 cell 3900 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 3900 / 60 = 65.0 s^(-1)*mM^(-1); the exported value is 64.04785714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row 'Benzyl alcohol', isoenzyme column ADH-1: Km = 1.4 mM; kcat = 5380 min^-1; kcat/Km = 3900 mM^-1 min^-1.

substrate: benzyl alcohol


sequence_source: UniProtKB reviewed accession P12711 (ADHX_RAT) REST/FASTA direct check on 2026-05-31

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 'Benzyl alcohol'; isoenzyme column group ADH-3; Km (mM) cell = 0.05; kcat (min^-1) cell = 60; kcat/Km (mM^-1 min^-1) cell = 1200.

normalized_value_unit_evidence: Km: printed Table 5 cell 0.05 mM; already in mM, no unit conversion applies; the exported value is 0.05 mM. kcat: printed Table 5 cell 60 min^-1; the printed turnover column is per MINUTE, so 60 / 60 = 1.0 s^(-1); the exported value is 1.0 s^(-1). kcat/Km: printed Table 5 cell 1200 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 1200 / 60 = 20.0 s^(-1)*mM^(-1); the exported value is 20.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 185, Table 5, substrate row 'Benzyl alcohol', isoenzyme column ADH-3: Km = 0.05 mM; kcat = 60 min^-1; kcat/Km = 1200 mM^-1 min^-1.


kcat_over_km_display: Not reported

sequence_source: UniProtKB reviewed accession P00330 (ADH1_YEAST) REST/FASTA direct check on 2026-05-31

assay_conditions_summary: pH 6.5; 303.15 K; buffer a standardised reaction; cofactor NADPH

column_label: Table label: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]". Reaction: ADH. Isoenzyme: Adh1p. Rows read: ADH | Adh1p | kcat -> Value cell 176, Unit cell s−1; ADH | Adh1p | Kacald -> Value cell 0.462, Unit cell mM. kcat/Km: no printed cell (Table 2 has no kcat/Km column).

normalized_value_unit_evidence: kcat 176 s−1 = 176.0 s^(-1) (printed unit s−1 is the export unit s^(-1), no conversion); decimal-equal to the catalog kcat 176.0; Km (Kacald) 0.462 mM = 0.462 mM (already the export unit, no conversion); decimal-equal to the catalog km 0.462. In the on-disk transcription the printed superscript minus renders as the flattened `s−1` (U+2212) and empty SEM/Ref cells render as empty ` | ` fields.

raw_value_unit_evidence: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]" | header row: Reaction | Isoenzyme | Parameter | Value | SEM (%) | Ref. [23] | Unit | kcat evidence: ADH | Adh1p | kcat | 176 | 1.3 |  | s−1 | Km evidence: ADH | Adh1p | Kacald | 0.462 | 5.3 | 1.11 | mM | cells read: kcat = 176 s−1 (Value column); Kacald = 0.462 mM

row_label: ADH | Adh1p


substrate_name: glycolaldehyde

sequence_source: UniProtKB reviewed accession P28625 direct check on 2026-05-31; not accepted for EC 1.1.1.1 because the accession lacks matching EC/family support.

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

smiles: O=CCO

substrate: glycolaldehyde


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB Q4J702 direct lookup; active TrEMBL entry Q4J702_SULAC, RefSeq WP_011278925.1, EMBL protein AAY81423.1

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.


substrate_name: ethyl benzoylformate

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 'Ethyl benzoylformate'; column kcat (s-1) = 2.35; column Km (mM) = 5.3; column kcat/Km (s-1 mM-1) = 0.44. captured primary segment: Ethyl benzoylformate | kcat 2.35 s^-1 | Km 5.3 mM | kcat/Km 0.44 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 2.35 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 2.35 s^(-1). Km: printed Table 3 cell 5.3 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 5.3 mM. kcat/Km: printed Table 3 cell 0.44 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 0.44 s^(-1)*mM^(-1). Quotient disclosure for this row: 2.35 / 5.3 = 0.4433962264150943 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.44 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'Ethyl benzoylformate': kcat = 2.35 s^-1; Km = 5.3 mM; printed kcat/Km = 0.44 s^-1 mM^-1.

substrate: ethyl benzoylformate


substrate_name: NAD+

assay_conditions_summary: pH 8; 338.15 K; cofactor NAD+

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 'NAD+'; column kcat (s-1) = 3.7; column Km (mM) = 0.44; column kcat/Km (s-1 mM-1) = 8.4. captured primary segment: NAD+ | kcat 3.7 s^-1 | Km 0.44 mM | kcat/Km 8.4 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.7 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 3.7 s^(-1). Km: printed Table 3 cell 0.44 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 0.44 mM. kcat/Km: printed Table 3 cell 8.4 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 8.4 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.7 / 0.44 = 8.409090909090909 s^-1 mM^-1, against the printed catalytic-efficiency cell 8.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'NAD+': kcat = 3.7 s^-1; Km = 0.44 mM; printed kcat/Km = 8.4 s^-1 mM^-1.

row_label: Table 3, substrate row 'NAD+'

substrate: NAD+


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 '1-Phenyl-1,2-propanedione'; column kcat (s-1) = 3.1; column Km (mM) = 12.1; column kcat/Km (s-1 mM-1) = 0.25. captured primary segment: 1-Phenyl-1,2-propanedione | kcat 3.1 s^-1 | Km 12.1 mM | kcat/Km 0.25 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.1 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 3.1 s^(-1). Km: printed Table 3 cell 12.1 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 12.1 mM. kcat/Km: printed Table 3 cell 0.25 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 0.25 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.1 / 12.1 = 0.2561983471074380 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.25 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row '1-Phenyl-1,2-propanedione': kcat = 3.1 s^-1; Km = 12.1 mM; printed kcat/Km = 0.25 s^-1 mM^-1.


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 'cis-Decahydro-1-naphthol'; column kcat (s-1) = 0.98; column Km (mM) = 4.2; column kcat/Km (s-1 mM-1) = 0.23. captured primary segment: cis-Decahydro-1-naphthol | kcat 0.98 s^-1 | Km 4.2 mM | kcat/Km 0.23 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.98 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 0.98 s^(-1). Km: printed Table 3 cell 4.2 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 4.2 mM. kcat/Km: printed Table 3 cell 0.23 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 0.23 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.98 / 4.2 = 0.2333333333333333 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.23 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'cis-Decahydro-1-naphthol': kcat = 0.98 s^-1; Km = 4.2 mM; printed kcat/Km = 0.23 s^-1 mM^-1.


substrate_name: NADH

substrate: 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 '3-Methylcyclohexanone'; column kcat (s-1) = 3.8; column Km (mM) = 66.0; column kcat/Km (s-1 mM-1) = 0.06. captured primary segment: 3-Methylcyclohexanone | kcat 3.8 s^-1 | Km 66.0 mM | kcat/Km 0.06 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.8 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 3.8 s^(-1). Km: printed Table 3 cell 66.0 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 66.0 mM. kcat/Km: printed Table 3 cell 0.06 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 0.06 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.8 / 66.0 = 0.05757575757575758 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.06 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row '3-Methylcyclohexanone': kcat = 3.8 s^-1; Km = 66.0 mM; printed kcat/Km = 0.06 s^-1 mM^-1.


substrate_name: isatin

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 'Isatin'; column kcat (s-1) = 22.0; column Km (mM) = 0.71; column kcat/Km (s-1 mM-1) = 31. captured primary segment: Isatin | kcat 22.0 s^-1 | Km 0.71 mM | kcat/Km 31 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 22.0 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 22.0 s^(-1). Km: printed Table 3 cell 0.71 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 0.71 mM. kcat/Km: printed Table 3 cell 31 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 31.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 22.0 / 0.71 = 30.98591549295775 s^-1 mM^-1, against the printed catalytic-efficiency cell 31 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'Isatin': kcat = 22.0 s^-1; Km = 0.71 mM; printed kcat/Km = 31 s^-1 mM^-1.

row_label: Table 3, substrate row 'Isatin'

substrate: isatin


sequence_source: UniProtKB:Q4J9F2 canonical sequence; direct REST accession lookup on 2026-05-31


assay_conditions_summary: pH 10.5; 338.15 K; cofactor NAD+


organism: Sulfolobus solfataricus

substrate_name: Ethanol

sequence_source: UniProtKB:P39462 canonical sequence; direct REST accession lookup on 2026-05-31

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Ethanol`: Km (uM) = 260; kcat (min^-1) = 113; kcat/Km (min^-1 uM^-1) = 0.4.

normalized_value_unit_evidence: kcat: printed cell 113 min^-1 -> 113 / 60 = 1.8833333333333333 s^(-1); the catalog holds 1.883 s^(-1) (1.883 is that conversion cut to the catalog's printed precision). Km: printed cell 260 uM -> 260 / 1000 = 0.26 mM; the catalog holds 0.26 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.4` min^-1 uM^-1 for this row -> 0.4 * 1000 / 60 = 6.666666666666668 s^(-1)*mM^(-1). The catalog instead holds 7.242307692307692 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.

table_label: Table 3 (journal page 479) 'Substrate specificity of alcohol dehydrogenase from S. solfataricus'

substrate: Ethanol


smiles: CCC(C)O

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Butan-2-ol`: Km (uM) = 350; kcat (min^-1) = 213; kcat/Km (min^-1 uM^-1) = 0.6.

normalized_value_unit_evidence: kcat: printed cell 213 min^-1 -> 213 / 60 = 3.55 s^(-1); the catalog holds 3.55 s^(-1) (identical). Km: printed cell 350 uM -> 350 / 1000 = 0.35000000000000003 mM; the catalog holds 0.35 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.6` min^-1 uM^-1 for this row -> 0.6 * 1000 / 60 = 10.0 s^(-1)*mM^(-1). The catalog instead holds 10.142857142857142 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


column_label: Table 3 (journal page 479), decoded transcription, substrate row `3-Methyl-cyclohexanol`: Km (uM) = 21; kcat (min^-1) = 463; kcat/Km (min^-1 uM^-1) = 22.

normalized_value_unit_evidence: kcat: printed cell 463 min^-1 -> 463 / 60 = 7.716666666666667 s^(-1); the catalog holds 7.717 s^(-1) (7.717 is that conversion cut to the catalog's printed precision). Km: printed cell 21 uM -> 21 / 1000 = 0.021 mM; the catalog holds 0.021 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `22` min^-1 uM^-1 for this row -> 22 * 1000 / 60 = 366.6666666666667 s^(-1)*mM^(-1). The catalog instead holds 367.4761904761904 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


smiles: CC(C)O

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Propan-2-ol`: Km (uM) = 500; kcat (min^-1) = 415; kcat/Km (min^-1 uM^-1) = 0.83.

normalized_value_unit_evidence: kcat: printed cell 415 min^-1 -> 415 / 60 = 6.916666666666667 s^(-1); the catalog holds 6.917 s^(-1) (6.917 is that conversion cut to the catalog's printed precision). Km: printed cell 500 uM -> 500 / 1000 = 0.5 mM; the catalog holds 0.5 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.83` min^-1 uM^-1 for this row -> 0.83 * 1000 / 60 = 13.833333333333334 s^(-1)*mM^(-1). The catalog instead holds 13.834 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


smiles: CCC(O)CC

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Pentan-3-ol`: Km (uM) = 225; kcat (min^-1) = 175; kcat/Km (min^-1 uM^-1) = 0.77.

normalized_value_unit_evidence: kcat: printed cell 175 min^-1 -> 175 / 60 = 2.9166666666666665 s^(-1); the catalog holds 2.917 s^(-1) (2.917 is that conversion cut to the catalog's printed precision). Km: printed cell 225 uM -> 225 / 1000 = 0.225 mM; the catalog holds 0.225 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.77` min^-1 uM^-1 for this row -> 0.77 * 1000 / 60 = 12.833333333333334 s^(-1)*mM^(-1). The catalog instead holds 12.964444444444442 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


substrate_name: methyl o-chlorobenzoylformate

sequence_source: UniProtKB REST Q4J702, checked 2026-05-31

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 'Methyl o-chlorobenzoylformate'; column kcat (s-1) = 9.2; column Km (mM) = 2.8; column kcat/Km (s-1 mM-1) = 3.3. captured primary segment: Methyl o-chlorobenzoylformate | kcat 9.2 s^-1 | Km 2.8 mM | kcat/Km 3.3 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 9.2 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 9.2 s^(-1). Km: printed Table 3 cell 2.8 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 2.8 mM. kcat/Km: printed Table 3 cell 3.3 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 3.3 s^(-1)*mM^(-1). Quotient disclosure for this row: 9.2 / 2.8 = 3.285714285714286 s^-1 mM^-1, against the printed catalytic-efficiency cell 3.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'Methyl o-chlorobenzoylformate': kcat = 9.2 s^-1; Km = 2.8 mM; printed kcat/Km = 3.3 s^-1 mM^-1.

substrate: methyl o-chlorobenzoylformate


substrate_name: cycloheptanol

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 'Cycloheptanol'; column kcat (s-1) = 4.4; column Km (mM) = 9.3; column kcat/Km (s-1 mM-1) = 0.47. captured primary segment: Cycloheptanol | kcat 4.4 s^-1 | Km 9.3 mM | kcat/Km 0.47 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 4.4 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 4.4 s^(-1). Km: printed Table 3 cell 9.3 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 9.3 mM. kcat/Km: printed Table 3 cell 0.47 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 0.47 s^(-1)*mM^(-1). Quotient disclosure for this row: 4.4 / 9.3 = 0.4731182795698925 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.47 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'Cycloheptanol': kcat = 4.4 s^-1; Km = 9.3 mM; printed kcat/Km = 0.47 s^-1 mM^-1.

row_label: Table 3, substrate row 'Cycloheptanol'

substrate: cycloheptanol


substrate_name: methyl benzoylformate

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 'Methyl benzoylformate'; column kcat (s-1) = 6.2; column Km (mM) = 6.5; column kcat/Km (s-1 mM-1) = 0.95. captured primary segment: Methyl benzoylformate | kcat 6.2 s^-1 | Km 6.5 mM | kcat/Km 0.95 s^-1 mM^-1

normalized_value_unit_evidence: kcat: printed Table 3 cell 6.2 s^-1; the printed unit is already s^-1, so no unit conversion applies and the paper-side value is 6.2 s^(-1). Km: printed Table 3 cell 6.5 mM; the printed unit is already mM, so no unit conversion applies and the paper-side value is 6.5 mM. kcat/Km: printed Table 3 cell 0.95 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 0.95 s^(-1)*mM^(-1). Quotient disclosure for this row: 6.2 / 6.5 = 0.9538461538461538 s^-1 mM^-1, against the printed catalytic-efficiency cell 0.95 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, substrate row 'Methyl benzoylformate': kcat = 6.2 s^-1; Km = 6.5 mM; printed kcat/Km = 0.95 s^-1 mM^-1.

substrate: methyl benzoylformate


substrate_name: (R)-alpha-tetralol

column_label: Table 3 (PDF page 8 of 12, journal page 200) 'Steady-state kinetic constants of SaADH', substrate row `(R)-alpha-Tetralol`: kcat (s^-1) = 13.5; Km (mM) = 1.28; kcat/Km (s^-1 mM^-1) = 10.5.

normalized_value_unit_evidence: kcat: printed cell 13.5 s^-1 is already the export unit s^(-1); the exported value is 13.5 s^(-1). Km: printed cell 1.28 mM is already the export unit mM; the exported value is 1.3 mM. kcat/Km: the paper PRINTS the kcat/Km cell 10.5 s^-1 mM^-1 for this substrate line, already in the export unit s^(-1)*mM^(-1); the exported value is 10.384615384615385 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `(R)-alpha-Tetralol`

substrate: (R)-alpha-tetralol


substrate_name: (S)-alpha-tetralol

column_label: Table 3 (PDF page 8 of 12, journal page 200) 'Steady-state kinetic constants of SaADH', substrate row `(S)-alpha-Tetralol`: kcat (s^-1) = 2.1; Km (mM) = 1.05; kcat/Km (s^-1 mM^-1) = 2.0.

normalized_value_unit_evidence: kcat: printed cell 2.1 s^-1 is already the export unit s^(-1); the exported value is 2.1 s^(-1). Km: printed cell 1.05 mM is already the export unit mM; the exported value is 1.05 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.0 s^-1 mM^-1 for this substrate line, already in the export unit s^(-1)*mM^(-1); the exported value is 2.0 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `(S)-alpha-Tetralol`

substrate: (S)-alpha-tetralol


sequence_source: UniProtKB REST Q4J9F2, checked 2026-05-31


substrate_name: benzil

substrate: benzil


sequence_source: UniProtKB:P39462 direct lookup (reviewed Swiss-Prot), 2026-05-31

column_label: Table 3 (journal page 479), decoded transcription, substrate row `(+/-)-3-Methylcyclohexanone`: Km (uM) = 250; kcat (min^-1) = 130; kcat/Km (min^-1 uM^-1) = 0.52.

normalized_value_unit_evidence: kcat: printed cell 130 min^-1 -> 130 / 60 = 2.1666666666666665 s^(-1); the catalog holds 2.167 s^(-1) (2.167 is that conversion cut to the catalog's printed precision). Km: printed cell 250 uM -> 250 / 1000 = 0.25 mM; the catalog holds 0.25 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.52` min^-1 uM^-1 for this row -> 0.52 * 1000 / 60 = 8.666666666666668 s^(-1)*mM^(-1). The catalog instead holds 8.668 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


smiles: CCCO

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Propan-1-ol`: Km (uM) = 19; kcat (min^-1) = 242; kcat/Km (min^-1 uM^-1) = 12.7.

normalized_value_unit_evidence: kcat: printed cell 242 min^-1 -> 242 / 60 = 4.033333333333333 s^(-1); the catalog holds 4.033 s^(-1) (4.033 is that conversion cut to the catalog's printed precision). Km: printed cell 19 uM -> 19 / 1000 = 0.019 mM; the catalog holds 0.019 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `12.7` min^-1 uM^-1 for this row -> 12.7 * 1000 / 60 = 211.66666666666666 s^(-1)*mM^(-1). The catalog instead holds 212.26315789473688 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


substrate_name: p-Anisaldehyde

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Anisaldehyde`: Km (uM) = 2.5; kcat (min^-1) = 59; kcat/Km (min^-1 uM^-1) = 23.6.

normalized_value_unit_evidence: kcat: printed cell 59 min^-1 -> 59 / 60 = 0.9833333333333333 s^(-1); the catalog holds 0.983 s^(-1) (0.983 is that conversion cut to the catalog's printed precision). Km: printed cell 2.5 uM -> 2.5 / 1000 = 0.0025 mM; the catalog holds 0.003 mM (the two differ). kcat/Km: the paper PRINTS its own kcat/Km cell `23.6` min^-1 uM^-1 for this row -> 23.6 * 1000 / 60 = 393.33333333333337 s^(-1)*mM^(-1). The catalog instead holds 327.66666666666663 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.

substrate: p-Anisaldehyde


organism: Thermococcus kodakarensis

substrate_name: NADP+

sequence_source: UniProtKB:Q5JI09 direct lookup (unreviewed TrEMBL), 2026-05-31

assay_conditions_summary: pH 9; 343.15 K; cofactor NADP+

column_label: Exact Table 4 NADP+ row, meso-2,3-butanediol cosubstrate context, and same-row apparent Km/kcat/kcat-over-Km cells.

normalized_value_unit_evidence: Exact current components are Km 0.113 mM and kcat 30.0 s^-1; their stored-precision quotient is 265.4867256637168 s^-1 mM^-1; printed efficiency remains 265.

table_label: Table 4. Kinetic parameters for TkADH

substrate: NADP+


smiles: CC(O)C(C)O

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 `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)`


assay_conditions_summary: pH 6; 343.15 K; cofactor NADH


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)`


substrate_name: acetoin

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

column_label: Exact Table 4 Acetoin row, NADH cosubstrate column context, and same-row apparent Km/kcat/kcat-over-Km cells.

normalized_value_unit_evidence: Exact current components are Km 30.2 mM and kcat 13.7 s^-1; their stored-precision quotient is 0.45364238410596025 s^-1 mM^-1; printed efficiency remains 0.45.

substrate: acetoin


substrate_name: D-ribonate

sequence_source: UniProtKB A0A075B5H4; RCSB 4TKL SIFTS 100% coverage; PMCID PMC6011931 GenBank BAP40335.1

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

substrate: D-ribonate


substrate_name: D-talonate

substrate: D-talonate


substrate_name: D-Xylonate

substrate: D-Xylonate


organism: Struthio camelus

sequence_source: UniProtKB P80468 direct lookup; reviewed Struthio camelus ADH4 sequence


smiles: CCO

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

column_label: Table 1: Enzymatic properties of the present enzyme form, compared with those of the characterized human enzymes (PNAS 1995, 92(24):10904-10908); Table 1, substrate row Ethanol, Ostrich II column: the substrate line 'Ethanol' prints its Km values on the upper line and its kcat values on the lower line, and the Ostrich II column is the first numeric column; upper value (Km, mM) = 0.71; lower value (kcat, min^-1) = 36. Table 1 has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 36 min^-1; 1 min^-1 is 1/60 s^-1, so 36 / 60 = 0.6 s^-1; the paper value is 0.6 s^(-1). Km: printed Table 1 cell 0.71 mM; already in mM, no unit conversion applies; the paper value is 0.71 mM. kcat/Km: this article prints no kcat/Km cell for this measurement, so the exported 0.8450704225352113 s^(-1)*mM^(-1) is not a printed value; the paper-side efficiency is the quotient 0.6 / 0.71 = 0.8450704225352113 s^-1 mM^-1 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, substrate row Ethanol, Ostrich II column: Km = 0.71 mM (upper value of the substrate pair, printed column Ostrich II); kcat = 36 min^-1 (lower value of the substrate pair, printed column Ostrich II). No kcat/Km value is printed for this measurement.


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: ethyl benzoylformate

sequence_source: UniProtKB Q4J9F2 direct REST/FASTA lookup; PubMed PMID 22805786 and RCSB PDB 4FN4 structural anchor

substrate: ethyl benzoylformate


substrate_name: isoborneol

substrate: isoborneol


substrate_name: ethyl 3-methyl-2-oxobutyrate

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

substrate: ethyl 3-methyl-2-oxobutyrate


substrate_name: NADH

assay_conditions_summary: pH 5; 338.15 K; cofactor NADH

substrate: NADH


substrate_name: benzyl alcohol

sequence_source: UniProtKB reviewed accession P39462 direct REST check on 2026-05-31; primaryAccession=P39462, recommendedName=NAD-dependent alcohol dehydrogenase, EC=1.1.1.1, organism=Saccharolobus solfataricus strain P2 with common name Sulfolobus solfataricus, sequenceVersion=1, md5=A582302357142F677A9C9BA65429CCF8.

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Benzyl alcohol`: Km (uM) = 13; kcat (min^-1) = 101; kcat/Km (min^-1 uM^-1) = 7.8.

normalized_value_unit_evidence: kcat: printed cell 101 min^-1 -> 101 / 60 = 1.6833333333333333 s^(-1); the catalog holds 1.683 s^(-1) (1.683 is that conversion cut to the catalog's printed precision). Km: printed cell 13 uM -> 13 / 1000 = 0.013000000000000001 mM; the catalog holds 0.013 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `7.8` min^-1 uM^-1 for this row -> 7.8 * 1000 / 60 = 130.0 s^(-1)*mM^(-1). The catalog instead holds 129.46153846153848 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.

substrate: benzyl alcohol


substrate_name: Acetone

smiles: CC(C)=O

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Acetone`: Km (uM) = 6600; kcat (min^-1) = 19; kcat/Km (min^-1 uM^-1) = 0.003.

normalized_value_unit_evidence: kcat: printed cell 19 min^-1 -> 19 / 60 = 0.31666666666666665 s^(-1); the catalog holds 0.317 s^(-1) (0.317 is that conversion cut to the catalog's printed precision). Km: printed cell 6600 uM -> 6600 / 1000 = 6.6000000000000005 mM; the catalog holds 6.6 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.003` min^-1 uM^-1 for this row -> 0.003 * 1000 / 60 = 0.05 s^(-1)*mM^(-1). The catalog instead holds 0.048030303030303034 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.

substrate: Acetone


smiles: CCC(C)=O

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Butan-2-one`: Km (uM) = 14000; kcat (min^-1) = 116; kcat/Km (min^-1 uM^-1) = 0.008.

normalized_value_unit_evidence: kcat: printed cell 116 min^-1 -> 116 / 60 = 1.9333333333333333 s^(-1); the catalog holds 1.933 s^(-1) (1.933 is that conversion cut to the catalog's printed precision). Km: printed cell 14000 uM -> 14000 / 1000 = 14.0 mM; the catalog holds 14.0 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.008` min^-1 uM^-1 for this row -> 0.008 * 1000 / 60 = 0.13333333333333336 s^(-1)*mM^(-1). The catalog instead holds 0.13807142857142857 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


substrate_name: Cyclopetanone

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Cyclopentanone`: Km (uM) = 1300; kcat (min^-1) = 61; kcat/Km (min^-1 uM^-1) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 61 min^-1 -> 61 / 60 = 1.0166666666666666 s^(-1); the catalog holds 1.017 s^(-1) (1.017 is that conversion cut to the catalog's printed precision). Km: printed cell 1300 uM -> 1300 / 1000 = 1.3 mM; the catalog holds 1.3 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.05` min^-1 uM^-1 for this row -> 0.05 * 1000 / 60 = 0.8333333333333335 s^(-1)*mM^(-1). The catalog instead holds 0.7823076923076923 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.

substrate: Cyclopetanone


smiles: CCCCO

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Butan-1-ol`: Km (uM) = 55; kcat (min^-1) = 118; kcat/Km (min^-1 uM^-1) = 2.1.

normalized_value_unit_evidence: kcat: printed cell 118 min^-1 -> 118 / 60 = 1.9666666666666666 s^(-1); the catalog holds 1.967 s^(-1) (1.967 is that conversion cut to the catalog's printed precision). Km: printed cell 55 uM -> 55 / 1000 = 0.055 mM; the catalog holds 0.055 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `2.1` min^-1 uM^-1 for this row -> 2.1 * 1000 / 60 = 35.00000000000001 s^(-1)*mM^(-1). The catalog instead holds 35.763636363636365 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


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

column_label: Table 3 (journal page 479), decoded transcription, substrate row `3-Methylbutan-2-one`: Km (uM) = 7500; kcat (min^-1) = 73; kcat/Km (min^-1 uM^-1) = 0.01.

normalized_value_unit_evidence: kcat: printed cell 73 min^-1 -> 73 / 60 = 1.2166666666666666 s^(-1); the catalog holds 1.217 s^(-1) (1.217 is that conversion cut to the catalog's printed precision). Km: printed cell 7500 uM -> 7500 / 1000 = 7.5 mM; the catalog holds 7.5 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `0.01` min^-1 uM^-1 for this row -> 0.01 * 1000 / 60 = 0.16666666666666669 s^(-1)*mM^(-1). The catalog instead holds 0.16226666666666667 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


smiles: CCCC(C)O

column_label: Table 3 (journal page 479), decoded transcription, substrate row `Pentan-2-ol`: Km (uM) = 50; kcat (min^-1) = 229; kcat/Km (min^-1 uM^-1) = 4.6.

normalized_value_unit_evidence: kcat: printed cell 229 min^-1 -> 229 / 60 = 3.8166666666666664 s^(-1); the catalog holds 3.817 s^(-1) (3.817 is that conversion cut to the catalog's printed precision). Km: printed cell 50 uM -> 50 / 1000 = 0.05 mM; the catalog holds 0.05 mM (identical). kcat/Km: the paper PRINTS its own kcat/Km cell `4.6` min^-1 uM^-1 for this row -> 4.6 * 1000 / 60 = 76.66666666666667 s^(-1)*mM^(-1). The catalog instead holds 76.34 s^(-1)*mM^(-1), which is the full-precision quotient of the row's own kcat and Km cells and is not the printed ratio cell. The printed cell is the same quantity carried to the one or two significant figures that column prints.


substrate_name: methanol

substrate: methanol


substrate_name: NAD+

sequence_source: UniProtKB Q5JI09 direct FASTA

assay_conditions_summary: pH 9; 343.15 K; cofactor NAD+

column_label: Exact Table 4 NAD+ row, meso-2,3-butanediol cosubstrate context, and same-row apparent Km/kcat/kcat-over-Km cells.

normalized_value_unit_evidence: Exact current components are Km 0.127 mM and kcat 30.8 s^-1; their stored-precision quotient is 242.51968503937007 s^-1 mM^-1; printed efficiency remains 243.

substrate: NAD+


organism: Yokenella sp.

sequence_source: UniProtKB W6CX26 direct FASTA

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.


assay_conditions_summary: pH 8; 328.15 K; cofactor NADP+


column_label: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Benzyl alcohol` with cosubstrate NADP^+ (0.4): Apparent Vmax (U mg^-1) = 145.1 +/- 9.0; Apparent Km (mM) = 14 +/- 1.6; Apparent Kis (mM) = 101 +/- 1.5; Kcat (s^-1) = 93.3 +/- 5.8; Kcat/Km (s^-1 mM^-1) = 6.6 +/- 0.9.

normalized_value_unit_evidence: kcat: printed cell 93.3 s^-1 -> 93.3 s^(-1); the catalog holds 93.3 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 14 mM -> 14 mM; the catalog holds 14.0 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `6.6` s^-1 mM^-1 for this row -> 6.6 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 6.664285714285714 s^(-1)*mM^(-1), which is the full-precision quotient 93.3 / 14 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 `Benzyl alcohol` with cosubstrate NADP^+ (0.4): Km (mM) = 14; Kcat (s^-1) = 93.3; Kcat/Km (s^-1 mM^-1) = 6.6. 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/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.


substrate_name: 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: benzaldehyde


substrate_name: NADPH

column_label: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `NADPH` with cosubstrate Crotonaldehyde (4.9): Apparent Vmax (U mg^-1) = 672.7 +/- 17; Apparent Km (mM) = 0.6 +/- 0.1; Apparent Kis (mM) = (no value printed); Kcat (s^-1) = 433 +/- 0.5; Kcat/Km (s^-1 mM^-1) = 720 +/- 19.

normalized_value_unit_evidence: kcat: printed cell 433 s^-1 -> 433 s^(-1); the catalog holds 433.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 0.6 mM -> 0.6 mM; the catalog holds 0.6 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `720` s^-1 mM^-1 for this row -> 720.0 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 721.6666666666667 s^(-1)*mM^(-1), which is the full-precision quotient 433 / 0.6 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 `NADPH` with cosubstrate Crotonaldehyde (4.9): Km (mM) = 0.6; Kcat (s^-1) = 433; Kcat/Km (s^-1 mM^-1) = 720. 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: NADPH


enzyme_display_name: carboxylesterase

organism: Aspergillus niger

substrate_name: Vinylacetate

sequence_source: UniProtKB:Q6ED33 canonical sequence

smiles: C=CCC(=O)O

column_label: Table 3 (journal page 32), decoded transcription, enzyme row EstA, substrate column group Vinyl acetate (C2): kcat (s^-1) = 400; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 400 s^-1 -> 400.0 s^(-1); the catalog holds 400.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 133.33333333333334 s^(-1)*mM^(-1) is the exact quotient 400 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 3 (journal page 32) 'Kinetic parameters kcat and K0.5 of the hydrolysis of vinyl esters by members of the HSL family and other lipolytic and non-lipolytic carboxyesterases'

enzyme: carboxylesterase

substrate: Vinylacetate


substrate_name: vinyl propionate

smiles: C=COC(=O)CC

column_label: Table 3 (journal page 32), decoded transcription, enzyme row EstA, substrate column group Vinyl propionate (C3): kcat (s^-1) = 160; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 160 s^-1 -> 160.0 s^(-1); the catalog holds 160.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 53.333333333333336 s^(-1)*mM^(-1) is the exact quotient 160 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: vinyl propionate


substrate_name: tripropionin

smiles: CCC(=O)OCC(COC(=O)CC)OC(=O)CC

column_label: Table 1 (journal page 31), decoded transcription, enzyme row EstA, substrate column group Tripropionin (C3): kcat (s^-1) = 60; Km/K0.5 (mM) = 0.35.

normalized_value_unit_evidence: kcat: printed cell 60 s^-1 -> 60.0 s^(-1); the catalog holds 60.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.35 mM -> 0.35 mM; the catalog holds 0.35 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 171.42857142857144 s^(-1)*mM^(-1) is the exact quotient 60 / 0.35 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 1 (journal page 31) 'Kinetic parameters kcat and K0.5 of the hydrolysis of short chain triacylglycerols by members of the HSL family and other lipolytic and non-lipolytic carboxyesterases'

substrate: tripropionin


organism: Bacillus sp. SCSIO 15121

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Bacillus subtilis

substrate_name: vinyl butyrate

smiles: C=COC(=O)CCC

substrate: vinyl butyrate


substrate_name: vinyl laurate

smiles: C=COC(=O)CCCCCCCCCCC

substrate: vinyl laurate


substrate_name: Triacetin

smiles: CC(=O)OCC(COC(C)=O)OC(C)=O

substrate: Triacetin


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl butyrate

sequence_source: UniProtKB/TrEMBL Q7SIG1 direct REST lookup on 2026-05-31

column_label: Table 4 (journal page 33), decoded transcription, enzyme row EST2, substrate column group p-NPB (C4): kcat (s^-1) = 480; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 480 s^-1 -> 480.0 s^(-1); the catalog holds 480.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 9600.0 s^(-1)*mM^(-1) is the exact quotient 480 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

table_label: Table 4 (journal page 33) 'Kinetic parameters kcat and K0.5 of the hydrolysis of p-NPB by members of the HSL family'

substrate: p-Nitrophenyl butyrate


column_label: Table 3 (journal page 32), decoded transcription, enzyme row EST2, substrate column group Vinyl acetate (C2): kcat (s^-1) = 110; Km/K0.5 (mM) = 2.5.

normalized_value_unit_evidence: kcat: printed cell 110 s^-1 -> 110.0 s^(-1); the catalog holds 110.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2.5 mM -> 2.5 mM; the catalog holds 2.5 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 44.0 s^(-1)*mM^(-1) is the exact quotient 110 / 2.5 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row EST2, substrate column group Vinyl propionate (C3): kcat (s^-1) = 980; Km/K0.5 (mM) = 6.

normalized_value_unit_evidence: kcat: printed cell 980 s^-1 -> 980.0 s^(-1); the catalog holds 980.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 6 mM -> 6.0 mM; the catalog holds 6.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 163.33333333333334 s^(-1)*mM^(-1) is the exact quotient 980 / 6 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 1 (journal page 31), decoded transcription, enzyme row EST2, substrate column group Tripropionin (C3): kcat (s^-1) = 835; Km/K0.5 (mM) = 0.75.

normalized_value_unit_evidence: kcat: printed cell 835 s^-1 -> 835.0 s^(-1); the catalog holds 835.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.75 mM -> 0.75 mM; the catalog holds 0.75 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 1113.3333333333333 s^(-1)*mM^(-1) is the exact quotient 835 / 0.75 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


organism: Aquamicrobium sp. FPB-1

sequence_source: UniProtKB/TrEMBL A0A024CDT8 direct REST lookup on 2026-05-31