enzyme_display_name: aldose reductase

organism: Candida tenuis

substrate_name: D-Xylose

sequence_source: UniProt O74237 direct REST lookup; reviewed Candida tenuis XYL1_CANTE canonical sequence

enzyme: aldose reductase

substrate: D-Xylose


source_db: oed

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O74237 and applied mutation signature H113A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate; cofactor NADPH

column_label: Table 2: Apparent Kinetic Parameters for Xylose Reduction and Xylitol Oxidation Catalyzed by Wild-Type CtXR and H113A Mutant (Biochemistry 2004, 43, 4944-4954); printed column heads parameter | wild type | H113A; printed rows kcat red (s-1), Km xylose (mM), kcat red/Km xylose (M-1 s-1), Km NAD(P)H (uM), kcat ox (s-1), Km xylitol (mM), kcat ox/Km xylitol (M-1 s-1), Kd NAD(P)+ (uM). Table 2, H113A column, parenthetical NADPH values; row kcat red (s-1) = (0.12); row Km xylose (mM) = (391); row kcat red/Km xylose (M-1 s-1) = (0.32). captured primary segment: D-xylose | H113A CtXR | coenzyme NADPH | Km 391 mM | kcat 0.12 s^-1 | kcat/Km 0.32 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km xylose (mM) cell 391 mM, parenthetical NADPH value of the H113A column; already in mM, so no unit conversion applies; the paper value is 391.0 mM. kcat: printed Table 2 kcat red (s-1) cell 0.12 s^-1, parenthetical NADPH value of the H113A column; already in s^-1, so no unit conversion applies; the paper value is 0.12 s^(-1). kcat/Km: printed Table 2 kcat red/Km xylose (M-1 s-1) cell 0.32 M^-1 s^-1, parenthetical NADPH value of the H113A column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.32 / 1000 = 0.00032 s^(-1)*mM^(-1). Quotient disclosure for this column: 0.12 / 391 = 0.00030690537084398974 s^-1 mM^-1, against the printed efficiency cell 0.00032 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, H113A column, parenthetical NADPH values: Km xylose (mM) = 391 mM; kcat red (s-1) = 0.12 s^-1; printed kcat red/Km xylose (M-1 s-1) = 0.32 M^-1 s^-1.

row_label: Table 2, H113A column, values in parentheses obtained with NADPH (rows kcat red, Km xylose and kcat red/Km xylose)

data_origin: experimental

status: corrected

source: oed


substrate_name: NADH

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProt O74237 direct REST lookup; variant reconstructed from canonical sequence and selected mutation signature and applied mutation signature H113A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH

status: unverified


substrate_name: xylitol

mutation_signature: Unknown

kcat_over_km_origin: calculated

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

substrate: xylitol


sequence_variant_note: Resolved canonical sequence from UniProt O74237 direct REST lookup; variant reconstructed from canonical sequence and selected mutation signature and applied mutation signature N276D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O74237 direct REST lookup; variant reconstructed from canonical sequence and selected mutation signature and applied mutation signature K274M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt O74237 direct REST lookup; variant reconstructed from canonical sequence and selected mutation signature and applied mutation signature K274G to reconstruct the assayed variant sequence.


substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from UniProt O74237 direct REST lookup; variant reconstructed from canonical sequence and selected mutation signature and applied mutation signature K274R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: NADPH


sequence_source: UniProtKB O74237 canonical sequence with S275A substitution reconstructed during review

sequence_variant_note: Mutation signature S275A matches the mutant residue at offset +0 and the reference residue at offset +11; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB O74237 canonical sequence with R280H substitution reconstructed during review

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


sequence_source: UniProtKB O74237 canonical sequence with K274G substitution reconstructed during review


sequence_source: UniProtKB O74237 canonical sequence with K274R substitution reconstructed during review


sequence_source: UniProtKB O74237 canonical sequence with K274M substitution reconstructed during review


organism: Bos taurus

sequence_source: UniProtKB reviewed P16116 FASTA/JSON direct lookup


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


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


substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

assay_conditions_summary: pH 6.2; 310.15 K; buffer this record. Assay condition: 100 mM potassium phosphate; cofactor NADPH

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `DL-Glyceraldehyde`: Km (mM) = 0.123; kcat (s^-1) = 0.77; 10^3 x kcat/Km (M^-1 s^-1) = 6.41.

normalized_value_unit_evidence: kcat: printed cell 0.77 s^-1 is already the export unit s^(-1); the exported value is 0.77 s^(-1). Km: printed cell 0.123 mM is already the export unit mM; the exported value is 0.123 mM. kcat/Km: the printed efficiency cell 6.41 sits in the 10^3 x kcat/Km (M^-1 s^-1) column, and 10^3 M^-1 s^-1 equals 1 mM^-1 s^-1, so the printed cell is 6.41 s^(-1)*mM^(-1); the exported value is 6.260162601626017 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `DL-Glyceraldehyde`: Km (mM) = 0.123; Vmax (umol/min per mg of enzyme) = 1.27; kcat (s^-1) = 0.77; 10^3 x kcat/Km (M^-1 s^-1) = 6.41.

row_label: Table 2, decoded plain-numeral transcription, substrate row `DL-Glyceraldehyde`

substrate: Glyceraldehyde


substrate_name: D-Glucose

table_label: Table 2

row_label: D-Glucose

column_label: Km (mM) = 120; Vmax (umol/min per mg of enzyme) = 0.5; kcat (s^-1) = 0.3; kcat/Km-derived column value = 0.0025

substrate: D-Glucose


substrate_name: D-Glyceraldehyde 3-phosphate

verification_status: verified

sequence_source: UniProtKB reviewed accession P16116 direct REST lookup on 2026-05-31

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `Glyceraldehyde 3-phosphate`: Km (mM) = 0.2; kcat (s^-1) = 0.08; 10^3 x kcat/Km (M^-1 s^-1) = 0.4.

normalized_value_unit_evidence: kcat: printed cell 0.08 s^-1 is already the export unit s^(-1); the exported value is 0.08 s^(-1). Km: printed cell 0.2 mM is already the export unit mM; the exported value is 0.2 mM. kcat/Km: the printed efficiency cell 0.4 sits in the 10^3 x kcat/Km (M^-1 s^-1) column, and 10^3 M^-1 s^-1 equals 1 mM^-1 s^-1, so the printed cell is 0.4 s^(-1)*mM^(-1); the exported value is 0.39999999999999997 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `Glyceraldehyde 3-phosphate`: Km (mM) = 0.2; Vmax (umol/min per mg of enzyme) = 0.014; kcat (s^-1) = 0.08; 10^3 x kcat/Km (M^-1 s^-1) = 0.4.

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

substrate: D-Glyceraldehyde 3-phosphate

status: verified


substrate_name: D-Glucuronate

substrate: D-Glucuronate


substrate_name: Malondialdehyde

smiles: O=CCC=O

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `Malondialdehyde`: Km (mM) = 0.25; kcat (s^-1) = 0.13; 10^3 x kcat/Km (M^-1 s^-1) = 0.52.

normalized_value_unit_evidence: kcat: printed cell 0.13 s^-1 is already the export unit s^(-1); the exported value is 0.13 s^(-1). Km: printed cell 0.25 mM is already the export unit mM; the exported value is 0.25 mM. kcat/Km: the printed efficiency cell 0.52 sits in the 10^3 x kcat/Km (M^-1 s^-1) column, and 10^3 M^-1 s^-1 equals 1 mM^-1 s^-1, so the printed cell is 0.52 s^(-1)*mM^(-1); the exported value is 0.52 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `Malondialdehyde`: Km (mM) = 0.25; Vmax (umol/min per mg of enzyme) = 0.19; kcat (s^-1) = 0.13; 10^3 x kcat/Km (M^-1 s^-1) = 0.52.

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

substrate: Malondialdehyde


assay_conditions_summary: pH 6.2; 310.15 K; cofactor NADPH


substrate_name: p-Nitrobenzaldehyde

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `p-Nitrobenzaldehyde`: Km (mM) = 0.03; kcat (s^-1) = 0.27; 10^3 x kcat/Km (M^-1 s^-1) = 9.

normalized_value_unit_evidence: kcat: printed cell 0.27 s^-1 is already the export unit s^(-1); the exported value is 0.27 s^(-1). Km: printed cell 0.03 mM is already the export unit mM; the exported value is 0.03 mM. kcat/Km: the printed efficiency cell 9 sits in the 10^3 x kcat/Km (M^-1 s^-1) column, and 10^3 M^-1 s^-1 equals 1 mM^-1 s^-1, so the printed cell is 9 s^(-1)*mM^(-1); the exported value is 9.000000000000002 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `p-Nitrobenzaldehyde`: Km (mM) = 0.03; Vmax (umol/min per mg of enzyme) = 0.54; kcat (s^-1) = 0.27; 10^3 x kcat/Km (M^-1 s^-1) = 9.

row_label: Table 2, decoded plain-numeral transcription, substrate row `p-Nitrobenzaldehyde`

substrate: p-Nitrobenzaldehyde


column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `3-O-Methylglucose`: Km (mM) = 150; kcat (s^-1) = 0.06; 10^3 x kcat/Km (M^-1 s^-1) = 0.0004.

normalized_value_unit_evidence: kcat: printed cell 0.06 s^-1 is already the export unit s^(-1); the exported value is 0.06 s^(-1). Km: printed cell 150 mM is already the export unit mM; the exported value is 150.0 mM. kcat/Km: the printed efficiency cell 0.0004 sits in the 10^3 x kcat/Km (M^-1 s^-1) column, and 10^3 M^-1 s^-1 equals 1 mM^-1 s^-1, so the printed cell is 0.0004 s^(-1)*mM^(-1); the exported value is 0.00039999999999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `3-O-Methylglucose`: Km (mM) = 150; Vmax (umol/min per mg of enzyme) = 0.23; kcat (s^-1) = 0.06; 10^3 x kcat/Km (M^-1 s^-1) = 0.0004.

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


substrate_name: D-Fructose

substrate: D-Fructose


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_name: m-Nitrobenzaldehyde

substrate: m-Nitrobenzaldehyde


substrate_name: Benzaldehyde

substrate: Benzaldehyde


substrate_name: m-Fluorobenzaldehyde

substrate: m-Fluorobenzaldehyde


substrate_name: p-Tolualdehyde

substrate: p-Tolualdehyde


organism: Debaryomyces nepalensis

substrate_name: Glyoxal

sequence_source: UniProtKB:A0A0M4HL56 direct accession lookup, accessed 2026-05-31

smiles: O=CC=O

substrate: Glyoxal


substrate_name: D-ribose

substrate: D-ribose


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: D-Arabinose

substrate: D-Arabinose


substrate_name: isophthalaldehyde

substrate: isophthalaldehyde


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-Xylose

substrate: D-Xylose


sequence_source: UniProtKB reviewed entry O74237 (XYL1_CANTE), Candida tenuis/Yamadazyma tenuis, sequence version 1

assay_conditions_summary: pH 7; 298.15 K; buffer this record. Assay condition: 50 mM potassium phosphate; cofactor NADH

column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `3CN`: kcat (s^-1) = 19.6 +/- 0.7; Kaldehyde (mM) = 1.8 +/- 0.1; kcat/Kaldehyde (M^-1 s^-1) = 10641.

normalized_value_unit_evidence: kcat: printed cell 19.6 s^-1 -> 19.6 s^(-1) (unit already canonical); the exported value is 19.6 s^(-1). Km: printed Kaldehyde cell 1.8 mM -> 1.8 mM (unit already canonical); the exported value is 1.8 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 10641 M^-1 s^-1 for this substrate line -> 10.641 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 10.88888888888889 s^(-1)*mM^(-1).

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

table_label: Table 1 (PDF page 5 of 11, journal page 893) 'Kinetic parameters for NADH-dependent reduction of BA and derivatives thereof catalysed by CtXR at pH 7.0 and 25 C'


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `3CH3`: kcat (s^-1) = 11.3 +/- 1.2; Kaldehyde (mM) = 14.4 +/- 2.2; kcat/Kaldehyde (M^-1 s^-1) = 788.

normalized_value_unit_evidence: kcat: printed cell 11.3 s^-1 -> 11.3 s^(-1) (unit already canonical); the exported value is 11.3 s^(-1). Km: printed Kaldehyde cell 14.4 mM -> 14.4 mM (unit already canonical); the exported value is 14.4 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 788 M^-1 s^-1 for this substrate line -> 0.788 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 0.7847222222222222 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `3CH3`


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4Br`: kcat (s^-1) = 18.1 +/- 0.5; Kaldehyde (mM) = 1.5 +/- 0.1; kcat/Kaldehyde (M^-1 s^-1) = 12378.

normalized_value_unit_evidence: kcat: printed cell 18.1 s^-1 -> 18.1 s^(-1) (unit already canonical); the exported value is 18.1 s^(-1). Km: printed Kaldehyde cell 1.5 mM -> 1.5 mM (unit already canonical); the exported value is 1.5 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 12378 M^-1 s^-1 for this substrate line -> 12.378 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 12.066666666666668 s^(-1)*mM^(-1).

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


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4F`: kcat (s^-1) = 18.7 +/- 1.1; Kaldehyde (mM) = 9.1 +/- 0.9; kcat/Kaldehyde (M^-1 s^-1) = 2050.

normalized_value_unit_evidence: kcat: printed cell 18.7 s^-1 -> 18.7 s^(-1) (unit already canonical); the exported value is 18.7 s^(-1). Km: printed Kaldehyde cell 9.1 mM -> 9.1 mM (unit already canonical); the exported value is 9.1 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 2050 M^-1 s^-1 for this substrate line -> 2.05 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 2.0549450549450547 s^(-1)*mM^(-1).

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


substrate_name: xylitol

sequence_source: RCSB PDB 1R38 entity sequence linked to UniProt O74237 and PMID 15109252; paper H113A corresponds to H114A in UniProt numbering

sequence_variant_note: Mutation signature H113A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: xylitol


substrate_name: NADH

substrate: NADH


substrate_name: NADPH

substrate: NADPH


organism: Homo sapiens

substrate_name: Glyceraldehyde

sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P15121 canonical sequence using source/paper mutation numbering mapped to UniProt position n+1 and applied mutation signature C298A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

substrate: Glyceraldehyde


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P15121 canonical sequence using source/paper mutation numbering mapped to UniProt position n+1 and applied mutation signature R268A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB P15121 canonical sequence using source/paper mutation numbering mapped to UniProt position n+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 reconstructed from UniProtKB P15121 canonical sequence using source/paper mutation numbering mapped to UniProt position n+1 and applied mutation signature R293A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProtKB P15121 canonical sequence using source/paper mutation numbering mapped to UniProt position n+1 and applied mutation signature G213P with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.


substrate_name: Hydroxyacetone

smiles: CC(=O)CO

column_label: Table I (journal page 4365), substrate row `Acetol`: kcat (min^-1) = 73; Km (mM) = 2.2; kcat/Km (M^-1 min^-1) = 3.4 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 73 min^-1 -> 73/60 = 1.216666666666666666666666667 s^-1, carried here at the export's stored precision as 1.217 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.217 s^(-1). Km: printed cell 2.2 mM -> 2.2 mM; the catalog holds 2.2 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 3.4 x 10^4 M^-1 min^-1 -> 34000/(1000*60) = 0.5666666666666667 s^(-1)*mM^(-1); the catalog holds 0.5531818181818182 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.217 / 2.2) rather than the printed efficiency cell.

row_label: Table I, substrate row `Acetol`

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

substrate: Hydroxyacetone


substrate_name: L-Lactaldehyde

column_label: Table I (journal page 4365), substrate row `L-Lactaldehyde`: kcat (min^-1) = 96; Km (mM) = 0.019; kcat/Km (M^-1 min^-1) = 5.1 x 10^6.

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 0.019 mM -> 0.019 mM; the catalog holds 0.019 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 5.1 x 10^6 M^-1 min^-1 -> 5100000/(1000*60) = 85.0 s^(-1)*mM^(-1); the catalog holds 84.21052631578948 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.6 / 0.019) rather than the printed efficiency cell.

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

substrate: L-Lactaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P15121 and applied mutation signature W219A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P15121 and applied mutation signature R268A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P15121 and applied mutation signature G213P with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P15121 and applied mutation signature G213S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P15121 and applied mutation signature C298A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature S214A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature R293A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature S226A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature W219E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature G213S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P15121 canonical sequence plus source mutation signature; residue-numbering offset +1 inferred from the PMID 15769597 family context and applied mutation signature S210A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: all-trans-Retinal

sequence_source: UniProtKB:P15121 direct FASTA/JSON check (retrieved 2026-05-31)

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

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinaldehyde'; enzyme column head 'AKR1B1'; parameter rows 'K m (uM)' = 1.1, 'k cat (min^-1)' = 0.35 and 'k cat /K m (mM^-1 min^-1)' = 320. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.1 uM; 1.1 / 1000 = 0.0011 mM. kcat: printed Table 1 cell 0.35 min^-1; 0.35 / 60 = 0.005833333333333333 s^-1. kcat/Km: printed Table 1 cell 320 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 320 / 60 = 5.333333333333333 s^-1 mM^-1. The prior exported tuple for this row carried these same three quantities rounded to one significant digit; this pass writes the printed paper cells at their converted precision instead.

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinaldehyde', enzyme column 'AKR1B1': K m (uM) = 1.1; k cat (min^-1) = 0.35; printed k cat /K m (mM^-1 min^-1) = 320.

substrate: all-trans-Retinal


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O74237 and applied mutation signature K80A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

smiles: CC(F)CN

assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM potassium phosphate; cofactor NADH

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row '2-Fluoroethylamine'; column 'K amine (M)' = 0.54; column 'k max (s-1)' = 0.022; column 'k max /K amine (M-1 . s-1)' = 0.040; column 'pK a' = 9.0; column 'Mol. volume (A3)' = 80.5; column 'log P' = -0.29.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.54 M; 1 M is 1000 mM, so 0.54 x 1000 = 540 mM. kcat: printed Table 2 cell 0.022 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.022 s^(-1). kcat/Km: printed Table 2 cell 0.040 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.040 / 1000 = 0.00004 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.022 / 540 = 0.000040740741 s^-1 mM^-1, which in the printed unit is 0.040741 M-1 s-1, while the paper's own printed efficiency cell for the same amine row is 0.040 M-1 s-1 = 0.00004 s^-1 mM^-1; this record carries the printed cell.

raw_value_unit_evidence: Table 2, amine row '2-Fluoroethylamine': Km (K amine) = 0.54 M; kcat (k max) = 0.022 s-1; printed kcat/Km (k max /K amine) = 0.040 M-1 s-1.

row_label: Table 2, amine row '2-Fluoroethylamine' for the K80A mutant

table_label: Table 2: Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0 (Biochem. J. 2005, 389:507-515); printed column heads Amine | pK a | Mol. volume (A3) | log P | K amine (M) | k max (s-1) | k max /K amine (M-1 . s-1)


substrate_name: Propylamine

smiles: CCCN

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Propylamine'; column 'K amine (M)' = 0.23; column 'k max (s-1)' = 0.028; column 'k max /K amine (M-1 . s-1)' = 0.12; column 'pK a' = 10.5; column 'Mol. volume (A3)' = 94.2; column 'log P' = 0.26.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.23 M; 1 M is 1000 mM, so 0.23 x 1000 = 230 mM. kcat: printed Table 2 cell 0.028 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.028 s^(-1). kcat/Km: printed Table 2 cell 0.12 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.12 / 1000 = 0.00012 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.028 / 230 = 0.00012173913043478261 s^-1 mM^-1, which in the printed unit is 0.028 / 0.23 = 0.121739 M-1 s-1 and rounds, at the printed precision of the efficiency cell, to the 0.12 M-1 s-1 the table prints; the catalog carries that same full-precision quotient.

raw_value_unit_evidence: Table 2, amine row 'Propylamine': Km (K amine) = 0.23 M; kcat (k max) = 0.028 s-1; printed kcat/Km (k max /K amine) = 0.12 M-1 s-1.

row_label: Table 2, amine row 'Propylamine' for the K80A mutant

substrate: Propylamine


substrate_name: methylamine

smiles: CN

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Methylamine'; column 'K amine (M)' = 1.49; column 'k max (s-1)' = 0.097; column 'k max /K amine (M-1 . s-1)' = 0.065; column 'pK a' = 10.6; column 'Mol. volume (A3)' = 53.2; column 'log P' = -0.72.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.49 M; 1 M is 1000 mM, so 1.49 x 1000 = 1490 mM. kcat: printed Table 2 cell 0.097 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.097 s^(-1). kcat/Km: printed Table 2 cell 0.065 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.065 / 1000 = 0.000065 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.097 / 1490 = 0.0000651006711409396 s^-1 mM^-1, which in the printed unit is 0.097 / 1.49 = 0.065101 M-1 s-1 and rounds, at the printed precision of the efficiency cell, to the 0.065 M-1 s-1 the table prints; the catalog carries that same full-precision quotient.

raw_value_unit_evidence: Table 2, amine row 'Methylamine': Km (K amine) = 1.49 M; kcat (k max) = 0.097 s-1; printed kcat/Km (k max /K amine) = 0.065 M-1 s-1.

row_label: Table 2, amine row 'Methylamine' for the K80A mutant

substrate: methylamine


substrate_name: ethanolamine

smiles: NCCO

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Ethanolamine'; column 'K amine (M)' = 0.68; column 'k max (s-1)' = 0.0011; column 'k max /K amine (M-1 . s-1)' = 0.0016; column 'pK a' = 9.5; column 'Mol. volume (A3)' = 84.7; column 'log P' = -1.69.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.68 M; 1 M is 1000 mM, so 0.68 x 1000 = 680 mM. kcat: printed Table 2 cell 0.0011 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.0011 s^(-1). kcat/Km: printed Table 2 cell 0.0016 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.0016 / 1000 = 0.0000016 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.0011 / 680 = 0.000001617647 s^-1 mM^-1, which in the printed unit is 0.001618 M-1 s-1, while the paper's own printed efficiency cell for the same amine row is 0.0016 M-1 s-1 = 0.0000016 s^-1 mM^-1; this record carries the printed cell.

raw_value_unit_evidence: Table 2, amine row 'Ethanolamine': Km (K amine) = 0.68 M; kcat (k max) = 0.0011 s-1; printed kcat/Km (k max /K amine) = 0.0016 M-1 s-1.

row_label: Table 2, amine row 'Ethanolamine' for the K80A mutant

substrate: ethanolamine


smiles: N

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Ammonia'; column 'K amine (M)' = 0.41; column 'k max (s-1)' = 0.0021; column 'k max /K amine (M-1 . s-1)' = 0.0053; column 'pK a' = 9.2; column 'Mol. volume (A3)' = 31.9; column 'log P' = -1.19.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.41 M; 1 M is 1000 mM, so 0.41 x 1000 = 410 mM. kcat: printed Table 2 cell 0.0021 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.0021 s^(-1). kcat/Km: printed Table 2 cell 0.0053 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.0053 / 1000 = 0.0000053 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.0021 / 410 = 0.000005121951 s^-1 mM^-1, which in the printed unit is 0.005122 M-1 s-1, while the paper's own printed efficiency cell for the same amine row is 0.0053 M-1 s-1 = 0.0000053 s^-1 mM^-1; this record carries the printed cell.

raw_value_unit_evidence: Table 2, amine row 'Ammonia': Km (K amine) = 0.41 M; kcat (k max) = 0.0021 s-1; printed kcat/Km (k max /K amine) = 0.0053 M-1 s-1.

row_label: Table 2, amine row 'Ammonia' for the K80A mutant


substrate_name: Propargylamine

smiles: C#CCN

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Propargylamine'; column 'K amine (M)' = 0.21; column 'k max (s-1)' = 0.0030; column 'k max /K amine (M-1 . s-1)' = 0.015; column 'pK a' = 8.2; column 'Mol. volume (A3)' = 82.3; column 'log P' = -0.51.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.21 M; 1 M is 1000 mM, so 0.21 x 1000 = 210 mM. kcat: printed Table 2 cell 0.0030 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.003 s^(-1). kcat/Km: printed Table 2 cell 0.015 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.015 / 1000 = 0.000015 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.0030 / 210 = 0.000014285714 s^-1 mM^-1, which in the printed unit is 0.014286 M-1 s-1, while the paper's own printed efficiency cell for the same amine row is 0.015 M-1 s-1 = 0.000015 s^-1 mM^-1; this record carries the printed cell.

raw_value_unit_evidence: Table 2, amine row 'Propargylamine': Km (K amine) = 0.21 M; kcat (k max) = 0.0030 s-1; printed kcat/Km (k max /K amine) = 0.015 M-1 s-1.

row_label: Table 2, amine row 'Propargylamine' for the K80A mutant

substrate: Propargylamine


substrate_name: ethylamine

smiles: CCN

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row 'Ethylamine'; column 'K amine (M)' = 0.51; column 'k max (s-1)' = 0.058; column 'k max /K amine (M-1 . s-1)' = 0.11; column 'pK a' = 10.6; column 'Mol. volume (A3)' = 73.8; column 'log P' = -0.23.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.51 M; 1 M is 1000 mM, so 0.51 x 1000 = 510 mM. kcat: printed Table 2 cell 0.058 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.058 s^(-1). kcat/Km: printed Table 2 cell 0.11 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.11 / 1000 = 0.00011 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.058 / 510 = 0.00011372549019607843 s^-1 mM^-1, which in the printed unit is 0.058 / 0.51 = 0.113725 M-1 s-1 and rounds, at the printed precision of the efficiency cell, to the 0.11 M-1 s-1 the table prints; the catalog carries that same full-precision quotient.

raw_value_unit_evidence: Table 2, amine row 'Ethylamine': Km (K amine) = 0.51 M; kcat (k max) = 0.058 s-1; printed kcat/Km (k max /K amine) = 0.11 M-1 s-1.

row_label: Table 2, amine row 'Ethylamine' for the K80A mutant

substrate: ethylamine


smiles: NCC(F)(F)F

assay_conditions_summary: pH 5.5; 298.15 K; buffer 50 mM potassium phosphate; cofactor NADH

column_label: Table 2 (Chemical rescue of xylose reductase activity in K80A by external amines at pH 7.0), amine row '2,2,2-Trifluoroethylamine'; column 'K amine (M)' = 0.20; column 'k max (s-1)' = 0.0016; column 'k max /K amine (M-1 . s-1)' = 0.0081; column 'pK a' = 5.7; column 'Mol. volume (A3)' = 94.2; column 'log P' = 0.19.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.20 M; 1 M is 1000 mM, so 0.20 x 1000 = 200 mM. kcat: printed Table 2 cell 0.0016 s-1; the printed unit is already s^-1, so no unit conversion applies and the paper value is 0.0016 s^(-1). kcat/Km: printed Table 2 cell 0.0081 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.0081 / 1000 = 0.0000081 s^-1 mM^-1. Closure disclosure: the quotient of the two printed component cells is 0.0016 / 200 = 0.000008 s^-1 mM^-1, which in the printed unit is 0.008 M-1 s-1, while the paper's own printed efficiency cell for the same amine row is 0.0081 M-1 s-1 = 0.0000081 s^-1 mM^-1; this record carries the printed cell.

raw_value_unit_evidence: Table 2, amine row '2,2,2-Trifluoroethylamine': Km (K amine) = 0.20 M; kcat (k max) = 0.0016 s-1; printed kcat/Km (k max /K amine) = 0.0081 M-1 s-1.

row_label: Table 2, amine row '2,2,2-Trifluoroethylamine' for the K80A mutant


sequence_source: UniProtKB reviewed record O60218 retrieved 2026-05-31; canonical Homo sapiens AKR1B10 sequence.

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinaldehyde'; enzyme column head 'AKR1B10'; parameter rows 'K m (uM)' = 0.6, 'k cat (min^-1)' = 27 and 'k cat /K m (mM^-1 min^-1)' = 45000. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.6 uM; 0.6 / 1000 = 0.0006 mM. kcat: printed Table 1 cell 27 min^-1; 27 / 60 = 0.45 s^-1. kcat/Km: printed Table 1 cell 45000 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 45000 / 60 = 750.0 s^-1 mM^-1. Each of these converted quantities reproduces the exported value for this row: kcat 0.45 s^(-1), km 0.0006 mM and kcat_over_km 750.0000000000001 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinaldehyde', enzyme column 'AKR1B10': K m (uM) = 0.6; k cat (min^-1) = 27; printed k cat /K m (mM^-1 min^-1) = 45000.


substrate_name: Retinol

column_label: Table 1: Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids (Biochem. J. 2006, 399:101-109); substrate block 'All-trans-Retinol'; enzyme column head 'AKR1B10'; parameter rows 'K m (uM)' = 0.4, 'k cat (min^-1)' = 7.2 and 'k cat /K m (mM^-1 min^-1)' = 18000. The six enzyme column heads read, left to right, AKR1B1, AKR1B10, ADH4, ADH1B2, RDH11* and RoDH-4.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.4 uM; 0.4 / 1000 = 0.0004 mM. kcat: printed Table 1 cell 7.2 min^-1; 7.2 / 60 = 0.12 s^-1. kcat/Km: printed Table 1 cell 18000 mM^-1 min^-1; 1 mM^-1 min^-1 is 1/60 of 1 s^-1 mM^-1, so 18000 / 60 = 300.0 s^-1 mM^-1. Each of these converted quantities reproduces the exported value for this row: kcat 0.12 s^(-1), km 0.0004 mM and kcat_over_km 300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 'All-trans-Retinol', enzyme column 'AKR1B10': K m (uM) = 0.4; k cat (min^-1) = 7.2; printed k cat /K m (mM^-1 min^-1) = 18000.

substrate: Retinol


sequence_source: UniProtKB reviewed record O60218 retrieved 2026-05-31; canonical sequence checked at K125 and V301, then K125L/V301L applied by 1-based residue coordinates.

sequence_variant_note: Mutation signature K125L/V301L matches the mutant residue at offset +0 and the reference residue at offset -30; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB reviewed record O60218 retrieved 2026-05-31; canonical sequence checked at V301, then V301L applied by 1-based residue coordinates.

sequence_variant_note: Mutation signature V301L matches the mutant residue at offset +0 and the reference residue at offset -30; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProtKB reviewed record P15121 retrieved 2026-05-31; canonical Homo sapiens AKR1B1 sequence.


sequence_source: UniProtKB reviewed record O60218 retrieved 2026-05-31; canonical sequence checked at K125, then K125L applied by 1-based residue coordinates.

sequence_variant_note: Mutation signature K125L matches the mutant residue at offset +0 and the reference residue at offset -30; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


enzyme_display_name: Aldo-keto reductase family 1 member B10

sequence_source: UniProtKB reviewed canonical sequence O60218 with direct reconstruction of V301L

enzyme: Aldo-keto reductase family 1 member B10


sequence_source: UniProtKB reviewed canonical sequence O60218 with direct reconstruction of K125L


sequence_source: UniProtKB reviewed canonical sequence O60218


sequence_source: UniProtKB reviewed canonical sequence O60218 with direct reconstruction of K125L/V301L


enzyme_display_name: Aldo-keto reductase family 1 member B1

sequence_source: UniProtKB reviewed canonical sequence P15121

enzyme: Aldo-keto reductase family 1 member B1


substrate_name: D-Glucuronate

substrate: D-Glucuronate


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: Phenylglyoxal

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

substrate: Phenylglyoxal


substrate_name: p-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


substrate_name: D-Xylose

substrate: D-Xylose


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'


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`


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

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

smiles: CCC=O

substrate: propanal


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

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

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


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`

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.


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