sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) accession P04075 direct REST check on 2026-05-31


enzyme_display_name: fructose-bisphosphate aldolase

organism: Lampetra japonica

substrate_name: D-Fructose 1,6-bisphosphate

source_db: oed

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) accession P53445 direct REST check on 2026-05-31

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

data_origin: experimental

enzyme: fructose-bisphosphate aldolase

substrate: D-Fructose 1,6-bisphosphate

source: oed


substrate_name: D-Fructose 1-phosphate

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) accession P53446 direct REST check on 2026-05-31

substrate: D-Fructose 1-phosphate


enzyme_display_name: alcohol dehydrogenase

organism: Coturnix coturnix japonica

verification_status: corrected

sequence_source: UniProtKB reviewed accession P19631 (ADH1_COTJA), direct REST/FASTA lookup 2026-05-31

smiles: CCCCCO

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

column_label: Table III: Kinetic Constants of ADH-3 (Biochemistry 1989, volume 28, pages 6245-6251); printed column heads substrate | Km (mM) | kcat (min^-1) | kcat/Km (mM^-1 min^-1). Table III, substrate row 1-pentanol; column Km (mM) = 0.2; column kcat (min^-1) = 175; column kcat/Km (mM^-1 min^-1) = 648. captured primary segment: 1-pentanol | Km 0.2 mM | kcat 175 min^-1 | kcat/Km 648 mM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table III cell 0.2 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.2 mM; the exported value is 0.2 mM. kcat: printed Table III cell 175 min^-1; 1 min^-1 is 1/60 s^-1, so 175 / 60 = 2.9166666666666665 s^(-1); the exported value is 2.917 s^(-1), the same cell rounded to three decimals. kcat/Km: printed Table III cell 648 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 648 / 60 = 10.8 s^(-1)*mM^(-1); the exported value is 14.584999999999999 s^(-1)*mM^(-1), the quotient of the exported kcat 2.917 and Km 0.2.

raw_value_unit_evidence: Table III, substrate row 1-pentanol: Km = 0.2 mM; kcat = 175 min^-1; printed kcat/Km = 648 mM^-1 min^-1.

row_label: Table III, substrate row 1-pentanol

enzyme: alcohol dehydrogenase

status: corrected


substrate_name: Ethanol

verification_status: unverified

smiles: CCO

substrate: Ethanol

status: unverified


substrate_name: benzyl alcohol

column_label: Table III: Kinetic Constants of ADH-3 (Biochemistry 1989, volume 28, pages 6245-6251); printed column heads substrate | Km (mM) | kcat (min^-1) | kcat/Km (mM^-1 min^-1). Table III, substrate row benzyl alcohol; column Km (mM) = 0.013; column kcat (min^-1) = 151; column kcat/Km (mM^-1 min^-1) = 11700. captured primary segment: benzyl alcohol | Km 0.013 mM | kcat 151 min^-1 | kcat/Km 11700 mM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table III cell 0.013 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.013 mM; the exported value is 0.013 mM. kcat: printed Table III cell 151 min^-1; 1 min^-1 is 1/60 s^-1, so 151 / 60 = 2.5166666666666666 s^(-1); the exported value is 2.517 s^(-1), the same cell rounded to three decimals. kcat/Km: printed Table III cell 11700 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 11700 / 60 = 195.0 s^(-1)*mM^(-1); the exported value is 193.6153846153846 s^(-1)*mM^(-1), the quotient of the exported kcat 2.517 and Km 0.013.

raw_value_unit_evidence: Table III, substrate row benzyl alcohol: Km = 0.013 mM; kcat = 151 min^-1; printed kcat/Km = 11700 mM^-1 min^-1.

row_label: Table III, substrate row benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCCCCO

column_label: Table III: Kinetic Constants of ADH-3 (Biochemistry 1989, volume 28, pages 6245-6251); printed column heads substrate | Km (mM) | kcat (min^-1) | kcat/Km (mM^-1 min^-1). Table III, substrate row 1-octanol; column Km (mM) = 0.011; column kcat (min^-1) = 111; column kcat/Km (mM^-1 min^-1) = 9740. captured primary segment: 1-octanol | Km 0.011 mM | kcat 111 min^-1 | kcat/Km 9740 mM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table III cell 0.011 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.011 mM; the exported value is 0.011 mM. kcat: printed Table III cell 111 min^-1; 1 min^-1 is 1/60 s^-1, so 111 / 60 = 1.85 s^(-1); the exported value is 1.85 s^(-1). kcat/Km: printed Table III cell 9740 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 9740 / 60 = 162.33333333333334 s^(-1)*mM^(-1); the exported value is 168.1818181818182 s^(-1)*mM^(-1), the quotient of the exported kcat 1.85 and Km 0.011.

raw_value_unit_evidence: Table III, substrate row 1-octanol: Km = 0.011 mM; kcat = 111 min^-1; printed kcat/Km = 9740 mM^-1 min^-1.

row_label: Table III, substrate row 1-octanol


smiles: CCCCCCCC=O


substrate_name: NADH

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADH

substrate: NADH


substrate_name: Cyclohexanol

verification_status: verified

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

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

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

row_label: Table III, substrate row cyclohexanol

substrate: Cyclohexanol

status: verified


substrate_name: 12-Hydroxydodecanoic acid

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


organism: Drosophila lebanonensis

sequence_source: UniProtKB:P10807 reviewed Swiss-Prot REST/FASTA direct check

smiles: CCCCCC(C)O


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

column_label: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. R-(-)-Hexan-2-ol; column 'Km (phi2/phi0) (mM)' = 0.16; column 'Vm (1/phi0) (s^-1), the catalytic centre activity per active site' = 8.0; column 'Vm/Km (1/phi2) (s^-1 . mM^-1)' = 50.0.

normalized_value_unit_evidence: Km: printed cell 0.16 mM converts to 0.16 mM; the exported value is 0.16 mM. kcat: printed cell 8.0 s^-1 converts to 8.0 s^(-1); the exported value is 8.0 s^(-1). kcat/Km: printed cell 50.0 s^-1 mM^-1 converts to 50.0 s^(-1)*mM^(-1); the exported value is 50.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. R-(-)-Hexan-2-ol: Km = 0.16 mM; kcat = 8.0 s^-1; printed kcat/Km = 50.0 s^-1 mM^-1.


smiles: CCCC(C)O


smiles: CC(C)O


organism: Arabidopsis thaliana

substrate_name: farnesol

sequence_source: UniProtKB:Q96533 via UniProt REST

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

column_label: Table label: Table II. Kinetic properties of Arabidopsis FALDH. Row: Farnesol (pH 10). Columns read: Km (μM) cell 3, Kcat (min^-1) cell 126, Kcat/Km (mM^-1 min^-1) cell 42,000. metric: Km; raw value: 3; raw unit: μM; normalized value: 0.003 mM; metric: kcat; raw value: 126; raw unit: min^-1; normalized value: 2.1 s^(-1); metric: kcat/Km; normalized value: 700.0 s^-1 mM^-1; assay condition: Arabidopsis FALDH (glutathione-dependent formaldehyde dehydrogenase) purified after expression in yeast; Table II note: Activity versus S-hydroxymethylglutathione was measured in 0.1 m sodium phosphate (pH 8). Activity with other substrates was measured in 0.1 m sodium phosphate (pH 7.5) or in 0.1 m glycine buffer (pH 10). In all cases, 2.4 mm NAD was used. This row was measured at pH 10 (0.1 m glycine buffer). Export row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Table II row Farnesol (pH 10): Km 3 μM = 0.003 mM (1 μM = 0.001 mM); kcat 126 min^-1 / 60 = 2.1 s^(-1) exactly (1 min^-1 = 1/60 s^-1); kcat/Km 42,000 mM^-1 min^-1 / 60 = 700.0 s^-1 mM^-1 exactly, decimal-matching the exported kcat_over_km. Rendering quirks of the on-disk extract: the units row prints as `μm min-1 mm-1min-1` because superscripts are flattened (min-1 is min^-1, mm-1min-1 is mM^-1 min^-1) and the journal's small-capital M renders as a lowercase m, so `μm` is μM and `mm` is mM; thousands separators are printed with commas (e.g. 42,000).

raw_value_unit_evidence: Table II. | Kinetic properties of Arabidopsis FALDH | header row: Substrate Km Kcat Kcat/Km | units row: μm min-1 mm-1min-1 (i.e. Km in μM, Kcat in min^-1, Kcat/Km in mM^-1 min^-1) | table note: Activity versus S-hydroxymethylglutathione was measured in 0.1 m sodium phosphate (pH 8). Activity with other substrates was measured in 0.1 m sodium phosphate (pH 7.5) or in 0.1 m glycine buffer (pH 10). In all cases, 2.4 mm NAD was used. | data row: Farnesol (pH 10) 3 126 42,000 | cells read: Km = 3 μM; Kcat = 126 min^-1; Kcat/Km = 42,000 mM^-1 min^-1

row_label: Farnesol (pH 10)

substrate: farnesol


substrate_name: Geraniol

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

column_label: Table label: Table II. Kinetic properties of Arabidopsis FALDH. Row: Geraniol (pH 10). Columns read: Km (μM) cell 800, Kcat (min^-1) cell 1,200, Kcat/Km (mM^-1 min^-1) cell 1,500. metric: Km; raw value: 800; raw unit: μM; normalized value: 0.8 mM; metric: kcat; raw value: 1,200; raw unit: min^-1; normalized value: 20.0 s^(-1); metric: kcat/Km; normalized value: 25.0 s^-1 mM^-1; assay condition: Arabidopsis FALDH (glutathione-dependent formaldehyde dehydrogenase) purified after expression in yeast; Table II note: Activity versus S-hydroxymethylglutathione was measured in 0.1 m sodium phosphate (pH 8). Activity with other substrates was measured in 0.1 m sodium phosphate (pH 7.5) or in 0.1 m glycine buffer (pH 10). In all cases, 2.4 mm NAD was used. This row was measured at pH 10 (0.1 m glycine buffer). Export row conditions: pH 10; 298.15 K.

normalized_value_unit_evidence: Table II row Geraniol (pH 10): Km 800 μM = 0.8 mM (1 μM = 0.001 mM); kcat 1,200 min^-1 / 60 = 20.0 s^(-1) exactly (1 min^-1 = 1/60 s^-1); kcat/Km 1,500 mM^-1 min^-1 / 60 = 25.0 s^-1 mM^-1 exactly, decimal-matching the exported kcat_over_km. Rendering quirks of the on-disk extract: the units row prints as `μm min-1 mm-1min-1` because superscripts are flattened (min-1 is min^-1, mm-1min-1 is mM^-1 min^-1) and the journal's small-capital M renders as a lowercase m, so `μm` is μM and `mm` is mM; thousands separators are printed with commas (e.g. 1,500).

raw_value_unit_evidence: Table II. | Kinetic properties of Arabidopsis FALDH | header row: Substrate Km Kcat Kcat/Km | units row: μm min-1 mm-1min-1 (i.e. Km in μM, Kcat in min^-1, Kcat/Km in mM^-1 min^-1) | table note: Activity versus S-hydroxymethylglutathione was measured in 0.1 m sodium phosphate (pH 8). Activity with other substrates was measured in 0.1 m sodium phosphate (pH 7.5) or in 0.1 m glycine buffer (pH 10). In all cases, 2.4 mm NAD was used. | data row: Geraniol (pH 10) 800 1,200 1,500 | cells read: Km = 800 μM; Kcat = 1,200 min^-1; Kcat/Km = 1,500 mM^-1 min^-1

row_label: Geraniol (pH 10)

substrate: Geraniol


organism: Branchiostoma lanceolatum

substrate_name: S-(Hydroxymethyl)glutathione

sequence_source: UniProtKB:Q9NJC3 via UniProt REST

substrate: S-(Hydroxymethyl)glutathione


sequence_source: UniProtKB:P19631 via UniProt REST

smiles: CCCCO


substrate_name: NAD+

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Aeropyrum pernix

sequence_source: UniProtKB Q9Y9P9 REST JSON and FASTA; https://rest.uniprot.org/uniprotkb/Q9Y9P9.json and https://rest.uniprot.org/uniprotkb/Q9Y9P9.fasta; accessed 2026-05-31


smiles: CCCCCCO


assay_conditions_summary: pH 8; 333.15 K; cofactor NADH


smiles: CCCC(C)=O


substrate_name: ethanol

substrate: ethanol


sequence_source: UniProtKB:P10807 direct REST/FASTA lookup; reviewed Swiss-Prot entry ADH_DROLE

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

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

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

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

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

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


substrate_name: isobutanol

smiles: CC(C)CO

substrate: isobutanol


substrate_name: R-(+)-cis-Verbenol

substrate: R-(+)-cis-Verbenol


smiles: CCCCC(C)O


smiles: CC(C)CCCO


sequence_source: UniProtKB direct REST lookup for Q9Y9P9 on 2026-05-31; entry Q9Y9P9_AERPE; Aeropyrum pernix strain K1; EC 1.1.1.1; sequence.length=344.


smiles: CCCCC(C)=O


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: 4-Methoxybenzyl alcohol

substrate: 4-Methoxybenzyl alcohol


smiles: CCCCCCCCC(C)=O


smiles: CCCCCC(C)=O


smiles: CCC(C)O


sequence_source: UniProtKB reviewed Swiss-Prot P10807 direct REST lookup on 2026-05-31

column_label: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. cis-4-Methylcyclohexanol; column 'Km (phi2/phi0) (mM)' = 1.0; column 'Vm (1/phi0) (s^-1), the catalytic centre activity per active site' = 7.1; column 'Vm/Km (1/phi2) (s^-1 . mM^-1)' = 7.1.

normalized_value_unit_evidence: Km: printed cell 1.0 mM converts to 1.0 mM; the exported value is 1.0 mM. kcat: printed cell 7.1 s^-1 converts to 7.1 s^(-1); the exported value is 7.1 s^(-1). kcat/Km: printed cell 7.1 s^-1 mM^-1 converts to 7.1 s^(-1)*mM^(-1); the exported value is 7.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. cis-4-Methylcyclohexanol: Km = 1.0 mM; kcat = 7.1 s^-1; printed kcat/Km = 7.1 s^-1 mM^-1.


column_label: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. R-(-)-Octan-2-ol; column 'Km (phi2/phi0) (mM)' = 0.50; column 'Vm (1/phi0) (s^-1), the catalytic centre activity per active site' = 8.1; column 'Vm/Km (1/phi2) (s^-1 . mM^-1)' = 16.2.

normalized_value_unit_evidence: Km: printed cell 0.50 mM converts to 0.5 mM; the exported value is 0.5 mM. kcat: printed cell 8.1 s^-1 converts to 8.1 s^(-1); the exported value is 8.1 s^(-1). kcat/Km: printed cell 16.2 s^-1 mM^-1 converts to 16.2 s^(-1)*mM^(-1); the exported value is 16.2 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3. Activity and kinetic coefficients for the oxidation of primary and secondary alcohols by NAD+ and Drosophila lebanonensis alcohol dehydrogenase at 23.5 C and pH 9.5; part (b), kinetic coefficients. R-(-)-Octan-2-ol: Km = 0.50 mM; kcat = 8.1 s^-1; printed kcat/Km = 16.2 s^-1 mM^-1.


assay_conditions_summary: pH 9.5; 296.65 K; cofactor NAD+


smiles: CCCC(O)CCC


sequence_source: UniProtKB TrEMBL accession Q9Y9P9 (Q9Y9P9_AERPE), direct REST/FASTA lookup 2026-05-31; NAD-dependent alcohol dehydrogenase, EC 1.1.1.1, Aeropyrum pernix strain K1, sequence version 2.

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


smiles: CCCCCCC(C)=O


smiles: CCCCCCCC(C)=O

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

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

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


substrate_name: tert-butyl acetoacetate

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

substrate: tert-butyl acetoacetate


smiles: CCCO


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cinnamyl alcohol

sequence_source: UniProtKB reviewed accession Q96533 (ADHX_ARATH), direct REST/FASTA lookup 2026-05-31; Alcohol dehydrogenase class-3, EC 1.1.1.1, Arabidopsis thaliana, sequence version 2.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

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

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

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

substrate: cinnamyl alcohol


organism: Equus caballus

sequence_source: UniProtKB:P00327 direct JSON/FASTA lookup; reviewed Swiss-Prot ADH1E_HORSE

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

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

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

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

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

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


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

normalized_value_unit_evidence: kcat: printed V1 cell 3.8 s^-1 -> 3.8 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.076 mM -> 0.076 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 3.8 s^-1 / 0.076 mM = 50.0 s^(-1)*mM^(-1).

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

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


smiles: CCCCCO

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

normalized_value_unit_evidence: kcat: printed V1 cell 4.3 s^-1 -> 4.3 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.15 mM -> 0.15 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 4.3 s^-1 / 0.15 mM = 28.666666666666668 s^(-1)*mM^(-1).

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

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


substrate_name: methanol

smiles: CO

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

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

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

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

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

substrate: methanol


smiles: CCCCO

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

normalized_value_unit_evidence: kcat: paper V1 cell 5.2 s^-1 -> 5.2 s^-1; catalog holds 5.2 s^(-1); no unit conversion (the paper's unit row already prints s^-1, so no min^-1/60-style conversion is involved). Km: paper cell 0.27 mM -> 0.27 mM; catalog holds 0.27 mM; no conversion. kcat/Km: not printed; catalog 19.25925925925926 s^(-1)*mM^(-1) is exactly the quotient of the two confirmed cells.

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

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


substrate_name: Ethanol

smiles: CCO

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

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

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

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

substrate: Ethanol


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCCCCO


sequence_source: UniProtKB reviewed entry P10807 canonical sequence, sequence version 1, checked via UniProt REST on 2026-05-31.


sequence_source: UniProtKB reviewed entry P00328 canonical sequence, sequence version 3, checked via UniProt REST on 2026-05-31.


sequence_source: UniProtKB reviewed entry P00327 canonical sequence, sequence version 2, checked via UniProt REST on 2026-05-31.

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

normalized_value_unit_evidence: kcat: printed V1 cell 8.2 s^-1 -> 8.2 s^(-1); no unit conversion (the printed unit row is already s^-1). Km: printed cell 0.39 mM -> 0.39 mM; no unit conversion (the printed unit row is already mM). kcat/Km: Table III prints no kcat/Km column, so the ratio is not an independently printed cell: it is the exact quotient of this row's own printed cells, 8.2 s^-1 / 0.39 mM = 21.025641025641022 s^(-1)*mM^(-1).

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

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


organism: Geobacillus stearothermophilus

substrate_name: NADH

sequence_source: UniProtKB reviewed accession P42328 (ADH3_GEOSE), direct REST/FASTA lookup 2026-05-31; alcohol dehydrogenase, EC 1.1.1.1, Geobacillus stearothermophilus, sequence version 1.

substrate: NADH


substrate_name: 12-oxolauric acid methyl ester

smiles: COC(=O)CCCCCCCCCCC=O

substrate: 12-oxolauric acid methyl ester


substrate_name: 12-hydroxylauric acid methyl ester

smiles: COC(=O)CCCCCCCCCCCO

substrate: 12-hydroxylauric acid methyl ester


substrate_name: n-butanol / 1-Butanol

substrate: n-butanol / 1-Butanol


substrate_name: iso-propanol

smiles: CC(C)O

substrate: iso-propanol


substrate_name: tert-butanol

smiles: CC(C)(C)O

substrate: tert-butanol


substrate_name: 12-Hydroxydodecanoic acid

sequence_source: UniProtKB:P00327 REST lookup on 2026-05-31

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


substrate_name: NAD+

kcat_over_km_display: Not reported

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

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

substrate: NAD+


smiles: NCCCCO


sequence_source: UniProtKB:P42328 REST lookup on 2026-05-31


substrate_name: ethanol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P42328 REST lookup on 2026-05-31; C257L reconstructed from canonical sequence and applied mutation signature C257L to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: ethanol


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


sequence_source: UniProtKB:P42328 REST lookup on 2026-05-31; C257L reconstructed from canonical sequence


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


sequence_source: UniProtKB:P42328 REST record sequence.value


smiles: CCC(C)O


smiles: OCCCO


organism: Geobacillus thermodenitrificans


substrate_name: NADP+

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

substrate: NADP+


organism: Homo sapiens

substrate_name: Benzaldehyde

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

substrate: Benzaldehyde


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+


substrate_name: p-Nitrophenyl acetate

substrate: p-Nitrophenyl acetate


sequence_source: UniProtKB:P00325 direct accession lookup (reviewed Swiss-Prot; retrieved 2026-05-31)


sequence_source: UniProtKB reviewed accession P00326, retrieved 2026-05-31


substrate_name: S-Nitrosoglutathione

sequence_source: UniProtKB reviewed accession P11766, retrieved 2026-05-31

substrate: S-Nitrosoglutathione


substrate_name: S-(Hydroxymethyl)glutathione

substrate: S-(Hydroxymethyl)glutathione


sequence_source: UniProtKB reviewed P08319/ADH4_HUMAN exact accession lookup; FASTA header sequence version 5.

column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 21 +/- 3, kcat (min^-1) cell 18 +/- 2, kcat/Km (mM^-1 min^-1) cell 860 +/- 155. metric: Km; raw value: 21 +/- 3; raw unit: uM; normalized value: 0.021 mM; metric: kcat; raw value: 18 +/- 2; raw unit: min^-1; normalized value: 0.3 s^(-1); metric: kcat/Km; raw value: 860 +/- 155; raw unit: mM^-1 min^-1; normalized value: 14.333333333333334 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 21 +/- 3 uM in the Human ADH4 column; 21 uM / 1000 = 0.021 mM, which is the catalog km exactly. kcat: printed cell 18 +/- 2 min^-1 in the Human ADH4 column; 18 min^-1 / 60 = 0.3 s^-1, an exact terminating conversion, which is the catalog kcat exactly. kcat/Km: the paper prints an independent catalytic-efficiency cell 860 +/- 155 mM^-1 min^-1 in the Human ADH4 column; 860 mM^-1 min^-1 / 60 = 14.333333333333334 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 14.285714285714285 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.3 / 0.021). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 18 min^-1 / 0.021 mM = 857.1428571428571 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

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

row_label: Human ADH4 | 11-cis-retinal


sequence_source: UniProtKB reviewed P00325/ADH1B_HUMAN exact accession lookup; FASTA header sequence version 3.


column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 13-cis-retinal. Enzyme column: Human ADH4. Columns read from the decoded plain-numeral Table 3 block: Km (uM) cell 25 +/- 6, kcat (min^-1) cell 11 +/- 1, kcat/Km (mM^-1 min^-1) cell 440 +/- 115. metric: Km; raw value: 25 +/- 6; raw unit: uM; normalized value: 0.025 mM; metric: kcat; raw value: 11 +/- 1; raw unit: min^-1; normalized value: 0.183 s^(-1); metric: kcat/Km; raw value: 440 +/- 115; raw unit: mM^-1 min^-1; normalized value: 7.333333333333333 s^(-1)*mM^(-1); explicit printed primary cell; assay condition: 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, 25 C (298.15 K); 1 mM NADH (0.77 mM for human ADH4) for the retinal reductions; recombinant enzyme, kinetic constants determined by the authors. Catalog row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: Km: printed cell 25 +/- 6 uM in the Human ADH4 column; 25 uM / 1000 = 0.025 mM, which is the catalog km exactly. kcat: printed cell 11 +/- 1 min^-1 in the Human ADH4 column; 11 min^-1 / 60 = 0.18333333333333332 s^-1, a non-terminating quotient, and the catalog stores that quotient at its own 3-decimal precision as 0.183 s^-1, so the paper kcat field carries the catalog value 0.183 and this metric is not a corrected field. kcat/Km: the paper prints an independent catalytic-efficiency cell 440 +/- 115 mM^-1 min^-1 in the Human ADH4 column; 440 mM^-1 min^-1 / 60 = 7.333333333333333 s^-1 mM^-1. The paper kcat_over_km field carries that printed cell. The catalog instead stores 7.319999999999999 s^-1 mM^-1, which is the quotient of the catalog's own kcat and Km (0.183 / 0.025). This is a real disagreement and not a printed-precision artifact: the row's own printed components give 11 min^-1 / 0.025 mM = 440.0 mM^-1 min^-1, which is not the printed cell, so the printed cell is the authors' independently fitted catalytic efficiency and not a coarser rendering of the catalog's own kcat and Km.

raw_value_unit_evidence: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers | decoded plain-numeral Table 3 block | column header row: | Substrate | Constant | Human ADH1B1 | Human ADH1B2 | Human ADH4 | Mouse ADH1 | Mouse ADH4 | | Km row: | 13-cis-retinal | Km (uM) | NA | NA | 25 +/- 6 | ND | ND | | kcat row: | 13-cis-retinal | kcat (min^-1) | NA | NA | 11 +/- 1 | ND | ND | | kcat/Km row: | 13-cis-retinal | kcat/Km (mM^-1 min^-1) | NA | NA | 440 +/- 115 | ND | ND | | Human ADH4 column cells read: Km = 25 +/- 6 uM; kcat = 11 +/- 1 min^-1; kcat/Km = 440 +/- 115 mM^-1 min^-1 | table caption: Table 3. Kinetic constants of alcohol dehydrogenases with retinal isomers. Activities were determined in 0.1M sodium phosphate, pH 7.5, 0.02% Tween-80, using 1 mM NADH (0.77 mM for human ADH4), at 25 C.

row_label: Human ADH4 | 13-cis-retinal


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

column_label: Table label: Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids. Substrate block: 3,4-Didehydroretinol. Enzyme column: ADH4. Columns read: Km (uM) cell 28, kcat (min^-1) cell 150, kcat/Km (mM^-1 min^-1) cell 5400. metric: kcat; raw value: 150; raw unit: min^-1; normalized value: 2.5 s^(-1); metric: Km; raw value: 28; raw unit: uM; normalized value: 0.028 mM; metric: kcat/Km; raw value: 5400 ± 1400; raw unit: mM^-1 min^-1; normalized value: 90 s^-1 mM^-1; explicit printed primary cell; assay condition: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH (0.77 mM for ADH4) for retinal reductions, at 25 C. Export row conditions: pH 7.5; 298.15 K.

normalized_value_unit_evidence: kcat raw 150 min^-1 -> 2.5 s^(-1); Km raw 28 uM -> 0.028 mM; explicit printed kcat/Km raw 5400 ± 1400 mM^-1 min^-1 -> 90 s^-1 mM^-1. Conversion: 5400 mM^-1 min^-1 / 60 = 90 s^-1 mM^-1. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence:
Table 1 Kinetic constants of human alcohol dehydrogenases with retinoids | enzyme column header row: Substrate                                                              ADH1B1                      ADH1B2                 ADH4 | Km row: 3,4-Didehydroretinol              Km (lM)                              ND                             24 ± 5                   28 ± 7 | kcat row: kcat (min1)                                                       5.3 ± 0.4                150 ± 14 | kcat/Km row: kcat/Km (mM1 min1)                                               220 ± 50                5400 ± 1400 | ADH4 cells read: Km = 28 uM; kcat = 150 min^-1; kcat/Km = 5400 mM^-1 min^-1 | table footnote: Activities were determined in 0.1 M sodium phosphate, pH 7.5, 0.02% Tween 80, using 2.4 mM NAD+ for retinol oxidations, or 1 mM NADH
(0.77 mM for ADH4) for retinal reductions, at 25 C. ND, not determined.

row_label: ADH4 | 3,4-Didehydroretinol


column_label: The literal 4-Hydroxy-retinol row and ADH1B2 column bind all three cells. Rounding 170/60 to the current stored kcat precision and dividing by 0.011 gives the current quotient, which lies inside the printed interval.

raw_value_unit_evidence: ADH1B2 cells: kcat 170 ± 20 min^-1; Km 11 ± 2 uM; printed kcat/Km 15,200 ± 3300 mM^-1 min^-1.

row_label: 4-Hydroxy-retinol | ADH1B2

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


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

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

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

row_label: 3,4-Didehydroretinol | ADH1B2


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+


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

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

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

row_label: Human ADH1B2 | 11-cis-retinal


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

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

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

row_label: Human ADH4 | 11-cis-retinol


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

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

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

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

row_label: Human ADH1B2 | 9-cis-retinol


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

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

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

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

row_label: Human ADH4 | 7-cis-retinal


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

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

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

row_label: Human ADH4 | 13-cis-retinol


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

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

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

row_label: Human ADH4 | 7-cis-retinol


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

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

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

row_label: 4-Hydroxy-retinol | ADH4


substrate_name: all-trans-Dehydroretinal

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

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

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

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

row_label: ADH1B2 | 3,4-Didehydroretinal

substrate: all-trans-Dehydroretinal


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

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

row_label: 4-Oxo-retinal | ADH4


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

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

row_label: 4-Oxo-retinal | ADH1B2


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

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

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

row_label: ADH4 | 3,4-Didehydroretinal


substrate_name: methanol

substrate: methanol


substrate_name: Cyclohexanol

substrate: Cyclohexanol


sequence_source: UniProtKB REST P11766 reviewed canonical sequence

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

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

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

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


smiles: CCCCCCCCCCCCO

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

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

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

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


smiles: CCCC=CCO

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

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

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


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: OCCCCCCCCO


smiles: OCC=CCO


smiles: CCCCCCCCCCO

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

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

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

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


substrate_name: cinnamyl alcohol

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

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

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

substrate: cinnamyl alcohol


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


substrate_name: Retinol

substrate: Retinol


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

smiles: CCCCCCO


smiles: CCCCCCCCCCCCCCO

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

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

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

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


substrate_name: Prenol

smiles: CC(C)=CCO

substrate: Prenol


smiles: CCCCCCCCCO

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

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

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

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


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

smiles: CCCO


smiles: CCCCCCCCO


substrate_name: 12-Hydroxydodecanoic acid

smiles: O=C(O)CCCCCCCCCCCO

substrate: 12-Hydroxydodecanoic acid


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

smiles: CCCCO


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


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCO


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

substrate_name: all-trans-Retinal

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

substrate: all-trans-Retinal


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


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

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


enzyme_display_name: Alcohol dehydrogenase class-3

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

smiles: OCCCCCCO

enzyme: Alcohol dehydrogenase class-3


substrate_name: farnesol

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

substrate: farnesol


substrate_name: Methylcrotyl alcohol

smiles: CC=CC(C)O

substrate: Methylcrotyl alcohol


smiles: CCC/C=C\CO

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

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

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


substrate_name: Glycol

smiles: OCCO

substrate: Glycol


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

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

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

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

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

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

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


smiles: CO


smiles: CCO


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

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

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

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

row_label: (c) ethylene glycol

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


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


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

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

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

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

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


sequence_source: UniProtKB:P11766 direct REST lookup

smiles: CCCCCCCC=O


substrate_name: NADH

assay_conditions_summary: pH 6.8; 298.15 K; cofactor NADPH

substrate: NADH


sequence_source: UniProtKB:P08319 direct REST lookup


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


smiles: CC(C)O


assay_conditions_summary: pH 9; 298.15 K; cofactor NADH


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

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


organism: Kluyveromyces lactis

substrate_name: Acetaldehyde

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

smiles: CC=O

substrate: Acetaldehyde


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: NADPH


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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH


organism: Macaca mulatta

smiles: CC(C)CCO

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

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

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

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

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


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

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADH


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


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

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

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

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

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


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

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

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

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


substrate_name: NAD+

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NAD+

substrate: NAD+


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

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: methanol

sequence_source: UniProtKB:P28469 FASTA

substrate: methanol


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

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

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

row_label: Ethanol row under Primary alcohols


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

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

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

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


smiles: CCCO

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

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

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

row_label: Propanol row under Primary alcohols


substrate_name: Cyclohexanol

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

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

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

substrate: Cyclohexanol


organism: Mus musculus

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

smiles: CCCCCCO


substrate_name: Cyclohexanone

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

substrate: Cyclohexanone


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

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

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

row_label: Hexanol row under Primary alcohols


substrate_name: benzyl alcohol

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

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

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

substrate: benzyl alcohol


smiles: CCC(O)CC

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

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

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

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


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

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

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

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


substrate_name: isobutanol

smiles: CC(C)CO

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

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

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

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

substrate: isobutanol


smiles: CCCCO

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

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

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

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

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


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


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

smiles: O=C(O)CCCCCCCCCCCO


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


smiles: CCCCCCCCO


substrate_name: Ethanol

sequence_source: UniProtKB:Q9QYY9 FASTA

substrate: Ethanol


sequence_source: UniProtKB:P00329 FASTA

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

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

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

row_label: Mouse ADH1 | 11-cis-retinol


substrate_name: Retinol

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

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

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

row_label: Mouse ADH4 | all-trans-retinol

substrate: Retinol