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.


enzyme_display_name: alcohol dehydrogenase

organism: Mycobacterium sp.

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

smiles: CCCCO

data_origin: experimental

enzyme: alcohol dehydrogenase

status: unverified

source: oed


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


organism: Rattus norvegicus

verification_status: verified

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'Butanal'; isoenzyme column group ADH-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.

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)

status: verified


verification_status: corrected

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.

status: corrected


organism: Geobacillus stearothermophilus

substrate_name: Butyraldehyde

substrate: Butyraldehyde


organism: Homo sapiens

smiles: CCC/C=C\CO

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

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

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

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

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


organism: Drosophila lebanonensis

assay_conditions_summary: pH 9.5; 296.65 K; buffer 0.5 mM-NAD+ in 0.1 M-glycine/NaOH; cofactor NAD+

column_label: Table 3 (journal page 487, PDF page 7), part (b) Kinetic coefficients; substrate row 'cis-4-Methylcyclohexanol'; column 'Vm (1/phi0) (s^-1)' = 7.1; column 'Km (phi2/phi0) (mM)' = 1.0; column 'Vm/Km (1/phi2) (s^-1 mM^-1)' = 7.1; part (a) column 'Rate relative to ethanol' = 1100.

normalized_value_unit_evidence: kcat: printed Table 3(b) Vm cell 7.1 s^-1 (Vm is the catalytic centre activity, molecules of product produced per second per enzyme active site); already in s^-1, no conversion applies; the exported value is 7.1 s^(-1). Km: printed Table 3(b) cell 1.0 mM; already in mM, no conversion applies; the exported value is 1.0 mM. kcat/Km: printed Table 3(b) Vm/Km cell 7.1 s^-1 mM^-1; already in s^-1 mM^-1, no conversion applies; the exported value is 7.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3(b), journal page 487, substrate row 'cis-4-Methylcyclohexanol': Vm = kcat = 7.1 s^-1; Km = 1.0 mM; printed Vm/Km = kcat/Km = 7.1 s^-1 mM^-1.

row_label: Table 3(b), substrate row 'cis-4-Methylcyclohexanol' (journal page 487, PDF page 7)

table_label: Table 3: Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b) Kinetic coefficients, columns Vm (1/phi0) (s^-1), Km (phi2/phi0) (mM) and Vm/Km (1/phi2) (s^-1 mM^-1) (Biochem. J. 1986, 235:481-490)


organism: Arabidopsis thaliana

substrate_name: cinnamyl alcohol

column_label: Table II. Kinetic properties of Arabidopsis FALDH. Substrate row 'Cinnamylalcohol (pH 7.5)'; column 'Km (uM)' = 22,000; column 'Kcat (min^-1)' = 324; column 'Kcat/Km (mM^-1 min^-1)' = 15.

normalized_value_unit_evidence: Km: printed Table II cell 22,000 uM; 22,000 / 1000 = 22.0 mM; the exported value is 3.5 mM. kcat: printed Table II cell 324 min^-1; the printed turnover column is per MINUTE, so 324 / 60 = 5.4 s^(-1); the exported value is 20.333 s^(-1). kcat/Km: printed Table II cell 15 mM^-1 min^-1; the printed efficiency column is also per MINUTE, so 15 / 60 = 0.25 s^(-1)*mM^(-1); the exported value is 5.809428571428571 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, substrate row 'Cinnamylalcohol (pH 7.5)': Km = 22,000 uM; Kcat = 324 min^-1; Kcat/Km = 15 mM^-1 min^-1.

substrate: cinnamyl alcohol


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

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

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


organism: Sulfolobus acidocaldarius

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 '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: 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


organism: Aeropyrum pernix

substrate_name: Cyclohexanol

substrate: Cyclohexanol


organism: Coturnix coturnix japonica

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

column_label: Table III: Kinetic Constants of ADH-3 (Biochemistry 1989, volume 28, pages 6245-6251); printed column heads substrate | Km (mM) | kcat (min^-1) | kcat/Km (mM^-1 min^-1). Table III, substrate row cyclohexanol; column Km (mM) = 5.2; column kcat (min^-1) = 213; column kcat/Km (mM^-1 min^-1) = 41. captured primary segment: cyclohexanol | Km 5.2 mM | kcat 213 min^-1 | kcat/Km 41 mM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table III cell 5.2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.2 mM; the exported value is 5.2 mM. kcat: printed Table III cell 213 min^-1; 1 min^-1 is 1/60 s^-1, so 213 / 60 = 3.55 s^(-1); the exported value is 3.55 s^(-1). kcat/Km: printed Table III cell 41 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 41 / 60 = 0.6833333333333333 s^(-1)*mM^(-1). Quotient disclosure for this row: 3.55 / 5.2 = 0.6826923076923076 s^-1 mM^-1, the exported value, and 213 / 5.2 = 40.96 mM^-1 min^-1 rounds to the printed catalytic-efficiency cell 41 mM^-1 min^-1.

raw_value_unit_evidence: Table III, substrate row cyclohexanol: Km = 5.2 mM; kcat = 213 min^-1; printed kcat/Km = 41 mM^-1 min^-1.

row_label: Table III, substrate row cyclohexanol


organism: Equus caballus

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

column_label: Table III (journal page 12594); row `Cyclohexanol`; column group `EqADH`; column `V1` (printed unit row `s^-1`) = 6.1; column `Km` (printed unit row `mM`) = 1.1. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 6.1 s^-1 -> 6.1 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 1.1 mM -> 1.1 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 6.1 s^-1 / 1.1 mM = 5.545454545454545 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Cyclohexanol`, EqADH columns: V1 = 6.1 (printed unit row: s^-1); Km = 1.1 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

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

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


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

mutation_type: substitution


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


organism: Macaca mulatta

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

column_label: Table III (journal page 12594); row `Cyclohexanol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 3.0; column `Km` (unit row `mM`) = 0.024. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 3.0 s^-1 -> 3.0 s^-1; catalog holds 3.0 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.024 mM -> 0.024 mM; catalog holds 0.024 mM; no conversion. kcat/Km: not printed; catalog 125.0 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Cyclohexanol`, MmADHalpha columns: V1 = 3.0 (unit row: s^-1); Km = 0.024 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

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


column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row '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)


organism: Struthio camelus


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: Cyclohexanone

substrate: Cyclohexanone


organism: Sulfolobus solfataricus

substrate_name: Cyclopetanone

substrate: Cyclopetanone


organism: Sphingomonas sp. A1

substrate_name: D-allonate

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row '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


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-mannonate

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-ribonate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-ribonate'; column 'K m (mM)' = 16 ± 1; column 'V max (mU mg-1)' = 10 ± 0.2; column 'k cat (s-1)' = 5.2 x 10^-3 ± 0.1 x 10^-3; column 'k cat/K m (mM-1 s-1)' = 3.3 x 10^-4 ± 0.3 x 10^-4; column 'k cat/K m (%)' = 0.3.

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 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 3.3 x 10^-4 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 0.00033 s^(-1)*mM^(-1); the exported value is 0.000325 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-ribonate': K m = 16 ± 1 mM; V max = 10 ± 0.2 mU mg^-1; k cat = 5.2 x 10^-3 ± 0.1 x 10^-3 s^-1; printed k cat/K m = 3.3 x 10^-4 ± 0.3 x 10^-4 mM^-1 s^-1; printed relative k cat/K m = 0.3 per cent.

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

substrate: D-ribonate


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-talonate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-talonate'; column 'K m (mM)' = 6 ± 1; column 'V max (mU mg-1)' = 42 ± 2; column 'k cat (s-1)' = 2.1 x 10^-2 ± 0.1 x 10^-2; column 'k cat/K m (mM-1 s-1)' = 3.4 x 10^-3 ± 0.9 x 10^-3; column 'k cat/K m (%)' = 3.

normalized_value_unit_evidence: Km: printed Table 1 cell 6 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 6.0 mM; the exported value is 6.0 mM. kcat: printed Table 1 cell 2.1 x 10^-2 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 0.021 s^(-1); the exported value is 0.021 s^(-1). kcat/Km: printed Table 1 cell 3.4 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 0.0034 s^(-1)*mM^(-1); the exported value is 0.0035 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-talonate': K m = 6 ± 1 mM; V max = 42 ± 2 mU mg^-1; k cat = 2.1 x 10^-2 ± 0.1 x 10^-2 s^-1; printed k cat/K m = 3.4 x 10^-3 ± 0.9 x 10^-3 mM^-1 s^-1; printed relative k cat/K m = 3 per cent.

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

substrate: D-talonate


substrate_name: ethanol

smiles: CCO

substrate: ethanol


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


organism: Geobacillus thermodenitrificans


organism: Ogataea angusta


substrate_name: Ethanol

substrate: Ethanol


column_label: Table III (journal page 12594); row `Ethanol`; column group `EqADH`; column `V1` (printed unit row `s^-1`) = 7.8; column `Km` (printed unit row `mM`) = 0.80. Table III has no kcat/Km column.

normalized_value_unit_evidence: kcat: printed V1 cell 7.8 s^-1 -> 7.8 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.80 mM -> 0.8 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 7.8 s^-1 / 0.80 mM = 9.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III, row `Ethanol`, EqADH columns: V1 = 7.8 (printed unit row: s^-1); Km = 0.80 (printed unit row: mM). The table prints V1 (turnover number) and Km only; it has no ratio column.

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


substrate_name: D-Xylonate

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-xylonate'; column 'K m (mM)' = 24 ± 2; column 'V max (mU mg-1)' = 66 ± 4; column 'k cat (s-1)' = 3.2 x 10^-2 ± 0.2 x 10^-2; column 'k cat/K m (mM-1 s-1)' = 1.4 x 10^-3 ± 0.2 x 10^-3; column 'k cat/K m (%)' = 1.

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 3.2 x 10^-2 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 0.032 s^(-1); the exported value is 0.032 s^(-1). kcat/Km: printed Table 1 cell 1.4 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 0.0014 s^(-1)*mM^(-1); the exported value is 0.0013333333333333333 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-xylonate': K m = 24 ± 2 mM; V max = 66 ± 4 mU mg^-1; k cat = 3.2 x 10^-2 ± 0.2 x 10^-2 s^-1; printed k cat/K m = 1.4 x 10^-3 ± 0.2 x 10^-3 mM^-1 s^-1; printed relative k cat/K m = 1 per cent.

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

substrate: D-Xylonate


substrate_name: D-Arabitol

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row 'd-arabitol'; column 'K m (mM)' = 2.2 x 10^2 ± 0.2 x 10^2; column 'V max (mU mg-1)' = 39 ± 1; column 'k cat (s-1)' = 19 x 10^-3 ± 0.6 x 10^-3; column 'k cat/K m (mM-1 s-1)' = 8.7 x 10^-5 ± 1 x 10^-5; column 'k cat/K m (%)' = 0.08.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.2 x 10^2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 220.0 mM; the exported value is 220.0 mM. kcat: printed Table 1 cell 19 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 0.019 s^(-1); the exported value is 0.0019 s^(-1). kcat/Km: printed Table 1 cell 8.7 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 0.000087 s^(-1)*mM^(-1); the exported value is 0.000008636363636363637 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, body row 'd-arabitol': K m = 2.2 x 10^2 ± 0.2 x 10^2 mM; V max = 39 ± 1 mU mg^-1; k cat = 19 x 10^-3 ± 0.6 x 10^-3 s^-1; printed k cat/K m = 8.7 x 10^-5 ± 1 x 10^-5 mM^-1 s^-1; printed relative k cat/K m = 0.08 per cent.

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

substrate: D-Arabitol


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


organism: Kluyveromyces lactis

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


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


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


organism: Moraxella sp.

sequence: MLYANPNTESSPVGFRKKYDNFI

wild_type_sequence: MLYANPNTESSPVGFRKKYDNFI


organism: Mus musculus


organism: Rattus norvegicus


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.


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


substrate_name: ethyl 3-methyl-2-oxobutyrate

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

substrate: ethyl 3-methyl-2-oxobutyrate


substrate_name: ethyl benzoylformate

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 '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


organism: Saccharomyces cerevisiae

substrate_name: furfural

substrate: furfural


substrate_name: Geraniol

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

column_label: Plant Physiology 132(4):2248-2255 (2003); Table II. Kinetic properties of Arabidopsis FALDH; substrate row 'Geraniol (pH 10)': column 'Km (uM)' = 800; column 'Kcat (min^-1)' = 1,200; column 'Kcat/Km (mM^-1 min^-1)' = 1,500.

normalized_value_unit_evidence: Km: printed cell 800 uM / 1000 = 0.8 mM, matching the catalog km 0.8 mM exactly. kcat: printed cell 1,200 min^-1 / 60 = 20.0 s^-1, matching the catalog kcat 20.0 s^(-1) exactly. Kcat/Km: printed cell 1,500 mM^-1 min^-1 / 60 = 25.0 s^(-1)*mM^(-1), which EQUALS the catalog kcat_over_km 25.0 exactly (and also equals the quotient of the row's own pair, 20.0 / 0.8), so the ratio provenance is typed primary_reported.

raw_value_unit_evidence: Table II, substrate row 'Geraniol (pH 10)': Km = 800 uM; Kcat = 1,200 min^-1; printed Kcat/Km = 1,500 mM^-1 min^-1.

substrate: Geraniol


organism: Pyrobaculum calidifontis

substrate_name: Glutaraldehyde

smiles: O=CCCCC=O

substrate: Glutaraldehyde


organism: Homo sapiens

substrate_name: Glycol

smiles: OCCO

substrate: Glycol


assay_conditions_summary: pH 10

column_label: Table I row ethylene glycol, isoenzyme column (6), printed header 7,7,, raw cell 57000 microM, normalized 57 mM; Table II row ethylene glycol, isoenzyme column (6), printed header 7,7,, raw cell 85 min^-1, normalized 1.41666666667 s^-1; Table III row ethylene glycol, isoenzyme column (6), printed header 7,7,, raw cell 0.015 x 10^5 M^-1*min^-1, normalized 0.025 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=57 normalized_unit=mM; kcat normalized_value=1.41666666667 normalized_unit=s^-1; kcat/Km normalized_value=0.025 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=57000 raw_unit=microM; kcat raw_value=85 raw_unit=min^-1; kcat/Km raw_value=0.015 raw_unit=10^5 M^-1*min^-1

row_label: ethylene glycol

table_label: Tables I-III. Human class I ADH isoenzyme kinetic constants toward various alcohols


substrate_name: glycolaldehyde

smiles: O=CCO

substrate: glycolaldehyde


organism: Drosophila lebanonensis

smiles: CCCCCC(C)O


organism: Sulfolobus acidocaldarius

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


substrate_name: isoborneol

substrate: isoborneol


organism: Geobacillus stearothermophilus

substrate_name: iso-propanol

smiles: CC(C)O

substrate: iso-propanol


substrate_name: methanol

smiles: CO

substrate: methanol


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: Methylcrotyl alcohol

smiles: CC=CC(C)O

substrate: Methylcrotyl alcohol


substrate_name: methyl o-chlorobenzoylformate

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


organism: Equus caballus

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

column_label: Table III (journal page 12594); row `Methanol`; column group `EqADH`; column `V1` (unit row `s^-1`) = 0.16; column `Km` (unit row `mM`) = 310. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 0.16 s^-1 -> 0.16 s^-1; catalog holds 0.16 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 310 mM -> 310.0 mM; catalog holds 310.0 mM; no conversion. kcat/Km: not printed; catalog 0.0005161290322580645 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Methanol`, EqADH columns: V1 = 0.16 (unit row: s^-1); Km = 310 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

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


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-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.

substrate: 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.


organism: Aeropyrum pernix

substrate_name: NAD+

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

substrate: NAD+


organism: Coturnix coturnix japonica


assay_conditions_summary: pH 9.5; 296.65 K; cofactor NAD+


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


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

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


organism: Macaca mulatta

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -9, so it is treated as a source-provided variant sequence.


organism: Mycobacterium sp.

assay_conditions_summary: pH 7; 303.15 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+'


assay_conditions_summary: pH 10.5; 338.15 K; cofactor NAD+


organism: Sulfolobus solfataricus

assay_conditions_summary: pH 8; 338.15 K; cofactor NADH


organism: Thermococcus kodakarensis

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

column_label: Table 4. Kinetic parameters for TkADH; substrate cell `NAD+ (0-1.0)`; cosubstrate cell `meso-2,3-Butanediol (100)`; column `Apparent Km (mM)` = 0.127 (printed with its error term); column `kcat (s^-1)` = 30.8 (printed with its error term); column `kcat/Km (s^-1 mM^-1)` = 243 +/- 10 (printed, rounded).

normalized_value_unit_evidence: Km: paper cell 0.127 mM -> 0.127 mM; catalog holds 0.127 mM; no conversion (the paper's Km column already prints mM, so no uM/1000 step applies). kcat: paper cell 30.8 s^-1 -> 30.8 s^-1; catalog holds 30.8 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 243 +/- 10 s^-1 mM^-1 for this row, but the catalog holds 242.51968503937007 s^(-1)*mM^(-1), which is exactly 30.8 / 0.127.

raw_value_unit_evidence: Table 4, substrate row `NAD+ (0-1.0)`, cosubstrate `meso-2,3-Butanediol (100)`: Apparent Km = 0.127 (column unit mM); kcat = 30.8 (column unit s^-1); printed kcat/Km = 243 +/- 10 (column unit s^-1 mM^-1).

row_label: Table 4 substrate row `NAD+ (0-1.0)` with cosubstrate `meso-2,3-Butanediol (100)`

table_label: Table 4. Kinetic parameters for TkADH


substrate_name: NADH

assay_conditions_summary: pH 8; 333.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH


organism: Geobacillus thermodenitrificans


assay_conditions_summary: pH 9; 298.15 K; cofactor NADH


assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADH


organism: Kluyveromyces lactis

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADH


organism: Moraxella sp.

assay_conditions_summary: pH 6; 298.15 K; cofactor NADH


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


substrate_name: R-(+)-cis-Verbenol

substrate: R-(+)-cis-Verbenol


assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH

column_label: Table 3 (PDF page 8 of 12, journal page 200) 'Steady-state kinetic constants of SaADH', substrate row `NADH`: kcat (s^-1) = 28.0; Km (mM) = 0.16; kcat/Km (s^-1 mM^-1) = 175.

normalized_value_unit_evidence: kcat: printed cell 28.0 s^-1 is already the export unit s^(-1); the exported value is 5.0 s^(-1). Km: printed cell 0.16 mM is already the export unit mM; the exported value is 0.16 mM. kcat/Km: the paper PRINTS the kcat/Km cell 175 s^-1 mM^-1 for this substrate line, already in the export unit s^(-1)*mM^(-1); the exported value is 31.25 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `NADH`


assay_conditions_summary: pH 5; 338.15 K; cofactor NADH


assay_conditions_summary: pH 6; 343.15 K; cofactor NADH


substrate_name: NADP+

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


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

column_label: Table 4. Kinetic parameters for TkADH; substrate cell `NADP+ (0-1.0)`; cosubstrate cell `meso-2,3-Butanediol (100)`; column `Apparent Km (mM)` = 0.113 (printed with its error term); column `kcat (s^-1)` = 30.0 (printed with its error term); column `kcat/Km (s^-1 mM^-1)` = 265 +/- 15 (printed, rounded).

normalized_value_unit_evidence: Km: paper cell 0.113 mM -> 0.113 mM; catalog holds 0.113 mM; no conversion (the paper's Km column already prints mM, so no uM/1000 step applies). kcat: paper cell 30.0 s^-1 -> 30.0 s^-1; catalog holds 30.0 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 265 +/- 15 s^-1 mM^-1 for this row, but the catalog holds 265.4867256637168 s^(-1)*mM^(-1), which is exactly 30.0 / 0.113.

raw_value_unit_evidence: Table 4, substrate row `NADP+ (0-1.0)`, cosubstrate `meso-2,3-Butanediol (100)`: Apparent Km = 0.113 (column unit mM); kcat = 30.0 (column unit s^-1); printed kcat/Km = 265 +/- 15 (column unit s^-1 mM^-1).

row_label: Table 4 substrate row `NADP+ (0-1.0)` with cosubstrate `meso-2,3-Butanediol (100)`


organism: Yokenella sp.

assay_conditions_summary: pH 8; 328.15 K; cofactor NADP+


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 6.5; 338.15 K; cofactor 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_name: n-butanol

substrate: n-butanol


smiles: OCCCCCCCCO


substrate_name: p-Anisaldehyde

substrate: p-Anisaldehyde


smiles: CCC(O)CC

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

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

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

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

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


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


substrate_name: Prenol

smiles: CC(C)=CCO

substrate: Prenol


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

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

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

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


assay_conditions_summary: pH 9.5; 296.65 K; buffer 0.5 mM-NAD+ in 0.1 M-glycine/NaOH; cofactor NAD+

column_label: Table 3 (journal page 486, PDF page 6), part (b) Kinetic coefficients; substrate row 'R-(-)-Hexan-2-ol'; column 'Vm (1/phi0) (s^-1)' = 8.0; column 'Km (phi2/phi0) (mM)' = 0.16; column 'Vm/Km (1/phi2) (s^-1 mM^-1)' = 50.0; part (a) column 'Rate relative to ethanol' = 2238.

normalized_value_unit_evidence: kcat: printed Table 3(b) Vm cell 8.0 s^-1 (Vm is the catalytic centre activity, molecules of product produced per second per enzyme active site); already in s^-1, no conversion applies; the exported value is 8.0 s^(-1). Km: printed Table 3(b) cell 0.16 mM; already in mM, no conversion applies; the exported value is 0.16 mM. kcat/Km: printed Table 3(b) Vm/Km cell 50.0 s^-1 mM^-1; already in s^-1 mM^-1, no conversion applies; the exported value is 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3(b), journal page 486, substrate row 'R-(-)-Hexan-2-ol': Vm = kcat = 8.0 s^-1; Km = 0.16 mM; printed Vm/Km = kcat/Km = 50.0 s^-1 mM^-1.

row_label: Table 3(b), substrate row 'R-(-)-Hexan-2-ol' (journal page 486, PDF page 6)


column_label: Table 3 (journal page 486, PDF page 6), part (b) Kinetic coefficients; substrate row 'R-(-)-3-Methylbutan-2-ol'; column 'Vm (1/phi0) (s^-1)' = 8.0; column 'Km (phi2/phi0) (mM)' = 1.02; column 'Vm/Km (1/phi2) (s^-1 mM^-1)' = 8.0; part (a) column 'Rate relative to ethanol' = 1301.

normalized_value_unit_evidence: kcat: printed Table 3(b) Vm cell 8.0 s^-1 (Vm is the catalytic centre activity, molecules of product produced per second per enzyme active site); already in s^-1, no conversion applies; the exported value is 8.0 s^(-1). Km: printed Table 3(b) cell 1.02 mM; already in mM, no conversion applies; the exported value is 1.02 mM. kcat/Km: printed Table 3(b) Vm/Km cell 8.0 s^-1 mM^-1; already in s^-1 mM^-1, no conversion applies; the exported value is 7.8431372549019605 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3(b), journal page 486, substrate row 'R-(-)-3-Methylbutan-2-ol': Vm = kcat = 8.0 s^-1; Km = 1.02 mM; printed Vm/Km = kcat/Km = 8.0 s^-1 mM^-1.

row_label: Table 3(b), substrate row 'R-(-)-3-Methylbutan-2-ol' (journal page 486, PDF page 6)


substrate_name: (R)-alpha-tetralol

assay_conditions_summary: pH 8; 338.15 K; cofactor NAD+

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: Retinol

substrate: Retinol


organism: Mus musculus

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

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

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

row_label: Mouse ADH1 | all-trans-retinol


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

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

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

row_label: Mouse ADH4 | all-trans-retinol


column_label: Table 3 (journal page 486, PDF page 6), part (b) Kinetic coefficients; substrate row 'R-(-)-Octan-2-ol'; column 'Vm (1/phi0) (s^-1)' = 8.1; column 'Km (phi2/phi0) (mM)' = 0.50; column 'Vm/Km (1/phi2) (s^-1 mM^-1)' = 16.2; part (a) column 'Rate relative to ethanol' = 1931.

normalized_value_unit_evidence: kcat: printed Table 3(b) Vm cell 8.1 s^-1 (Vm is the catalytic centre activity, molecules of product produced per second per enzyme active site); already in s^-1, no conversion applies; the exported value is 8.1 s^(-1). Km: printed Table 3(b) cell 0.50 mM; already in mM, no conversion applies; the exported value is 0.5 mM. kcat/Km: printed Table 3(b) Vm/Km cell 16.2 s^-1 mM^-1; already in s^-1 mM^-1, no conversion applies; the exported value is 16.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3(b), journal page 486, substrate row 'R-(-)-Octan-2-ol': Vm = kcat = 8.1 s^-1; Km = 0.50 mM; printed Vm/Km = kcat/Km = 16.2 s^-1 mM^-1.

row_label: Table 3(b), substrate row 'R-(-)-Octan-2-ol' (journal page 486, PDF page 6)


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

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

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

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


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


organism: Branchiostoma lanceolatum

substrate_name: S-(Hydroxymethyl)glutathione

substrate: S-(Hydroxymethyl)glutathione


organism: Homo sapiens


substrate_name: S-Nitrosoglutathione

substrate: S-Nitrosoglutathione


substrate_name: tert-butanol

smiles: CC(C)(C)O

substrate: tert-butanol


substrate_name: tert-butyl acetoacetate

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

substrate: tert-butyl acetoacetate


smiles: CCCC=CCO

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

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

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

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


organism: Drosophila lebanonensis


substrate_name: methanol

assay_conditions_summary: pH 10

column_label: Table I row methanol, isoenzyme column (6), printed header 7,7,, raw cell 74000 microM, normalized 74 mM; Table II row methanol, isoenzyme column (6), printed header 7,7,, raw cell 22 min^-1, normalized 0.366666666667 s^-1; Table III row methanol, isoenzyme column (6), printed header 7,7,, raw cell 0.003 x 10^5 M^-1*min^-1, normalized 0.005 s^-1*mM^-1

normalized_value_unit_evidence: Km normalized_value=74 normalized_unit=mM; kcat normalized_value=0.366666666667 normalized_unit=s^-1; kcat/Km normalized_value=0.005 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=74000 raw_unit=microM; kcat raw_value=22 raw_unit=min^-1; kcat/Km raw_value=0.003 raw_unit=10^5 M^-1*min^-1

row_label: methanol

substrate: methanol


organism: Sulfolobus acidocaldarius


organism: Sphingomonas sp. A1

substrate_name: D-Gluconate

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

column_label: Table 1: Kinetic parameters of SpsADH with various substrates (Microbial Biotechnology 2018, volume 11, issue 4, page 747), body row '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: isobutanol

smiles: CC(C)CO

substrate: isobutanol


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

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

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

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

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


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 '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.


organism: Rattus norvegicus

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_name: benzyl alcohol

substrate: benzyl alcohol


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

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

normalized_value_unit_evidence: Km: printed Table I cell 7 uM; 7 / 1000 = 0.007 mM; the exported value is 0.008 mM. kcat: printed Table II cell 127 min^-1; the printed turnover column is per MINUTE, so 127 / 60 = 2.1166666666666667 s^(-1); the exported value is 2.117 s^(-1). kcat/Km: printed Table III cell 180 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 180 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 300.0 s^(-1)*mM^(-1); the exported value is 264.625 s^(-1)*mM^(-1).

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

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

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


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

column_label: Table III (journal page 12594); row `Benzyl alcohol`; column group `MmADHalpha`; column `V1` (unit row `s^-1`) = 0.75; column `Km` (unit row `mM`) = 0.036. No kcat/Km column exists in Table III.

normalized_value_unit_evidence: kcat: paper V1 cell 0.75 s^-1 -> 0.75 s^-1; catalog holds 0.75 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.036 mM -> 0.036 mM; catalog holds 0.036 mM; no conversion. kcat/Km: not printed; catalog 20.833333333333336 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

raw_value_unit_evidence: Table III, row `Benzyl alcohol`, MmADHalpha columns: V1 = 0.75 (unit row: s^-1); Km = 0.036 (unit row: mM). The table prints V1 (turnover number) and Km only; no ratio column.

row_label: Table III row `Benzyl alcohol`, MmADHalpha column group


column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row '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.


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.


organism: Aeropyrum pernix

smiles: CCCCO


organism: Arabidopsis thaliana

substrate_name: farnesol

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table II. Kinetic properties of Arabidopsis FALDH. Substrate row 'Farnesol (pH 7.5)'; column 'Km (uM)' = 7.7; column 'Kcat (min^-1)' = 6; column 'Kcat/Km (mM^-1 min^-1)' = 780.

normalized_value_unit_evidence: Km: printed Table II cell 7.7 uM; 7.7 / 1000 = 0.0077 mM; the exported value is 0.003 mM. kcat: printed Table II cell 6 min^-1; the printed turnover column is per MINUTE, so 6 / 60 = 0.1 s^(-1); the exported value is 2.1 s^(-1). kcat/Km: printed Table II cell 780 mM^-1 min^-1; the printed efficiency column is also per MINUTE, so 780 / 60 = 13.0 s^(-1)*mM^(-1); the exported value is 700.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table II, substrate row 'Farnesol (pH 7.5)': Km = 7.7 uM; Kcat = 6 min^-1; Kcat/Km = 780 mM^-1 min^-1.

substrate: farnesol


substrate_name: Cyclohexanol

kcat_over_km_display: Not reported

substrate: Cyclohexanol


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


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

column_label: Table I (Km, uM), Table II (kcat, min^-1) and Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row '16-HHA'; isoenzyme column (7) b1g1; Table I cell = 13; Table II cell = 72; Table III cell = 55.

normalized_value_unit_evidence: Km: printed Table I cell 13 uM; 13 / 1000 = 0.013000000000000001 mM; the exported value is 0.013 mM. kcat: printed Table II cell 72 min^-1; the printed turnover column is per MINUTE, so 72 / 60 = 1.2 s^(-1); the exported value is 1.2 s^(-1). kcat/Km: printed Table III cell 55 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 55 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 91.66666666666667 s^(-1)*mM^(-1); the exported value is not carried by this catalog row, which exports only kcat and Km.

raw_value_unit_evidence: Journal page 1860, substrate row '16-HHA', isoenzyme column (7) b1g1: Table I Km = 13 uM; Table II kcat = 72 min^-1; Table III kcat/Km = 55 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 55 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row '16-HHA', isoenzyme column (7) b1g1

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCCCCO

column_label: Table I (Km, uM), Table II (kcat, min^-1) and Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row 'octanol'; isoenzyme column (5) b1g2; Table I cell = 5; Table II cell = 70; Table III cell = 140.

normalized_value_unit_evidence: Km: printed Table I cell 5 uM; 5 / 1000 = 0.005 mM; the exported value is 0.009 mM. kcat: printed Table II cell 70 min^-1; the printed turnover column is per MINUTE, so 70 / 60 = 1.1666666666666667 s^(-1); the exported value is 1.167 s^(-1). kcat/Km: printed Table III cell 140 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 140 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 233.33333333333334 s^(-1)*mM^(-1); the exported value is not carried by this catalog row, which exports only kcat and Km.

raw_value_unit_evidence: Journal page 1860, substrate row 'octanol', isoenzyme column (5) b1g2: Table I Km = 5 uM; Table II kcat = 70 min^-1; Table III kcat/Km = 140 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 140 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row 'octanol', isoenzyme column (5) b1g2


substrate_name: Ethanol

smiles: CCO

column_label: Table I (Km, uM), Table II (kcat, min^-1) and Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row 'ethanol'; isoenzyme column (7) b1g1; Table I cell = 1100; Table II cell = 150; Table III cell = 1.4.

normalized_value_unit_evidence: Km: printed Table I cell 1100 uM; 1100 / 1000 = 1.1 mM; the exported value is 1.4 mM. kcat: printed Table II cell 150 min^-1; the printed turnover column is per MINUTE, so 150 / 60 = 2.5 s^(-1); the exported value is 2.5 s^(-1). kcat/Km: printed Table III cell 1.4 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 1.4 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 2.3333333333333335 s^(-1)*mM^(-1); the exported value is not carried by this catalog row, which exports only kcat and Km.

raw_value_unit_evidence: Journal page 1860, substrate row 'ethanol', isoenzyme column (7) b1g1: Table I Km = 1100 uM; Table II kcat = 150 min^-1; Table III kcat/Km = 1.4 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 1.4 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row 'ethanol', isoenzyme column (7) b1g1

substrate: Ethanol


assay_conditions_summary: pH 10; 298.15 K; buffer 2.4 mM NAD+ and 0.1 M glycine; cofactor NAD+

column_label: Table I row ethanol, isoenzyme column (3), alpha-beta1, raw cell 2000 microM, normalized 2 mM; Table II row ethanol, isoenzyme column (3), alpha-beta1, raw cell 200 min^-1, normalized 3.333333333333333333333333333333333333333 s^-1

normalized_value_unit_evidence: Km normalized_value=2 normalized_unit=mM; kcat normalized_value=3.333333333333333333333333333333333333333 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=2000 raw_unit=microM; kcat raw_value=200 raw_unit=min^-1

row_label: ethanol / isoenzyme column (3), alpha-beta1

table_label: Tables I-II. Human class I ADH isoenzyme kinetic constants toward various alcohols


substrate_name: Glycol

smiles: OCCO

column_label: Table I row ethylene glycol, isoenzyme column (5), beta1-gamma2, raw cell 36000 microM, normalized 36 mM; Table II row ethylene glycol, isoenzyme column (5), beta1-gamma2, raw cell 55 min^-1, normalized 0.9166666666666666666666666666666666666667 s^-1

normalized_value_unit_evidence: Km normalized_value=36 normalized_unit=mM; kcat normalized_value=0.9166666666666666666666666666666666666667 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=36000 raw_unit=microM; kcat raw_value=55 raw_unit=min^-1

row_label: ethylene glycol / isoenzyme column (5), beta1-gamma2

substrate: Glycol


column_label: Table I row ethylene glycol, isoenzyme column (7), beta1-gamma1, raw cell 220000 microM, normalized 220 mM; Table II row ethylene glycol, isoenzyme column (7), beta1-gamma1, raw cell 50 min^-1, normalized 0.8333333333333333333333333333333333333333 s^-1

normalized_value_unit_evidence: Km normalized_value=220 normalized_unit=mM; kcat normalized_value=0.8333333333333333333333333333333333333333 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=220000 raw_unit=microM; kcat raw_value=50 raw_unit=min^-1

row_label: ethylene glycol / isoenzyme column (7), beta1-gamma1


column_label: Table I row ethylene glycol, isoenzyme column (3), alpha-beta1, raw cell 47000 microM, normalized 47 mM; Table II row ethylene glycol, isoenzyme column (3), alpha-beta1, raw cell 50 min^-1, normalized 0.8333333333333333333333333333333333333333 s^-1

normalized_value_unit_evidence: Km normalized_value=47 normalized_unit=mM; kcat normalized_value=0.8333333333333333333333333333333333333333 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=47000 raw_unit=microM; kcat raw_value=50 raw_unit=min^-1

row_label: ethylene glycol / isoenzyme column (3), alpha-beta1


organism: Equus caballus

substrate_name: NAD+

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

substrate: NAD+


column_label: Table I (Km, uM), Table II (kcat, min^-1) and Table III (kcat/Km x 10^-5, M^-1 min^-1), journal page 1860 (PDF page 4). Substrate row 'methanol'; isoenzyme column (5) b1g2; Table I cell = 18000; Table II cell = 12; Table III cell = 0.007.

normalized_value_unit_evidence: Km: printed Table I cell 18000 uM; 18000 / 1000 = 18.0 mM; the exported value is 18.0 mM. kcat: printed Table II 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 III cell 0.007 under the spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 0.007 x 10^5 M^-1 min^-1; 1 M^-1 min^-1 = 1/60000 s^(-1)*mM^(-1), so the printed cell is 0.011666666666666667 s^(-1)*mM^(-1); the exported value is not carried by this catalog row, which exports only kcat and Km.

raw_value_unit_evidence: Journal page 1860, substrate row 'methanol', isoenzyme column (5) b1g2: Table I Km = 18000 uM; Table II kcat = 12 min^-1; Table III kcat/Km = 0.007 under the printed spanning column head kcat/Km x 10^-5 (M^-1 min^-1), i.e. 0.007 x 10^5 M^-1 min^-1.

row_label: Tables I-III, substrate row 'methanol', isoenzyme column (5) b1g2


column_label: Table I row methanol, isoenzyme column (7), beta1-gamma1, raw cell 21000 microM, normalized 21 mM; Table II row methanol, isoenzyme column (7), beta1-gamma1, raw cell 12 min^-1, normalized 0.2 s^-1

normalized_value_unit_evidence: Km normalized_value=21 normalized_unit=mM; kcat normalized_value=0.2 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=21000 raw_unit=microM; kcat raw_value=12 raw_unit=min^-1

row_label: methanol / isoenzyme column (7), beta1-gamma1


column_label: Table I row methanol, isoenzyme column (3), alpha-beta1, raw cell 15000 microM, normalized 15 mM; Table II row methanol, isoenzyme column (3), alpha-beta1, raw cell 12 min^-1, normalized 0.2 s^-1

normalized_value_unit_evidence: Km normalized_value=15 normalized_unit=mM; kcat normalized_value=0.2 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=15000 raw_unit=microM; kcat raw_value=12 raw_unit=min^-1

row_label: methanol / isoenzyme column (3), alpha-beta1


column_label: Table I row benzyl alcohol, isoenzyme column (5), beta1-gamma2, raw cell 11 microM, normalized 0.011 mM; Table II row benzyl alcohol, isoenzyme column (5), beta1-gamma2, raw cell 58 min^-1, normalized 0.9666666666666666666666666666666666666667 s^-1

normalized_value_unit_evidence: Km normalized_value=0.011 normalized_unit=mM; kcat normalized_value=0.9666666666666666666666666666666666666667 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=11 raw_unit=microM; kcat raw_value=58 raw_unit=min^-1

row_label: benzyl alcohol / isoenzyme column (5), beta1-gamma2


column_label: Table I row benzyl alcohol, isoenzyme column (7), beta1-gamma1, raw cell 26 microM, normalized 0.026 mM; Table II row benzyl alcohol, isoenzyme column (7), beta1-gamma1, raw cell 115 min^-1, normalized 1.916666666666666666666666666666666666667 s^-1

normalized_value_unit_evidence: Km normalized_value=0.026 normalized_unit=mM; kcat normalized_value=1.916666666666666666666666666666666666667 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=26 raw_unit=microM; kcat raw_value=115 raw_unit=min^-1

row_label: benzyl alcohol / isoenzyme column (7), beta1-gamma1


column_label: Table I row benzyl alcohol, isoenzyme column (3), alpha-beta1, raw cell 4 microM, normalized 0.004 mM; Table II row benzyl alcohol, isoenzyme column (3), alpha-beta1, raw cell 170 min^-1, normalized 2.833333333333333333333333333333333333333 s^-1

normalized_value_unit_evidence: Km normalized_value=0.004 normalized_unit=mM; kcat normalized_value=2.833333333333333333333333333333333333333 normalized_unit=s^-1

raw_value_unit_evidence: Km raw_value=4 raw_unit=microM; kcat raw_value=170 raw_unit=min^-1

row_label: benzyl alcohol / isoenzyme column (3), alpha-beta1


organism: Saccharolobus solfataricus

source_db: brenda

source: brenda


smiles: CCC(CC)O


smiles: CCC(C)O


kcat_display: Not reported

smiles: CCCC(C)O


organism: Zea mays

assay_conditions_summary: cofactor NAD+


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: ethanol

substrate: ethanol


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Geobacillus stearothermophilus

substrate_name: n-butanol

assay_conditions_summary: pH 8

substrate: n-butanol


assay_conditions_summary: pH 8; cofactor NADH


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


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


organism: Saccharomyces cerevisiae

substrate_name: furfural

substrate: furfural


organism: Alligator mississippiensis

smiles: CO


substrate_name: Octanol

substrate: Octanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: butanol

substrate: butanol


organism: Oenococcus oeni

assay_conditions_summary: pH 9; cofactor NAD+


assay_conditions_summary: pH 9


smiles: CC(CO)O


smiles: C(CO)CO


organism: Mycobacterium sp.

assay_conditions_summary: pH 7; cofactor NAD+


substrate_name: Butanal

assay_conditions_summary: pH 7; cofactor NADH

substrate: Butanal


organism: Parageobacillus thermoglucosidasius

assay_conditions_summary: pH 6


assay_conditions_summary: pH 6; cofactor NADH


organism: Drosophila virilis


smiles: CC(C)O


enzyme_display_name: alcohol dehydrogenase (NADP+)

organism: Homo sapiens

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7; cofactor NADP+

column_label: Table 6 (journal page 496), substrate row `1,2-Naphthoquinone` (chemical structure 29), enzyme sub-row `AKR7A2`; column `Km (uM)` = 102 +/- 10; column `kcat (min^-1)` = 435 +/- 27; column `kcat/Km (min^-1 . M^-1)` = 4.2 x 10^6.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `1,2-Naphthoquinone` (chemical structure 29), enzyme sub-row `AKR7A2`: Km (uM) = 102 +/- 10; kcat (min^-1) = 435 +/- 27; kcat/Km (min^-1 . M^-1) = 4.2 x 10^6.

table_label: Table 6  Kinetic properties of recombinant human AKR1A1 and AKR7A2 (journal page 496)

enzyme: alcohol dehydrogenase (NADP+)


column_label: Table 6 (journal page 496), substrate row `1,2-Naphthoquinone` (chemical structure 29), enzyme sub-row `AKR1A1`; column `Km (uM)` = 144 +/- 17; column `kcat (min^-1)` = 881 +/- 42; column `kcat/Km (min^-1 . M^-1)` = 6.2 x 10^6.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `1,2-Naphthoquinone` (chemical structure 29), enzyme sub-row `AKR1A1`: Km (uM) = 144 +/- 17; kcat (min^-1) = 881 +/- 42; kcat/Km (min^-1 . M^-1) = 6.2 x 10^6.


smiles: OCCCCCO

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


column_label: Table 6 (journal page 496), substrate row `16-Ketoestrone` (chemical structure 32), enzyme sub-row `AKR7A2`; column `Km (uM)` = 55 +/- 6; column `kcat (min^-1)` = 49 +/- 3; column `kcat/Km (min^-1 . M^-1)` = 9.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `16-Ketoestrone` (chemical structure 32), enzyme sub-row `AKR7A2`: Km (uM) = 55 +/- 6; kcat (min^-1) = 49 +/- 3; kcat/Km (min^-1 . M^-1) = 9.0 x 10^5.


column_label: Table 6 (journal page 496), substrate row `16-Ketoestrone` (chemical structure 32), enzyme sub-row `AKR1A1`; column `Km (uM)` = 213 +/- 2; column `kcat (min^-1)` = 425 +/- 5; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^6.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `16-Ketoestrone` (chemical structure 32), enzyme sub-row `AKR1A1`: Km (uM) = 213 +/- 2; kcat (min^-1) = 425 +/- 5; kcat/Km (min^-1 . M^-1) = 2.0 x 10^6.


organism: Escherichia coli

smiles: CCCCO

assay_conditions_summary: pH 7.7; 295.15 K; cofactor NADP+


organism: Mycobacterium bovis

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+


smiles: CCCCCCCC=O

assay_conditions_summary: pH 7.3; 295.15 K; cofactor NADP+


smiles: CCCCCO


smiles: CCCO


organism: Thermococcus guaymasensis

assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADP+


smiles: CCC(C)=O

column_label: Table 3 (Kinetic parameter values for T. guaymasensis ADH), substrate row '2-Butanone'; column 'Cosubstrate (mM)' = NADPH (0.2 mM); column 'Apparent Km (mM)' = 0.31; column 'Apparent Vmax (U/mg)' = 285; column 'kcat (s-1)' = 190; column 'kcat/Km (s-1 M-1)' = 613,000.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.31 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.31 mM; the exported value is 0.31 mM. kcat: printed Table 3 cell 190 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 190.0 s^(-1); the exported value is 190.0 s^(-1). kcat/Km: printed Table 3 cell 613,000 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 613,000 / 1000 = 613.0 s^-1 mM^-1; the exported value is 612.9032258064516 s^(-1)*mM^(-1), which is the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 3, substrate row '2-Butanone' with cosubstrate NADPH (0.2 mM): apparent Km = 0.31 mM; apparent Vmax = 285 U/mg; kcat = 190 s^-1; printed kcat/Km = 613,000 s^-1 M^-1.

table_label: Table 3: Kinetic parameter values for T. guaymasensis ADH (Journal of Bacteriology 2011, 193(12):3009-3019)


column_label: Table 6 (journal page 496), substrate row `2-Chlorobenzaldehyde` (chemical structure 5), enzyme sub-row `AKR7A2`; column `Km (uM)` = 8584 +/- 269; column `kcat (min^-1)` = 149 +/- 4; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `2-Chlorobenzaldehyde` (chemical structure 5), enzyme sub-row `AKR7A2`: Km (uM) = 8584 +/- 269; kcat (min^-1) = 149 +/- 4; kcat/Km (min^-1 . M^-1) = 2.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `2-Chlorobenzaldehyde` (chemical structure 5), enzyme sub-row `AKR1A1`; column `Km (uM)` = 657 +/- 21; column `kcat (min^-1)` = 9 +/- 1; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `2-Chlorobenzaldehyde` (chemical structure 5), enzyme sub-row `AKR1A1`: Km (uM) = 657 +/- 21; kcat (min^-1) = 9 +/- 1; kcat/Km (min^-1 . M^-1) = 2.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `2-Nitrobenzaldehyde` (chemical structure 8), enzyme sub-row `AKR7A2`; column `Km (uM)` = 1060 +/- 130; column `kcat (min^-1)` = 95 +/- 7; column `kcat/Km (min^-1 . M^-1)` = 9.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `2-Nitrobenzaldehyde` (chemical structure 8), enzyme sub-row `AKR7A2`: Km (uM) = 1060 +/- 130; kcat (min^-1) = 95 +/- 7; kcat/Km (min^-1 . M^-1) = 9.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `2-Nitrobenzaldehyde` (chemical structure 8), enzyme sub-row `AKR1A1`; column `Km (uM)` = 54 +/- 4; column `kcat (min^-1)` = 3 +/- 0.1; column `kcat/Km (min^-1 . M^-1)` = 5.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `2-Nitrobenzaldehyde` (chemical structure 8), enzyme sub-row `AKR1A1`: Km (uM) = 54 +/- 4; kcat (min^-1) = 3 +/- 0.1; kcat/Km (min^-1 . M^-1) = 5.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `3-Chlorobenzaldehyde` (chemical structure 6), enzyme sub-row `AKR7A2`; column `Km (uM)` = 1913 +/- 249; column `kcat (min^-1)` = 9 +/- 1; column `kcat/Km (min^-1 . M^-1)` = 5.0 x 10^3.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `3-Chlorobenzaldehyde` (chemical structure 6), enzyme sub-row `AKR7A2`: Km (uM) = 1913 +/- 249; kcat (min^-1) = 9 +/- 1; kcat/Km (min^-1 . M^-1) = 5.0 x 10^3.


column_label: Table 6 (journal page 496), substrate row `3-Chlorobenzaldehyde` (chemical structure 6), enzyme sub-row `AKR1A1`; column `Km (uM)` = 2413 +/- 232; column `kcat (min^-1)` = 442 +/- 7; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `3-Chlorobenzaldehyde` (chemical structure 6), enzyme sub-row `AKR1A1`: Km (uM) = 2413 +/- 232; kcat (min^-1) = 442 +/- 7; kcat/Km (min^-1 . M^-1) = 2.0 x 10^5.


smiles: CC(CCO)CCO


smiles: CC(C)CCO


organism: Sus scrofa

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 10; 298.15 K; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14550 and applied mutation signature R308A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM phosphate; cofactor NADP+

column_label: Table 1, substrate block p-carboxybenzaldehyde, value column R308A: the kcat line of that block prints 6.8, the Km line prints 0.11 and the kcat/Km line prints 63170. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 6.8 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 6.8 s^(-1). Km: printed cell 0.11 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 0.11 mM. kcat/Km: printed cell 63170 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 63170 / 1000 = 63.17 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 6.8 / 0.11 = 61.81818181818181 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block p-carboxybenzaldehyde, column R308A: kcat = 6.8; Km = 0.11; printed kcat/Km = 63170. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.

table_label: Table 1: Kinetic Constants of Wild-type and Mutant Aldehyde Reductase (Biochemistry 1996, 35, 14276-14280). Each substrate name is a block label and the three lines under it are that block's kcat, Km and kcat/Km lines. Each block line carries five value columns: the wild-type column, the two single-substitution enzyme-form columns and the two wild-type-to-enzyme-form comparison columns. The table footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.