substrate_name: 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: D-Xylose


enzyme_display_name: aldose reductase

organism: Candida tenuis

source_db: oed

verification_status: unverified

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_accession and applied mutation signature K274G to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: aldose reductase

status: unverified

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K274M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K274R to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K80A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N276D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R280H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S275A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


mutation_signature: Unknown

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


organism: Homo sapiens

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


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession 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 and applied mutation signature R293A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S210A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S214A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S226A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession 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 and applied mutation signature W219E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus


organism: Sus scrofa


substrate_name: Glucuronate

substrate: Glucuronate


organism: Bos taurus

substrate_name: Glyceraldehyde

verification_status: corrected

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

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O60218 and applied mutation signature K125L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; buffer that same reaction

column_label: Table 1: Kinetic analysis for human AKRs and mutant enzymes using the BSA/HPLC method (PNAS 2007, vol. 104, no. 52), line 'AKR1B10 K125L'; D,L-glyceraldehyde column 'Km (mM)' = 5.2; D,L-glyceraldehyde column 'kcat (min^-1)' = 35.6; D,L-glyceraldehyde column 'kcat/Km (mM^-1 min^-1)' = 7.

normalized_value_unit_evidence: Km: printed Table 1 cell 5.2 mM; the printed millimolar column needs no conversion, so the canonical value is 5.2 mM. kcat: printed Table 1 cell 35.6 min^-1; one min^-1 is 1/60 s^-1, so 35.6 / 60 = 0.5933333333333334 s^-1. kcat/Km: printed Table 1 cell 7 mM^-1 min^-1; one mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 7.0 / 60 = 0.11666666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, row AKR1B10 K125L, D,L-glyceraldehyde columns: Km = 5.2 mM; kcat = 35.6 min^-1; printed kcat/Km = 7 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O60218 and applied mutation signature K125L/V301L to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic analysis for human AKRs and mutant enzymes using the BSA/HPLC method (PNAS 2007, vol. 104, no. 52), line 'AKR1B10 K125L/V301L'; D,L-glyceraldehyde column 'Km (mM)' = 7.3; D,L-glyceraldehyde column 'kcat (min^-1)' = 35.4; D,L-glyceraldehyde column 'kcat/Km (mM^-1 min^-1)' = 4.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 7.3 mM; the printed millimolar column needs no conversion, so the canonical value is 7.3 mM. kcat: printed Table 1 cell 35.4 min^-1; one min^-1 is 1/60 s^-1, so 35.4 / 60 = 0.59 s^-1. kcat/Km: printed Table 1 cell 4.9 mM^-1 min^-1; one mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 4.9 / 60 = 0.08166666666666668 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, row AKR1B10 K125L/V301L, D,L-glyceraldehyde columns: Km = 7.3 mM; kcat = 35.4 min^-1; printed kcat/Km = 4.9 mM^-1 min^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O60218 and applied mutation signature V301L to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic analysis for human AKRs and mutant enzymes using the BSA/HPLC method (PNAS 2007, vol. 104, no. 52), line 'AKR1B10 V301L'; D,L-glyceraldehyde column 'Km (mM)' = 6.0; D,L-glyceraldehyde column 'kcat (min^-1)' = 41; D,L-glyceraldehyde column 'kcat/Km (mM^-1 min^-1)' = 7.

normalized_value_unit_evidence: Km: printed Table 1 cell 6.0 mM; the printed millimolar column needs no conversion, so the canonical value is 6.0 mM. kcat: printed Table 1 cell 41 min^-1; one min^-1 is 1/60 s^-1, so 41 / 60 = 0.6833333333333333 s^-1. kcat/Km: printed Table 1 cell 7 mM^-1 min^-1; one mM^-1 min^-1 is 1/60 s^-1 mM^-1, so 7.0 / 60 = 0.11666666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, row AKR1B10 V301L, D,L-glyceraldehyde columns: Km = 6.0 mM; kcat = 41 min^-1; printed kcat/Km = 7 mM^-1 min^-1.


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

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

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

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

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

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


substrate_name: formaldehyde

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

smiles: C=O

substrate: formaldehyde


substrate_name: ethylamine

sequence_variant_note: Mutation signature K80A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

smiles: CCN

substrate: ethylamine


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

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

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

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


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


substrate_name: Glyceraldehyde 3-phosphate

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

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

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

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

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

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

substrate: Glyceraldehyde 3-phosphate


organism: Debaryomyces nepalensis

substrate_name: Glyoxal

smiles: O=CC=O

substrate: Glyoxal


substrate_name: Glyoxylate

smiles: O=CC(=O)O

substrate: Glyoxylate


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`

substrate: Hydroxyacetone


substrate_name: isophthalaldehyde

substrate: isophthalaldehyde


substrate_name: L-Glyceraldehyde

substrate: L-Glyceraldehyde


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


substrate_name: L-Xylose

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

substrate: L-Xylose


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

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

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

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

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


substrate_name: glycolaldehyde

smiles: O=CCO

substrate: glycolaldehyde


substrate_name: Malondialdehyde

verification_status: verified

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

status: verified


substrate_name: m-Fluorobenzaldehyde

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

column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `3F`: kcat (s^-1) = 19.3 +/- 1.3; Kaldehyde (mM) = 4.7 +/- 0.5; kcat/Kaldehyde (M^-1 s^-1) = 4077.

normalized_value_unit_evidence: kcat: printed cell 19.3 s^-1 -> 19.3 s^(-1) (unit already canonical); the exported value is 19.3 s^(-1). Km: printed Kaldehyde cell 4.7 mM -> 4.7 mM (unit already canonical); the exported value is 4.7 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 4077 M^-1 s^-1 for this substrate line -> 4.077 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 4.1063829787234045 s^(-1)*mM^(-1).

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

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'

substrate: m-Fluorobenzaldehyde


substrate_name: m-Nitrobenzaldehyde

column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `3NO2`: kcat (s^-1) = 15.1 +/- 1.1; Kaldehyde (mM) = 1.2 +/- 0.1; kcat/Kaldehyde (M^-1 s^-1) = 12155.

normalized_value_unit_evidence: kcat: printed cell 15.1 s^-1 -> 15.1 s^(-1) (unit already canonical); the exported value is 15.1 s^(-1). Km: printed Kaldehyde cell 1.2 mM -> 1.2 mM (unit already canonical); the exported value is 1.2 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 12155 M^-1 s^-1 for this substrate line -> 12.155000000000001 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 12.583333333333334 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `3NO2`

substrate: m-Nitrobenzaldehyde


substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_accession 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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.


substrate_name: NADPH

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `NADPH`: Km (mM) = 0.009; kcat (s^-1) = 0.28; 10^3 x kcat/Km (M^-1 s^-1) = 31.0.

normalized_value_unit_evidence: kcat: printed cell 0.28 s^-1 is already the export unit s^(-1); the exported value is 0.77 s^(-1). Km: printed cell 0.009 mM is already the export unit mM; the exported value is 0.001 mM. kcat/Km: the printed efficiency cell 31.0 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 31.0 s^(-1)*mM^(-1); the exported value is 770.0 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 `NADPH`: Km (mM) = 0.009; Vmax (umol/min per mg of enzyme) = 0.49; kcat (s^-1) = 0.28; 10^3 x kcat/Km (M^-1 s^-1) = 31.0.

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

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K274G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K274M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K274R to reconstruct the assayed variant sequence.


substrate_name: p-Nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


smiles: N


substrate_name: Phenylacetaldehyde

substrate: Phenylacetaldehyde


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


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`


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4NO2`: kcat (s^-1) = 22.4 +/- 0.9; Kaldehyde (mM) = 0.38 +/- 0.05; kcat/Kaldehyde (M^-1 s^-1) = 58955.

normalized_value_unit_evidence: kcat: printed cell 22.4 s^-1 -> 22.4 s^(-1) (unit already canonical); the exported value is 22.4 s^(-1). Km: printed Kaldehyde cell 0.38 mM -> 0.38 mM (unit already canonical); the exported value is 0.38 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 58955 M^-1 s^-1 for this substrate line -> 58.955 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 58.94736842105263 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `4NO2`


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

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

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


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


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

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

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


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

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

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

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


substrate_name: Propargylamine

smiles: C#CCN

substrate: Propargylamine


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


substrate_name: p-Tolualdehyde

column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4CH3`: kcat (s^-1) = 15.8 +/- 1.0; Kaldehyde (mM) = 8.2 +/- 0.9; kcat/Kaldehyde (M^-1 s^-1) = 1932.

normalized_value_unit_evidence: kcat: printed cell 15.8 s^-1 -> 15.8 s^(-1) (unit already canonical); the exported value is 15.8 s^(-1). Km: printed Kaldehyde cell 8.2 mM -> 8.2 mM (unit already canonical); the exported value is 8.2 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 1932 M^-1 s^-1 for this substrate line -> 1.932 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 1.926829268292683 s^(-1)*mM^(-1).

row_label: Table 1, decoded plain-numeral transcription, substrate row `4CH3`

substrate: p-Tolualdehyde


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

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

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

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


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

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

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


substrate_name: 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


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: ethanolamine

smiles: NCCO

substrate: ethanolamine


substrate_name: succinate

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

substrate: succinate


substrate_name: methylamine

smiles: CN

substrate: methylamine


substrate_name: glycerone phosphate

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

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

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

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

substrate: glycerone phosphate


substrate_name: xylitol

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 NAD+

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; row kcat ox (s-1) = 9 × 10-4; row Km xylitol (mM) = 452; row kcat ox/Km xylitol (M-1 s-1) = 0.0021. captured primary segment: xylitol | H113A CtXR | coenzyme NAD+ | Km 452 mM | kcat 9 x 10^-4 s^-1 | kcat/Km 0.0021 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km xylitol (mM) cell 452 mM, H113A column; already in mM, so no unit conversion applies; the paper value is 452.0 mM. kcat: printed Table 2 kcat ox (s-1) cell 9 x 10^-4 s^-1, H113A column; already in s^-1, so no unit conversion applies; 9 x 10^-4 = 0.0009 s^(-1). kcat/Km: printed Table 2 kcat ox/Km xylitol (M-1 s-1) cell 0.0021 M^-1 s^-1, H113A column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.0021 / 1000 = 0.0000021 s^(-1)*mM^(-1). Quotient disclosure for this column: 0.0009 / 452 = 0.000001991150442477876 s^-1 mM^-1, against the printed efficiency cell 0.0000021 s^-1 mM^-1.

raw_value_unit_evidence: Table 2, H113A column, xylitol oxidation cells: Km xylitol (mM) = 452 mM; kcat ox (s-1) = 9 x 10^-4 s^-1 (printed 9 × 10-4); printed kcat ox/Km xylitol (M-1 s-1) = 0.0021 M^-1 s^-1.

row_label: Table 2, H113A column, rows kcat ox (s-1), Km xylitol (mM) and kcat ox/Km xylitol (M-1 s-1)

substrate: xylitol


column_label: Table 2: Apparent Kinetic Parameters for Xylose Reduction and Xylitol Oxidation Catalyzed by Wild-Type CtXR and the His-113 alanine mutant (Biochemistry 2004, 43, 4944-4954); printed column heads parameter, wild type and the mutant column; 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, wild type column; row kcat ox (s-1) = 1.1; row Km xylitol (mM) = 334; row kcat ox/Km xylitol (M-1 s-1) = 3.3. captured primary segment: xylitol | wild-type CtXR | coenzyme NAD+ | Km 334 mM | kcat 1.1 s^-1 | kcat/Km 3.3 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 Km xylitol (mM) cell 334 mM, wild type column; already in mM, so no unit conversion applies; the paper value is 334.0 mM. kcat: printed Table 2 kcat ox (s-1) cell 1.1 s^-1, wild type column; already in s^-1, so no unit conversion applies; the paper value is 1.1 s^(-1). kcat/Km: printed Table 2 kcat ox/Km xylitol (M-1 s-1) cell 3.3 M^-1 s^-1, wild type column; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.3 / 1000 = 0.0033 s^(-1)*mM^(-1). Quotient disclosure for this column: 1.1 / 334 = 0.003293413173652695 s^-1 mM^-1, which is 3.29 M^-1 s^-1 and rounds to the printed 3.3 at the printed two-figure precision.

raw_value_unit_evidence: Table 2, wild type column, xylitol oxidation cells: Km xylitol (mM) = 334 mM; kcat ox (s-1) = 1.1 s^-1; printed kcat ox/Km xylitol (M-1 s-1) = 3.3 M^-1 s^-1.

row_label: Table 2, wild type column, rows kcat ox (s-1), Km xylitol (mM) and kcat ox/Km xylitol (M-1 s-1)


substrate_name: D-Xylose

substrate: D-Xylose


substrate_name: D-Arabinose

substrate: D-Arabinose


column_label: Table III (journal page 11434), decoded transcription, substrate row `Methylglyoxal`, AR column group: Km (mM) = 0.024; kcat (min^-1) = 846. Table III prints no kcat/Km cell.

normalized_value_unit_evidence: kcat: printed cell 846 min^-1 -> 14.1 s^(-1) by the exact unit conversion 1 min^-1 = 1/60 s^(-1); the catalog holds 14.1 s^(-1), and 846 is an exact multiple of 60 so the conversion is exact with no rounding. Km: printed cell 0.024 mM -> 0.024 mM; the catalog holds 0.024 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: Table III prints no kcat/Km cell for any row. The exported kcat_over_km is the derived same-measurement quotient of this row's own printed cells: 846 min^-1 / 0.024 mM, converted to s^(-1)*mM^(-1), which is typed in kcat_over_km_provenance with kind=derived_same_measurement and equals the stored kcat_over_km 587.5 s^(-1)*mM^(-1).


source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

source: uniprot


enzyme_display_name: UDP-glucose 6-dehydrogenase

organism: Arabidopsis thaliana

substrate_name: NAD+

assay_conditions_summary: pH 8.7; 295.15 K; buffer of 40 mM TRIS-HCl; cofactor NAD+

column_label: Table 2, UGD4 isoform row: column 'Km NAD+ (µM)' = 44 (0.044 mM) and column 'kcat (s^-1)' = 1.17; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 44 µM converts exactly to 0.044 mM. kcat: 1.17 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 1.17 / 0.044 = 26.59090909090909 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD4 row, NAD+ column: Km 44 µM and kcat 1.17 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD4', column 'Km NAD+ (µM)' with the same row's 'kcat (s^-1)' cell

table_label: Table 2: Kinetic analysis of UGD2, 3, and 4 from Arabidopsis thaliana (Journal of Experimental Botany, volume 58, issue 13, 2007)

enzyme: UDP-glucose 6-dehydrogenase

substrate: NAD+


column_label: Table 2, UGD3 isoform row: column 'Km NAD+ (µM)' = 42 (0.042 mM) and column 'kcat (s^-1)' = 2.52; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 42 µM converts exactly to 0.042 mM. kcat: 2.52 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 2.52 / 0.042 = 60.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD3 row, NAD+ column: Km 42 µM and kcat 2.52 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD3', column 'Km NAD+ (µM)' with the same row's 'kcat (s^-1)' cell


column_label: Table 2, UGD2 isoform row: column 'Km NAD+ (µM)' = 43 (0.043 mM) and column 'kcat (s^-1)' = 1.92; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 43 µM converts exactly to 0.043 mM. kcat: 1.92 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 1.92 / 0.043 = 44.651162790697676 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD2 row, NAD+ column: Km 43 µM and kcat 1.92 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD2', column 'Km NAD+ (µM)' with the same row's 'kcat (s^-1)' cell


organism: Campylobacter jejuni subsp. jejuni

assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A222Q/S233G with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


organism: Sphingomonas sanxanigenens

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+


organism: Streptococcus pyogenes

assay_conditions_summary: pH 8.7; 303.15 K; cofactor NAD+


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E161Q with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


substrate_name: UDPglucose

assay_conditions_summary: pH 8.7; 295.15 K; buffer of 40 mM TRIS-HCl

column_label: Table 2, UGD4 isoform row: column 'Km UDP-Glc (µM)' = 171 (0.171 mM) and column 'kcat (s^-1)' = 1.17; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 171 µM converts exactly to 0.171 mM. kcat: 1.17 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 1.17 / 0.171 = 6.842105263157894 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD4 row, UDP-Glc column: Km 171 µM and kcat 1.17 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD4', column 'Km UDP-Glc (µM)' with the same row's 'kcat (s^-1)' cell

substrate: UDPglucose


column_label: Table 2, UGD3 isoform row: column 'Km UDP-Glc (µM)' = 335 (0.335 mM) and column 'kcat (s^-1)' = 2.52; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 335 µM converts exactly to 0.335 mM. kcat: 2.52 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 2.52 / 0.335 = 7.522388059701492 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD3 row, UDP-Glc column: Km 335 µM and kcat 2.52 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD3', column 'Km UDP-Glc (µM)' with the same row's 'kcat (s^-1)' cell


column_label: Table 2, UGD2 isoform row: column 'Km UDP-Glc (µM)' = 123 (0.123 mM) and column 'kcat (s^-1)' = 1.92; no kcat/Km column is present in Table 2.

normalized_value_unit_evidence: Km: 123 µM converts exactly to 0.123 mM. kcat: 1.92 s^-1 needs no conversion. kcat/Km: exact same-measurement quotient 1.92 / 0.123 = 15.609756097560975 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, UGD2 row, UDP-Glc column: Km 123 µM and kcat 1.92 s^-1; no kcat/Km cell is printed.

row_label: Table 2, isoform row 'UGD2', column 'Km UDP-Glc (µM)' with the same row's 'kcat (s^-1)' cell


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E141Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E145Q with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T118A to reconstruct the assayed variant sequence.


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


substrate_name: UDP-glucose

assay_conditions_summary: cofactor NAD+

column_label: Table 2 row UGD3 reports Km UDP-Glc 335+/-16 uM.

normalized_value_unit_evidence: Km normalized_value=0.335 mM

raw_value_unit_evidence: Km raw_value=335+/-16 raw_unit=uM

table_label: Table 2

substrate: UDP-glucose


enzyme_display_name: histidinol dehydrogenase

organism: Salmonella typhimurium

substrate_name: L-Histidinol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C116S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

enzyme: histidinol dehydrogenase

substrate: L-Histidinol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C153A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: Imidazolyl propanediol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H326N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: Imidazolyl propanediol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H366N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H418Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; 303.15 K; buffer of 50 mM sodium glycine

column_label: Table 3 (Kinetics with Imidazolyl Propanediol), row 'WT'; column 'KM imidazolyl propanediol (uM)' = 240 +/- 30; column 'kcat (s-1)' = 0.08; column 'NAD (mM)' = 7.3 +/- 1.4. Table 3 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.08 s-1; already in s^-1, no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.08 s^(-1). Km: printed Table 3 cell 240 uM; 240 / 1000 = 0.24 mM; the paper value is 0.24 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.33333333333333337 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.08 / 0.24 of this row's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, row WT: Km imidazolyl propanediol = 240 +/- 30 uM; kcat = 0.08 s-1; Table 3 carries no kcat/Km column.

row_label: Table 3, row 'WT'

table_label: Table 3: Kinetics with Imidazolyl Propanediol (Biochemistry 1999, 38(22):7363-7371)


organism: Mycobacterium tuberculosis

substrate_name: L-histidinol

substrate: L-histidinol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C116A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C153S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H98N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H261N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


enzyme_display_name: quinate/shikimate dehydrogenase (NAD+)

organism: Eucalyptus camaldulensis

enzyme: quinate/shikimate dehydrogenase (NAD+)


organism: Corynebacterium glutamicum

substrate_name: L-quinate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: L-quinate


substrate_name: NADH

substrate: NADH


substrate_name: shikimate

substrate: shikimate


enzyme_display_name: shikimate dehydrogenase (NADP+)

enzyme: shikimate dehydrogenase (NADP+)


organism: Camellia sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+


substrate_name: NADP+

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D423N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+

substrate: NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9SQT8 and applied mutation signature K385A to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), NADP+ block of enzyme row 'K385A'; column 'kcat (s-1)' = 0.008; column 'KM (µM)' = 17; column 'kcat/KM (×103 s-1 M-1)' = 0.453.

normalized_value_unit_evidence: Km: printed Table 3 cell 17 uM; 17 / 1000 = 0.017 mM; the exported value is 0.017 mM. kcat: printed Table 3 cell 0.008 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.008 s^(-1). kcat/Km: printed Table 3 cell 0.453 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.453 x 10^3 / 1000 = 0.453 s^-1 mM^-1; the exported kcat_over_km 0.47058823529411764 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.008 / 0.017), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, NADP+ block of enzyme row 'K385A': Km = 17 uM; kcat = 0.008 s^-1; printed kcat/Km = 0.453 x 10^3 M^-1 s^-1.

table_label: Table 3: Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain (Biochemistry 2006, 45(25):7787-7796)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K385N with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9SQT8 and applied mutation signature K385N/D423N to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), NADP+ block of enzyme row 'K385N/D423N'; column 'kcat (s-1)' = 0.036; column 'KM (µM)' = 22; column 'kcat/KM (×103 s-1 M-1)' = 1.62.

normalized_value_unit_evidence: Km: printed Table 3 cell 22 uM; 22 / 1000 = 0.022 mM; the exported value is 0.022 mM. kcat: printed Table 3 cell 0.036 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.036 s^(-1). kcat/Km: printed Table 3 cell 1.62 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.62 x 10^3 / 1000 = 1.62 s^-1 mM^-1; the exported kcat_over_km 1.6363636363636362 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.036 / 0.022), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, NADP+ block of enzyme row 'K385N/D423N': Km = 22 uM; kcat = 0.036 s^-1; printed kcat/Km = 1.62 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S338A to reconstruct the assayed variant sequence.


column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), NADP+ block of enzyme row 'wild type'; column 'kcat (s-1)' = 399; column 'KM (µM)' = 131; column 'kcat/KM (×103 s-1 M-1)' = 3046.

normalized_value_unit_evidence: Km: printed Table 3 cell 131 uM; 131 / 1000 = 0.131 mM; the exported value is 0.131 mM. kcat: printed Table 3 cell 399 s^-1; already in s^-1, no unit conversion applies; the exported value is 399.0 s^(-1). kcat/Km: the exported value 3045.801526717557 s^(-1)*mM^(-1) is the full-precision quotient of those two printed component cells, 399 / 0.131; the paper's own printed efficiency cell 3046 x 10^3 M^-1 s^-1 converts to 3046.0 s^-1 mM^-1 because 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, and the exported quotient re-expressed in the printed column's units is 3045801.526717557 M^-1 s^-1, which lies inside the rounding interval of the printed cell 3046 x 10^3.

raw_value_unit_evidence: Table 3, NADP+ block of enzyme row 'wild type': Km = 131 uM; kcat = 399 s^-1; printed kcat/Km = 3046 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y550A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y550F with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


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


organism: Escherichia coli

assay_conditions_summary: pH 9; 293.15 K; cofactor NADP+


organism: Haemophilus influenzae

assay_conditions_summary: pH 8.8; 303.15 K; cofactor NADP+


organism: Vitis vinifera


substrate_name: NADPH

substrate: NADPH


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), shikimate block of enzyme row 'K385A'; column 'kcat (s-1)' = 0.013; column 'KM (µM)' = 263; column 'kcat/KM (×103 s-1 M-1)' = 0.051.

normalized_value_unit_evidence: Km: printed Table 3 cell 263 uM; 263 / 1000 = 0.263 mM; the exported value is 0.263 mM. kcat: printed Table 3 cell 0.013 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.013 s^(-1). kcat/Km: printed Table 3 cell 0.051 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.051 x 10^3 / 1000 = 0.051 s^-1 mM^-1; the exported kcat_over_km 0.0494296577946768 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.013 / 0.263), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, shikimate block of enzyme row 'K385A': Km = 263 uM; kcat = 0.013 s^-1; printed kcat/Km = 0.051 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9SQT8 and applied mutation signature K385N to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), shikimate block of enzyme row 'K385N'; column 'kcat (s-1)' = 0.063; column 'KM (µM)' = 470; column 'kcat/KM (×103 s-1 M-1)' = 0.133.

normalized_value_unit_evidence: Km: printed Table 3 cell 470 uM; 470 / 1000 = 0.47 mM; the exported value is 0.47 mM. kcat: printed Table 3 cell 0.063 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.063 s^(-1). kcat/Km: printed Table 3 cell 0.133 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.133 x 10^3 / 1000 = 0.133 s^-1 mM^-1; the exported kcat_over_km 0.13404255319148936 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.063 / 0.47), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, shikimate block of enzyme row 'K385N': Km = 470 uM; kcat = 0.063 s^-1; printed kcat/Km = 0.133 x 10^3 M^-1 s^-1.


column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), shikimate block of enzyme row 'K385N/D423N'; column 'kcat (s-1)' = 0.043; column 'KM (µM)' = 131; column 'kcat/KM (×103 s-1 M-1)' = 0.324.

normalized_value_unit_evidence: Km: printed Table 3 cell 131 uM; 131 / 1000 = 0.131 mM; the exported value is 0.131 mM. kcat: printed Table 3 cell 0.043 s^-1; already in s^-1, no unit conversion applies; the exported value is 0.043 s^(-1). kcat/Km: printed Table 3 cell 0.324 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.324 x 10^3 / 1000 = 0.324 s^-1 mM^-1; the exported kcat_over_km 0.32824427480916024 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (0.043 / 0.131), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, shikimate block of enzyme row 'K385N/D423N': Km = 131 uM; kcat = 0.043 s^-1; printed kcat/Km = 0.324 x 10^3 M^-1 s^-1.


column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), shikimate block of enzyme row 'wild type'; column 'kcat (s-1)' = 428; column 'KM (µM)' = 685; column 'kcat/KM (×103 s-1 M-1)' = 624.

normalized_value_unit_evidence: Km: printed Table 3 cell 685 uM; 685 / 1000 = 0.685 mM; the exported value is 0.685 mM. kcat: printed Table 3 cell 428 s^-1; already in s^-1, no unit conversion applies; the exported value is 428.0 s^(-1). kcat/Km: printed Table 3 cell 624 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 624 x 10^3 / 1000 = 624.0 s^-1 mM^-1; the exported kcat_over_km 624.8175182481751 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (428.0 / 0.685), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, shikimate block of enzyme row 'wild type': Km = 685 uM; kcat = 428 s^-1; printed kcat/Km = 624 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q9SQT8 and applied mutation signature Y550F to reconstruct the assayed variant sequence.

column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), shikimate block of enzyme row 'Y550F'; column 'kcat (s-1)' = 3.9; column 'KM (µM)' = 1058; column 'kcat/KM (×103 s-1 M-1)' = 3.67.

normalized_value_unit_evidence: Km: printed Table 3 cell 1058 uM; 1058 / 1000 = 1.058 mM; the exported value is 1.058 mM. kcat: printed Table 3 cell 3.9 s^-1; already in s^-1, no unit conversion applies; the exported value is 3.9 s^(-1). kcat/Km: printed Table 3 cell 3.67 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.67 x 10^3 / 1000 = 3.67 s^-1 mM^-1; the exported kcat_over_km 3.6862003780718333 s^(-1)*mM^(-1) is the quotient of the exported kcat and Km (3.9 / 1.058), not a printed cell, so the printed primary cell replaces it.

raw_value_unit_evidence: Table 3, shikimate block of enzyme row 'Y550F': Km = 1058 uM; kcat = 3.9 s^-1; printed kcat/Km = 3.67 x 10^3 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K69A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADP+


organism: Homo sapiens

source_db: brenda

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

proof_lines: in 0.1 M potassium phosphate, pH 7.4, at 25°C

source: brenda


smiles: CCCCCCCCCCCCCCO


smiles: CCCCCCCCCCO


smiles: CCCCCCCCCO


substrate_name: geranylgeraniol

smiles: CC(=CCCC(=CCCC(=CCCC(=CCO)C)C)C)C

substrate: geranylgeraniol


substrate_name: nerol

smiles: CC(=CCCC(=CCO)C)C

substrate: nerol


substrate_name: trans,trans-farnesol

smiles: CC(=CCCC(=CCCC(=CCO)C)C)C

substrate: trans,trans-farnesol


smiles: CCCCCCO


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


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


smiles: CCCC=CC=O


substrate_name: isatin

substrate: isatin


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


smiles: CCCCCCCCCCCC=O


smiles: CCCC=O


smiles: CCCC(=O)C(=O)C


smiles: CCCCCCC=CC=O


smiles: CCCCCCCC=O


smiles: CCCCCCCCC=O


substrate_name: isocaproaldehyde

smiles: CC(C)CCC=O

substrate: isocaproaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


smiles: CCCCCCCC=CC=O


smiles: CCCCCCC=O


smiles: CCCCCC=O


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

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADP+


proof_lines: pH 7.5, 22°C, wild-type DELTA88DHQ-SDH enzyme variant


proof_lines: pH and temperature not specified in the publication, wild-type enzyme


assay_conditions_summary: 295.15 K; cofactor NADP+


organism: Euonymus japonicus


assay_conditions_summary: cofactor NADPH


substrate_name: hexanal

substrate: hexanal


substrate_name: n-Pentanal

smiles: CCCCC=O

substrate: n-Pentanal


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: glycoaldehyde

substrate: glycoaldehyde


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


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


substrate_name: D-erythrose

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

substrate: D-erythrose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: L-arabinose

substrate: L-arabinose


substrate_name: L-quinate

proof_lines: pH and temperature not specified in the publication, mutant S338G/T381G

substrate: L-quinate


proof_lines: pH and temperature not specified in the publication, mutant T381G


proof_lines: pH and temperature not specified in the publication, mutant T381S


proof_lines: pH and temperature not specified in the publication, mutant T381A


substrate_name: shikimate

substrate: shikimate


proof_lines: pH and temperature not specified in the publication, mutant S338G


enzyme_display_name: inositol 2-dehydrogenase

organism: Bacillus subtilis (strain 168)

substrate_name: NADH (in the presence of 5 mM 2-inosose at 25 degrees Celsius and pH 7)

assay_conditions_summary: pH 7; cofactor NADH

enzyme: inositol 2-dehydrogenase


substrate_name: 2-inosose (in the presence of 0.1 mM NADH at 25 degrees Celsius and pH 7)


substrate_name: alpha-D-glucose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)

assay_conditions_summary: pH 9


substrate_name: D-xylose (in the presence of 0.5 mM NAD at 25 degrees Celsius and pH 9)


enzyme_display_name: glucuronate reductase

organism: Mus musculus

substrate_name: D-glucuronate

enzyme: glucuronate reductase

substrate: D-glucuronate


enzyme_display_name: glucuronolactone reductase

enzyme: glucuronolactone reductase


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: p-nitrobenzaldehyde

assay_conditions_summary: pH 5; buffer triplicate with 50 mM potassium phosphate; cofactor NADPH

column_label: Abstract kinetic specificity prose, row/segment p-nitrobenzaldehyde, metric Km, raw value 46 microM, normalized 0.046 mM

raw_value_unit_evidence: Km raw_value=46 microM raw_unit=microM raw_segment="p-nitrobenzaldehyde (Km = 46 microM; kcat/Km = 52,100 s-1 M-1)"

row_label: p-nitrobenzaldehyde

table_label: Abstract kinetic specificity prose

substrate: p-nitrobenzaldehyde


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: NADPH

substrate: NADPH


substrate_name: prostaglandin H2

column_label: The abstract reports AKR1B7 displayed PGH2 affinity with Km = 3.8 microM.

raw_value_unit_evidence: Km raw_value=3.8 microM raw_unit=microM

row_label: Prose segment: mouse AKR1B7 PGH2 Km

table_label: PubMed PMID 19010934 abstract

substrate: prostaglandin H2


organism: Rattus norvegicus

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: The primary-paper prose contrasts NADH with NADPH and reports low Km 1.5 uM for NADPH.

raw_value_unit_evidence: Km raw_value=1.5 raw_unit=uM

row_label: NADPH coenzyme specificity prose

table_label: PMID 21048316 J-STAGE Specificity for Coenzymes and Substrates prose


substrate_name: NADH

column_label: The primary-paper prose states Km and kcat/Km values for NADH determined in the presence of 0.8 mM 4-nitrobenzaldehyde were 220 uM and 0.25 min^-1.

raw_value_unit_evidence: Km raw_value=220 raw_unit=uM

row_label: NADH coenzyme specificity prose

substrate: NADH


substrate_name: geraniol

smiles: CC(=CCCC(=CCO)C)C

substrate: geraniol


column_label: Table 1 row 4-Nitrobenzaldehyde, Km column (uM), value 1.5.

table_label: PMID 21048316 J-STAGE Table 1: Kinetic Constants for Carbonyl Compounds


organism: Arabidopsis thaliana

substrate_name: NAD(+)

assay_conditions_summary: cofactor NAD+

column_label: Table 2 row UGD4 reports Km NAD+ 44+/-7 uM.

normalized_value_unit_evidence: Km normalized_value=0.044 mM

raw_value_unit_evidence: Km raw_value=44+/-7 raw_unit=uM

substrate: NAD(+)


substrate_name: UDP-glucose

column_label: Table 2 row UGD4 reports Km UDP-Glc 171+/-9 uM.

normalized_value_unit_evidence: Km normalized_value=0.171 mM

raw_value_unit_evidence: Km raw_value=171+/-9 raw_unit=uM

substrate: UDP-glucose


column_label: Table 2 row UGD2 reports Km NAD+ 43+/-6 uM.

normalized_value_unit_evidence: Km normalized_value=0.043 mM

raw_value_unit_evidence: Km raw_value=43+/-6 raw_unit=uM


column_label: Table 2 row UGD2 reports Km UDP-Glc 123+/-9 uM.

normalized_value_unit_evidence: Km normalized_value=0.123 mM

raw_value_unit_evidence: Km raw_value=123+/-9 raw_unit=uM


column_label: Table 2 row UGD3 reports Km NAD+ 42+/-7 uM.

normalized_value_unit_evidence: Km normalized_value=0.042 mM

raw_value_unit_evidence: Km raw_value=42+/-7 raw_unit=uM


substrate_name: NAD

substrate: NAD


organism: [Bacillus] caldolyticus

substrate_name: L-histidinol

column_label: Abstract states all enzymes had similar affinities for histidinol and NAD+ (Km = 48 micron and 0.2 mM respectively).

raw_value_unit_evidence: Km raw_value=48 micron raw_unit=microM

row_label: Histidinol dehydrogenases from bacilli / histidinol

table_label: PubMed XML abstract PMID 921748

substrate: L-histidinol


organism: Paenarthrobacter histidinolovorans

substrate_name: NAD+

substrate: NAD+


raw_value_unit_evidence: Km raw_value=0.2 mM raw_unit=mM

row_label: Histidinol dehydrogenases from bacilli / NAD+


organism: Neurospora crassa

substrate_name: quinate

substrate: quinate


substrate_name: shikimate


organism: Cucumis sativus

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Capsicum annuum


organism: Bacillus subtilis

substrate_name: myo-inositol

source_db: skid

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: multiple

source_databases_merged: skid uniprot

substrate: myo-inositol

source: skid


source_license: CC BY-NC-ND 4.0


substrate_name: melibiose

substrate: melibiose


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

proof_lines: kcat is 2.7 sec(-1) with myo-inositol as substrate. kcat is 1 sec(-1) with 1D-chiro-inositol as substrate.


substrate_name: S-nitroso-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

substrate: S-nitroso-CoA


substrate_name: D-glucuronate

substrate: D-glucuronate


substrate_name: D,L-glyceraldehyde

substrate: D,L-glyceraldehyde


substrate_name: S-nitroso-glutathione

substrate: S-nitroso-glutathione


organism: Bos taurus

proof_lines: kcat is 627 min(-1) for S-nitroso-CoA as substrate (PubMed:25512491). kcat is 471 min(-1) for S-nitroso-glutathione as substrate (PubMed:31649033).


substrate_name: D-glucuronic acid

proof_lines: Rat aldo-keto reductase substrate profile study with glyceraldehyde, methylglyoxal, 3-deoxyglucosone, D-glucuronic acid, and D-glucurono-gamma-lactone activities

substrate: D-glucuronic acid


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


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


substrate_name: D-glucurono-gamma-lactone

substrate: D-glucurono-gamma-lactone


substrate_name: acrolein

smiles: C=CC=O

proof_lines: kcat is 3.0 sec(-1) for D,L glyceraldehyde as substrate (PubMed:22820017). kcat is 3.0 sec(-1) for methylglyoxal as substrate (PubMed:22820017). kcat is 3.4 sec(-1) for 3-deoxyglucosone as substrate (PubMed:22820017). kcat is 3.1 sec(-1) fo

substrate: acrolein


substrate_name: mevaldate

substrate: mevaldate


organism: Sus scrofa

proof_lines: kcat is 11000 min(-1) for pyridine-3-carbaldehyde as substrate. kcat is 2500 min(-1) for D,L-glyceraldehyde as substrate.


organism: Debaryomyces nepalensis


substrate_name: D-ribose

substrate: D-ribose


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-arabinose

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

substrate: D-arabinose


organism: Homo sapiens

smiles: CCCCCCCCCCCCCCO


smiles: CCCC=O


smiles: CCCC=CC=O


smiles: CCCCCCCCCCO


smiles: CCCCCCCC=O


substrate_name: nerol

substrate: nerol


smiles: CCCCCCCCC=O


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCCCCCO


smiles: CCCCCCCCCCCC=O


smiles: CCCCCCCC=CC=O


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


substrate_name: isocaproaldehyde

smiles: CC(C)CCC=O

substrate: isocaproaldehyde


smiles: CCCCCCO


smiles: CCCCCC=O


substrate_name: isatin

substrate: isatin


smiles: CCCC(=O)C(=O)C


smiles: CCCCCCC=CC=O


substrate_name: D-glucose

proof_lines: Human aldose reductase substrate profile study covering retinal isomers, acrolein, and pyridine-3-carbaldehyde

substrate: D-glucose


substrate_name: isophthalaldehyde

substrate: isophthalaldehyde


substrate_name: NADPH

assay_conditions_summary: pH 7; 318.15 K; cofactor NADPH

substrate: NADPH


substrate_name: geranylgeraniol

smiles: CC(=CCCC(=CCCC(=CCCC(=CCO)C)C)C)C

substrate: geranylgeraniol


substrate_name: trans,trans-farnesol

smiles: CC(=CCCC(=CCCC(=CCO)C)C)C

substrate: trans,trans-farnesol


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


substrate_name: D,L-glyceraldehyde

substrate: D,L-glyceraldehyde


substrate_name: all-trans-retinal

substrate: all-trans-retinal


proof_lines: Substrate specificity and catalytic efficiency of aldo-keto reductases with phospholipid aldehydes


substrate_name: acrolein

smiles: C=CC=O

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

substrate: acrolein


smiles: CC(=CC=O)C


smiles: CCCC=CC=O


smiles: CC=CC=CC=O


smiles: CCCCCC(C=CC=O)O


substrate_name: prostaglandin H2

substrate: prostaglandin H2


proof_lines: Mouse aldose reductase substrate profile study covering glyceraldehyde, xylose, glucose, galactose, and glucuronate


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucuronate

substrate: D-glucuronate


organism: Caenorhabditis elegans

substrate_name: UDP-alpha-D-glucose

proof_lines:
pH 7.5, 25°C
Hill coefficient 1, pH 7.5, 25°C
pH 8.7, 22°C

source_databases_merged: brenda skid

substrate: UDP-alpha-D-glucose


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: K0.5 value, Hill coefficient 0.8, pH 7.5, 25°C

substrate: NAD+


organism: Sphingomonas elodea

assay_conditions_summary: pH 8.7; cofactor NAD+


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Pyrobaculum islandicum

assay_conditions_summary: pH 10.5; 323.15 K; cofactor NAD+


organism: Phoma herbarum


assay_conditions_summary: pH 8.4; cofactor NAD+


organism: Burkholderia cepacia


assay_conditions_summary: pH 8.7; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.7
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=22°C, pH=7.4


organism: Campylobacter jejuni subsp. jejuni

proof_lines: kcat is 1.2 sec(-1) with UDP-glucose as substrate. kcat is 0.80 sec(-1) with NAD(+) as substrate.


substrate_name: NAD(+)

proof_lines: kcat is 0.55 sec(-1) with UDP-glucose as substrate.

substrate: NAD(+)


organism: Brucella suis

substrate_name: L-histidinol

substrate: L-histidinol


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: L-histidinol (at 25 degrees Celsius)

substrate: L-histidinol (at 25 degrees Celsius)


substrate_name: NAD (at 25 degrees Celsius)

substrate: NAD (at 25 degrees Celsius)


organism: Corynebacterium glutamicum

substrate_name: L-quinate

proof_lines: The catalytic efficiency with quinate is 3.3-fold higher than that with shikimate. With NADP(+) instead of NAD(+) as cosubstrate, activity decreases by more than 300-fold with either shikimate or quinate as a substrate.

substrate: L-quinate


proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=9.0-9.5
Raw SKiD Env: Temp=30°C, pH=10.0-10.5


substrate_name: shikimate

substrate: shikimate


organism: Aspergillus nidulans

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
with NADP+, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


organism: Eucalyptus camaldulensis

proof_lines: pH 10.5, 30°C, EcDQD/SDH2, gallate formation

proof_lines: pH 8.5, 30°C, EcDQD/SDH1, shikimate formation


organism: Toxoplasma gondii

substrate_name: NADP+

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

proof_lines: pH 8.8, temperature not specified in the publication

substrate: NADP+


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADP+


substrate_name: NADPH

proof_lines: pH 8.5, temperature not specified in the publication

proof_lines: pH 6.5, 30°C, EcDQD/SDH1, shikimate formation

substrate: NADPH


proof_lines: pH 9.0, 30°C, EcDQD/SDH1, shikimate oxidation

proof_lines: pH 9.0, temperature not specified in the publication

proof_lines: pH 9.0, 30°C, EcDQD/SDH3, shikimate oxidation


proof_lines: pH 9.0, 30°C, EcDQD/SDH2, shikimate oxidation


proof_lines:
with shikimate, pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7


organism: Cucumis sativus

substrate_name: shikimic acid

substrate: shikimic acid


organism: Capsicum annuum


organism: Aquifex aeolicus

proof_lines: kcat is 55.5 sec(-1) for dehydrogenase activity (at pH 9 and 25 degrees Celsius).


assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


organism: Escherichia coli

proof_lines: kcat is 14.2 min(-1) for dehydrogenase activity with NADP or shikimate.


organism: Staphylococcus epidermidis RP62A

assay_conditions_summary: pH 8

proof_lines: kcat is 22.8 sec(-1) for dehydrogenase activity with shikimate (at pH 8 and at 25 degrees Celsius). kcat is 87 sec(-1) for dehydrogenase activity with NAD (at pH 8 and at 25 degrees Celsius).


organism: Arabidopsis thaliana

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=22°C, pH=8.8


assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+

column_label: Table 3 (Steady-State Kinetic Profiles of the Wild Type and Active Site Mutants of the SDH Domain), NADP+ block of enzyme row 'wild type'; column 'kcat (s-1)' = 399; column 'KM (µM)' = 131; column 'kcat/KM (×103 s-1 M-1)' = 3046.

raw_value_unit_evidence: Table 3, NADP+ block of enzyme row 'wild type': Km = 131 uM; kcat = 399 s^-1; printed kcat/Km = 3046 x 10^3 M^-1 s^-1.


organism: Pseudomonas putida

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.8
Raw SKiD Env: Temp=25°C, pH=8.8


proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.8
Raw SKiD Env: Temp=-----, pH=8.8


assay_conditions_summary: pH 8.8; cofactor NAD+


assay_conditions_summary: pH 8.8; cofactor NADP+


organism: Escherichia coli (strain K12)

substrate_name: NADP

substrate: NADP


organism: Helicobacter pylori

substrate_name: shikimate (at pH 8 and 25 degrees Celsius)

proof_lines: kcat is 5.2 sec(-1) for dehydrogenase activity with NAD (at pH 8 and 25 degrees Celsius). kcat is 7.1 sec(-1) for dehydrogenase activity with NADP (at pH 8 and 25 degrees Celsius). kcat is 7.7 sec(-1) for dehydrogenase activity with shikima


substrate_name: NADP (at pH 8 and 25 degrees Celsius)

substrate: NADP (at pH 8 and 25 degrees Celsius)


substrate_name: NAD (at pH 8 and 25 degrees Celsius)

substrate: NAD (at pH 8 and 25 degrees Celsius)


organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)


substrate_name: NADP(+)

substrate: NADP(+)


organism: Bacillus subtilis

substrate_name: myo-inositol

substrate: myo-inositol


proof_lines: pH 9.0, 25°C, recombinant wild-type enzyme


substrate_name: NAD+

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 9


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from uniprotkb:P15770 and applied mutation signature N149D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P15770 and applied mutation signature N149D/V152F to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant N149D/V152F


sequence_variant_note: Resolved canonical sequence from uniprotkb:P15770 and applied mutation signature S131A/N149D/V152F to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant S131A/N149D/V152F


sequence_variant_note: Resolved canonical sequence from uniprotkb:P15770 and applied mutation signature S131A/L135A/N149D/V152F to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 25°C, recombinant mutant S131A/L135A/N149D/V152F


organism: Mus musculus

assay_conditions_summary: cofactor NADPH


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: DL-glyceraldehyde

substrate: DL-glyceraldehyde


substrate_name: D-glucuronate

substrate: D-glucuronate


substrate_name: D-arabinose

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

substrate: D-arabinose


substrate_name: D-ribose

substrate: D-ribose


substrate_name: D-galactose

substrate: D-galactose


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


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature W220E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7

proof_lines: The structure of Apo R268A human aldose reductase: Hinges and latches that control the kinetic mechanism


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature R294A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature W220A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature R269A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature S227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature S211A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature S215A to reconstruct the assayed variant sequence.


sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature G214S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature C299A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_residue_signature_disambiguation and applied mutation signature G214P to reconstruct the assayed variant sequence.


substrate_name: Unknown

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T113A/C303D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T113A/C303N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S302R/C303D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F115Y with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T113Y/S302R/C303D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C80N/T113Y/S302R/C303D with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

smiles: CCCCCCCCC=O


proof_lines:
in 0.1 M potassium phosphate, pH 7.4
pH 6.0, 25°C, healthy heart
pH 6.0, 25°C, ischemic heart


smiles: CCCCC(=O)C(=O)C


smiles: CCCC=O


organism: Debaryomyces nepalensis

substrate_name: isophthalaldehyde

substrate: isophthalaldehyde


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


substrate_name: NADPH

assay_conditions_summary: pH 7; 318.15 K; cofactor NADPH


organism: Galdieria sulphuraria

substrate_name: D-fructose

substrate: D-fructose


smiles: C(C(C(C(C=O)O)O)O)OP(=O)(O)O


substrate_name: D-xylose

substrate: D-xylose


substrate_name: L-rhamnose

substrate: L-rhamnose


substrate_name: D-fucose

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

substrate: D-fucose


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: L-ribose

substrate: L-ribose


organism: Streptococcus pyogenes

substrate_name: aldehyde intermediate

substrate: aldehyde intermediate


substrate_name: UDP-glucose

substrate: UDP-glucose


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: DL-glyceraldehyde

substrate: DL-glyceraldehyde


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: D-Lyxose

substrate: D-Lyxose


organism: Sus scrofa

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: D-glyceraldehyde

substrate: D-glyceraldehyde


substrate_name: L-gulonate

substrate: L-gulonate


substrate_name: D-glucuronate

substrate: D-glucuronate


organism: Yamadazyma tenuis

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


substrate_name: D-galactose

substrate: D-galactose


substrate_name: acrolein

substrate: acrolein


substrate_name: propanal

smiles: CCC=O

substrate: propanal


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


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Vigna radiata var. radiata

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NADPH


substrate_name: quinate

substrate: quinate


substrate_name: UDP-alpha-D-glucose

proof_lines: wild-type, K0.5 value, Hill coefficient 1, pH 7.5, 25°C

substrate: UDP-alpha-D-glucose


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: wild-type, pH 7.5, 25°C, Hill coefficient 0.74


proof_lines: mutant A136M, Hill coefficient, pH 7.5, 25°C


organism: Zea mays

proof_lines: in 50 mM sodium phosphate at pH 7.0 and 30°C


substrate_name: D-ribose

substrate: D-ribose


substrate_name: D-xylitol

smiles: C(C(C(C(CO)O)O)O)O

substrate: D-xylitol


substrate_name: D-sorbitol

smiles: C(C(C(C(C(CO)O)O)O)O)O

substrate: D-sorbitol


substrate_name: D-arabinose

substrate: D-arabinose


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: L-Xylose

substrate: L-Xylose


substrate_name: NAD+

substrate: NAD+


substrate_name: myo-inositol

substrate: myo-inositol


substrate_name: alpha-D-glucose

substrate: alpha-D-glucose


substrate_name: D-xylose

substrate: D-xylose


organism: Staphylococcus epidermidis RP62A

substrate_name: shikimate

sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5HNV1 and applied mutation signature Y211F to reconstruct the assayed variant sequence.

substrate: shikimate


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


substrate_name: NADP+

substrate: NADP+


organism: Penicillium camemberti

substrate_name: D-glucuronate

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: pH 7.5, 37°C, cosubstrate: NADH, spectrometric assay

proof_lines: pH 7.5, 37°C, cosubstrate: NADH, HPLC assay

proof_lines: pH 7.5, 37°C, cosubstrate: NADPH, spectrometric assay

substrate: D-glucuronate


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

proof_lines: pH 7.5, 37°C, cosubstrate: D-glucuronate


substrate_name: NADPH

substrate: NADPH


substrate_name: D-glucose

proof_lines: recombinant from baculovirus system in Spodoptera frugiperda cells

substrate: D-glucose


substrate_name: DL-glyceraldehyde

proof_lines: recombinant from baculovirus system with Spodoptera frugiperda cells

substrate: DL-glyceraldehyde


assay_conditions_summary: pH 6; 303.15 K; cofactor NADPH


substrate: NADH


organism: Bos taurus

substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


substrate_name: D-erythrose

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

substrate: D-erythrose


substrate_name: D-glucuronolactone

substrate: D-glucuronolactone


organism: Cyberlindnera jadinii

substrate_name: NAD(P)H

substrate: NAD(P)H


substrate_name: NAD(P)+

substrate: NAD(P)+


substrate_name: xylitol

substrate: xylitol


substrate_name: Succinic semialdehyde

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

substrate: Succinic semialdehyde


substrate_name: xylose

substrate: xylose


substrate_name: D-glucose 6-phosphate

smiles: C(C(C(C(C(C=O)O)O)O)O)OP(=O)(O)O

substrate: D-glucose 6-phosphate


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprotkb:O60701 and applied mutation signature A104L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


substrate_name: UDP-alpha-D-glucose

substrate: UDP-alpha-D-glucose


substrate_name: UDP

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A222Q/S233G to reconstruct the assayed variant sequence.

substrate: UDP


proof_lines:
wild-type, pH 8.7, 22°C
wild type enzyme, at pH 8.7 and 25°C


assay_conditions_summary: pH 8.7; 295.15 K; cofactor NAD+


proof_lines: mutant enzyme A222Q/S233G, at pH 8.7 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T325D to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant His-tagged mutant T325D


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T325A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 37°C, recombinant His-tagged mutant T325A


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NAD+


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: L-histidinal

substrate: L-histidinal


organism: Eucalyptus camaldulensis

substrate_name: L-quinate

proof_lines: pH 9.0, 30°C, EcDQD/SDH4a, quinate oxidation

substrate: L-quinate


assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


proof_lines: pH 7.5, 30°C, EcDQD/SDH4a, quinate formation


substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH


organism: Pinus taeda

substrate_name: NADPH

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


substrate_name: dehydroquinate

substrate: dehydroquinate


substrate_name: quinate

substrate: quinate


organism: Pseudomonas putida KT2440

proof_lines:
in the presence of quinate
in the presence of shikimate


substrate_name: shikimate

proof_lines:
in the presence of 2 mM NAD+
in the presence of 2 mM NADP+

substrate: shikimate


organism: Pseudomonas putida

assay_conditions_summary: pH 8.8; 298.15 K; cofactor NADP+

proof_lines:
pH 8.8, presence of 2 mM NAD+
pH 8.8, presence of 2 mM NADP+
pH 8.8, 25°C, with NADP+


proof_lines:
pH 8.8, presence of 2 mM shikimate
pH 8.8, 25°C, with shikimate


assay_conditions_summary: pH 8.8; cofactor NAD+

proof_lines:
pH 8.8, presence of 2 mM shikimate
pH 8.8, presence of 2 mM quinate


organism: Mycobacterium tuberculosis


assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH


organism: Rattus norvegicus

assay_conditions_summary: cofactor NADPH


substrate_name: D-galacturonic acid

substrate: D-galacturonic acid


substrate_name: D-glucuronolactone

substrate: D-glucuronolactone


organism: Bacillus subtilis


substrate_name: melibiose

substrate: melibiose


organism: Arabidopsis thaliana

substrate_name: UDP-glucose

proof_lines:
isoform Ugd4, pH 8.7, 22°C
isoform Ugd2, pH 8.7, 22°C
isoform Ugd3, pH 8.7, 22°C

substrate: UDP-glucose


proof_lines:
isoform Ugd3, pH 8.7, 22°C
isoform Ugd2, pH 8.7, 22°C
isoform Ugd4, pH 8.7, 22°C


substrate_name: Unknown

proof_lines:
isoform Ugd2, pH 8.7, 22°C
isoform Ugd3, pH 8.7, 22°C
isoform Ugd4, pH 8.7, 22°C

substrate: Unknown


substrate_name: D-xylose

proof_lines: pH 6.2, 25°C, enzyme from ischemic heart

substrate: D-xylose


substrate_name: D-glucuronate

substrate: D-glucuronate


substrate_name: D-galactose

substrate: D-galactose


organism: Escherichia coli

substrate_name: NAD+

assay_conditions_summary: pH 9.5; 310.15 K; cofactor NAD+

substrate: NAD+


proof_lines: pH 9.5, 37°C, recombinant wild-type enzyme, from different strains

proof_lines: pH 9.5, 37°C, recombinant wild-type enzyme, with 0.025-1.0 mM ATP


organism: Saccharum spp.


assay_conditions_summary: pH 8.4; 298.15 K; cofactor NAD+


organism: Glycine max


assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NAD+

proof_lines:
pH 7.2, 25°C, with Ficoll at 200 g/l
pH 7.2, 25°C, with Ficoll at 100 g/l
pH 7.2, 25°C


substrate_name: L-histidinol

proof_lines: pH 7.2, 25°C, with Ficoll at 100-200 g/l

substrate: L-histidinol


organism: Corynebacterium glutamicum


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: 30°C, pH 10.0-10.5, cosubstrate: shikimate


substrate_name: L-quinate


organism: Aspergillus niger

assay_conditions_summary: cofactor NAD+

proof_lines:
+ quinate
+ shikimate


assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 303.15 K; cofactor NADPH

proof_lines:
pH 9.0, 30°C
with NADPH, pH 8.6, 30°C
pH 7.0, 30°C


organism: Helicobacter pylori

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

proof_lines:
pH 8.0, 60°C, recombinant enzyme
with shikimate, pH 8.0, 25°C


proof_lines:
pH 8.0, 60°C, recombinant enzyme
with NADP+, pH 8.0, 25°C


organism: Galdieria sulphuraria

substrate_name: scyllo-inosose

substrate: scyllo-inosose


substrate_name: myo-inositol

substrate: myo-inositol


substrate_name: NADP+

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

proof_lines:
pH 7.0, 25°C, recombinant AroE
pH 7.0, 25°C, with shikimate
pH 9.0, 25°C


proof_lines:
pH 7.0, 25°C, recombinant AroE
pH 7.0, 25°C, with NADP+
pH 9.0, 25°C


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines:
pH 7.0, 25°C, recombinant AroE
pH 7.0, 25°C, with 3-dehydroshikimate
25°C, pH 7.3

substrate: NADPH


organism: Canis lupus familiaris


substrate_name: L-gulonate

substrate: L-gulonate


organism: Homo sapiens


substrate_name: Isobutyraldehyde

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM MOPS

substrate: Isobutyraldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


proof_lines: recombinant from baculovirus system in Spodoptera frugiperda cells


proof_lines: recombinant fron baculovirus system in Spodoptera frugiperda cells


organism: Xerophyta viscosa

substrate_name: DL-glyceraldehyde

proof_lines: pH 6.2, temperature not specified in the publication, recombinant His-tagged enzyme

substrate: DL-glyceraldehyde


substrate_name: methylglyoxal

substrate: methylglyoxal


organism: Bos taurus


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Meyerozyma guilliermondii


assay_conditions_summary: pH 6.2; 295.15 K; cofactor NADPH


substrate_name: UDP-alpha-D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E161Q to reconstruct the assayed variant sequence.

substrate: UDP-alpha-D-glucose


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Streptococcus pyogenes

substrate_name: UDPglucose

substrate: UDPglucose


organism: Burkholderia cenocepacia J2315

substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Pseudomonas aeruginosa


assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+


organism: Campylobacter jejuni subsp. jejuni


organism: Burkholderia cepacia

assay_conditions_summary: pH 8.7; 303.15 K; cofactor NAD+

proof_lines: wild-type, pH 8.7, 30°C, Hill-coefficient 1.5


proof_lines: wild-type, pH 8.7, 30°C, Hill-coefficient 0.89


organism: Sphingomonas sanxanigenens

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+


organism: Phaseolus vulgaris


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K339A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.4; 295.15 K; cofactor NAD+


organism: Capra hircus


assay_conditions_summary: pH 8.8; 298.15 K; cofactor NAD+


organism: Escherichia coli


proof_lines: recombinant glutathione-S-transferase fusion protein


organism: Lilium longiflorum


organism: Sporosarcina psychrophila


organism: Xenopus laevis


organism: Geobacillus stearothermophilus


organism: Bacillus subtilis


organism: Staphylococcus aureus

substrate_name: shikimate

assay_conditions_summary: 298.15 K; cofactor NADP+

proof_lines: pH not specified in the publication, 25°C, with NADP+

substrate: shikimate


proof_lines: pH not specified in the publication, 25°C, with shikimate

substrate: NADP+


organism: Staphylococcus epidermidis


assay_conditions_summary: pH 9; 293.15 K; cofactor NADP+


organism: Arabidopsis thaliana

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+


organism: Solanum lycopersicum

assay_conditions_summary: cofactor NADP+


organism: Lathyrus oleraceus


organism: Vigna mungo


organism: Nicotiana tabacum

assay_conditions_summary: pH 9; 295.15 K; cofactor NADP+


organism: Rattus norvegicus

substrate_name: gamma-hydroxybutyrate

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

proof_lines: coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction, brain and kidney

proof_lines: enzyme from brain, D-glucuronate reduction-coupled assay

substrate: gamma-hydroxybutyrate


organism: Archaeoglobus fulgidus

assay_conditions_summary: pH 7.3; 360.15 K; cofactor NADP+

proof_lines:
87°C, pH 7.3
with NADP+, pH 7.3, 87°C


substrate_name: NAD+

assay_conditions_summary: pH 7.3; 360.15 K; cofactor NAD+

substrate: NAD+


organism: Mesocricetus auratus

proof_lines: coupled reaction of gamma-hydroxybutyrate oxidation and D-glucuronate reduction


organism: Bos taurus

substrate_name: D-glucuronate

proof_lines: no exact differentiation between organisms in the reference

substrate: D-glucuronate


organism: Homo sapiens


substrate_name: D-glucose

substrate: D-glucose


substrate_name: propionaldehyde

substrate: propionaldehyde


organism: Leishmania donovani

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

proof_lines: recombinant enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C, in the presence of 0.3 mM trypanothione

proof_lines: recombinant enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 25°C, in the presence of 0.3 mM glutathione


assay_conditions_summary: pH 6.2; 303.15 K; cofactor NADPH

substrate: NADPH


sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


proof_lines:
pH 9.4
pH 8.6
native enzyme


assay_conditions_summary: pH 8.7; 298.15 K; cofactor NAD+


organism: Zea mays

proof_lines:
20°C, pH 8, UDPGDH-A
20°C, pH 8, UDPGDH-B


organism: Brassica oleracea

substrate_name: L-histidinol

proof_lines: recombinant enzyme without transit peptide

substrate: L-histidinol


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Brucella suis

proof_lines: pH and temperature not specified in the publication


organism: Escherichia coli

assay_conditions_summary: cofactor NAD+


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH

proof_lines:
25°C, pH 7.3
pH 7.0, 25°C, recombinant AroE
pH 7.0, 25°C, with NADPH


organism: Actinidia deliciosa

substrate_name: quinic acid

proof_lines: purification step Q1 HiTrapQ, cofactor NAD+

proof_lines: purification step Q2 HiTrapQ, cofactor NADP+

proof_lines: purification step Q1 HiTrapQ, cofactor NADP+

substrate: quinic acid


organism: Aquifex aeolicus

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

proof_lines:
25°C, pH 9.0
with NADP+, pH 9.0, 25°C


substrate_name: NADP+

proof_lines:
with shikimate, pH 9.0, 25°C
25°C, pH 9.0


proof_lines:
with shikimate, pH 7.3, 87°C
87°C, pH 7.3


organism: Corynebacterium glutamicum

substrate_name: quinate

substrate: quinate


organism: Chlamydomonas reinhardtii


organism: Rhodopirellula baltica


organism: Physcomitrium patens


organism: Pinus taeda


organism: Selaginella moellendorffii


organism: Populus trichocarpa

substrate_name: L-quinate

proof_lines: mutant S275G/T318G, pH and temperature not specified in the publication

substrate: L-quinate


organism: Staphylococcus aureus

substrate_name: Unknown

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines:
pH 8.0, 25°C, versus NADP+
pH 8.0, 25°C, versus shikimate

substrate: Unknown


assay_conditions_summary: pH 7.5; 298.15 K; buffer unstructured_notes 'potassium phosphate; cofactor NADPH

proof_lines: 25?potassium phosphate buffer, pH 7.5, 25°C, cofactor NADPH


organism: Unknown

substrate_name: SPC_28905_Cell; SPC_37_Cell

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

substrate: SPC_28905_Cell; SPC_37_Cell


organism: Sungouiella intermedia

substrate_name: D-xylose

assay_conditions_summary: cofactor NADPH

proof_lines:
isozyme ALR 2, NADPH
isozyme ALR 1, NADPH

substrate: D-xylose


substrate_name: SPC_37_Cell; SPC_3918_Cell; SPC_40_Cell

substrate: SPC_37_Cell; SPC_3918_Cell; SPC_40_Cell


substrate_name: SPC_40_Cell; SPC_5283_Cell; SPC_37_Cell

substrate: SPC_40_Cell; SPC_5283_Cell; SPC_37_Cell


substrate_name: SPC_1263_Cell; SPC_5117_Cell

substrate: SPC_1263_Cell; SPC_5117_Cell


organism: Camellia sinensis

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADP+

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with shikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with shikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with shikimate

substrate: NADP+


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHd, with NADPH

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with NADPH

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with NADPH


substrate_name: NADPH

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHD, with 3-dehydroshikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHc, with 3-dehydroshikimate

proof_lines: pH 7.5, 30°C, recombinant isozyme CsDQD/SDHa, with 3-dehydroshikimate