substrate_name: D-Xylose

substrate: D-Xylose


enzyme_display_name: aldose reductase

organism: Homo sapiens

source_db: oed

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB:P15121 reviewed Swiss-Prot REST lookup on 2026-05-31

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Chloro PG`: kcat (min^-1) = 45; Km (uM) = 1; kcat/Km (M^-1 min^-1) = 4.5 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 45 min^-1 -> 0.75 s^(-1) (divide by 60); the exported value is 0.75 s^(-1). Km: printed cell 1 uM -> 0.001 mM (divide by 1000); the exported value is 0.001 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.5 x 10^7 M^-1 min^-1 for this substrate line -> 750.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 750.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Chloro PG`

table_label: Table 2 (PDF page 4 of 10, journal page 120) 'Substrate specificity of aldose reductase for aromatic 2-ketoaldehydes'

data_origin: experimental

enzyme: aldose reductase

status: verified

source: oed


verification_status: corrected

column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Methyl PG`: kcat (min^-1) = 119; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 6.0 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 119 min^-1 -> 1.9833333333333334 s^(-1) (divide by 60); the exported value is 1.983 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 6.0 x 10^7 M^-1 min^-1 for this substrate line -> 1000.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 991.5 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Methyl PG`

status: corrected


column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `2,4,6-Trimethyl PG`: kcat (min^-1) = 97; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 4.9 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 97 min^-1 -> 1.6166666666666667 s^(-1) (divide by 60); the exported value is 1.617 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.9 x 10^7 M^-1 min^-1 for this substrate line -> 816.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 808.5 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `2,4,6-Trimethyl PG`


sequence_source: UniProtKB reviewed accession P15121 (ALDR_HUMAN), direct REST/FASTA check on 2026-05-31; entry is Homo sapiens AKR1B1/aldose reductase and lists EC 1.1.1.21.

column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Benzoyloxy PG`: kcat (min^-1) = 92; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 4.6 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 92 min^-1 -> 1.5333333333333332 s^(-1) (divide by 60); the exported value is 1.533 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.6 x 10^7 M^-1 min^-1 for this substrate line -> 766.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 766.5 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Benzoyloxy PG`


substrate_name: Glyoxylate

smiles: O=CC(=O)O

column_label: Table 1 (PDF page 2 of 10, journal page 118), substrate row `Glyoxylic acid`: kcat (min^-1) = 71; Km (uM) = 1,060; kcat/Km (M^-1 min^-1) = 6.7 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 71 min^-1 -> 1.1833333333333333 s^(-1) (divide by 60); the exported value is 1.183 s^(-1). Km: printed cell 1,060 uM -> 1.06 mM (divide by 1000); the exported value is 1.06 mM. kcat/Km: the paper PRINTS the kcat/Km cell 6.7 x 10^4 M^-1 min^-1 for this substrate line -> 1.1166666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 1.1160377358490565 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `Glyoxylic acid`

table_label: Table 1 (PDF page 2 of 10, journal page 118) 'Aliphatic substrates of human aldose reductase'

substrate: Glyoxylate


column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `2-Chloro BA`: kcat (min^-1) = 138; Km (uM) = 14; kcat/Km (M^-1 min^-1) = 9.9 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 138 min^-1 -> 2.3 s^(-1) (divide by 60); the exported value is 2.3 s^(-1). Km: printed cell 14 uM -> 0.014 mM (divide by 1000); the exported value is 0.014 mM. kcat/Km: the paper PRINTS the kcat/Km cell 9.9 x 10^6 M^-1 min^-1 for this substrate line -> 165.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 164.28571428571428 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `2-Chloro BA`

table_label: Table 3 (PDF page 5 of 10, journal page 121) 'Substrate specificity of aldose reductase for aromatic aldehydes'


column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `3-Methoxy PG`: kcat (min^-1) = 85; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 4.3 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 85 min^-1 -> 1.4166666666666667 s^(-1) (divide by 60); the exported value is 1.417 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.3 x 10^7 M^-1 min^-1 for this substrate line -> 716.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 708.5 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `3-Methoxy PG`


substrate_name: Acetaldehyde

smiles: CC=O

column_label: Table 1 (PDF page 2 of 10, journal page 118), substrate row `Acetaldehyde`: kcat (min^-1) = 111; Km (uM) = 67,000; kcat/Km (M^-1 min^-1) = 1.7 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 111 min^-1 -> 1.85 s^(-1) (divide by 60); the exported value is 1.85 s^(-1). Km: printed cell 67,000 uM -> 67.0 mM (divide by 1000); the exported value is 67.0 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.7 x 10^3 M^-1 min^-1 for this substrate line -> 0.028333333333333335 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 0.027611940298507463 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `Acetaldehyde`

substrate: Acetaldehyde


substrate_name: glycolaldehyde

smiles: O=CCO

column_label: Table 1 (PDF page 2 of 10, journal page 118), substrate row `Glycolaldehyde`: kcat (min^-1) = 106; Km (uM) = 112; kcat/Km (M^-1 min^-1) = 9.5 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 106 min^-1 -> 1.7666666666666666 s^(-1) (divide by 60); the exported value is 1.767 s^(-1). Km: printed cell 112 uM -> 0.112 mM (divide by 1000); the exported value is 0.112 mM. kcat/Km: the paper PRINTS the kcat/Km cell 9.5 x 10^5 M^-1 min^-1 for this substrate line -> 15.833333333333334 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 15.776785714285714 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `Glycolaldehyde`

substrate: glycolaldehyde


column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `4-Chloro BA`: kcat (min^-1) = 160; Km (uM) = 7; kcat/Km (M^-1 min^-1) = 2.3 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 160 min^-1 -> 2.6666666666666665 s^(-1) (divide by 60); the exported value is 2.667 s^(-1). Km: printed cell 7 uM -> 0.007 mM (divide by 1000); the exported value is 0.007 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3 x 10^7 M^-1 min^-1 for this substrate line -> 383.33333333333337 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 380.99999999999994 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `4-Chloro BA`


substrate_name: Glyoxal

smiles: O=CC=O

column_label: Table 1 (PDF page 2 of 10, journal page 118), substrate row `Glyoxal`: kcat (min^-1) = 154; Km (uM) = 514; kcat/Km (M^-1 min^-1) = 3.0 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 154 min^-1 -> 2.5666666666666664 s^(-1) (divide by 60); the exported value is 2.567 s^(-1). Km: printed cell 514 uM -> 0.514 mM (divide by 1000); the exported value is 0.514 mM. kcat/Km: the paper PRINTS the kcat/Km cell 3.0 x 10^5 M^-1 min^-1 for this substrate line -> 5.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 4.994163424124514 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `Glyoxal`

substrate: Glyoxal


sequence_source: UniProtKB:P15121 reviewed entry, direct REST/FASTA lookup

column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `2,4-Dimethyl PG`: kcat (min^-1) = 72; Km (uM) = 6; kcat/Km (M^-1 min^-1) = 1.2 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 72 min^-1 -> 1.2 s^(-1) (divide by 60); the exported value is 1.2 s^(-1). Km: printed cell 6 uM -> 0.006 mM (divide by 1000); the exported value is 0.006 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.2 x 10^7 M^-1 min^-1 for this substrate line -> 200.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 200.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `2,4-Dimethyl PG`


column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Bromo PG`: kcat (min^-1) = 100; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 5.0 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 100 min^-1 -> 1.6666666666666667 s^(-1) (divide by 60); the exported value is 1.667 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 5.0 x 10^7 M^-1 min^-1 for this substrate line -> 833.3333333333334 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 833.5 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Bromo PG`


substrate_name: Phenylacetaldehyde

column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `Phenylacetaldehyde`: kcat (min^-1) = 155; Km (uM) = 8; kcat/Km (M^-1 min^-1) = 1.9 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 155 min^-1 -> 2.5833333333333335 s^(-1) (divide by 60); the exported value is 2.583 s^(-1). Km: printed cell 8 uM -> 0.008 mM (divide by 1000); the exported value is 0.008 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.9 x 10^7 M^-1 min^-1 for this substrate line -> 316.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 322.875 s^(-1)*mM^(-1).

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

substrate: Phenylacetaldehyde


column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `2-Napthaldehyde`: kcat (min^-1) = 203; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 1.0 x 10^8.

normalized_value_unit_evidence: kcat: printed cell 203 min^-1 -> 3.3833333333333333 s^(-1) (divide by 60); the exported value is 3.383 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.0 x 10^8 M^-1 min^-1 for this substrate line -> 1666.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 1691.5 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `2-Napthaldehyde`


substrate_name: Benzaldehyde

column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `Benzaldehyde (BA)`: kcat (min^-1) = 148; Km (uM) = 7; kcat/Km (M^-1 min^-1) = 2.1 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 148 min^-1 -> 2.466666666666667 s^(-1) (divide by 60); the exported value is 2.467 s^(-1). Km: printed cell 7 uM -> 0.007 mM (divide by 1000); the exported value is 0.007 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.1 x 10^7 M^-1 min^-1 for this substrate line -> 350.0 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 352.42857142857144 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `Benzaldehyde (BA)`

substrate: Benzaldehyde


column_label: Table 3 (PDF page 5 of 10, journal page 121), substrate row `1-Napthaldehyde`: kcat (min^-1) = 156; Km (uM) = 8; kcat/Km (M^-1 min^-1) = 2.0 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 156 min^-1 -> 2.6 s^(-1) (divide by 60); the exported value is 2.6 s^(-1). Km: printed cell 8 uM -> 0.008 mM (divide by 1000); the exported value is 0.008 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.0 x 10^7 M^-1 min^-1 for this substrate line -> 333.33333333333337 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 325.0 s^(-1)*mM^(-1).

row_label: Table 3, decoded plain-numeral transcription, substrate row `1-Napthaldehyde`


smiles: CCCCCC(O)/C=C/C=O

column_label: Table 1 (PDF page 2 of 10, journal page 118), substrate row `4-Hydroxynonenal`: kcat (min^-1) = 102; Km (uM) = 22; kcat/Km (M^-1 min^-1) = 4.6 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 102 min^-1 -> 1.7 s^(-1) (divide by 60); the exported value is 1.7 s^(-1). Km: printed cell 22 uM -> 0.022 mM (divide by 1000); the exported value is 0.022 mM. kcat/Km: the paper PRINTS the kcat/Km cell 4.6 x 10^6 M^-1 min^-1 for this substrate line -> 76.66666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 77.27272727272728 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `4-Hydroxynonenal`


substrate_name: propanal

verification_status: unverified

kcat_over_km_origin: calculated

smiles: CCC=O

substrate: propanal

status: unverified


sequence_source: UniProtKB REST P15121 reviewed Swiss-Prot; accessed 2026-05-31

column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Methoxy PG`: kcat (min^-1) = 45; Km (uM) = 2; kcat/Km (M^-1 min^-1) = 2.3 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 45 min^-1 -> 0.75 s^(-1) (divide by 60); the exported value is 0.75 s^(-1). Km: printed cell 2 uM -> 0.002 mM (divide by 1000); the exported value is 0.002 mM. kcat/Km: the paper PRINTS the kcat/Km cell 2.3 x 10^7 M^-1 min^-1 for this substrate line -> 383.33333333333337 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 375.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Methoxy PG`


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


column_label: Table 2 (PDF page 4 of 10, journal page 120), substrate row `4-Phenyl PG`: kcat (min^-1) = 82; Km (uM) = 1; kcat/Km (M^-1 min^-1) = 8.2 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 82 min^-1 -> 1.3666666666666667 s^(-1) (divide by 60); the exported value is 1.367 s^(-1). Km: printed cell 1 uM -> 0.001 mM (divide by 1000); the exported value is 0.001 mM. kcat/Km: the paper PRINTS the kcat/Km cell 8.2 x 10^7 M^-1 min^-1 for this substrate line -> 1366.6666666666667 s^(-1)*mM^(-1) (divide by 60 for min^-1 to s^-1 and by 1000 for M^-1 to mM^-1); the exported value is 1367.0 s^(-1)*mM^(-1).

row_label: Table 2, decoded plain-numeral transcription, substrate row `4-Phenyl PG`


substrate_name: Glyceraldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P15121 reviewed Swiss-Prot; accessed 2026-05-31 and applied mutation signature H110Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

smiles: O=CC(O)CO

mutation_type: substitution

substrate: Glyceraldehyde


substrate_name: D-Lyxose

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P15121 reviewed Swiss-Prot; accessed 2026-05-31 and applied mutation signature H110A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: D-Lyxose


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15121 and applied mutation signature Y48H with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM sodium phosphate; cofactor NADPH

column_label: Table 3, enzyme row 'Y48H', DL-glyceraldehyde column group; column 'Km (mM)' = 71; column 'kcat' = 0.01; column 'kcat/Km' = 0.2. Footnote a of the table gives kcat in s-1 and kcat/Km in s-1 M-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 71 mM; already in mM, so no unit conversion applies; normalized 71 mM. kcat: printed Table 3 cell 0.01 s-1; already in s^-1, so no unit conversion applies; normalized 0.01 s^(-1). kcat/Km: printed Table 3 cell 0.2 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.2 / 1000 = 0.0002 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Y48H', DL-glyceraldehyde column group: Km = 71 mM; kcat = 0.01 s-1; printed kcat/Km = 0.2 M-1 s-1.

table_label: Table 3: Apparent Kinetic Constants of Wild-Type Human Aldose Reductase and Its Y48, H110, and K77 Mutants (Biochemistry 1994, 33(8):2021-2032)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15121 and applied mutation signature H110A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'H110A', DL-glyceraldehyde column group; column 'Km (mM)' = 84; column 'kcat' = 0.07; column 'kcat/Km' = 0.9. Footnote a of the table gives kcat in s-1 and kcat/Km in s-1 M-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 84 mM; already in mM, so no unit conversion applies; normalized 84 mM. kcat: printed Table 3 cell 0.07 s-1; already in s^-1, so no unit conversion applies; normalized 0.07 s^(-1). kcat/Km: printed Table 3 cell 0.9 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.9 / 1000 = 0.0009 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'H110A', DL-glyceraldehyde column group: Km = 84 mM; kcat = 0.07 s-1; printed kcat/Km = 0.9 M-1 s-1.


substrate_name: Glucuronate

sequence_source: UniProtKB reviewed REST direct check: O60218

substrate: Glucuronate


substrate_name: D-Galactose

substrate: D-Galactose


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


assay_conditions_summary: pH 7; 303.15 K; buffer this record. Assay condition: 135 mM sodium phosphate; cofactor NADPH

column_label: Table III (journal page 11434), decoded transcription, substrate row `Pyridine-3-aldehyde`, ARL-1 column group: Km (mM) = 0.001; kcat (min^-1) = 2304. Table III prints no kcat/Km cell.

normalized_value_unit_evidence: kcat: printed cell 2304 min^-1 -> 38.4 s^(-1) by the exact unit conversion 1 min^-1 = 1/60 s^(-1); the catalog holds 38.4 s^(-1), and 2304 is an exact multiple of 60 so the conversion is exact with no rounding. Km: printed cell 0.001 mM -> 0.001 mM; the catalog holds 0.001 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: Table III prints no kcat/Km cell for any row. The exported kcat_over_km is the derived same-measurement quotient of this row's own printed cells: 2304 min^-1 / 0.001 mM, converted to s^(-1)*mM^(-1), which is typed in kcat_over_km_provenance with kind=derived_same_measurement and equals the stored kcat_over_km 38400.0 s^(-1)*mM^(-1).

table_label: Table III (journal page 11434) 'Kinetic constants for AR, ARL-1, and CHO reductase'


substrate_name: Dimethylglyoxal

sequence_source: UniProtKB reviewed REST direct check: P15121

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

substrate: Dimethylglyoxal


assay_conditions_summary: pH 6.2; 303.15 K; buffer this record. Assay condition: 135 mM sodium phosphate; cofactor NADPH

column_label: Table III (journal page 11434), decoded transcription, substrate row `Pyridine-3-aldehyde`, AR column group: Km (mM) = 0.002; kcat (min^-1) = 618. Table III prints no kcat/Km cell.

normalized_value_unit_evidence: kcat: printed cell 618 min^-1 -> 10.3 s^(-1) by the exact unit conversion 1 min^-1 = 1/60 s^(-1); the catalog holds 10.3 s^(-1), and 618 is an exact multiple of 60 so the conversion is exact with no rounding. Km: printed cell 0.002 mM -> 0.002 mM; the catalog holds 0.002 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: Table III prints no kcat/Km cell for any row. The exported kcat_over_km is the derived same-measurement quotient of this row's own printed cells: 618 min^-1 / 0.002 mM, converted to s^(-1)*mM^(-1), which is typed in kcat_over_km_provenance with kind=derived_same_measurement and equals the stored kcat_over_km 5150.0 s^(-1)*mM^(-1).


substrate_name: m-Nitrobenzaldehyde

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.

substrate: m-Nitrobenzaldehyde


sequence_source: UniProtKB:P15121 direct REST lookup 2026-05-31


substrate_name: D-Glucose

substrate: D-Glucose


organism: Rattus norvegicus

sequence_source: UniProtKB:P07943 direct REST lookup 2026-05-31


substrate_name: D-Xylose

substrate: D-Xylose


organism: Sus scrofa

substrate_name: D-Glucuronate

sequence_source: UniProtKB:P80276 direct REST lookup 2026-05-31

substrate: D-Glucuronate


substrate_name: succinate

smiles: O=C(O)CCC(=O)O

substrate: succinate


organism: Debaryomyces nepalensis

sequence_source: UniProtKB:A0A0M4HL56 direct REST lookup


sequence_source: UniProtKB:P15121 direct REST lookup


substrate_name: Glyceraldehyde 3-phosphate

smiles: O=CC(O)COP(=O)(O)O

column_label: Table I (journal page 4365), substrate row `DL-Glyceraldehyde-3P`: kcat (min^-1) = 96; Km (mM) = 2.1; kcat/Km (M^-1 min^-1) = 4.5 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 96 min^-1 -> 96/60 = 1.6 s^-1, carried here at the export's stored precision as 1.6 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.6 s^(-1). Km: printed cell 2.1 mM -> 2.1 mM; the catalog holds 2.1 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 4.5 x 10^4 M^-1 min^-1 -> 45000/(1000*60) = 0.75 s^(-1)*mM^(-1); the catalog holds 0.7619047619047619 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.6 / 2.1) rather than the printed efficiency cell.

row_label: Table I, substrate row `DL-Glyceraldehyde-3P`

table_label: Table I Substrate specificity of human aldose reductase (journal page 4365)

substrate: Glyceraldehyde 3-phosphate


substrate_name: D-Glyceraldehyde

substrate: D-Glyceraldehyde


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

column_label: Table I (journal page 4365), substrate row `Dihydroxyacetone`: kcat (min^-1) = 54; Km (mM) = 2.5; kcat/Km (M^-1 min^-1) = 2.1 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 54 min^-1 -> 54/60 = 0.9 s^-1, carried here at the export's stored precision as 0.9 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 0.9 s^(-1). Km: printed cell 2.5 mM -> 2.5 mM; the catalog holds 2.5 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 2.1 x 10^4 M^-1 min^-1 -> 21000/(1000*60) = 0.35000000000000003 s^(-1)*mM^(-1); the catalog holds 0.36 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (0.9 / 2.5) rather than the printed efficiency cell.

row_label: Table I, substrate row `Dihydroxyacetone`

substrate: Dihydroxyacetone


substrate_name: L-Glyceraldehyde

substrate: L-Glyceraldehyde


substrate_name: glycerone phosphate

smiles: O=C(CO)COP(=O)(O)O

column_label: Table I (journal page 4365), substrate row `Dihydroxyacetone-P`: kcat (min^-1) = 69; Km (mM) = 2.5; kcat/Km (M^-1 min^-1) = 2.7 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 69 min^-1 -> 69/60 = 1.15 s^-1, carried here at the export's stored precision as 1.15 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.15 s^(-1). Km: printed cell 2.5 mM -> 2.5 mM; the catalog holds 2.5 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 2.7 x 10^4 M^-1 min^-1 -> 27000/(1000*60) = 0.45 s^(-1)*mM^(-1); the catalog holds 0.45999999999999996 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.15 / 2.5) rather than the printed efficiency cell.

row_label: Table I, substrate row `Dihydroxyacetone-P`

substrate: glycerone phosphate


substrate_name: D-Lactaldehyde

column_label: Table I (journal page 4365), substrate row `D-Lactaldehyde`: kcat (min^-1) = 75; Km (mM) = 0.079; kcat/Km (M^-1 min^-1) = 9.5 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 75 min^-1 -> 75/60 = 1.25 s^-1, carried here at the export's stored precision as 1.25 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.25 s^(-1). Km: printed cell 0.079 mM -> 0.079 mM; the catalog holds 0.088 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 9.5 x 10^5 M^-1 min^-1 -> 950000/(1000*60) = 15.833333333333334 s^(-1)*mM^(-1); the catalog holds 14.204545454545455 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.25 / 0.088) rather than the printed efficiency cell.

row_label: Table I, substrate row `D-Lactaldehyde`

substrate: D-Lactaldehyde


substrate_name: p-Nitrobenzaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15121 and applied mutation signature Y48S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3, enzyme row 'Y48S', p-nitrobenzaldehyde column group; column 'Km (mM)' = 0.88; column 'kcat' = 0.002; column 'kcat/Km' = 2.5. Footnote a of the table gives kcat in s-1 and kcat/Km in s-1 M-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.88 mM; already in mM, so no unit conversion applies; normalized 0.88 mM. kcat: printed Table 3 cell 0.002 s-1; already in s^-1, so no unit conversion applies; normalized 0.002 s^(-1). kcat/Km: printed Table 3 cell 2.5 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 / 1000 = 0.0025 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Y48S', p-nitrobenzaldehyde column group: Km = 0.88 mM; kcat = 0.002 s-1; printed kcat/Km = 2.5 M-1 s-1.

substrate: p-Nitrobenzaldehyde


column_label: Table 3, enzyme row 'Y48H', p-nitrobenzaldehyde column group; column 'Km (mM)' = 0.1; column 'kcat' = 0.01; column 'kcat/Km' = 74. Footnote a of the table gives kcat in s-1 and kcat/Km in s-1 M-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.1 mM; already in mM, so no unit conversion applies; normalized 0.1 mM. kcat: printed Table 3 cell 0.01 s-1; already in s^-1, so no unit conversion applies; normalized 0.01 s^(-1). kcat/Km: printed Table 3 cell 74 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 74 / 1000 = 0.074 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'Y48H', p-nitrobenzaldehyde column group: Km = 0.1 mM; kcat = 0.01 s-1; printed kcat/Km = 74 M-1 s-1.


substrate_name: D-Lyxose

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P15121 and applied mutation signature H110Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 4, substrate row 'D-lyxose', H110Q column group; column 'Km (mM)' = 506; column 'kcat' = 0.0075; column 'kcat/Km' = 0.014. Footnote a of the table gives kcat in s-1 and kcat/Km in M-1 s-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 506 mM; already in mM, so no unit conversion applies; normalized 506 mM. kcat: printed Table 4 cell 0.0075 s-1; already in s^-1, so no unit conversion applies; normalized 0.0075 s^(-1). kcat/Km: printed Table 4 cell 0.014 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.014 / 1000 = 0.000014 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate row 'D-lyxose', H110Q column group: Km = 506 mM; kcat = 0.0075 s-1; printed kcat/Km = 0.014 M-1 s-1.

table_label: Table 4: apparent kinetic constants of wild-type and mutant human aldose reductase for the xylose isomers (Biochemistry 1994, 33(8):2021-2032)

substrate: D-Lyxose


sequence_source: UniProtKB:P15121 canonical sequence checked 2026-05-31


sequence_source: UniProtKB:O60218 canonical sequence checked 2026-05-31


column_label: Table III (journal page 11434), decoded transcription, substrate row `D-Galactose`, AR column group: Km (mM) = 21.0; kcat (min^-1) = 222. Table III prints no kcat/Km cell.

normalized_value_unit_evidence: kcat: printed cell 222 min^-1 -> 3.6999999999999997 s^(-1) by the exact unit conversion 1 min^-1 = 1/60 s^(-1); the catalog holds 3.7 s^(-1), and 222 is an exact multiple of 60 so the conversion is exact with no rounding. Km: printed cell 21.0 mM -> 21.0 mM; the catalog holds 21.0 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: Table III prints no kcat/Km cell for any row. The exported kcat_over_km is the derived same-measurement quotient of this row's own printed cells: 222 min^-1 / 21.0 mM, converted to s^(-1)*mM^(-1), which is typed in kcat_over_km_provenance with kind=derived_same_measurement and equals the stored kcat_over_km 0.1761904761904762 s^(-1)*mM^(-1).


substrate_name: Glyceraldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_accession_variant_reconstruction and applied mutation signature Y48S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: Glyceraldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession_variant_reconstruction and applied mutation signature H110Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: L-Xylose

column_label: Table 4, substrate row 'L-xylose', H110Q column group; column 'Km (mM)' = 1190; column 'kcat' = 0.0065; column 'kcat/Km' = 0.0059. Footnote a of the table gives kcat in s-1 and kcat/Km in M-1 s-1.

normalized_value_unit_evidence: Km: printed Table 4 cell 1190 mM; already in mM, so no unit conversion applies; normalized 1190 mM. kcat: printed Table 4 cell 0.0065 s-1; already in s^-1, so no unit conversion applies; normalized 0.0065 s^(-1). kcat/Km: printed Table 4 cell 0.0059 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.0059 / 1000 = 0.0000059 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, substrate row 'L-xylose', H110Q column group: Km = 1190 mM; kcat = 0.0065 s-1; printed kcat/Km = 0.0059 M-1 s-1.

substrate: L-Xylose


sequence_variant_note: Resolved canonical sequence from uniprot_accession_variant_reconstruction and applied mutation signature H110A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


column_label: Table 3, enzyme row 'H110A', p-nitrobenzaldehyde column group; column 'Km (mM)' = 0.19; column 'kcat' = 0.03; column 'kcat/Km' = 146. Footnote a of the table gives kcat in s-1 and kcat/Km in s-1 M-1.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.19 mM; already in mM, so no unit conversion applies; normalized 0.19 mM. kcat: printed Table 3 cell 0.03 s-1; already in s^-1, so no unit conversion applies; normalized 0.03 s^(-1). kcat/Km: printed Table 3 cell 146 M^-1 s^-1; one M^-1 s^-1 is 0.001 s^-1 mM^-1, so 146 / 1000 = 0.146 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, enzyme row 'H110A', p-nitrobenzaldehyde column group: Km = 0.19 mM; kcat = 0.03 s-1; printed kcat/Km = 146 M-1 s-1.


sequence_source: UniProtKB reviewed accession P80276 FASTA, checked 2026-05-31


enzyme_display_name: fructose-bisphosphate aldolase

organism: Escherichia coli

substrate_name: D-Fructose 1,6-bisphosphate

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

enzyme: fructose-bisphosphate aldolase

substrate: D-Fructose 1,6-bisphosphate


sequence_source: UniProtKB:P0AB71 full sequence; variant reconstructed from source mutation signature using UniProt chain 2-359 mature numbering mapped to full-sequence positions by +1.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 full sequence; variant reconstructed from source mutation signature using UniProt chain 2-359 mature numbering mapped to full-sequence positions by +1. and applied mutation signature E182A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AB71 canonical sequence; D290A variant not reconstructed

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.


sequence_source: UniProtKB:P0AB71 canonical sequence; D288A variant not reconstructed


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 plus N286A reconstruction with sequence_variant_offset=1 and applied mutation signature N286A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 plus D109A reconstruction with sequence_variant_offset=1 and applied mutation signature D109A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AB71 plus N286A reconstruction with sequence_variant_offset=1


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 plus D144A reconstruction with sequence_variant_offset=1 and applied mutation signature D144A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Giardia intestinalis

substrate_name: D-fructose 1,6-bisphosphate

sequence_source: UniProtKB:A8B2U2; source O97447 resolves to primary accession A8B2U2

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

substrate: D-fructose 1,6-bisphosphate


sequence_source: UniProtKB reviewed accession P0AB71 canonical sequence from direct REST/TSV lookup


sequence_source: UniProtKB reviewed accession P0AB71 canonical sequence with selected-record mutation C112A applied after residue-coordinate check

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


sequence_source: UniProtKB reviewed accession P0AB71 canonical sequence with selected-record mutation H142A applied after residue-coordinate check

sequence_variant_note: Mutation signature H142A matches the mutant residue at offset +0 and the reference residue at offset -12; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB reviewed accession P0A991 canonical sequence from direct REST/TSV lookup


substrate_name: D-Fructose 1-phosphate

substrate: D-Fructose 1-phosphate


sequence_source: UniProtKB reviewed accession P0A991 canonical sequence with selected-record mutation K237A applied after residue-coordinate check


sequence_source: UniProtKB reviewed accession P0A991 canonical sequence with selected-record mutation K239A applied after residue-coordinate check


sequence_variant_note: Resolved canonical sequence from UniProt REST A8B2U2; source accession O97447; PMID 19236002 reports D255A glFBPA and the source accession O97447 resolves as a secondary accession of UniProt A8B2U2. and applied mutation signature D255A to reconstruct the assayed variant sequence.


organism: Giardia lamblia

sequence_source: UniProt REST A8B2U2; source accession O97447; PMID 17166851 describes Giardia lamblia FBPA; source accession O97447 resolves as a secondary accession of UniProt A8B2U2.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Retained PDF journal page 4861, wild-type glFBPA FBP-cleavage prose: kcat 3.55 +/- 0.05; Km 1.7 +/- 0.1; kcat/Km 2.1 x 10^6.

normalized_value_unit_evidence: Kinetic characterization prose: kcat 3.55 s^-1; Km 1.7 uM = 0.0017 mM; independently printed kcat/Km 2.1 x 10^6 s^-1 M^-1 = 2100 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic constants: kcat 3.55 +/- 0.05 s^-1; Km 1.7 +/- 0.1 uM; independently printed kcat/Km 2.1 x 10^6 s^-1 M^-1.

row_label: wild-type recombinant glFBPA / FBP cleavage


sequence_variant_note: Resolved canonical sequence from UniProt REST P05062; source accession P05062; PMID 12417303 names Q354E aldolase B; UniProt P05062 is human ALDOB EC 4.1.2.13. and applied mutation signature Q354E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P05062; source accession P05062; PMID 12417303 names L256P aldolase B; UniProt P05062 is human ALDOB EC 4.1.2.13. and applied mutation signature L256P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P05062; source accession P05062; PMID 12417303 names W147R aldolase B; UniProt P05062 is human ALDOB EC 4.1.2.13. and applied mutation signature W147R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P05062; source accession P05062; PMID 12417303 names N334K aldolase B; UniProt P05062 is human ALDOB EC 4.1.2.13. and applied mutation signature N334K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P05062; source accession P05062; PMID 10970798 reports Arg303->Gln in human liver aldolase; UniProt P05062 is human ALDOB EC 4.1.2.13. and applied mutation signature R303Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P05062; source accession P05062; PMID 12417303 names Q354E aldolase B; UniProt P05062 is human ALDOB EC 4.1.2.13.


organism: Bacillus methanolicus

substrate_name: D-glyceraldehyde 3-phosphate

sequence_source: UniProtKB:I3EBM6 direct REST lookup on 2026-05-31

substrate: D-glyceraldehyde 3-phosphate


sequence_source: UniProtKB:I3DTM2 direct REST lookup on 2026-05-31


substrate_name: D-Glyceraldehyde 3-phosphate

substrate: D-Glyceraldehyde 3-phosphate


organism: Edwardsiella ictaluri

sequence_source: UniProtKB:O52402 direct REST lookup on 2026-05-31


organism: Entamoeba histolytica

sequence_source: UniProtKB:C4LXD7 direct REST lookup on 2026-05-31


enzyme_display_name: Fructose-bisphosphate aldolase B

sequence_variant_note: Resolved canonical sequence from UniProt:P05062 reviewed canonical sequence plus N334K reconstruction and applied mutation signature N334K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

enzyme: Fructose-bisphosphate aldolase B


sequence_variant_note: Resolved canonical sequence from UniProt:P05062 reviewed canonical sequence plus W147R reconstruction and applied mutation signature W147R with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P05062 reviewed canonical sequence plus L256P reconstruction and applied mutation signature L256P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P05062 reviewed canonical sequence plus R303W reconstruction and applied mutation signature R303W with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P05062 reviewed canonical sequence plus R303Q reconstruction and applied mutation signature R303Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProt:P05062 reviewed canonical wild-type sequence


enzyme_display_name: Fructose-bisphosphate aldolase A

sequence_source: UniProt:P04075 reviewed canonical wild-type sequence

enzyme: Fructose-bisphosphate aldolase A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A991 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature K239A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature D144A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature D329A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature N286D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature D288A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB71 REST lookup 2026-05-31; variant handling by CatRange mutation_sequence.annotate_mutation_sequence and applied mutation signature D109A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Lampetra japonica

sequence_source: UniProtKB reviewed entry P53445


organism: Magnaporthe grisea 70-15

sequence_source: UniProtKB unreviewed entry G4NDL4

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

column_label: Retained PDF journal page 116, native untagged pT7-7/MGFBA3 FBP-cleavage measurement: kcat 45.7 +/- 0.4; Km 51 +/- 1; no printed kcat/Km cell.

normalized_value_unit_evidence: Normalized evidence: kcat 45.7 s^-1; Km 51 uM = 0.051 mM; same-measurement quotient 45.7/0.051 = 896.0784313725492 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic characterization prose: kcat 45.7 +/- 0.4 s^-1; Km 51 +/- 1 uM; no kcat/Km ratio cell was printed.

row_label: native untagged pT7-7/MGFBA3 recombinant enzyme / FBP cleavage


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed entry P9WQA3; source accession P67475 is listed as a secondary accession


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature G167A/G166A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.8; 295.15 K; cofactor NADH

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row G167A, G166A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 6.6; column 'Km (uM)' = 21; column 'kcat/Km (uM-1 min-1)' = 0.32.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row G167A, G166A: kcat = 6.6 min^-1; Km = 21 uM; printed kcat/Km = 0.32 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row G167A, G166A

table_label: Table 2: Kinetic Parameters for MtFBA, panel A: Fructose 1,6-bisphosphate (H2O) (Biochemistry 2013, 52(5):912-925, author manuscript page 28)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature G167A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row G167A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 10; column 'Km (uM)' = 21; column 'kcat/Km (uM-1 min-1)' = 0.48.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row G167A: kcat = 10 min^-1; Km = 21 uM; printed kcat/Km = 0.48 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row G167A


sequence_source: Reconstructed from UniProtKB reviewed P9WQA3 by applying D276A after confirming canonical residue 276 is aspartate

sequence_variant_note: Mutation signature D276A matches the mutant residue at offset +0 and the reference residue at offset +2; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature E169A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row E169A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 0.40; column 'Km (uM)' = 18; column 'kcat/Km (uM-1 min-1)' = 0.017.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row E169A: kcat = 0.40 min^-1; Km = 18 uM; printed kcat/Km = 0.017 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row E169A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P9WQA3 and applied mutation signature E168A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row E168A; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 160; column 'Km (uM)' = 30; column 'kcat/Km (uM-1 min-1)' = 5.3.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row E168A: kcat = 160 min^-1; Km = 30 uM; printed kcat/Km = 5.3 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row E168A


organism: Trypanosoma brucei

sequence_source: UniProtKB direct lookup for Q38B42 on 2026-05-31


sequence_source: UniProtKB direct lookup for P07752 on 2026-05-31


organism: Oryctolagus cuniculus


organism: Saccharomyces cerevisiae

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

column_label: Table label: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]". Reaction: FBA. Isoenzyme: Fba1p. Rows read: Parameter kcat, Value cell 4.14, Unit cell s−1; Parameter Kf16bp, Value cell 0.451, Unit cell mM. metric: kcat; raw value: 4.14; raw unit: s^-1; normalized value: 4.14 s^(-1); metric: Km; raw value: 0.451; raw unit: mM; normalized value: 0.451 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 9.179600886917958 s^-1 mM^-1; assay condition: Spectrophotometric assays of the glycolytic isoenzymes measuring consumption or production of NADH or NADPH; all assays were performed in a standardised reaction buffer at 30 °C in 384-well format plates with a 60 μl reaction volume, reagents in 45 μl, enzyme in 5 μl and substrate in 10 μl, with duplicate initial-rate measurements fitted to Michaelis-Menten kinetics. Export row conditions: pH 6.5; 303.15 K.

normalized_value_unit_evidence: Table 2 rows for FBA | Fba1p: kcat 4.14 s−1 = 4.14 s^(-1) (the paper's unit s−1 is already the export unit s^(-1), no conversion); Kf16bp 0.451 mM = 0.451 mM (the paper's Km-equivalent cell is already in the export unit mM, no conversion); kcat/Km 4.14 s^-1 mM^-1 = 9.179600886917958 s^-1 mM^-1 divided as 4.14 / 0.451. In the on-disk transcription the superscript minus one renders as the flattened `s−1` (U+2212 minus sign) and empty SEM/Ref cells render as empty ` | ` fields, so the kcat row prints as `FBA | Fba1p | kcat | 4.14 | 1.5 |  | s−1`.

raw_value_unit_evidence: Table 2, "Enzyme kinetics parameters determined in this project and contrasted with those of Ref. [23]" | header row: Reaction | Isoenzyme | Parameter | Value | SEM (%) | Ref. [23] | Unit | kcat row: FBA | Fba1p | kcat | 4.14 | 1.5 |  | s−1 | Kf16bp row: FBA | Fba1p | Kf16bp | 0.451 | 5.3 | 0.3 | mM | cells read: kcat = 4.14 s−1 (Value column, Unit column s−1); Kf16bp = 0.451 mM (Value column, Unit column mM)

row_label: FBA | Fba1p


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8; 321.15 K; cofactor NADPH

column_label: Table 1 (Activities of wild type and mutants of ST0318), FBPA (anabolic direction) block, row 'Wild type'; column 'kcat (s^-1)' = 0.91; column 'Km (mM)' = 0.19; column 'kcat/Km (s^-1 mM^-1)' = 4.7. The kcat and Km cells also print the standard deviations 0.04 and 0.02, which the export does not carry.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.91 s^-1; already in s^-1, so no unit conversion applies; the value carried forward is 0.91 s^(-1). Km: printed Table 1 cell 0.19 mM; already in mM, so no unit conversion applies; the value carried forward is 0.19 mM. kcat/Km: printed Table 1 cell 4.7 s^-1 mM^-1; already in s^-1 mM^-1, so no unit conversion applies; the value carried forward is 4.7 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, FBPA (anabolic direction) block, row 'Wild type': kcat = 0.91 s^-1; Km = 0.19 mM; printed kcat/Km = 4.7 s^-1 mM^-1.

table_label: Table 1: Activities of wild type and mutants of ST0318 (Nature 2011, 478:538-541)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F9VMT6 and applied mutation signature Y348F with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 1 (Activities of wild type and mutants of ST0318), FBPA (anabolic direction) block, row 'Y348F'; column 'kcat (s^-1)' = 0.10; column 'Km (mM)' = 0.34; column 'kcat/Km (s^-1 mM^-1)' = 0.29. The kcat and Km cells also print the standard deviations 0.01 and 0.04, which the export does not carry.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.10 s^-1; already in s^-1, so no unit conversion applies; the value carried forward is 0.1 s^(-1). Km: printed Table 1 cell 0.34 mM; already in mM, so no unit conversion applies; the value carried forward is 0.34 mM. kcat/Km: the printed Table 1 cell 0.29 s^-1 mM^-1 is the rounded rendering of the exact same-row quotient 0.10 / 0.34 = 0.29411764705882354 s^(-1)*mM^(-1), and that exact quotient is the value carried forward.

raw_value_unit_evidence: Table 1, FBPA (anabolic direction) block, row 'Y348F': kcat = 0.10 s^-1; Km = 0.34 mM; printed kcat/Km = 0.29 s^-1 mM^-1.


row_label: Table 1, FBPA (anabolic direction) block, row 'Wild type'


row_label: Table 1, FBPA (anabolic direction) block, row 'Y348F'


sequence_source: UniProtKB P9WQA3 canonical sequence from direct REST accession lookup on 2026-05-31.

column_label: Table 2 (Kinetic Parameters for MtFBA), panel A (Fructose 1,6-bisphosphate (H2O)), enzyme row wt; printed column heads Enzyme | kcat (min-1) | Km (uM) | kcat/Km (uM-1 min-1); column 'kcat (min-1)' = 720; column 'Km (uM)' = 40; column 'kcat/Km (uM-1 min-1)' = 18.

normalized_value_unit_evidence: Km: printed Table 2 panel A cell 40 uM; 1 uM is 1/1000 mM, so 40 / 1000 = 0.04 mM. kcat: printed Table 2 panel A cell 720 min^-1; the printed turnover column is per MINUTE, so 720 / 60 = 12.0 s^(-1). kcat/Km: printed Table 2 panel A cell 18 uM^-1 min^-1; 1 uM^-1 min^-1 is (1/60) s^-1 x 1000 mM^-1 = 16.666666666666668 s^-1 mM^-1, so 18 x 16.666666666666668 = 300.0 s^(-1)*mM^(-1). Each of the three converted cells equals the value the catalog already carries.

raw_value_unit_evidence: Table 2 panel A (Fructose 1,6-bisphosphate, H2O), enzyme row wt: kcat = 720 min^-1; Km = 40 uM; printed kcat/Km = 18 uM^-1 min^-1.

row_label: Table 2 panel A, enzyme row wt


sequence_source: Reconstructed from UniProtKB P00883 canonical sequence by applying mutation_signature with accession position = mature-paper position + 1; checked on 2026-05-31.

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00883 and applied mutation signature Q60E/P71Q/R91K/G102I/L320K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; buffer triplicate in a final volume of 350 ul. One; cofactor NADH

column_label: Table 2 (Steady-state kinetics of aldolase chimeras), enzyme row 'AB_DSP'; under the substrate group head 'Fru 1,6-P2' the column 'kcat (sec-1)' = 7.2 and the column 'Km (uM)' = 8.5. Table 2 prints only kcat and Km columns for each of its two substrate groups and prints no catalytic-efficiency column.

normalized_value_unit_evidence: kcat: printed cell 7.2 sec-1; sec-1 is the canonical s^(-1), so no unit conversion applies and the canonical value is 7.2 s^(-1). Km: printed cell 8.5 uM; 1 uM is 0.001 mM, so 8.5 / 1000 = 0.0085 mM. kcat/Km: no efficiency value is printed for this measurement, so the canonical efficiency is the quotient of the two printed cells of this one measurement, 7.2 / 0.0085 = 847.0588235294117 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Table 2, enzyme row 'AB_DSP', substrate group 'Fru 1,6-P2': printed kcat = 7.2 sec-1; printed Km = 8.5 uM. No catalytic-efficiency value is printed for this measurement.

table_label: Table 2: Steady-state kinetics of aldolase chimeras (Biochemistry 2007, 46(45):13010-13018)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00883 and applied mutation signature Y58F/I182L/Y327F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetics of aldolase chimeras), enzyme row 'AB_NPB'; under the substrate group head 'Fru 1,6-P2' the column 'kcat (sec-1)' = 9.7 and the column 'Km (uM)' = 6.8. Table 2 prints only kcat and Km columns for each of its two substrate groups and prints no catalytic-efficiency column.

normalized_value_unit_evidence: kcat: printed cell 9.7 sec-1; sec-1 is the canonical s^(-1), so no unit conversion applies and the canonical value is 9.7 s^(-1). Km: printed cell 6.8 uM; 1 uM is 0.001 mM, so 6.8 / 1000 = 0.0068 mM. kcat/Km: no efficiency value is printed for this measurement, so the canonical efficiency is the quotient of the two printed cells of this one measurement, 9.7 / 0.0068 = 1426.4705882352941 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Table 2, enzyme row 'AB_NPB', substrate group 'Fru 1,6-P2': printed kcat = 9.7 sec-1; printed Km = 6.8 uM. No catalytic-efficiency value is printed for this measurement.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00883 and applied mutation signature S38T/I39M/A40G/S45R/K311A/S353T/E354Q/I358T/S359A/H361Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetics of aldolase chimeras), enzyme row 'AB_TSP'; under the substrate group head 'Fru 1,6-P2' the column 'kcat (sec-1)' = 1.3 and the column 'Km (uM)' = 7.1. Table 2 prints only kcat and Km columns for each of its two substrate groups and prints no catalytic-efficiency column.

normalized_value_unit_evidence: kcat: printed cell 1.3 sec-1; sec-1 is the canonical s^(-1), so no unit conversion applies and the canonical value is 1.3 s^(-1). Km: printed cell 7.1 uM; 1 uM is 0.001 mM, so 7.1 / 1000 = 0.0071 mM. kcat/Km: no efficiency value is printed for this measurement, so the canonical efficiency is the quotient of the two printed cells of this one measurement, 1.3 / 0.0071 = 183.09859154929578 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Table 2, enzyme row 'AB_TSP', substrate group 'Fru 1,6-P2': printed kcat = 1.3 sec-1; printed Km = 7.1 uM. No catalytic-efficiency value is printed for this measurement.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00883 and applied mutation signature S38T/I39M/A40G/S45R/Q60E/P71Q/R91K/G102I/K311A/L320K/S353T/E354Q/I358T/S359A/H361Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetics of aldolase chimeras), enzyme row 'AB_P'; under the substrate group head 'Fru 1,6-P2' the column 'kcat (sec-1)' = 2.4 and the column 'Km (uM)' = 5.1. Table 2 prints only kcat and Km columns for each of its two substrate groups and prints no catalytic-efficiency column.

normalized_value_unit_evidence: kcat: printed cell 2.4 sec-1; sec-1 is the canonical s^(-1), so no unit conversion applies and the canonical value is 2.4 s^(-1). Km: printed cell 5.1 uM; 1 uM is 0.001 mM, so 5.1 / 1000 = 0.0051 mM. kcat/Km: no efficiency value is printed for this measurement, so the canonical efficiency is the quotient of the two printed cells of this one measurement, 2.4 / 0.0051 = 470.5882352941176 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, Table 2, enzyme row 'AB_P', substrate group 'Fru 1,6-P2': printed kcat = 2.4 sec-1; printed Km = 5.1 uM. No catalytic-efficiency value is printed for this measurement.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324) and applied mutation signature Y58F/V113A/H156Q/I182L/P262A/A296K/Y327F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324) and applied mutation signature S38T/I39M/A40G/S45R/K311A/S353T/E354Q/I358T/S359A/H361Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324) and applied mutation signature Y58F/I182L/Y327F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00883 and applied mutation signature C239A/C289A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Results prose, oxidation section: the gBi construct sentence states the turnover value 'kcat was 14 s-1' and the Michaelis value 'Km toward Fru 1,6-P2 was 8.6 uM'. No catalytic-efficiency value is printed for gBi.

normalized_value_unit_evidence: kcat: printed cell 14 s-1; s-1 is the canonical s^(-1), so no unit conversion applies and the canonical value is 14.0 s^(-1). Km: printed cell 8.6 uM; 1 uM is 0.001 mM, so 8.6 / 1000 = 0.0086 mM. kcat/Km: no efficiency value is printed for this measurement, so the canonical efficiency is the quotient of the two printed cells of this one measurement, 14.0 / 0.0086 = 1627.906976744186 s^-1 mM^-1.

raw_value_unit_evidence: Results prose, oxidation section, Results prose, the gBi construct, substrate Fru 1,6-P2: printed kcat = 14 s-1; printed Km = 8.6 uM. No catalytic-efficiency value is printed for this measurement.

table_label: Results prose sentence reporting the steady-state kinetics of the gBi aldolase variant (Biochemistry 2007, 46(45):13010-13018)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324) and applied mutation signature V113A/H156Q/P262A/A296K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00883 reviewed Swiss-Prot ALDOA_RABIT sequence (SV=2, CRC64 E61BCBC60F668324) and applied mutation signature S38T/I39M/A40G/S45R/Q60E/P71Q/R91K/G102I/K311A/L320K/S353T/E354Q/I358T/S359A/H361Y with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


organism: Homo sapiens

sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) accession P09972 direct REST check on 2026-05-31


sequence_source: UniProtKB UniProtKB reviewed (Swiss-Prot) accession P05062 direct REST check on 2026-05-31


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


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


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


enzyme_display_name: alcohol dehydrogenase

organism: Coturnix coturnix japonica

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


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


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

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


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.

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+

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.

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+


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.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table label: Table 3 Kinetic constants of alcohol dehydrogenases with retinal isomers. Substrate block: 11-cis-retinal. Enzyme column: Human 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