sequence_source: UniProtKB reviewed accession P12711

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row '1-Butanol'; isoenzyme column group ADH-3; Km (mM) cell = 0.17; kcat (min^-1) cell = 50; kcat/Km (mM^-1 min^-1) cell = 300.

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

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


enzyme_display_name: alcohol dehydrogenase

organism: Rattus norvegicus

substrate_name: m-Nitrobenzaldehyde

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor 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 '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.

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)

data_origin: experimental

enzyme: alcohol dehydrogenase

substrate: m-Nitrobenzaldehyde

status: corrected

source: oed


substrate_name: 12-Hydroxydodecanoic acid

sequence_source: UniProtKB reviewed accession P06757

smiles: O=C(O)CCCCCCCCCCCO

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row '12-Hydroxydodecanoic acid'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 1200; kcat/Km (mM^-1 min^-1) cell = 860.

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

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

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

substrate: 12-Hydroxydodecanoic acid


smiles: CCCCCO

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row '1-Pentanol'; isoenzyme column group ADH-1; Km (mM) cell = 3.1; kcat (min^-1) cell = 2930; kcat/Km (mM^-1 min^-1) cell = 950.

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

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


substrate_name: Butanal

verification_status: verified

smiles: CCCC=O

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

substrate: Butanal

status: verified


verification_status: unverified

kcat_over_km_origin: calculated

smiles: CC=CCO

status: unverified


substrate_name: methanol

smiles: CO

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row 'Methanol'; isoenzyme column group ADH-3; Km (mM) cell = 380; kcat (min^-1) cell = 12; kcat/Km (mM^-1 min^-1) cell = 0.03.

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

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

substrate: methanol


column_label: Table 6 (Kinetic constants of rat ADH isoenzymes toward various alcohols and aldehydes at pH 7.5), journal page 186, PDF page 8. Substrate row 'm-Nitrobenzaldehyde'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 58800; kcat/Km (mM^-1 min^-1) cell = 42000.

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

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


organism: Saccharomyces cerevisiae

substrate_name: acetaldehyde

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

smiles: CC=O

substrate: acetaldehyde


substrate_name: furfural

substrate: furfural


organism: Sphingomonas sp. A1

substrate_name: D-mannonate

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

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NADH

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

normalized_value_unit_evidence: Km: printed Table 1 cell 14 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 14.0 mM; the exported value is 14.0 mM. kcat: printed Table 1 cell 5.3 x 10^-1 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.53 s^(-1); the exported value is 0.53 s^(-1). kcat/Km: printed Table 1 cell 3.8 x 10^-2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.038 s^(-1)*mM^(-1); the exported value is 0.03785714285714286 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

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

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

substrate: D-mannonate


substrate_name: D-sorbitol

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

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

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

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

substrate: D-sorbitol


substrate_name: D-altronate

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

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

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

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

substrate: D-altronate


substrate_name: D-Arabitol

substrate: D-Arabitol


substrate_name: D-Gluconate

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

normalized_value_unit_evidence: Km: printed Table 1 cell 12 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 12.0 mM; the exported value is 12.0 mM. kcat: printed Table 1 cell 9.8 x 10^-1 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.98 s^(-1); the exported value is 0.98 s^(-1). kcat/Km: printed Table 1 cell 8.2 x 10^-2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.082 s^(-1)*mM^(-1); the exported value is 0.08166666666666667 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

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

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

substrate: D-Gluconate


substrate_name: D-allonate

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

normalized_value_unit_evidence: Km: printed Table 1 cell 16 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 16.0 mM; the exported value is 16.0 mM. kcat: printed Table 1 cell 1.8 x 10^-1 s^-1; the printed unit s^-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 0.18 s^(-1); the exported value is 0.18 s^(-1). kcat/Km: printed Table 1 cell 1.1 x 10^-2 mM^-1 s^-1; mM^-1 s^-1 is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the paper value is 0.011 s^(-1)*mM^(-1); the exported value is 0.01125 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

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

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

substrate: D-allonate


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

smiles: CCCCO


substrate_name: benzyl alcohol

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row 'Benzyl alcohol'; isoenzyme column group ADH-1; Km (mM) cell = 1.4; kcat (min^-1) cell = 5380; kcat/Km (mM^-1 min^-1) cell = 3900.

normalized_value_unit_evidence: Km: printed Table 5 cell 1.4 mM; already in mM, no unit conversion applies; the exported value is 1.4 mM. kcat: printed Table 5 cell 5380 min^-1; the printed turnover column is per MINUTE, so 5380 / 60 = 89.66666666666667 s^(-1); the exported value is 89.667 s^(-1). kcat/Km: printed Table 5 cell 3900 mM^-1 min^-1; 1 mM^-1 min^-1 = 1/60 s^(-1)*mM^(-1), so 3900 / 60 = 65.0 s^(-1)*mM^(-1); the exported value is 64.04785714285715 s^(-1)*mM^(-1).

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

substrate: benzyl alcohol


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

column_label: Table 5 (Kinetic constants of rat ADH isoenzymes toward various alcohols at pH 10.0), journal page 185, PDF page 7. Substrate row 'Benzyl alcohol'; isoenzyme column group ADH-3; Km (mM) cell = 0.05; kcat (min^-1) cell = 60; kcat/Km (mM^-1 min^-1) cell = 1200.

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

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


smiles: CCCCCCCC=O


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: Acetaldehyde

kcat_over_km_display: Not reported

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

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

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

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

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

row_label: ADH | Adh1p

substrate: Acetaldehyde


substrate_name: glycolaldehyde

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

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

smiles: O=CCO

substrate: glycolaldehyde


organism: Sulfolobus acidocaldarius

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

assay_conditions_summary: pH 5.5; 338.15 K; cofactor NADH

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

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

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


substrate_name: ethyl benzoylformate

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'Ethyl benzoylformate'; column kcat (s-1) = 2.35; column Km (mM) = 5.3; column kcat/Km (s-1 mM-1) = 0.44. captured primary segment: Ethyl benzoylformate | kcat 2.35 s^-1 | Km 5.3 mM | kcat/Km 0.44 s^-1 mM^-1

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

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

substrate: ethyl benzoylformate


substrate_name: NAD+

assay_conditions_summary: pH 8; 338.15 K; cofactor NAD+

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'NAD+'; column kcat (s-1) = 3.7; column Km (mM) = 0.44; column kcat/Km (s-1 mM-1) = 8.4. captured primary segment: NAD+ | kcat 3.7 s^-1 | Km 0.44 mM | kcat/Km 8.4 s^-1 mM^-1

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

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

row_label: Table 3, substrate row 'NAD+'

substrate: NAD+


column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row '1-Phenyl-1,2-propanedione'; column kcat (s-1) = 3.1; column Km (mM) = 12.1; column kcat/Km (s-1 mM-1) = 0.25. captured primary segment: 1-Phenyl-1,2-propanedione | kcat 3.1 s^-1 | Km 12.1 mM | kcat/Km 0.25 s^-1 mM^-1

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

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


column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'cis-Decahydro-1-naphthol'; column kcat (s-1) = 0.98; column Km (mM) = 4.2; column kcat/Km (s-1 mM-1) = 0.23. captured primary segment: cis-Decahydro-1-naphthol | kcat 0.98 s^-1 | Km 4.2 mM | kcat/Km 0.23 s^-1 mM^-1

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

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


substrate_name: NADH

substrate: NADH


column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row '3-Methylcyclohexanone'; column kcat (s-1) = 3.8; column Km (mM) = 66.0; column kcat/Km (s-1 mM-1) = 0.06. captured primary segment: 3-Methylcyclohexanone | kcat 3.8 s^-1 | Km 66.0 mM | kcat/Km 0.06 s^-1 mM^-1

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

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


substrate_name: isatin

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'Isatin'; column kcat (s-1) = 22.0; column Km (mM) = 0.71; column kcat/Km (s-1 mM-1) = 31. captured primary segment: Isatin | kcat 22.0 s^-1 | Km 0.71 mM | kcat/Km 31 s^-1 mM^-1

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

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

row_label: Table 3, substrate row 'Isatin'

substrate: isatin


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


assay_conditions_summary: pH 10.5; 338.15 K; cofactor NAD+


organism: Sulfolobus solfataricus

substrate_name: Ethanol

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

smiles: CCO

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

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

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

substrate: Ethanol


smiles: CCC(C)O

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

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


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

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


smiles: CC(C)O

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

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


smiles: CCC(O)CC

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

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


substrate_name: methyl o-chlorobenzoylformate

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

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'Methyl o-chlorobenzoylformate'; column kcat (s-1) = 9.2; column Km (mM) = 2.8; column kcat/Km (s-1 mM-1) = 3.3. captured primary segment: Methyl o-chlorobenzoylformate | kcat 9.2 s^-1 | Km 2.8 mM | kcat/Km 3.3 s^-1 mM^-1

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

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

substrate: methyl o-chlorobenzoylformate


substrate_name: cycloheptanol

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'Cycloheptanol'; column kcat (s-1) = 4.4; column Km (mM) = 9.3; column kcat/Km (s-1 mM-1) = 0.47. captured primary segment: Cycloheptanol | kcat 4.4 s^-1 | Km 9.3 mM | kcat/Km 0.47 s^-1 mM^-1

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

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

row_label: Table 3, substrate row 'Cycloheptanol'

substrate: cycloheptanol


substrate_name: methyl benzoylformate

column_label: Table 3: Steady-state kinetic constants of SaADH (Extremophiles 2010, 14:193-204); printed column heads Substrate | kcat (s-1) | Km (mM) | kcat/Km (s-1 mM-1). Table 3, substrate row 'Methyl benzoylformate'; column kcat (s-1) = 6.2; column Km (mM) = 6.5; column kcat/Km (s-1 mM-1) = 0.95. captured primary segment: Methyl benzoylformate | kcat 6.2 s^-1 | Km 6.5 mM | kcat/Km 0.95 s^-1 mM^-1

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

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

substrate: methyl benzoylformate


substrate_name: (R)-alpha-tetralol

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

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

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

substrate: (R)-alpha-tetralol


substrate_name: (S)-alpha-tetralol

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

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

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

substrate: (S)-alpha-tetralol


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


substrate_name: benzil

substrate: benzil


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

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

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


smiles: CCCO

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

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


substrate_name: p-Anisaldehyde

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

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

substrate: p-Anisaldehyde


organism: Thermococcus kodakarensis

substrate_name: NADP+

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

assay_conditions_summary: pH 9; 343.15 K; cofactor NADP+

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

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

table_label: Table 4. Kinetic parameters for TkADH

substrate: NADP+


smiles: CC(O)C(C)O

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

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

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

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

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


assay_conditions_summary: pH 6; 343.15 K; cofactor NADH


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

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

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

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


substrate_name: acetoin

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

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

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

substrate: acetoin


substrate_name: D-ribonate

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

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

substrate: D-ribonate


substrate_name: D-talonate

substrate: D-talonate


substrate_name: D-Xylonate

substrate: D-Xylonate


organism: Struthio camelus

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

smiles: CCCCCCCCO


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

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

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

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


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: ethyl benzoylformate

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

substrate: ethyl benzoylformate


substrate_name: isoborneol

substrate: isoborneol


substrate_name: ethyl 3-methyl-2-oxobutyrate

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

substrate: ethyl 3-methyl-2-oxobutyrate


substrate_name: NADH

assay_conditions_summary: pH 5; 338.15 K; cofactor NADH

substrate: NADH


substrate_name: benzyl alcohol

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

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

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

substrate: benzyl alcohol


substrate_name: Acetone

smiles: CC(C)=O

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

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

substrate: Acetone


smiles: CCC(C)=O

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

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


substrate_name: Cyclopetanone

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

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

substrate: Cyclopetanone


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

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


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

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

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


smiles: CCCC(C)O

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

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


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: NAD+

sequence_source: UniProtKB Q5JI09 direct FASTA

assay_conditions_summary: pH 9; 343.15 K; cofactor NAD+

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

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

substrate: NAD+


organism: Yokenella sp.

sequence_source: UniProtKB W6CX26 direct FASTA

smiles: C/C=C/C=O

assay_conditions_summary: pH 6.5; 338.15 K; cofactor NADPH

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

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

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


assay_conditions_summary: pH 8; 328.15 K; cofactor NADP+


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

normalized_value_unit_evidence: kcat: printed cell 93.3 s^-1 -> 93.3 s^(-1); the catalog holds 93.3 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 14 mM -> 14 mM; the catalog holds 14.0 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `6.6` s^-1 mM^-1 for this row -> 6.6 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 6.664285714285714 s^(-1)*mM^(-1), which is the full-precision quotient 93.3 / 14 of the row's own kcat and Km cells and is not the printed ratio cell.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `Benzyl alcohol` with cosubstrate NADP^+ (0.4): Km (mM) = 14; Kcat (s^-1) = 93.3; Kcat/Km (s^-1 mM^-1) = 6.6. Every one of these three numerals is printed in the Table 5 cell shown; the +/- terms are the SD reported by Table 5 footnote a.


smiles: C/C=C/CO

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

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

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


substrate_name: benzaldehyde

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

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

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

substrate: benzaldehyde


substrate_name: NADPH

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

normalized_value_unit_evidence: kcat: printed cell 433 s^-1 -> 433 s^(-1); the catalog holds 433.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 0.6 mM -> 0.6 mM; the catalog holds 0.6 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: the paper PRINTS the Kcat/Km cell `720` s^-1 mM^-1 for this row -> 720.0 s^(-1)*mM^(-1); no unit conversion applied (the paper prints s^-1 mM^-1 directly). The catalog instead holds 721.6666666666667 s^(-1)*mM^(-1), which is the full-precision quotient 433 / 0.6 of the row's own kcat and Km cells and is not the printed ratio cell.

raw_value_unit_evidence: TABLE 5. Kinetic parameters of recombinant YsADH, substrate row `NADPH` with cosubstrate Crotonaldehyde (4.9): Km (mM) = 0.6; Kcat (s^-1) = 433; Kcat/Km (s^-1 mM^-1) = 720. Every one of these three numerals is printed in the Table 5 cell shown; the +/- terms are the SD reported by Table 5 footnote a.

substrate: NADPH


enzyme_display_name: carboxylesterase

organism: Aspergillus niger

substrate_name: Vinylacetate

sequence_source: UniProtKB:Q6ED33 canonical sequence

smiles: C=CCC(=O)O

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

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

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

enzyme: carboxylesterase

substrate: Vinylacetate


substrate_name: vinyl propionate

smiles: C=COC(=O)CC

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

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

substrate: vinyl propionate


substrate_name: tripropionin

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

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

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

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

substrate: tripropionin


organism: Bacillus sp. SCSIO 15121

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


organism: Bacillus subtilis

substrate_name: vinyl butyrate

smiles: C=COC(=O)CCC

substrate: vinyl butyrate


substrate_name: vinyl laurate

smiles: C=COC(=O)CCCCCCCCCCC

substrate: vinyl laurate


substrate_name: Triacetin

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

substrate: Triacetin


organism: Alicyclobacillus acidocaldarius

substrate_name: p-Nitrophenyl butyrate

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

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

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

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

substrate: p-Nitrophenyl butyrate


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

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


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

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


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

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


organism: Aquamicrobium sp. FPB-1

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


organism: Archaeoglobus fulgidus

substrate_name: tributyrin

sequence_source: UniProtKB O28558 direct FASTA lookup

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

column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Tributyrin (C4): kcat (s^-1) = 95; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 95 s^-1 -> 95.0 s^(-1); the catalog holds 95.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 1900.0 s^(-1)*mM^(-1) is the exact quotient 95 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: tributyrin


column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Tripropionin (C3): kcat (s^-1) = 110; Km/K0.5 (mM) = 0.30.

normalized_value_unit_evidence: kcat: printed cell 110 s^-1 -> 110.0 s^(-1); the catalog holds 110.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.30 mM -> 0.3 mM; the catalog holds 0.3 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 366.6666666666667 s^(-1)*mM^(-1) is the exact quotient 110 / 0.30 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl propionate (C3): kcat (s^-1) = 200; Km/K0.5 (mM) = 7.

normalized_value_unit_evidence: kcat: printed cell 200 s^-1 -> 200.0 s^(-1); the catalog holds 200.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 7 mM -> 7.0 mM; the catalog holds 7.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 28.571428571428573 s^(-1)*mM^(-1) is the exact quotient 200 / 7 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl acetate (C2): kcat (s^-1) = 50; Km/K0.5 (mM) = 4.

normalized_value_unit_evidence: kcat: printed cell 50 s^-1 -> 50.0 s^(-1); the catalog holds 50.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 4 mM -> 4.0 mM; the catalog holds 4.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 12.5 s^(-1)*mM^(-1) is the exact quotient 50 / 4 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row AFEST, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 210; Km/K0.5 (mM) = 2.5.

normalized_value_unit_evidence: kcat: printed cell 210 s^-1 -> 210.0 s^(-1); the catalog holds 210.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2.5 mM -> 2.5 mM; the catalog holds 2.5 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 84.0 s^(-1)*mM^(-1) is the exact quotient 210 / 2.5 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 1 (journal page 31), decoded transcription, enzyme row AFEST, substrate column group Triacetin (C2): kcat (s^-1) = 40; Km/K0.5 (mM) = 10.

normalized_value_unit_evidence: kcat: printed cell 40 s^-1 -> 40.0 s^(-1); the catalog holds 40.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 10 mM -> 10.0 mM; the catalog holds 10.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 4.0 s^(-1)*mM^(-1) is the exact quotient 40 / 10 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


sequence_source: UniProtKB Q6ED33 direct FASTA lookup

column_label: Table 1 (journal page 31), decoded transcription, enzyme row EstA, substrate column group Triacetin (C2): kcat (s^-1) = 265; Km/K0.5 (mM) = 15.

normalized_value_unit_evidence: kcat: printed cell 265 s^-1 -> 265.0 s^(-1); the catalog holds 265.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 15 mM -> 15.0 mM; the catalog holds 15.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 17.666666666666668 s^(-1)*mM^(-1) is the exact quotient 265 / 15 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row EstA, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 25; Km/K0.5 (mM) = 2.

normalized_value_unit_evidence: kcat: printed cell 25 s^-1 -> 25.0 s^(-1); the catalog holds 25.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 2 mM -> 2.0 mM; the catalog holds 2.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 12.5 s^(-1)*mM^(-1) is the exact quotient 25 / 2 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


organism: Actinidia eriantha

substrate_name: 4-Methylumbelliferyl butyrate

sequence_source: UniProtKB Q0ZPV7 direct lookup on 2026-05-31

substrate: 4-Methylumbelliferyl butyrate


organism: Aeropyrum pernix

substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


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

mutation_type: substitution


substrate_name: 4-nitrophenyl dodecanoate

substrate: 4-nitrophenyl dodecanoate


organism: Cavia porcellus


organism: Escherichia coli

substrate_name: p-Nitrophenyl propionate

substrate: p-Nitrophenyl propionate


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


substrate_name: p-Nitrophenyl laurate

substrate: p-Nitrophenyl laurate


substrate_name: p-Nitrophenyl caproate

sequence_source: UniProtKB:P13001 canonical sequence, REST lookup on 2026-05-31; RCSB/SIFTS PDB 1M33 maps BioH to P13001.

substrate: p-Nitrophenyl caproate


organism: Ferroplasma acidiphilum

sequence_source: UniProtKB:Q2PCE5 canonical sequence, REST lookup on 2026-05-31; EMBL AJ850914/CAH64533.1 and RCSB/SIFTS PDB 3WJ2 support the same accession.


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl propionate

substrate: 4-nitrophenyl propionate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474V/R526V/T560W to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 333.15 K; buffer 50 mmol/L phosphate

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S022; second column 'Mutant' = W474V/R526V/T560W; column 'kcat (s−1)' = 23.50; column 'Km (μmol/L)' = 2.43; column 'kcat/Km (s−1 /mmol·L−1)' = 9662.

normalized_value_unit_evidence: kcat: printed Table 2 cell 23.50 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 23.5 s^(-1). Km: printed Table 2 cell 2.43 under the column head μmol/L; 2.43 / 1000 = 0.0024300000000000003 mM; the exported value is 0.00243 mM. kcat/Km: printed Table 2 cell 9662 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 9662.0 s^-1 mM^-1; the exported value is 9670.781893004116 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S022: kcat = 23.50 in the column head unit s−1; Km = 2.43 in the column head unit μmol/L; printed kcat/Km = 9662 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S022 (the W474V/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488A/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S011; second column 'Mutant' = F488A/R526V/T560W; column 'kcat (s−1)' = 12.08; column 'Km (μmol/L)' = 7.37; column 'kcat/Km (s−1 /mmol·L−1)' = 1638.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.08 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 12.08 s^(-1). Km: printed Table 2 cell 7.37 under the column head μmol/L; 7.37 / 1000 = 0.00737 mM; the exported value is 0.00737 mM. kcat/Km: printed Table 2 cell 1638 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1638.0 s^-1 mM^-1; the exported value is 1639.0773405698778 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S011: kcat = 12.08 in the column head unit s−1; Km = 7.37 in the column head unit μmol/L; printed kcat/Km = 1638 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S011 (the F488A/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature R526V to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = P01; second column 'Mutant' = R526V; column 'kcat (s−1)' = 5.47; column 'Km (μmol/L)' = 11.8; column 'kcat/Km (s−1 /mmol·L−1)' = 462.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 5.47 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 5.47 s^(-1). Km: printed Table 2 cell 11.8 under the column head μmol/L; 11.8 / 1000 = 0.011800000000000001 mM; the exported value is 0.0118 mM. kcat/Km: printed Table 2 cell 462.5 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 462.5 s^-1 mM^-1; the exported value is 463.5593220338983 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row P01: kcat = 5.47 in the column head unit s−1; Km = 11.8 in the column head unit μmol/L; printed kcat/Km = 462.5 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row P01 (the R526V site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474V/F488G/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = C01; second column 'Mutant' = W474V/F488G/R526V/T560W; column 'kcat (s−1)' = 26.25; column 'Km (μmol/L)' = 2.34; column 'kcat/Km (s−1 /mmol·L−1)' = 11218.

normalized_value_unit_evidence: kcat: printed Table 2 cell 26.25 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 26.25 s^(-1). Km: printed Table 2 cell 2.34 under the column head μmol/L; 2.34 / 1000 = 0.00234 mM; the exported value is 0.00234 mM. kcat/Km: printed Table 2 cell 11218 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 11218.0 s^-1 mM^-1; the exported value is 11217.948717948717 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row C01: kcat = 26.25 in the column head unit s−1; Km = 2.34 in the column head unit μmol/L; printed kcat/Km = 11218 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row C01 (the W474V/F488G/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488P/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S013; second column 'Mutant' = F488P/R526V/T560W; column 'kcat (s−1)' = 8.17; column 'Km (μmol/L)' = 3.88; column 'kcat/Km (s−1 /mmol·L−1)' = 2107.

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.17 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 8.17 s^(-1). Km: printed Table 2 cell 3.88 under the column head μmol/L; 3.88 / 1000 = 0.0038799999999999998 mM; the exported value is 0.00388 mM. kcat/Km: printed Table 2 cell 2107 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 2107.0 s^-1 mM^-1; the exported value is 2105.6701030927834 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S013: kcat = 8.17 in the column head unit s−1; Km = 3.88 in the column head unit μmol/L; printed kcat/Km = 2107 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S013 (the F488P/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature W474A/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S02; second column 'Mutant' = W474A/R526V/T560W; column 'kcat (s−1)' = 12.61; column 'Km (μmol/L)' = 1.83; column 'kcat/Km (s−1 /mmol·L−1)' = 6876.

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.61 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 12.61 s^(-1). Km: printed Table 2 cell 1.83 under the column head μmol/L; 1.83 / 1000 = 0.00183 mM; the exported value is 0.00183 mM. kcat/Km: printed Table 2 cell 6876 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 6876.0 s^-1 mM^-1; the exported value is 6890.710382513661 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S02: kcat = 12.61 in the column head unit s−1; Km = 1.83 in the column head unit μmol/L; printed kcat/Km = 6876 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S02 (the W474A/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488W/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S015; second column 'Mutant' = F488W/R526V/T560W; column 'kcat (s−1)' = 1.73; column 'Km (μmol/L)' = 1.01; column 'kcat/Km (s−1 /mmol·L−1)' = 1712.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.73 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 1.73 s^(-1). Km: printed Table 2 cell 1.01 under the column head μmol/L; 1.01 / 1000 = 0.00101 mM; the exported value is 0.00101 mM. kcat/Km: printed Table 2 cell 1712 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1712.0 s^-1 mM^-1; the exported value is 1712.8712871287128 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S015: kcat = 1.73 in the column head unit s−1; Km = 1.01 in the column head unit μmol/L; printed kcat/Km = 1712 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S015 (the F488W/R526V/T560W site-directed variant of apAAP)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9YBQ2 and applied mutation signature F488S/R526V/T560W to reconstruct the assayed variant sequence.

column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = S012; second column 'Mutant' = F488S/R526V/T560W; column 'kcat (s−1)' = 10.45; column 'Km (μmol/L)' = 5.79; column 'kcat/Km (s−1 /mmol·L−1)' = 1804.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10.45 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 10.45 s^(-1). Km: printed Table 2 cell 5.79 under the column head μmol/L; 5.79 / 1000 = 0.00579 mM; the exported value is 0.00579 mM. kcat/Km: printed Table 2 cell 1804 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 1804.0 s^-1 mM^-1; the exported value is 1804.8359240069083 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row S012: kcat = 10.45 in the column head unit s−1; Km = 5.79 in the column head unit μmol/L; printed kcat/Km = 1804 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row S012 (the F488S/R526V/T560W site-directed variant of apAAP)


column_label: Table 2: Kinetic parameters of wild type apAAP and its mutants for the hydrolysis of pNP-C12 at 60°C (Protein & Cell 2011, 2(6): 497-506); first column 'Enzyme' = WT; second column 'Mutant' = Wild type; column 'kcat (s−1)' = 1.35; column 'Km (μmol/L)' = 8.62; column 'kcat/Km (s−1 /mmol·L−1)' = 157.2.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.35 under the column head s−1; already in s^-1, no unit conversion applies; the exported value is 1.35 s^(-1). Km: printed Table 2 cell 8.62 under the column head μmol/L; 8.62 / 1000 = 0.00862 mM; the exported value is 0.00862 mM. kcat/Km: printed Table 2 cell 157.2 under the column head s−1 /mmol·L−1; one mmol·L−1 is one mM, so the printed cell is already 157.2 s^-1 mM^-1; the exported value is 156.6125290023202 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row WT: kcat = 1.35 in the column head unit s−1; Km = 8.62 in the column head unit μmol/L; printed kcat/Km = 157.2 in the column head unit s−1 /mmol·L−1.

row_label: Table 2, row WT (the wild type apAAP parent of that table)


substrate_name: p-Nitrophenyl dodecanoate

substrate: p-Nitrophenyl dodecanoate


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


sequence_variant_note: Mutation signature M211S matches the mutant residue at offset +0 and the reference residue at offset -1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 1 (journal page 31), decoded transcription, enzyme row EST2, substrate column group Triacetin (C2): kcat (s^-1) = 945; Km/K0.5 (mM) = 12.

normalized_value_unit_evidence: kcat: printed cell 945 s^-1 -> 945.0 s^(-1); the catalog holds 945.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 12 mM -> 12.0 mM; the catalog holds 12.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 78.75 s^(-1)*mM^(-1) is the exact quotient 945 / 12 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 3 (journal page 32), decoded transcription, enzyme row EST2, substrate column group Vinyl butyrate (C4): kcat (s^-1) = 1930; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 1930 s^-1 -> 1930.0 s^(-1); the catalog holds 1930.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 643.3333333333334 s^(-1)*mM^(-1) is the exact quotient 1930 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


column_label: Table 1 (journal page 31), decoded transcription, enzyme row EST2, substrate column group Tributyrin (C4): kcat (s^-1) = 1290; Km/K0.5 (mM) = 0.07.

normalized_value_unit_evidence: kcat: printed cell 1290 s^-1 -> 1290.0 s^(-1); the catalog holds 1290.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.07 mM -> 0.07 mM; the catalog holds 0.07 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 18428.571428571428 s^(-1)*mM^(-1) is the exact quotient 1290 / 0.07 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


sequence_source: UniProtKB A0A024CDT8 direct accession lookup


organism: Arabidopsis thaliana

substrate_name: Methyl indole-3-acetate

sequence_source: UniProtKB Q9SG92 direct accession lookup

substrate: Methyl indole-3-acetate


substrate_name: 4-nitrophenyl pentanoate

sequence_source: UniProtKB O28558 direct accession lookup

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl palmitate

sequence_source: UniProtKB O28511 direct accession lookup

substrate: 4-nitrophenyl palmitate


organism: Homo sapiens

substrate_name: L-Methylphenidate

substrate: L-Methylphenidate


substrate_name: D-Methylphenidate

substrate: D-Methylphenidate


substrate_name: Irinotecan

substrate: Irinotecan


substrate_name: vinyl laurate

substrate: vinyl laurate


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


substrate_name: vinyl propionate

substrate: vinyl propionate


substrate_name: vinyl butyrate

substrate: vinyl butyrate


substrate_name: Vinylacetate

substrate: Vinylacetate


enzyme_display_name: Carboxylesterase

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q2PCE5|exact_accession_lookup and applied mutation signature N248A/P256Q/E257G/S283F to reconstruct the assayed variant sequence.

enzyme: Carboxylesterase


enzyme_display_name: Carboxylic ester hydrolase Est55

organism: Geobacillus stearothermophilus

substrate_name: p-Nitrophenyl caproate

enzyme: Carboxylic ester hydrolase Est55

substrate: p-Nitrophenyl caproate


enzyme_display_name: Carboxylesterase Est30

enzyme: Carboxylesterase Est30


enzyme_display_name: Liver carboxylesterase 1

kcat_display: Not reported

enzyme: Liver carboxylesterase 1


enzyme_display_name: Carboxylesterase 2

enzyme: Carboxylesterase 2


substrate_name: Capecitabine

sequence_source: UniProtKB:Q6LAP9 checked 2026-05-31; displayed sequence is a 17-aa TrEMBL fragment, not accepted as a resolved full enzyme sequence

substrate: Capecitabine


sequence_source: UniProtKB:O00748 displayed Swiss-Prot canonical sequence, fetched 2026-05-31


substrate_name: tributyrin

substrate: tributyrin


substrate_name: Triacetin

substrate: Triacetin


substrate_name: tripropionin

substrate: tripropionin


organism: Klebsiella sp.

substrate_name: 4-nitrophenyl dodecanoate

sequence_source: UniProtKB Q52NW7 direct accession lookup

substrate: 4-nitrophenyl dodecanoate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl propanoate

substrate: 4-nitrophenyl propanoate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WK87 direct accession lookup

column_label: Table 4 (journal page 33), decoded transcription, enzyme row Rv1399c, substrate column group p-NPB (C4): kcat (s^-1) = 185; Km/K0.5 (mM) = 0.05.

normalized_value_unit_evidence: kcat: printed cell 185 s^-1 -> 185.0 s^(-1); the catalog holds 185.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.05 mM -> 0.05 mM; the catalog holds 0.05 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 3700.0 s^(-1)*mM^(-1) is the exact quotient 185 / 0.05 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.


organism: Oryctolagus cuniculus

substrate_name: Resmethrin

sequence_source: UniProtKB P12337 direct accession lookup

substrate: Resmethrin


organism: Pyrobaculum calidifontis

substrate_name: 4-nitrophenyl octanoate

sequence_source: UniProtKB Q8NKS0 direct accession lookup

substrate: 4-nitrophenyl octanoate


organism: Saccharolobus solfataricus

substrate_name: 4-nitrophenyl butyrate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q97VU1 and applied mutation signature R210A to reconstruct the assayed variant sequence.

column_label: Table 1 on journal page 1154, p-Nitrophenyl butyrate block, enzyme row R210A; column kcat/Km (s^-1 mM^-1) = 17; column Km (mM) = 0.63; column kcat (s^-1) = 10.

normalized_value_unit_evidence: kcat: printed Table 1 cell 10 s^-1; the printed column is already per second, so no unit conversion applies and the value carries over as 10.0 s^(-1). Km: printed Table 1 cell 0.63 mM; the printed column is already in mM, so no unit conversion applies and the value carries over as 0.63 mM. kcat/Km: printed Table 1 cell 17 s^-1 mM^-1; the printed unit is the canonical s^(-1)*mM^(-1), so no unit conversion applies and the cell carries over as 17.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme row R210A, p-Nitrophenyl butyrate block: kcat/Km = 17 s^-1 mM^-1; Km = 0.63 mM; kcat = 10 s^-1.

table_label: Table 1: Kinetic parameters of wild-type SsoPEst and R210A (Biotechnology Letters 2010, volume 32, pages 1151-1157)

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl hexanoate

sequence_source: UniProtKB M5DDN2 direct accession lookup.

substrate: 4-nitrophenyl hexanoate


substrate_name: 4-nitrophenyl hexadecanoate

substrate: 4-nitrophenyl hexadecanoate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


organism: Sulfurisphaera tokodaii

sequence_source: UniProtKB Q976W8 direct accession lookup.


sequence_source: UniProtKB Q976W8 direct accession lookup


substrate_name: 4-nitrophenyl tetradecanoate

substrate: 4-nitrophenyl tetradecanoate


substrate_name: Cypermethrin

sequence_source: UniProtKB reviewed accession P23141 (EST1_HUMAN; CES1; liver carboxylesterase 1)

substrate: Cypermethrin


sequence_source: UniProtKB reviewed accession O00748 (EST2_HUMAN; CES2; carboxylesterase 2/cocaine esterase)


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


organism: Sus scrofa

sequence_source: UniProtKB:Q29550 reviewed Swiss-Prot EST1_PIG sequence


substrate_name: Irinotecan

substrate: Irinotecan


substrate_name: p-Nitrophenyl butyrate

substrate: p-Nitrophenyl butyrate


organism: Pyrococcus furiosus

substrate_name: 4-Methylumbelliferyl butyrate

sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q8TZJ1 canonical sequence; W194A reconstructed directly and applied mutation signature W194A to reconstruct the assayed variant sequence.

substrate: 4-Methylumbelliferyl butyrate


substrate_name: 4-Methylumbelliferyl heptanoate

sequence_source: UniProt REST accession Q8TZJ1 canonical sequence

substrate: 4-Methylumbelliferyl heptanoate


sequence_variant_note: Resolved canonical sequence from UniProt REST accession Q8TZJ1 canonical sequence; F198A reconstructed directly and applied mutation signature F198A to reconstruct the assayed variant sequence.


organism: Rhizomucor miehei


substrate_name: vinyl propionate

substrate: vinyl propionate


substrate_name: vinyl laurate

substrate: vinyl laurate


substrate_name: tripropionin

substrate: tripropionin


substrate_name: L-Phenylalanine ethyl ester

sequence_source: UniProtKB reviewed entry Q29550 (EST1_PIG) direct accession lookup

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

substrate: L-Phenylalanine ethyl ester


substrate_name: N-Acetyl-L-phenylalanine ethyl ester

substrate: N-Acetyl-L-phenylalanine ethyl ester


substrate_name: L-Phenylalanine benzyl ester

substrate: L-Phenylalanine benzyl ester


substrate_name: valacyclovir

substrate: valacyclovir


substrate_name: 4-nitrophenyl propanoate

substrate: 4-nitrophenyl propanoate


substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


substrate_name: 4-nitrophenyl hexanoate

substrate: 4-nitrophenyl hexanoate


organism: Pyrobaculum sp.

substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl octanoate

substrate: 4-nitrophenyl octanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: 4-nitrophenyl decanoate

substrate: 4-nitrophenyl decanoate


sequence_variant_note: Resolved canonical sequence from uniprot_accession_w194a_reconstruction and applied mutation signature W194A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q29550 direct accession lookup


substrate_name: Triacetin

column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Triacetin (C2): kcat (s^-1) = 60; Km/K0.5 (mM) = 3.

normalized_value_unit_evidence: kcat: printed cell 60 s^-1 -> 60.0 s^(-1); the catalog holds 60.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 3 mM -> 3.0 mM; the catalog holds 3.0 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 20.0 s^(-1)*mM^(-1) is the exact quotient 60 / 3 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.

substrate: Triacetin


column_label: Table 1 (journal page 31), decoded transcription, enzyme row PLEst, substrate column group Tripropionin (C3): kcat (s^-1) = 50; Km/K0.5 (mM) = 0.30.

normalized_value_unit_evidence: kcat: printed cell 50 s^-1 -> 50.0 s^(-1); the catalog holds 50.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly, written `s/C01` in the raw text layer). Km: printed K0.5 cell 0.30 mM -> 0.3 mM; the catalog holds 0.3 mM; no unit conversion applied (the paper prints mM directly). The paper prints no kcat/Km cell; the catalog kcat_over_km 166.66666666666669 s^(-1)*mM^(-1) is the exact quotient 50 / 0.30 of this same measurement's two printed cells, and is exported under typed derived_same_measurement provenance.