organism: Streptomyces griseoflavus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature H165F to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic parameters of the SgfSL variants), ABTS block, protein row 'H165F'; column 'Km (mM)' = 0.45 ± 0.03; column 'kcat (s-1)' = 0.12 ± 0.009; column 'kcat/Km (mM-1 s-1)' = 0.26; column 'Activity nM O2 min-1 ug-1' = 0.13 ± 0.06.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.12 under the column head kcat (s-1); the cell is already in s^-1, so no unit conversion applies and the canonical value is 0.12 s^(-1). Km: printed Table 3 cell 0.45 under the column head Km (mM); the cell is already in mM, so no unit conversion applies and the canonical value is 0.45 mM. kcat/Km: printed Table 3 cell 0.26 under the column head kcat/Km (mM-1 s-1); the cell is already in mM^-1 s^-1, so no unit conversion applies and the canonical value is 0.26 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, ABTS block, protein row 'H165F': Km = 0.45 mM; kcat = 0.12 s-1; printed kcat/Km = 0.26 mM-1 s-1.

table_label: Table 3: Kinetic parameters of the SgfSL variants (Int. J. Mol. Sci. 2019, volume 20, article 3184, page 6); printed column heads Substrate | Protein | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1) | Activity nM O2 min-1 ug-1


enzyme_display_name: laccase

source_db: oed

verification_status: verified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature H165A to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 3 (Kinetic parameters of the SgfSL variants), 2,6-DMP block, protein row 'H165A'; column 'Km (mM)' = 6.10 ± 0.34; column 'kcat (s-1)' = 1.10 ± 0.06; column 'kcat/Km (mM-1 s-1)' = 0.18.

normalized_value_unit_evidence: kcat: printed Table 3 cell 1.10 under the column head kcat (s-1); the cell is already in s^-1, so no unit conversion applies and the canonical value is 1.1 s^(-1). Km: printed Table 3 cell 6.10 under the column head Km (mM); the cell is already in mM, so no unit conversion applies and the canonical value is 6.1 mM. kcat/Km: printed Table 3 cell 0.18 under the column head kcat/Km (mM-1 s-1); the cell is already in mM^-1 s^-1, so no unit conversion applies and the printed cell carries over as 0.18 s^-1 mM^-1, while the full-precision quotient of the same line's two printed component cells is 1.10 / 6.10 = 0.18032786885245905 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, 2,6-DMP block, protein row 'H165A': Km = 6.10 mM; kcat = 1.10 s-1; printed kcat/Km = 0.18 mM-1 s-1.

data_origin: experimental

enzyme: laccase

status: verified

source: oed


sequence_source: UniProtKB REST accession A0A0M4FJ81 checked 2026-05-31; I170F reconstructed from canonical sequence

sequence_variant_note: Mutation signature I170F matches the mutant residue at offset +0 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


column_label: Table 3 (Kinetic parameters of the SgfSL variants), ABTS block, protein row 'H165A'; column 'Km (mM)' = 0.12 ± 0.01; column 'kcat (s-1)' = 10.80 ± 0.21; column 'kcat/Km (mM-1 s-1)' = 90.00; column 'Activity nM O2 min-1 ug-1' = 1.45 ± 0.10.

normalized_value_unit_evidence: kcat: printed Table 3 cell 10.80 under the column head kcat (s-1); the cell is already in s^-1, so no unit conversion applies and the canonical value is 10.8 s^(-1). Km: printed Table 3 cell 0.12 under the column head Km (mM); the cell is already in mM, so no unit conversion applies and the canonical value is 0.12 mM. kcat/Km: printed Table 3 cell 90.00 under the column head kcat/Km (mM-1 s-1); the cell is already in mM^-1 s^-1, so no unit conversion applies and the canonical value is 90.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, ABTS block, protein row 'H165A': Km = 0.12 mM; kcat = 10.80 s-1; printed kcat/Km = 90.00 mM-1 s-1.


organism: Bacillus subtilis

mutation_signature: Unknown

sequence_source: UniProtKB:H8WGE7 REST lookup, checked 2026-05-31

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


substrate_name: Syringaldazine

substrate: Syringaldazine


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed with L431F, checked 2026-05-31 and applied mutation signature L431F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 313.15 K; buffer ethanol plus 100 mM citrate-phosphate

status: corrected


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed with R146K, checked 2026-05-31 and applied mutation signature R146K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 313.15 K; buffer pH 4


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed with R476K, checked 2026-05-31 and applied mutation signature R476K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P07788 canonical sequence reconstructed with T480A, checked 2026-05-31 and applied mutation signature T480A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P07788 canonical sequence reconstructed with L431F, checked 2026-05-31


verification_status: unverified

sequence_source: UniProtKB A0A0M4FJ81 canonical sequence fetched 2026-05-31; H165A and R240H applied after direct residue-position check.

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

status: unverified


sequence_source: UniProtKB A0A0M4FJ81 canonical sequence fetched 2026-05-31; H165A and M199G applied after direct residue-position check.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0M4FJ81 and applied mutation signature M199G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4; 303.15 K; buffer 50 mM Britton-Robinson

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'ABTS', protein row 'Met199Gly'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.20 ± 0.06; column 'kcat (s-1)' = 45 ± 7; column 'kcat/Km(s-1 mM-1)' = 226.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.20 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.2 mM. kcat: printed Table 2 cell 45 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 45.0 s^(-1). kcat/Km: printed Table 2 cell 226 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 226.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 45 / 0.20 = 225.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (225.0); the paper's own printed efficiency cell is 226.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'ABTS', protein row 'Met199Gly': Km = 0.20 ± 0.06 mM; kcat = 45 ± 7 s^-1; printed kcat/Km = 226 s^-1 mM^-1; printed pHopt = 4.0.


sequence_source: UniProtKB A0A0M4FJ81 canonical sequence fetched 2026-05-31.

column_label: Table 2: Kinetic constants and pHopt of ABTS, 2.6-DMP, and K4[Fe(CN)6] oxidation by SgfSL-mutant forms and SgfSLwt (Int J Mol Sci 2022, 23(1):65), substrate block 'K4[Fe(CN)6]', protein row 'SgfSLwt'; column 'pHopt' = 4.0; column 'Km(mM)' = 0.10 ± 0.02; column 'kcat (s-1)' = 38 ± 2; column 'kcat/Km(s-1 mM-1)' = 383.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.10 mM; the printed unit is already mM, so no conversion applies and the paper value is 0.1 mM. kcat: printed Table 2 cell 38 s^-1; the printed unit is already s^-1, so no conversion applies and the paper value is 38.0 s^(-1). kcat/Km: printed Table 2 cell 383 s^-1 mM^-1; the printed unit is already s^-1 mM^-1, so no conversion applies and the paper value is 383.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of the two printed component cells is 38 / 0.10 = 380.0 s^-1 mM^-1, which is the value the export stores for kcat_over_km (380.0); the paper's own printed efficiency cell is 383.0 s^-1 mM^-1, computed by the authors from their unrounded fitted parameters, and this record carries the printed cell.

raw_value_unit_evidence: Table 2, substrate block 'K4[Fe(CN)6]', protein row 'SgfSLwt': Km = 0.10 ± 0.02 mM; kcat = 38 ± 2 s^-1; printed kcat/Km = 383 s^-1 mM^-1; printed pHopt = 4.0.


organism: Streptomyces ipomoeae

sequence_source: UniProtKB A3QVH2 canonical sequence fetched 2026-05-31.


organism: Streptomyces coelicolor

substrate_name: Morin

sequence_source: UniProt Q9XAL8 direct REST/FASTA check; RCSB 3CG8 SIFTS confirms Q9XAL8 alignment.

substrate: Morin


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt Q9XAL8 canonical sequence by direct S292A substitution; full-length residue 292 is S. and applied mutation signature S292A to reconstruct the assayed variant sequence.


substrate_name: quercetin

substrate: quercetin


sequence_source: Reconstructed from UniProt Q9XAL8 canonical sequence by direct S292A substitution; full-length residue 292 is S.


substrate_name: myricetin

substrate: myricetin


organism: Streptomyces sviceus

sequence_source: UniProt B5HSR1 FASTA; M220L applied after direct residue check showed canonical residue 220 is M.

sequence_variant_note: Mutation signature M220L 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: UniProt B5HSR1 FASTA; M195L applied after direct residue check showed canonical residue 195 is M.


sequence_source: UniProt B5HSR1 FASTA; M220L and T222L applied after direct residue checks showed canonical residues 220=M and 222=T.

sequence_variant_note: Mutation signature M220L/T222L matches the mutant residue at offset +0 and the reference residue at offset +24; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_source: UniProt B5HSR1 FASTA; M293L applied after direct residue check showed canonical residue 293 is M.


sequence_source: UniProt B5HSR1 FASTA; M195A, V287N, M293G, and M295L applied after direct residue checks showed canonical residues 195=M, 287=V, 293=M, and 295=M.


sequence_source: UniProt B5HSR1 FASTA; M295V applied after direct residue check showed canonical residue 295 is M.


sequence_source: UniProt B5HSR1 FASTA; M293G applied after direct residue check showed canonical residue 293 is M.


sequence_source: UniProt B5HSR1 FASTA; M295T applied after direct residue check showed canonical residue 295 is M.


enzyme_display_name: Copper oxidase

sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M293G/M295L reconstructed from validated canonical residue(s): M293G validated against canonical residue M293; M295L validated against canonical residue M295.

enzyme: Copper oxidase


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M295A reconstructed from validated canonical residue(s): M295A validated against canonical residue M295.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M295F reconstructed from validated canonical residue(s): M295F validated against canonical residue M295.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M295Y reconstructed from validated canonical residue(s): M295Y validated against canonical residue M295.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M295I reconstructed from validated canonical residue(s): M295I validated against canonical residue M295.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M295L reconstructed from validated canonical residue(s): M295L validated against canonical residue M295.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; V287N reconstructed from validated canonical residue(s): V287N validated against canonical residue V287.


sequence_source: UniProtKB B5HSR1 FASTA fetched 2026-05-31; M195A/M293G/M295L reconstructed from validated canonical residue(s): M195A validated against canonical residue M195; M293G validated against canonical residue M293; M295L validated against canonical residue M295.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with I170A and applied mutation signature I170A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with M199A and applied mutation signature M199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with M199G/R240H and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with M199G and applied mutation signature M199G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with H165A/R240H and applied mutation signature H165A/R240H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB A0A0M4FJ81 FASTA; reconstructed with M199A


sequence_source: UniProtKB A0A0M4FJ81 FASTA; reconstructed with H165A/R240H


sequence_variant_note: Resolved canonical sequence from UniProtKB A0A0M4FJ81 FASTA; reconstructed with Y230A and applied mutation signature Y230A to reconstruct the assayed variant sequence.


organism: Thermus thermophilus

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: catechol

substrate: catechol


substrate_name: Guaiacol

substrate: Guaiacol


sequence_source: UniProt:F6DF14 canonical sequence; D106L reconstructed on 2026-05-31 by replacing canonical residue 106 D with L from the selected source mutation signature.

sequence_variant_note: Mutation signature D106L matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:B5HSR1 direct accession lookup; row-specific M195A sequence reconstructed from the canonical sequence. and applied mutation signature M195A to reconstruct the assayed variant sequence.


organism: Streptomyces viridochromogenes

sequence_source: UniProtKB:J9S5G3 direct accession lookup.

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


substrate_name: Potassium ferrocyanide

substrate: Potassium ferrocyanide


organism: Thermobaculum terrenum


organism: Thermobifida fusca

sequence_source: UniProt Q47QW5 / NCBI Protein AAZ55152.1 canonical sequence with R49K reconstructed after confirming residue 49 is R.


organism: Thermus sp.

sequence_source: NCBI Protein KHG66454.1 from the PMID 30756202 paper-linked Thermus sp. 2.9 LAC_2.9 route; source UniProt A0A0B0SEJ6 is inactive.


sequence_source: UniProt Q4H436 / NCBI Protein BAE16261.1 canonical wild-type sequence.


sequence_source: UniProt F6DF14 / NCBI Protein AEG34143.1 canonical wild-type sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81; direct REST/FASTA check 2026-05-31 and applied mutation signature Y230A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81; direct REST/FASTA check 2026-05-31 and applied mutation signature M199G/R240H to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A0M4FJ81; direct REST/FASTA check 2026-05-31


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81; direct REST/FASTA check 2026-05-31 and applied mutation signature M199A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0M4FJ81; direct REST/FASTA check 2026-05-31 and applied mutation signature M199G to reconstruct the assayed variant sequence.


substrate_name: guaiacol

sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D394N to reconstruct the assayed variant sequence.

substrate: guaiacol


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D394E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D394R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D396M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D396A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D394M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 direct lookup; mutant sequence reconstructed from selected mutation_signature when present and applied mutation signature D396N to reconstruct the assayed variant sequence.


organism: Toxicodendron vernicifluum

substrate_name: ferrocyanide

substrate: ferrocyanide


substrate_name: dopamine

substrate: dopamine


substrate_name: ferrocenemonocarboxylic acid

substrate: ferrocenemonocarboxylic acid


organism: Trametes hirsuta


substrate_name: Eugenol

substrate: Eugenol


organism: Trametes sp.


substrate_name: syringaldazine

substrate: syringaldazine


organism: Trametes sp. C30


sequence_source: UniProtKB Q02497 direct REST lookup; LAC1_TRAHI reviewed laccase, Trametes hirsuta, EC 1.10.3.2, sequence length 520.


substrate_name: sinapate

sequence_source: UniProtKB B2L9C1 direct REST lookup; B2L9C1_TRAHI unreviewed laccase, Trametes hirsuta, EC 1.10.3.2, sequence length 520.

substrate: sinapate


substrate_name: hydroquinone

substrate: hydroquinone


organism: Streptomyces sp. C1

substrate_name: L-Dopa

substrate: L-Dopa


assay_conditions_summary: pH 9; 295.15 K; buffer pH 9


assay_conditions_summary: pH 8; 295.15 K; buffer pH 8


assay_conditions_summary: pH 4; 295.15 K; buffer pH 4


sequence_variant_note: Resolved canonical sequence from uniprot:B5HSR1 plus M295L reconstruction and applied mutation signature M295L to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProt F6DF14 canonical sequence after direct residue check: position 106 is D and was changed to R.

sequence_variant_note: Mutation signature D106R matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6DF14 and applied mutation signature E456L to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent steady-state kinetic constants measured at the saturating concentrations of O2 for guaiacol by the lacTT proteins (Appl Microbiol Biotechnol 2018, 102:4049-4061); printed column heads LacTT | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1); enzyme row E456L; column 'Km (uM)' = 135; column 'kcat (s^-1)' = 0.059; column 'kcat/Km (s^-1 mM^-1)' = 0.44. captured primary segment: Table 1 row E456L | construct lacTT E456L | substrate guaiacol | condition pH 6.0 | Km 135 uM | kcat 0.059 s^-1 | kcat/Km 0.44 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 135 uM; 135 / 1000 = 0.135 mM. kcat: printed Table 1 cell 0.059 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.059 s^(-1). kcat/Km: printed Table 1 cell 0.44 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.44 s^(-1)*mM^(-1). Closure disclosure for this row: the quotient of the two printed component cells is 0.059 / 0.135 = 0.437037037037037 s^-1 mM^-1, which is the exported catalytic efficiency, and the paper's own printed efficiency cell 0.44 s^-1 mM^-1 is that same quotient written at the table's printed precision.

raw_value_unit_evidence: Table 1, enzyme row E456L: Km = 135 uM; kcat = 0.059 s^-1; kcat/Km = 0.44 s^-1 mM^-1.

row_label: Table 1, enzyme row E456L


sequence_source: Reconstructed from UniProt F6DF14 canonical sequence after direct residue check: position 106 is D and was changed to E.

sequence_variant_note: Mutation signature D106E matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6DF14 and applied mutation signature E456D to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent steady-state kinetic constants measured at the saturating concentrations of O2 for guaiacol by the lacTT proteins (Appl Microbiol Biotechnol 2018, 102:4049-4061); printed column heads LacTT | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1); enzyme row E456D; column 'Km (uM)' = 380; column 'kcat (s^-1)' = 0.78; column 'kcat/Km (s^-1 mM^-1)' = 2.1. captured primary segment: Table 1 row E456D | construct lacTT E456D | substrate guaiacol | condition pH 6.0 | Km 380 uM | kcat 0.78 s^-1 | kcat/Km 2.1 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 380 uM; 380 / 1000 = 0.38 mM. kcat: printed Table 1 cell 0.78 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.78 s^(-1). kcat/Km: printed Table 1 cell 2.1 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 2.1 s^(-1)*mM^(-1). Closure disclosure for this row: the quotient of the two printed component cells is 0.78 / 0.38 = 2.0526315789473686 s^-1 mM^-1, which is the exported catalytic efficiency, and the paper's own printed efficiency cell 2.1 s^-1 mM^-1 is that same quotient written at the table's printed precision.

raw_value_unit_evidence: Table 1, enzyme row E456D: Km = 380 uM; kcat = 0.78 s^-1; kcat/Km = 2.1 s^-1 mM^-1.

row_label: Table 1, enzyme row E456D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6DF14 and applied mutation signature E456R to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent steady-state kinetic constants measured at the saturating concentrations of O2 for guaiacol by the lacTT proteins (Appl Microbiol Biotechnol 2018, 102:4049-4061); printed column heads LacTT | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1); enzyme row E456R; column 'Km (uM)' = 512; column 'kcat (s^-1)' = 0.32; column 'kcat/Km (s^-1 mM^-1)' = 0.62. captured primary segment: Table 1 row E456R | construct lacTT E456R | substrate guaiacol | condition pH 6.0 | Km 512 uM | kcat 0.32 s^-1 | kcat/Km 0.62 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 512 uM; 512 / 1000 = 0.512 mM. kcat: printed Table 1 cell 0.32 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 0.32 s^(-1). kcat/Km: printed Table 1 cell 0.62 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 0.62 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.32 / 0.512 = 0.625 s^-1 mM^-1, against the paper's own printed efficiency cell 0.62 s^-1 mM^-1, which is the value carried forward here.

raw_value_unit_evidence: Table 1, enzyme row E456R: Km = 512 uM; kcat = 0.32 s^-1; kcat/Km = 0.62 s^-1 mM^-1.

row_label: Table 1, enzyme row E456R


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6DF14 and applied mutation signature D423A to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent steady-state kinetic constants measured at the saturating concentrations of O2 for guaiacol by the lacTT proteins (Appl Microbiol Biotechnol 2018, 102:4049-4061); printed column heads LacTT | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1); enzyme row D423A; column 'Km (uM)' = 476; column 'kcat (s^-1)' = 3.51; column 'kcat/Km (s^-1 mM^-1)' = 7.37. captured primary segment: Table 1 row D423A | construct lacTT D423A | substrate guaiacol | condition pH 6.0 | Km 476 uM | kcat 3.51 s^-1 | kcat/Km 7.37 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 476 uM; 476 / 1000 = 0.476 mM. kcat: printed Table 1 cell 3.51 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 3.51 s^(-1). kcat/Km: printed Table 1 cell 7.37 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 7.37 s^(-1)*mM^(-1). Closure disclosure for this row: the quotient of the two printed component cells is 3.51 / 0.476 = 7.373949579831932 s^-1 mM^-1, which is the exported catalytic efficiency, and the paper's own printed efficiency cell 7.37 s^-1 mM^-1 is that same quotient written at the table's printed precision.

raw_value_unit_evidence: Table 1, enzyme row D423A: Km = 476 uM; kcat = 3.51 s^-1; kcat/Km = 7.37 s^-1 mM^-1.

row_label: Table 1, enzyme row D423A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:F6DF14 and applied mutation signature E356A to reconstruct the assayed variant sequence.

column_label: Table 1: Apparent steady-state kinetic constants measured at the saturating concentrations of O2 for guaiacol by the lacTT proteins (Appl Microbiol Biotechnol 2018, 102:4049-4061); printed column heads LacTT | Km (uM) | kcat (s^-1) | kcat/Km (s^-1 mM^-1); enzyme row E356A; column 'Km (uM)' = 1466; column 'kcat (s^-1)' = 1.70; column 'kcat/Km (s^-1 mM^-1)' = 1.16. captured primary segment: Table 1 row E356A | construct lacTT E356A | substrate guaiacol | condition pH 6.0 | Km 1466 uM | kcat 1.70 s^-1 | kcat/Km 1.16 s^-1 mM^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 1466 uM; 1466 / 1000 = 1.466 mM. kcat: printed Table 1 cell 1.70 s^-1; the printed turnover column is per second, so no unit conversion applies and the value is 1.7 s^(-1). kcat/Km: printed Table 1 cell 1.16 s^-1 mM^-1; the printed efficiency column is already per second per millimolar, so no unit conversion applies and the value is 1.16 s^(-1)*mM^(-1). Closure disclosure for this row: the quotient of the two printed component cells is 1.7 / 1.466 = 1.159618008185539 s^-1 mM^-1, which is the exported catalytic efficiency, and the paper's own printed efficiency cell 1.16 s^-1 mM^-1 is that same quotient written at the table's printed precision.

raw_value_unit_evidence: Table 1, enzyme row E356A: Km = 1466 uM; kcat = 1.70 s^-1; kcat/Km = 1.16 s^-1 mM^-1.

row_label: Table 1, enzyme row E356A


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt F6DF14 canonical sequence after direct residue check: position 460 is M and was changed to Q. and applied mutation signature M460Q to reconstruct the assayed variant sequence.


sequence_source: UniProtKB exact accession Q8NID5 direct lookup

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


sequence_source: UniProtKB exact accession Q6TH77 direct lookup


organism: Trametes versicolor

substrate_name: Methyl syringate

sequence_source: UniProtKB exact accession Q12718 direct lookup

substrate: Methyl syringate


substrate_name: acetosyringone

substrate: acetosyringone


substrate_name: syringaldehyde

substrate: syringaldehyde


organism: unknown prokaryotic organism

sequence_source: UniProtKB exact accession Q1EIR0 direct lookup


substrate_name: Syringaldazine

sequence_source: UniProtKB Q1EIR0 direct FASTA/JSON lookup on 2026-05-31

substrate: Syringaldazine


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


substrate_name: alpha-Naphthol

substrate: alpha-Naphthol


substrate_name: catechol

substrate: catechol


sequence_source: UniProtKB A0ACD6B8I0, direct live replacement for inactive/demerged E1ACR6


substrate_name: Guaiacol

sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 and applied mutation signature M460H to reconstruct the assayed variant sequence.

substrate: Guaiacol


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 and applied mutation signature M460L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 and applied mutation signature M460A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 and applied mutation signature M460F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q72HW2 and applied mutation signature M455L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q72HW2 and applied mutation signature M456A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:F6DF14 and applied mutation signature D396E to reconstruct the assayed variant sequence.


sequence_source: NCBI GenBank KP752045.1 CDS translation, protein_id AKN79754.1; source UniProt A0A0H4CVT8 is inactive/deleted and was not promoted

assay_conditions_summary: pH 7; 333.15 K; buffer pH 7


enzyme_display_name: phosphoglycerate kinase

organism: Homo sapiens

substrate_name: ADP

sequence_source: UniProtKB P00558 canonical PGK1_HUMAN sequence retrieved directly on 2026-05-31; validated source residue E at 1-based position 344 and applied E344A substitution.

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ADP

enzyme: phosphoglycerate kinase

substrate: ADP


substrate_name: dADP

sequence_source: UniProtKB P00558 canonical PGK1_HUMAN sequence retrieved directly on 2026-05-31; validated source residue N at 1-based position 337 and applied N337D substitution.

substrate: dADP


substrate_name: dATP

sequence_source: UniProtKB P00558 canonical PGK1_HUMAN FASTA/JSON retrieved directly on 2026-05-31.

column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row dATP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 73.6 uM, kcat 1.8 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.03 s^-1 / 0.074 mM = 0.40540540540540543 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 73.6 uM; kcat 1.8 min^-1 (Table II, wild-type PGK).

row_label: dATP (Table II)

substrate: dATP


substrate_name: ATP

sequence_source: UniProtKB P00558 canonical PGK1_HUMAN sequence retrieved directly on 2026-05-31; validated source residue K at 1-based position 220 and applied K220A substitution.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: dCTP

substrate: dCTP


substrate_name: dTTP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00558 and applied mutation signature N337D to reconstruct the assayed variant sequence.

column_label: Table VI (Dephosphorylation of nucleoside analog triphosphates by the Asn337 substitution mutants of human PGK), N337D enzyme-form block, nucleoside analog triphosphate row 'TTP'; column 'Km' with printed unit uM = 78.0 +/- 3.2; column 'kcat' with printed unit min^-1 = 8.7 +/- 1.8, followed by the parenthesised mutant-over-wild-type kcat term (8.2). The N337D block prints no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table VI cell 78.0 uM; 78.0 / 1000 = 0.078 mM, carried exactly. kcat: printed Table VI cell 8.7 min^-1; 8.7 / 60 = 0.145 s^-1 exactly, a terminating quotient that needs no rounding; the paper value is 0.145 s^(-1). kcat/Km: the paper value 1.8589743589743588 s^(-1)*mM^(-1) is the quotient 0.145 / 0.078 of this same Table VI line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table VI, N337D enzyme-form block, nucleoside analog triphosphate row 'TTP': Km = 78.0 +/- 3.2 uM in the column headed Km with printed unit uM; kcat = 8.7 +/- 1.8 min^-1 in the column headed kcat with printed unit min^-1. The N337D block of this table prints no catalytic-efficiency column.

table_label: Table VI: Dephosphorylation of nucleoside analog triphosphates by the Asn337 substitution mutants of human PGK, N337D enzyme-form block (J. Biol. Chem. 2002, 277(35):31593-31600)

substrate: dTTP


substrate_name: CTP

substrate: CTP


sequence_source: UniProtKB P00558 canonical PGK1_HUMAN sequence retrieved directly on 2026-05-31; validated source residue N at 1-based position 337 and applied N337Q substitution.


sequence_source: UniProtKB:P00558 direct REST lookup (reviewed Swiss-Prot canonical sequence)

column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row CTP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 86.7 uM, kcat 0.5 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.008 s^-1 / 0.087 mM = 0.09195402298850576 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 86.7 uM; kcat 0.5 min^-1 (Table II, wild-type PGK).

row_label: CTP (Table II)


sequence_source: reconstructed from UniProtKB:P00558 canonical sequence by K220R


substrate_name: CDP

column_label: PMID 12080078 Table I Phosphorylation of nucleoside analog diphosphates by PGK; row CDP (Table I); column headers Km and kcat with the table's own printed units line (micromolar Km and s^-1 kcat); printed cells Km 885.0 uM, kcat 0.9 s^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.9 s^-1 / 0.885 mM = 1.0169491525423728 s^-1 mM^-1); derived from this same row's own two printed cells; Table I prints a Km column and a kcat column only and carries no kcat/Km column, so no printed ratio cell exists for this row.

raw_value_unit_evidence: Table row as printed: Km 885.0 uM; kcat 0.9 s^-1 (Table I, wild-type PGK).

row_label: CDP (Table I)

substrate: CDP


sequence_source: reconstructed from UniProtKB:P00558 canonical sequence by K220A


substrate_name: ddCTP

sequence_source: reconstructed from UniProtKB:P00558 canonical sequence by N337Q

substrate: ddCTP


sequence_source: reconstructed from UniProtKB:P00558 canonical sequence by N337D


column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row ddCTP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 692.8 uM, kcat 0.9 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.015 s^-1 / 0.693 mM = 0.021645021645021644 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 692.8 uM; kcat 0.9 min^-1 (Table II, wild-type PGK).

row_label: ddCTP (Table II)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00558 canonical sequence fetched by REST/FASTA on 2026-05-31; K220A reconstructed after direct residue check K220. and applied mutation signature K220A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00558 and applied mutation signature K220A to reconstruct the assayed variant sequence.

column_label: Table IV (Phosphorylation of nucleoside analog diphosphates by the single amino acid mutants of human PGK), K220A enzyme-form block, nucleoside analog diphosphate row 'ADP'; column 'Km' with printed unit uM = 1150.0 +/- 10.0; column 'kcat' with printed unit s^-1 = 55.3 +/- 15.3, followed by the parenthesised mutant-over-wild-type kcat term (1/110). The K220A block prints no catalytic-efficiency column.

normalized_value_unit_evidence: Km: printed Table IV cell 1150.0 uM; 1150.0 / 1000 = 1.15 mM, carried exactly. kcat: printed Table IV cell 55.3 s^-1; already in s^-1, so no unit conversion applies; the paper value is 55.3 s^(-1). kcat/Km: the paper value 48.08695652173913 s^(-1)*mM^(-1) is the quotient 55.3 / 1.15 of this same Table IV line's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table IV, K220A enzyme-form block, nucleoside analog diphosphate row 'ADP': Km = 1150.0 +/- 10.0 uM in the column headed Km with printed unit uM; kcat = 55.3 +/- 15.3 s^-1 in the column headed kcat with printed unit s^-1. The K220A block of this table prints no catalytic-efficiency column.

table_label: Table IV: Phosphorylation of nucleoside analog diphosphates by the single amino acid mutants of human PGK, K220A enzyme-form block (J. Biol. Chem. 2002, 277(35):31593-31600)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00558 canonical sequence fetched by REST/FASTA on 2026-05-31; K220R reconstructed after direct residue check K220. and applied mutation signature K220R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00558 canonical sequence fetched by REST/FASTA on 2026-05-31; K220R reconstructed after direct residue check K220.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P00558 canonical sequence fetched by REST/FASTA on 2026-05-31; N337D reconstructed after direct residue check N337. and applied mutation signature N337D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P00558 canonical sequence fetched by REST/FASTA on 2026-05-31; K220A reconstructed after direct residue check K220.


sequence_source: UniProtKB:P00558 reviewed PGK1_HUMAN canonical sequence

column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row TTP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 101.8 uM, kcat 1.0 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.017 s^-1 / 0.102 mM = 0.16666666666666669 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 101.8 uM; kcat 1.0 min^-1 (Table II, wild-type PGK).

row_label: TTP (Table II)


column_label: PMID 12080078 Table I Phosphorylation of nucleoside analog diphosphates by PGK; row ADP (Table I); column headers Km and kcat with the table's own printed units line (micromolar Km and s^-1 kcat); printed cells Km 232.5 uM, kcat 6000.0 s^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (6000.0 s^-1 / 0.233 mM = 25751.07296137339 s^-1 mM^-1); derived from this same row's own two printed cells; Table I prints a Km column and a kcat column only and carries no kcat/Km column, so no printed ratio cell exists for this row.

raw_value_unit_evidence: Table row as printed: Km 232.5 uM; kcat 6000.0 s^-1 (Table I, wild-type PGK).

row_label: ADP (Table I)


sequence_source: UniProtKB:P00558 reviewed PGK1_HUMAN; variant reconstructed from selected OED mutation signature


substrate_name: TDP

substrate: TDP


organism: Saccharomyces cerevisiae

sequence_source: UniProt P00560 canonical sequence; row-specific variant reconstructed using PMID 8462685 mutation signature and UniProt initiator-methionine removal feature

sequence_variant_note: Mutation signature R121M matches the mutant residue at offset +1 and the reference residue at offset +10; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00560 and applied mutation signature R168M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

column_label: Table I (The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis) prints one enzyme-label column, PGK, followed by five numeric columns whose heads are Km 3-PGA (mM), Km MgATP (mM), kcat (s^-1), kcat/Km (s^-1 M^-1) and Kd 3-PGA (mM) in that printed order. The cited cell set is Table I, enzyme row R168M: column 'Km 3-PGA (mM)' = 6.40; column 'Km MgATP (mM)' = 1.34; column 'kcat (s^-1)' = 85.5; column 'kcat/Km (s^-1 M^-1)' = 1.3 x 10^4; column 'Kd 3-PGA (mM)' = 0.160.

normalized_value_unit_evidence: kcat: printed Table I cell 85.5 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 85.5 s^(-1). Km: printed Table I cell 6.40 mM; the printed Michaelis-constant columns of this paper are already in millimolar, so no unit conversion applies and the paper value is 6.4 mM. kcat/Km: printed Table I cell 1.3 x 10^4 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.3 x 10^4 / 1000 = 13.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 85.5 / 6.40 = 13.359375 s^-1 mM^-1, against the printed catalytic-efficiency cell 13.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, enzyme row R168M: Km 3-PGA = 6.40 mM; kcat = 85.5 s^-1; printed kcat/Km = 1.3 x 10^4 s^-1 M^-1.

row_label: Table I, row R168M

table_label: Table I: The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis (FEBS Letters 1993, 320(3):193-197)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00560 and applied mutation signature R121K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I (The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis) prints one enzyme-label column, PGK, followed by five numeric columns whose heads are Km 3-PGA (mM), Km MgATP (mM), kcat (s^-1), kcat/Km (s^-1 M^-1) and Kd 3-PGA (mM) in that printed order. The cited cell set is Table I, enzyme row R121K: column 'Km 3-PGA (mM)' = 1.92; column 'Km MgATP (mM)' = 0.36; column 'kcat (s^-1)' = 232.1; column 'kcat/Km (s^-1 M^-1)' = 1.2 x 10^5; column 'Kd 3-PGA (mM)' prints an en dash for an undetermined value.

normalized_value_unit_evidence: kcat: printed Table I cell 232.1 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 232.1 s^(-1). Km: printed Table I cell 1.92 mM; the printed Michaelis-constant columns of this paper are already in millimolar, so no unit conversion applies and the paper value is 1.92 mM. kcat/Km: printed Table I cell 1.2 x 10^5 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.2 x 10^5 / 1000 = 120.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 232.1 / 1.92 = 120.88541666666667 s^-1 mM^-1, against the printed catalytic-efficiency cell 120.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, enzyme row R121K: Km 3-PGA = 1.92 mM; kcat = 232.1 s^-1; printed kcat/Km = 1.2 x 10^5 s^-1 M^-1.

row_label: Table I, row R121K


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00560 and applied mutation signature R65M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I (The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis) prints one enzyme-label column, PGK, followed by five numeric columns whose heads are Km 3-PGA (mM), Km MgATP (mM), kcat (s^-1), kcat/Km (s^-1 M^-1) and Kd 3-PGA (mM) in that printed order. The cited cell set is Table I, enzyme row R65M: column 'Km MgATP (mM)' = 1.62; column 'Km 3-PGA (mM)' = 15.89; column 'kcat (s^-1)' = 48.9; column 'kcat/Km (s^-1 M^-1)' = 3.1 x 10^3, which is the efficiency on the 3-PGA axis; column 'Kd 3-PGA (mM)' prints a lower-bound entry rather than a determined value.

normalized_value_unit_evidence: kcat: printed Table I cell 48.9 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 48.9 s^(-1). Km: printed Table I cell 1.62 mM; the printed Michaelis-constant columns of this paper are already in millimolar, so no unit conversion applies and the paper value is 1.62 mM. kcat/Km: Table I prints one catalytic-efficiency column and it is computed on the 3-PGA axis, so the paper prints no MgATP-axis efficiency cell; the paper value 30.185185185185183 s^(-1)*mM^(-1) is the quotient 48.9 / 1.62 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table I, enzyme row R65M: Km MgATP = 1.62 mM; kcat = 48.9 s^-1; the printed kcat/Km column of this table is the 3-PGA axis and carries no MgATP-axis cell.

row_label: Table I, row R65M, MgATP axis


column_label: Table I (The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis) prints one enzyme-label column, PGK, followed by five numeric columns whose heads are Km 3-PGA (mM), Km MgATP (mM), kcat (s^-1), kcat/Km (s^-1 M^-1) and Kd 3-PGA (mM) in that printed order. The cited cell set is Table I, enzyme row R65M: column 'Km 3-PGA (mM)' = 15.89; column 'Km MgATP (mM)' = 1.62; column 'kcat (s^-1)' = 48.9; column 'kcat/Km (s^-1 M^-1)' = 3.1 x 10^3; column 'Kd 3-PGA (mM)' prints a lower-bound entry rather than a determined value.

normalized_value_unit_evidence: kcat: printed Table I cell 48.9 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 48.9 s^(-1). Km: printed Table I cell 15.89 mM; the printed Michaelis-constant columns of this paper are already in millimolar, so no unit conversion applies and the paper value is 15.89 mM. kcat/Km: printed Table I cell 3.1 x 10^3 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.1 x 10^3 / 1000 = 3.1 s^(-1)*mM^(-1). Quotient disclosure for this row: 48.9 / 15.89 = 3.077407174323474 s^-1 mM^-1, against the printed catalytic-efficiency cell 3.1 s^-1 mM^-1.

raw_value_unit_evidence: Table I, enzyme row R65M: Km 3-PGA = 15.89 mM; kcat = 48.9 s^-1; printed kcat/Km = 3.1 x 10^3 s^-1 M^-1.

row_label: Table I, row R65M


sequence_variant_note: Mutation signature R168K matches the mutant residue at offset +1 and the reference residue at offset +14; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00560 and applied mutation signature R65K with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table I (The kinetic parameters for over-expressed wild-type PGK and PGK modified at positions 65, 121 and 168 by site-directed mutagenesis) prints one enzyme-label column, PGK, followed by five numeric columns whose heads are Km 3-PGA (mM), Km MgATP (mM), kcat (s^-1), kcat/Km (s^-1 M^-1) and Kd 3-PGA (mM) in that printed order. The cited cell set is Table I, enzyme row R65K: column 'Km 3-PGA (mM)' = 1.70; column 'Km MgATP (mM)' = 0.33; column 'kcat (s^-1)' = 503.8; column 'kcat/Km (s^-1 M^-1)' = 3.0 x 10^5; column 'Kd 3-PGA (mM)' = 0.040.

normalized_value_unit_evidence: kcat: printed Table I cell 503.8 s^-1; the printed turnover column of this paper is already per second, so no unit conversion applies and the paper value is 503.8 s^(-1). Km: printed Table I cell 1.70 mM; the printed Michaelis-constant columns of this paper are already in millimolar, so no unit conversion applies and the paper value is 1.7 mM. kcat/Km: printed Table I cell 3.0 x 10^5 s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.0 x 10^5 / 1000 = 300.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 503.8 / 1.70 = 296.3529411764706 s^-1 mM^-1, against the printed catalytic-efficiency cell 300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table I, enzyme row R65K: Km 3-PGA = 1.70 mM; kcat = 503.8 s^-1; printed kcat/Km = 3.0 x 10^5 s^-1 M^-1.

row_label: Table I, row R65K


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed accession P16617 FASTA, retrieved 2026-05-31

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

assay_conditions_summary: pH 7.3; 303.15 K; cofactor NADH

column_label: Literal Table II backward 3-phosphoglycerate row. Current Kcat 3.983 and OED source efficiency select the native Kcat 239 and native Km 2.22 cells; current 2.72 Km is the modified cell and is corrected.

normalized_value_unit_evidence: 239 min^-1 is stored at source row precision as 3.983 s^-1; native Km=2.22 mM; corrected same-native-column quotient=3.983/2.22=1.7941441441441441 s^-1 mM^-1.

raw_value_unit_evidence: Table II native 3-phosphoglycerate cells: Kcat 239 min^-1 and Km,app 2.22 mM. Modified Km 2.72 mM is a distinct preparation cell.

row_label: backward direction; 3-phosphoglycerate; native

table_label: Table II. Kinetic Constants of Native and Iodoacetate-Modified Phosphoglycerate Kinase


assay_conditions_summary: pH 6.9; 303.15 K; cofactor ADP


substrate_name: Glycerate 3-phosphate

sequence_source: UniProtKB reviewed accession P00560 FASTA, retrieved 2026-05-31

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

substrate: Glycerate 3-phosphate


substrate_name: 2-Hydroxy-4-phosphonobutyric acid

smiles: O=C(O)C(O)CCP(=O)(O)O

substrate: 2-Hydroxy-4-phosphonobutyric acid


assay_conditions_summary: pH 7.5; 277.15 K; cofactor ATP


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


organism: Chlamydomonas reinhardtii

sequence_source: UniProtKB:A8JC04 canonical sequence fetched directly


assay_conditions_summary: pH 7.9; 298.15 K; cofactor ATP


organism: Entamoeba histolytica

sequence_source: UniProtKB:C4M192 canonical sequence fetched directly

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


sequence_source: UniProtKB:P00558 canonical sequence fetched directly

column_label: PMID 12080078 Table I Phosphorylation of nucleoside analog diphosphates by PGK; row dADP (Table I); column headers Km and kcat with the table's own printed units line (micromolar Km and s^-1 kcat); printed cells Km 488.1 uM, kcat 844.5 s^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (844.5 s^-1 / 0.488 mM = 1730.532786885246 s^-1 mM^-1); derived from this same row's own two printed cells; Table I prints a Km column and a kcat column only and carries no kcat/Km column, so no printed ratio cell exists for this row.

raw_value_unit_evidence: Table row as printed: Km 488.1 uM; kcat 844.5 s^-1 (Table I, wild-type PGK).

row_label: dADP (Table I)


column_label: PMID 12080078 Table I Phosphorylation of nucleoside analog diphosphates by PGK; row TDP (Table I); column headers Km and kcat with the table's own printed units line (micromolar Km and s^-1 kcat); printed cells Km 160.5 uM, kcat 0.3 s^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.3 s^-1 / 0.161 mM = 1.8633540372670807 s^-1 mM^-1); derived from this same row's own two printed cells; Table I prints a Km column and a kcat column only and carries no kcat/Km column, so no printed ratio cell exists for this row.

raw_value_unit_evidence: Table row as printed: Km 160.5 uM; kcat 0.3 s^-1 (Table I, wild-type PGK).

row_label: TDP (Table I)


sequence_source: UniProtKB:P00558 canonical sequence fetched directly; reconstructed N337D after confirming N337


sequence_source: UniProtKB:P00558 canonical sequence fetched directly; reconstructed N337Q after confirming N337


sequence_source: UniProtKB:P00558 canonical sequence fetched directly; reconstructed K220A after confirming K220


sequence_source: UniProtKB:P00560 direct REST/FASTA fetch


sequence_source: UniProtKB reviewed P00558 fetched 2026-05-31; validated residue 220=K in UniProt P00558 before applying K220R.


sequence_source: UniProtKB reviewed P00558 fetched 2026-05-31; validated residue 337=N in UniProt P00558 before applying N337D.


sequence_source: UniProtKB reviewed P00558 fetched 2026-05-31; canonical wild-type sequence used without mutation reconstruction.

column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row ATP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 58.8 uM, kcat 0.9 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.015 s^-1 / 0.059 mM = 0.2542372881355932 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 58.8 uM; kcat 0.9 min^-1 (Table II, wild-type PGK).

row_label: ATP (Table II)


sequence_source: UniProtKB reviewed P00558 fetched 2026-05-31; validated residue 337=N in UniProt P00558 before applying N337Q.


column_label: PMID 12080078 Table II Dephosphorylation of nucleoside analog triphosphates by PGK; row dCTP (Table II); column headers Km and kcat with the table's own printed units line (micromolar Km and min^-1 kcat); printed cells Km 109.8 uM, kcat 0.4 min^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.007 s^-1 / 0.11 mM = 0.06363636363636364 s^-1 mM^-1); derived from this same row's own two printed cells; Table II's third numeric column is the reverse-versus-forward efficiency comparison named by its own column header and footnote 2-a, not a kcat/Km cell for this row, so no printed kcat/Km cell exists for this row and the third column is not used.

raw_value_unit_evidence: Table row as printed: Km 109.8 uM; kcat 0.4 min^-1 (Table II, wild-type PGK).

row_label: dCTP (Table II)


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P00558 and applied mutation signature A199V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:P00558 and applied mutation signature M189I with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Methanothermus fervidus


organism: Pseudomonas sp.


organism: Pyrococcus woesei

assay_conditions_summary: pH 7.5; 343.15 K; cofactor ATP


assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP

column_label: Literal Table II backward MgATP row, modified columns: Vmax 0.22, Km,app 0.91 mM, Kcat 548 min^-1. Footnotes define the iodoacetate preparation and Kcat.

normalized_value_unit_evidence: 548 min^-1 is stored at source row precision as 9.133 s^-1; Km=0.91 mM; same-modified-column quotient=9.133/0.91=10.036263736263734 s^-1 mM^-1.

raw_value_unit_evidence: Table II modified MgATP cells: Kcat 548 min^-1 and Km,app 0.91 mM. No kcat/Km cell is printed.

row_label: backward direction; MgATP; modified


substrate_name: 3-Phospho-D-glyceroyl phosphate

column_label: Literal Table II forward 1,3-diphosphoglycerate row. Current Kcat 25.683 and OED source efficiency select the modified Kcat 1541 and modified Km 0.036 cells; current 0.042 Km is the native cell and is corrected.

normalized_value_unit_evidence: 1541 min^-1 is stored at source row precision as 25.683 s^-1; modified Km=0.036 mM; corrected same-modified-column quotient=25.683/0.036=713.4166666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table II modified 1,3-diphosphoglycerate cells: Kcat 1541 min^-1 and Km,app 0.036 mM. Native Km 0.042 mM is a distinct preparation cell.

row_label: forward direction; 1,3-diphosphoglycerate; modified

substrate: 3-Phospho-D-glyceroyl phosphate


sequence_source: UniProt:P00558 direct FASTA/JSON check

sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature K220R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature K215A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature R38M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature G166D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8; 355.15 K; cofactor NADH

column_label: PMID 29995887 Table 1 row Wild type; columns KM (mM), kcat (s^-1), and kcat/KM (s^-1 mM^-1).

raw_value_unit_evidence: Table 1 row Wild type: KM 0.40 mM; kcat 89.8 s^-1; kcat/KM 224.5 s^-1 mM^-1.

row_label: Wild type

table_label: Table 1. Kinetic parameters of PGK1 wild type and variants


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature V216F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature R65W with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt:P00558 direct FASTA/JSON check and applied mutation signature F241S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


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.

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)


substrate_name: NADH

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


substrate_name: xylitol

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

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


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

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


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


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


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