organism: Thermus thermophilus HB27

sequence_source: literature_accession_YP_003977_1; UniProt Q72LQ6 canonical sequence byte-identical (length 256). NCBI RefSeq YP_003977.1 (WP_011172461.1) cross-references UniProt Q72LQ6 (Thermus thermophilus HB27, 256 aa); cited in PMID 684583.

assay_conditions_summary: pH 10.5; 338.15 K; cofactor NAD+

column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `NAD+`: column 'kcat (s^-1)' = 0.84; column 'Km (mM)' = 0.24; column 'kcat/Km (s^-1 mM^-1)' = 3.50.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 0.84 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 0.84 s^(-1); the exported value is 0.84 s^(-1). Km: printed TABLE 4 cell 0.24 mM; the table already reports Km in mM, so no conversion is applied and the value is 0.24 mM; the exported value is 0.24 mM. kcat/Km: the paper PRINTS the kcat/Km cell 3.50 s^-1 mM^-1 for this substrate row; the table already reports kcat/Km in s^-1 mM^-1, so no conversion is applied and the value is 3.5 s^(-1)*mM^(-1); the exported value is 3.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `NAD+`: kcat (s^-1) = 0.84; Km (mM) = 0.24; kcat/Km (s^-1 mM^-1) = 3.50.

row_label: TABLE 4, decoded plain-numeral transcription, substrate row `NAD+`

table_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt' (Appl. Environ. Microbiol. 2008, 74(13): 3949-3958)


enzyme_display_name: alcohol dehydrogenase

organism: Saccharolobus solfataricus

substrate_name: Cyclohexanol

source_db: brenda

verification_status: verified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProt:P39462 (adh/SSO2536) matched to wild-type SsADH in Giordano et al. 1999 (PMID 10074357, DOI 10.1021/bi982326e) and the wild-type structure 1R37

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

assay_conditions_summary: pH 10.5; 338.15 K; buffer 0.1 M glycine-NaOH; cofactor NAD+

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'cyclohexanol', SsADH column group: kcat = 1.2; Km = 0.03; kcat/Km = 40.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.2 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 1.2 s^(-1). Km: printed Table 2 cell 0.03 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.03 mM. kcat/Km: printed Table 2 cell 40 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 40.0 s^(-1)*mM^(-1). Closure disclosure: 1.2 / 0.03 = 40.0 s^-1 mM^-1, identical to the printed efficiency cell and to the value the export carries, so this cell group closes exactly.

raw_value_unit_evidence: Table 2, substrate row 'cyclohexanol', SsADH column group: kcat = 1.2 s^-1; Km = 0.03 mM; printed kcat/Km = 40 s^-1 mM^-1.

row_label: Table 2, substrate row 'cyclohexanol', SsADH (wild type) column group

table_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054); printed column groups SsADH and mSsADH, each printing kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1)

data_origin: experimental

enzyme: alcohol dehydrogenase

substrate: Cyclohexanol

status: verified

source: brenda


verification_status: corrected

assay_conditions_summary: pH 7.5; 338.15 K; buffer 1 mL of 50 mM Tris-HCl; cofactor NADH

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row '4-methoxybenzaldehyde', SsADH column group: kcat = 3.3; Km = 0.024; kcat/Km = 137.0.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.3 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 3.3 s^(-1). Km: printed Table 2 cell 0.024 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.024 mM. kcat/Km: printed Table 2 cell 137.0 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 137.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 3.3 / 0.024 = 137.5 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row '4-methoxybenzaldehyde', SsADH column group: kcat = 3.3 s^-1; Km = 0.024 mM; printed kcat/Km = 137.0 s^-1 mM^-1.

row_label: Table 2, substrate row '4-methoxybenzaldehyde', SsADH (wild type) column group

status: corrected


substrate_name: NAD+

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'NAD+', SsADH column group: kcat = 3.4; Km = 0.5; kcat/Km = 6.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.4 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 3.4 s^(-1). Km: printed Table 2 cell 0.5 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.5 mM. kcat/Km: printed Table 2 cell 6.8 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 6.8 s^(-1)*mM^(-1). Closure disclosure: 3.4 / 0.5 = 6.8 s^-1 mM^-1, identical to the printed efficiency cell and to the value the export carries, so this cell group closes exactly.

raw_value_unit_evidence: Table 2, substrate row 'NAD+', SsADH column group: kcat = 3.4 s^-1; Km = 0.5 mM; printed kcat/Km = 6.8 s^-1 mM^-1.

row_label: Table 2, substrate row 'NAD+', SsADH (wild type) column group

substrate: NAD+


substrate_name: benzyl alcohol

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'benzyl alcohol', SsADH column group: kcat = 3.6; Km = 0.26; kcat/Km = 13.8.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.6 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 3.6 s^(-1). Km: printed Table 2 cell 0.26 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.26 mM. kcat/Km: printed Table 2 cell 13.8 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies. Quotient disclosure for this cell group: 3.6 / 0.26 = 13.846153846153847 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell is that same quotient carried to the precision Table 2 uses, and it sits inside the last-place rounding interval of the quotient.

raw_value_unit_evidence: Table 2, substrate row 'benzyl alcohol', SsADH column group: kcat = 3.6 s^-1; Km = 0.26 mM; printed kcat/Km = 13.8 s^-1 mM^-1.

row_label: Table 2, substrate row 'benzyl alcohol', SsADH (wild type) column group

substrate: benzyl alcohol


substrate_name: NADH

assay_conditions_summary: pH 10.5; 338.15 K; buffer 0.1 M glycine-NaOH; cofactor NADH

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'NADH', SsADH column group: kcat = 10.3; Km = 0.013; kcat/Km = 792.

normalized_value_unit_evidence: kcat: printed Table 2 cell 10.3 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 10.3 s^(-1). Km: printed Table 2 cell 0.013 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.013 mM. kcat/Km: printed Table 2 cell 792 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 792.0 s^(-1)*mM^(-1). Closure check on the paper's own cells: 10.3 / 0.013 = 792.3076923076924 s^-1 mM^-1, which the printed efficiency cell 792 reproduces at the precision Table 2 uses, so the three printed cells of this group are internally consistent.

raw_value_unit_evidence: Table 2, substrate row 'NADH', SsADH column group: kcat = 10.3 s^-1; Km = 0.013 mM; printed kcat/Km = 792 s^-1 mM^-1.

row_label: Table 2, substrate row 'NADH', SsADH (wild type) column group

substrate: NADH


substrate_name: benzaldehyde

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the SsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'benzaldehyde', SsADH column group: kcat = 11.3; Km = 0.03; kcat/Km = 376.0.

normalized_value_unit_evidence: kcat: printed Table 2 cell 11.3 in the SsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 11.3 s^(-1). Km: printed Table 2 cell 0.03 in the SsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.03 mM. kcat/Km: printed Table 2 cell 376.0 in the SsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 376.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 11.3 / 0.03 = 376.6666666666667 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row 'benzaldehyde', SsADH column group: kcat = 11.3 s^-1; Km = 0.03 mM; printed kcat/Km = 376.0 s^-1 mM^-1.

row_label: Table 2, substrate row 'benzaldehyde', SsADH (wild type) column group

substrate: benzaldehyde


verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProt:P39462 (adh/SSO2536) with the N249Y substitution matched to mSsADH in Giordano et al. 1999 (PMID 10074357, DOI 10.1021/bi982326e) and the N249Y structure 1NVG and applied mutation signature N249Y with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines:
SsADH
aliphatic alcohols

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39462 and applied mutation signature N249Y to reconstruct the assayed variant sequence.

smiles: CCCO

assay_conditions_summary: pH 10.5; 338.15 K; buffer 1 mL of standard assay mixture with 0.1 M glycine/NaOH; cofactor NAD+

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the mSsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row '1-propanol', mSsADH column group: kcat = 16.6; Km = 1.70; kcat/Km = 9.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 16.6 in the mSsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 16.6 s^(-1). Km: printed Table 2 cell 1.70 in the mSsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 1.7 mM. kcat/Km: printed Table 2 cell 9.7 in the mSsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 9.7 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 16.6 / 1.70 = 9.764705882352942 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row '1-propanol', mSsADH column group: kcat = 16.6 s^-1; Km = 1.70 mM; printed kcat/Km = 9.7 s^-1 mM^-1.

row_label: Table 2, substrate row '1-propanol', mSsADH (N249Y SsADH) column group


sequence_source: UniProt:P39462 (adh/SSO2536) with the N249Y substitution matched to mSsADH in Giordano et al. 1999 (PMID 10074357, DOI 10.1021/bi982326e) and the N249Y structure 1NVG

proof_lines:
SsADH
aromatic aldehydes


proof_lines:
benzyl alcohol
SsADH


column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the mSsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'NADH', mSsADH column group: kcat = 25.3; Km = 0.21; kcat/Km = 120.0.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25.3 in the mSsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 25.3 s^(-1). Km: printed Table 2 cell 0.21 in the mSsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.21 mM. kcat/Km: printed Table 2 cell 120.0 in the mSsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 120.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25.3 / 0.21 = 120.47619047619048 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row 'NADH', mSsADH column group: kcat = 25.3 s^-1; Km = 0.21 mM; printed kcat/Km = 120.0 s^-1 mM^-1.

row_label: Table 2, substrate row 'NADH', mSsADH (N249Y SsADH) column group


substrate_name: 4-methoxybenzyl alcohol

column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the mSsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row '4-methoxybenzyl alcohol', mSsADH column group: kcat = 25.5; Km = 1.24; kcat/Km = 20.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25.5 in the mSsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 25.5 s^(-1). Km: printed Table 2 cell 1.24 in the mSsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 1.24 mM. kcat/Km: printed Table 2 cell 20.5 in the mSsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 20.5 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25.5 / 1.24 = 20.56451612903226 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row '4-methoxybenzyl alcohol', mSsADH column group: kcat = 25.5 s^-1; Km = 1.24 mM; printed kcat/Km = 20.5 s^-1 mM^-1.

row_label: Table 2, substrate row '4-methoxybenzyl alcohol', mSsADH (N249Y SsADH) column group

substrate: 4-methoxybenzyl alcohol


column_label: Table 2: Kinetic Constants for SsADH and mSsADH (Biochemistry 1999, volume 38, number 10, pages 3043-3054). The substrate column is the printed row label; the mSsADH column group prints kcat (s^-1), Km (mM) and kcat/Km (s^-1 mM^-1). Body row 'benzaldehyde', mSsADH column group: kcat = 25.5; Km = 0.26; kcat/Km = 98.0.

normalized_value_unit_evidence: kcat: printed Table 2 cell 25.5 in the mSsADH kcat column, whose head prints s^-1, so no unit conversion applies and the paper value is 25.5 s^(-1). Km: printed Table 2 cell 0.26 in the mSsADH Km column, whose head prints mM, so no unit conversion applies and the paper value is 0.26 mM. kcat/Km: printed Table 2 cell 98.0 in the mSsADH kcat/Km column, whose head prints s^-1 mM^-1, the export unit, so no unit conversion applies and the paper value is 98.0 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 25.5 / 0.26 = 98.07692307692308 s^-1 mM^-1, which is the value the export carries; the printed efficiency cell lies outside the last-place rounding interval of that quotient, so this record carries the printed cell as the paper value for kcat_over_km alone.

raw_value_unit_evidence: Table 2, substrate row 'benzaldehyde', mSsADH column group: kcat = 25.5 s^-1; Km = 0.26 mM; printed kcat/Km = 98.0 s^-1 mM^-1.

row_label: Table 2, substrate row 'benzaldehyde', mSsADH (N249Y SsADH) column group


assay_conditions_summary: cofactor NAD+

proof_lines: Giordano et al. Biochemistry 1999 Table 2 matches the substrate and kinetic constants in this batch for SsADH and the Asn249Tyr mutant.


substrate_name: acetone

smiles: CC(=O)C

substrate: acetone


substrate_name: Cyclopentanone

substrate: Cyclopentanone


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


smiles: CCC(=O)C


smiles: CCCCO

column_label: Table 2: Kinetic constants for wild-type and mutant SsADHs (Extremophiles 2009, 13:751-761), Wild-type column group, substrate row '1-Butanol'; column 'kcat (s-1)' = 3.1; column 'Km (mM)' = 0.08; column 'kcat/Km (s-1 mM-1)' = 38.7.

normalized_value_unit_evidence: kcat: printed Table 2 cell 3.1 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 3.1 s^(-1); the exported value is 3.1 s^(-1). Km: printed Table 2 cell 0.08 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.08 mM; the exported value is 0.08 mM. kcat/Km: printed Table 2 cell 38.7 s-1 mM-1; s-1 mM-1 is the canonical s^(-1)*mM^(-1), no unit conversion applies; the paper value is 38.7 s^(-1)*mM^(-1); the exported value is 38.75 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row '1-Butanol', Wild-type column group: kcat = 3.1 s-1; Km = 0.08 mM; printed kcat/Km = 38.7 s-1 mM-1.

row_label: Table 2, Wild-type column group, substrate row '1-Butanol'


km_display: Not reported

kcat_over_km_display: Not reported


smiles: CCC(CC)O

column_label: Table 2: Kinetic constants for wild-type and mutant SsADHs (Extremophiles 2009, 13:751-761), Wild-type column group, substrate row '3-Pentanol'; column 'kcat (s-1)' = 1.5; column 'Km (mM)' = 0.27; column 'kcat/Km (s-1 mM-1)' = 5.5.

normalized_value_unit_evidence: kcat: printed Table 2 cell 1.5 s-1; the printed unit is already s^(-1), no unit conversion applies; the paper value is 1.5 s^(-1); the exported value is 1.5 s^(-1). Km: printed Table 2 cell 0.27 mM; the printed unit is already mM, no unit conversion applies; the paper value is 0.27 mM; the exported value is 0.27 mM. kcat/Km: printed Table 2 cell 5.5 s-1 mM-1; s-1 mM-1 is the canonical s^(-1)*mM^(-1), no unit conversion applies; the paper value is 5.5 s^(-1)*mM^(-1); the exported value is 5.55556 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row '3-Pentanol', Wild-type column group: kcat = 1.5 s-1; Km = 0.27 mM; printed kcat/Km = 5.5 s-1 mM-1.

row_label: Table 2, Wild-type column group, substrate row '3-Pentanol'


substrate_name: methanol

smiles: CO

substrate: methanol


smiles: CCC(C)O

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH

proof_lines: Role of tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase


kcat_display: Not reported


smiles: CCCC(C)O


organism: Equus caballus

proof_lines: Family context identifies horse alcohol dehydrogenase S chain (UniProt P00328), but it remains family-level evidence rather than a row-specific kinetic excerpt.


assay_conditions_summary: pH 8


substrate_name: Butyl alcohol

substrate: Butyl alcohol


substrate_name: hexyl alcohol

smiles: CCCCCCO

substrate: hexyl alcohol


substrate_name: Propyl alcohol

substrate: Propyl alcohol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: hexaldehyde

smiles: CCCCCC=O

substrate: hexaldehyde


organism: Scaptodrosophila lebanonensis

substrate_name: NAD+

substrate: NAD+


substrate_name: Cyclohexanol

substrate: Cyclohexanol


smiles: CC(C)CCCO


smiles: CC(C)O


smiles: CCCO


smiles: CC(C)CO


smiles: CCCCCO


smiles: CCCC(CCC)O


organism: Geobacillus stearothermophilus

kcat_over_km_origin: calculated

sequence_source: UniProt P42328 linked from the BRENDA literature page for PMID 762802


substrate_name: tert-butanol

smiles: CC(C)(C)O

substrate: tert-butanol


smiles: C(CO)CO


substrate_name: iso-propanol

substrate: iso-propanol


organism: Sulfolobus acidocaldarius

sequence_source: Resolved from BRENDA EC 1.1.1.1 organism table entry 718681 to UniProt Q4J9F2 / GenBank AAY80578.1 short chain dehydrogenase from Sulfolobus acidocaldarius DSM 639.

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

assay_conditions_summary: pH 5


substrate_name: benzil

substrate: benzil


substrate_name: isoborneol

substrate: isoborneol


substrate_name: ethyl 3-methyl-2-oxobutyrate

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

substrate: ethyl 3-methyl-2-oxobutyrate


organism: Yokenella sp.

substrate_name: benzyl alcohol

sequence_source: GenBank protein AHI87872.1 translated from KF887947.1 (YsADH from Yokenella sp. WZY002)

substrate: benzyl alcohol


smiles: CC=CCO


substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+

substrate: NADP+


substrate_name: benzaldehyde

substrate: benzaldehyde


smiles: CC=CC=O


substrate_name: NADPH

assay_conditions_summary: pH 6.5; cofactor NADPH

substrate: NADPH


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

assay_conditions_summary: pH 7


assay_conditions_summary: pH 7; cofactor NAD+


organism: Geobacillus thermodenitrificans


assay_conditions_summary: pH 8; cofactor NAD+


substrate_name: ethanol

substrate: ethanol


substrate_name: NADH

assay_conditions_summary: pH 8; cofactor NADH

substrate: NADH


organism: Rhodococcus ruber

sequence_source: GenBank:AJ491307 / CAD36475.1 encodes the Rhodococcus ruber strain 219 sadh secondary alcohol dehydrogenase expressed as RR-ADH6H in Giersberg et al. 2012; mapped in UniProt as Q8KLT9.

assay_conditions_summary: pH 6

proof_lines: Giersberg et al. 2012 describes RR-ADH6H from Rhodococcus ruber strain 219 expressed in Hansenula polymorpha, Saccharomyces cerevisiae, and Arxula adeninivorans, matching the three host-specific comments in this batch.


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: acetophenone

substrate: acetophenone


substrate_name: capronaldehyde

substrate: capronaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


organism: Homo sapiens

sequence_variant_note: Mutation signature H1C/R272Q/I350V could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: 5beta-cholanic acid-3-one

substrate: 5beta-cholanic acid-3-one


organism: Drosophila melanogaster

substrate_name: NAD+

sequence_source: UniProtKB:P00334 (Adh)

proof_lines:
NAD+ cofactor
NAD+ Km 0.26 mM

substrate: NAD+


smiles: CCC(C)O

proof_lines:
butan-2-ol + NAD+ -> butan-2-one + NADH
butan-2-ol Km 0.86 mM


proof_lines:
propan-2-ol + NAD+ -> acetone + NADH
propan-2-ol Km 1.87 mM


smiles: CCCCO

proof_lines:
butanol + NAD+ -> butyraldehyde + NADH
butanol Km 3.31 mM


smiles: CCO

proof_lines:
ethanol + NAD+ -> acetaldehyde + NADH
ethanol Km 8.92 mM


organism: Pyrobaculum calidifontis

smiles: C(CCO)CO

assay_conditions_summary: pH 10; 333.15 K; cofactor NAD+

column_label: Exact primary prose, PDF page 6: 1,4-butanediol paragraph reports Km 0.36 mM, Vmax 3.22 +/- 0.4 micromol min^-1 mg^-1, kcat 1.98 s^-1, and kcat/Km 5.5 mM^-1 s^-1.

row_label: 1,4-butanediol kinetic paragraph

table_label: Results prose adjacent to Table 1 on PDF page 6 (not a kinetic table cell)


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

assay_conditions_summary: pH 6; 353.15 K; cofactor NADH

column_label: Exact primary prose, PDF page 6: glutaraldehyde paragraph reports Km 0.67 mM, Vmax 150 +/- 8 micromol min^-1 mg^-1, kcat 93.13 s^-1, and kcat/Km 139 mM^-1 s^-1.

row_label: glutaraldehyde kinetic paragraph

table_label: Results prose adjacent to Table 2 on PDF page 6 (not a kinetic table cell)

substrate: Glutaraldehyde


assay_conditions_summary: pH 6; cofactor NADH

normalized_value_unit_evidence: Km normalized_value=0.072 normalized_unit=mM from 0.072 mM.

raw_value_unit_evidence: Article kinetic prose reports Pcal_1311 Km for NADH = 0.072 mM with 50 mM glutaraldehyde. Raw value 0.072 mM.

row_label: Pcal_1311 with 50 mM glutaraldehyde

table_label: Article kinetic prose, Pcal_1311 reduction paragraph


assay_conditions_summary: pH 10; cofactor NAD+

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM from 1.7 mM.

raw_value_unit_evidence: Article kinetic prose reports Pcal_1311 Km for NAD+ = 1.7 mM with 50 mM 1,4-butanediol. Raw value 1.7 mM.

row_label: Pcal_1311 with 50 mM 1,4-butanediol

table_label: Article kinetic prose, Pcal_1311 oxidation paragraph


organism: Pyrococcus furiosus

assay_conditions_summary: pH 6.1; cofactor NADH

proof_lines:
Pyrococcus furiosus AdhD
NAD(H)
NADP(H)


assay_conditions_summary: pH 8.8; cofactor NAD+


substrate_name: acetoin

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

proof_lines:
acetoin
diacetyl-acetoin
Pyrococcus furiosus AdhD

substrate: acetoin


smiles: CC(C(C)O)O

proof_lines:
2,3-butanediol
108.3 U/mg
Pyrococcus furiosus AdhD


enzyme_display_name: D-xylulose reductase

organism: Scheffersomyces stipitis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A/I208R/F209T to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; cofactor NADP+

proof_lines: Complete reversal of coenzyme specificity of xylitol dehydrogenase and increase of thermostability by the introduction of structural zinc

enzyme: D-xylulose reductase


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A/I208R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I208R/F209S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S96C/S99C/Y102C/D207A/I208R/F209S/N211R to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature S96C/S99C/Y102C 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_ec_organism_unique and applied mutation signature D207A/I208R/F209Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A/F209S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A/I208R/F209S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N211R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F209S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I208R to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D207A/I208R/F209S/N211R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S96C/S99C/Y102C/D207A/I208R/F209S to reconstruct the assayed variant sequence.


substrate_name: xylitol

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

substrate: xylitol


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A/I208R to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature N211R to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme N211R


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature I208R to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme I208R


proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme S96C/S99C/Y102C


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature F209S to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme F209S


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A/F209S to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209T


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A/I208R/F209Y to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209Y


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A/I208R/F209S to reconstruct the assayed variant sequence.

proof_lines: pH 9.0, 35°C, cofactor: NAD+, mutant enzyme D207A/I208R/F209S


sequence_variant_note: Resolved canonical sequence from genbank_x55392_caa39066_uniprot_p22144 and applied mutation signature D207A/I208R/F209T to reconstruct the assayed variant sequence.


organism: Rhizomucor pusillus

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

proof_lines: recombinant mutant D205A/I206R, pH 9.0, 35°C


proof_lines: recombinant mutant D205A/I206R, pH 9.0, 35°C, with NAD+


sequence_variant_note: Resolved canonical sequence from ncbi_protein_accession:BAO45794.1 and applied mutation signature D205A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


column_label: Table 4; row RpWT; NAD+ block columns Km=0.186 mM, kcat=381 min^-1, kcat/Km=1942 min^-1 mM^-1

normalized_value_unit_evidence: normalized explicit table cells: kcat=6.35 s^-1; Km=0.186 mM; kcat/Km=32.3667 s^-1 mM^-1

raw_value_unit_evidence: Table 4 row RpWT, NAD+ block: Km=0.186 mM; kcat=381 min^-1; kcat/Km=1942 min^-1 mM^-1

row_label: RpWT

table_label: Table 4


proof_lines: recombinant wild-type enzyme, pH 9.0, 35°C, with NAD+


proof_lines: recombinant mutant D205A, pH 9.0, 35°C, with NAD+


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

column_label: Table 2; row NAD+ (Xylitol); column Km (mM)

normalized_value_unit_evidence: normalized: Km=0.027 mM

raw_value_unit_evidence: Table 2 cells for native RpXDH, coenzyme NAD+ with xylitol: Km=0.027 mM

row_label: NAD+ (Xylitol)

table_label: Table 2


column_label: Table 2; row Xylitol; column Km (mM)

normalized_value_unit_evidence: normalized: Km=7.83 mM

raw_value_unit_evidence: Table 2 cells for native RpXDH, substrate Xylitol: Km=7.83 mM

row_label: Xylitol


substrate_name: D-sorbitol

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

column_label: Table 2; row D-Sorbitol; column Km (mM)

normalized_value_unit_evidence: normalized: Km=31.5 mM

raw_value_unit_evidence: Table 2 cells for native RpXDH, substrate D-Sorbitol: Km=31.5 mM

row_label: D-Sorbitol

substrate: D-sorbitol


substrate_name: glycerone phosphate

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

substrate: glycerone phosphate


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


proof_lines: mutant enzyme R269A/N270A, at pH 7.5 and 25°C


enzyme_display_name: glycerol dehydrogenase

organism: Escherichia coli

smiles: CC(CCO)O

enzyme: glycerol dehydrogenase


proof_lines: mutant protein Q70H/G193C/E291Q/A310T, pH 9.5, 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D121A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


proof_lines: mutant protein Q70H/D121A/G193C/E291Q/A310T, pH 9.5, 30°C


assay_conditions_summary: pH 9.5; cofactor NAD+


organism: Gluconobacter oxydans

substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+

substrate: NADP+


proof_lines: pH 7.0, cofactor: NADP+mutant enzyme D38S/M39R


proof_lines: pH 7.0, cofactor: NADP+ mutant enzyme D38S/M39R


organism: Leishmania mexicana

assay_conditions_summary: cofactor NADH


substrate_name: dihydroxyacetone phosphate

substrate: dihydroxyacetone phosphate


assay_conditions_summary: cofactor NAD+


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


sequence_source: UniProtKB:P13706 (GPDA_DROME/Gpdh1)


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


substrate_name: glycerol 3-phosphate

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

substrate: glycerol 3-phosphate


organism: Oryctolagus cuniculus

substrate_name: Hydroxyacetone phosphate

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

proof_lines: PMID 287271 is a comment on a focal-disease paper; PMID 287270 is a dermatology-viewpoint paper.

substrate: Hydroxyacetone phosphate


substrate_name: DL-propane-1,2-diol 1-phosphate

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

proof_lines: PMID 287271 is a comment on a focal-disease paper, not a kinetics paper.

substrate: DL-propane-1,2-diol 1-phosphate


substrate_name: Cyclohexanol

source_db: oed

proof_lines: Kinetic properties of human liver alcohol dehydrogenase: oxidation of alcohols by class I isoenzymes

data_origin: curated

substrate: Cyclohexanol

source: oed


substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCCCCO


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


substrate_name: Glycol

smiles: OCCO

substrate: Glycol


organism: Equus caballus

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+

proof_lines: PubMed lists PMID 4314596 as a 1970 J Biol Chem paper on horse liver alcohol dehydrogenase, but it provides no abstract or row-level kinetic excerpt for the NAD+ record.


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Aeropyrum pernix

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

sequence_source: multiple

source_databases_merged: brenda skid


substrate_name: tert-butyl acetoacetate

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

substrate: tert-butyl acetoacetate


substrate_name: ethanol

substrate: ethanol


smiles: CC(C)O


smiles: CCCO


smiles: CCCCCCO


substrate_name: NAD+

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

substrate: NAD+


smiles: CCCCCCCCC(=O)C


smiles: CCCCO


substrate_name: NADH

assay_conditions_summary: pH 8; 333.15 K; cofactor NADH

substrate: NADH


smiles: CCCCCO


smiles: CCC(C)O


smiles: CCCC(C)O


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


smiles: CCCCCCCC(=O)C


smiles: CCCCCC(=O)C


smiles: CCCCCCC(=O)C


smiles: CCCC(=O)C


smiles: CCCCC(=O)C


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cyclohexanone

substrate: cyclohexanone


organism: Saccharomyces cerevisiae

source_db: skid

smiles: CCO

proof_lines:
PMID 2201405 / ADH family context
Raw SKiD Env: Temp=25\u00b0C, pH=8

source_databases_merged: skid uniprot

source: skid


organism: Arabidopsis thaliana

proof_lines: kcat is 328 min(-1) with NAD(+) as substrate (at pH 10.5 and 25 degrees Celsius).


substrate_name: NAD(+) (at pH 10.5 and 25 degrees Celsius)

source_db: uniprot

source: uniprot


substrate_name: S-(hydroxymethyl)glutathione

assay_conditions_summary: pH 8

proof_lines: Shared abstract context confirms Arabidopsis formaldehyde dehydrogenase and Km for S-hydroxymethylglutathione.

substrate: S-(hydroxymethyl)glutathione


substrate_name: S-hydroxymethylglutathione (at pH 8 and 25 degrees Celsius)

column_label: Table II columns Substrate, Km (uM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); S-hydroxymethylglutathione (pH 8) Km cell 7 uM.

raw_value_unit_evidence: S-hydroxymethylglutathione (pH 8) row: Km 7 uM in Table II.

row_label: S-hydroxymethylglutathione (pH 8)

table_label: Official PMC HTML Table II, Kinetic properties of Arabidopsis FALDH


substrate_name: farnesol (at pH 7.5 and 25 degrees Celsius)

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

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: SABIO reaction 48165: NAD+ + Farnesol = NADH + H+ + Farnesal


substrate_name: geraniol (at pH 10 and 25 degrees Celsius)

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

assay_conditions_summary: pH 8; buffer Chrome Assay condition: 0.1 M glycine; cofactor NAD+

column_label: Table II columns Substrate, Km (uM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); Geraniol (pH 10) Km cell 800 uM.

raw_value_unit_evidence: Geraniol (pH 10) row: Km 800 uM in Table II.

row_label: Geraniol (pH 10)


substrate_name: 12-Hydroxydodecanoic acid (at pH 10 and 25 degrees Celsius)

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

column_label: Table II columns Substrate, Km (uM), Kcat (min^-1), Kcat/Km (mM^-1 min^-1); 12-Hydroxydodecanoic acid (pH 10) Km cell 4700 uM.

raw_value_unit_evidence: 12-Hydroxydodecanoic acid (pH 10) row: Km 4700 uM in Table II.

row_label: 12-Hydroxydodecanoic acid (pH 10)


organism: Moraxella sp. (strain TAE123)

substrate_name: ethanol (at pH 7.4 and 25 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: kcat is 549.1 min(-1) for the oxidation of ethanol (at pH 7.4 and 30 degrees Celsius). kcat is 488.8 min(-1) for the oxidation of propan-1-ol (at pH 7.4 and 30 degrees Celsius). kcat is 486.7 min(-1) for the oxidation of butan-1-ol (at pH 7


substrate_name: propan-1-ol (at pH 7.4 and 25 degrees Celsius)


substrate_name: butan-1-ol (at pH 7.4 and 25 degrees Celsius)


substrate_name: propan-2-ol (at pH 7.4 and 25 degrees Celsius)

smiles: CC(C)O


substrate_name: acetone (at pH 6.0 and 25 degrees Celsius)

smiles: CC(=O)C


substrate_name: NAD(+) (at pH 7.4 and 25 degrees Celsius)


substrate_name: NADH (at pH 6.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: Purification and characterization of an alcohol dehydrogenase from the Antarctic psychrophile Moraxella sp. TAE123

substrate: NADH (at pH 6.0 and 25 degrees Celsius)


organism: Pisum sativum

substrate_name: octanol (at pH 10)

smiles: CCCCCCCCO

assay_conditions_summary: pH 10

proof_lines:
class III alcohol dehydrogenase
octanol
pea enzyme

substrate: octanol (at pH 10)


substrate_name: NAD(+) (at pH 10)

assay_conditions_summary: pH 10; cofactor NAD+

proof_lines:
class III alcohol dehydrogenase
NAD+
pea enzyme

substrate: NAD(+) (at pH 10)


substrate_name: S-(hydroxymethyl)glutathione (at pH 8)

proof_lines:
class III alcohol dehydrogenase
S-(hydroxymethyl)glutathione
pea enzyme

substrate: S-(hydroxymethyl)glutathione (at pH 8)


organism: Thermococcus barophilus

substrate_name: ethanol

proof_lines: kcat is 0.27 sec(-1) for ethanol oxidation. kcat is 69 sec(-1) for acetaldehyde reduction.


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: (R,R)-butanediol dehydrogenase

organism: Bacillus subtilis subsp. subtilis

assay_conditions_summary: pH 7

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme

enzyme: (R,R)-butanediol dehydrogenase


substrate_name: (R)-acetoin

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

substrate: (R)-acetoin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E221S/I222R/A223S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E221S/I222R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E221S to reconstruct the assayed variant sequence.


organism: Homo sapiens

substrate_name: sorbitol

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

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

assay_conditions_summary: pH 7.1; cofactor NAD+

proof_lines: PMID 12962626 gives human SDH kinetic context for sorbitol, NAD+, and NADH.

proof_lines: The preserved row note still mixes commentary across multiple substrates, so the exact record is not safely isolated.

substrate: sorbitol


substrate_name: NAD(+)

proof_lines: PMID 12962626 reports human SDH kinetic context that includes NAD+.

proof_lines: The saved row note still does not isolate a clean NAD(+) measurement for this exact export record.

substrate: NAD(+)


substrate_name: NADH

assay_conditions_summary: pH 7.1; cofactor NADH

proof_lines: PMID 12962626 reports human SDH kinetic context that includes NADH.

proof_lines: The saved row note still does not isolate a clean NADH measurement for this exact export record.


substrate_name: xylitol (at pH 10.0)

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

proof_lines: kcat is 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat i

substrate: xylitol (at pH 10.0)


substrate_name: L-threitol (at pH 10.0)

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

substrate: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

smiles: CC(C(C)O)O

substrate: (2R,3R)-2,3-butanediol (at pH 10.0)


substrate_name: D-fructose (at pH 7.1)

substrate: D-fructose (at pH 7.1)


organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

column_label: Springer abstract reports stereospecific oxidation of (2R,3R)-2,3-BD with Km = 0.16 mM and kcat/Km = 673 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.16 raw_unit=mM for (2R,3R)-2,3-BD

row_label: Abstract sentence for oxidation of (2R,3R)-2,3-BD

table_label: PMID 33763825 Springer abstract/prose


proof_lines: kcat is 102.2 sec(-1) with (R,R)-butane-2,3-diol as substrate.

proof_lines: kcat is 115.9 sec(-1) with meso-butane-2,3-diol as substrate.


column_label: Springer abstract reports NgBDH could reduce (3R/3S)-acetoin with a Km of 0.14 mM and a kcat/Km of 885 s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.14 raw_unit=mM for (3R/3S)-acetoin

row_label: Abstract sentence for reduction of (3R/3S)-acetoin


substrate: NADH


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


substrate_name: Glycerone

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

assay_conditions_summary: pH 6; cofactor NADH

substrate: Glycerone


organism: Thermotoga maritima

assay_conditions_summary: pH 7.9; cofactor NADH

proof_lines: pH 7.9, 50°C, recombinant wild-type enzyme


substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V44A/K157G to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 50°C, recombinant mutant V44A/K157G

substrate: NAD+


proof_lines: pH 7.4, 50°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K157N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K157G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V44A/K157N to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 50°C, recombinant mutant V44A/K157N


organism: Schizosaccharomyces pombe

substrate_name: dihydroxyacetone

assay_conditions_summary: pH 6

proof_lines: Purification and properties of glycerol:NAD+ 2-oxidoreductase (glycerol dehydrogenase) from Schizosaccharomyces pombe

substrate: dihydroxyacetone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V44A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I154A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I154A/K157G to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 50°C, recombinant mutant I154A/K157G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V44A/I154A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 50°C, recombinant mutant V44A/I154A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V44A/I154A/K157G to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 50°C, recombinant mutant V44A/I154A/K157G


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines:
D-1-amino-2-propanol oxidoreductase
E. coli K12
hydroxyacetone reduction


proof_lines: pH 10.3, 30 C, recombinant enzyme, in presence of 30 mM NH4Cl

proof_lines: pH 10.3, 30 C, recombinant enzyme, in presence of 20 mM KCl


organism: Escherichia coli (strain K12)

smiles: CC(CO)O

assay_conditions_summary: cofactor NAD+


smiles: CCC(CO)O


smiles: CC(CN)O


organism: Escherichia coli

proof_lines: pH 6.5, 30 C, recombinant enzyme, in presence of 30 mM NH4Cl

proof_lines: pH 6.5, 30 C, recombinant enzyme, in presence of 20 mM KCl


substrate_name: glycolaldehyde (at 25 degrees Celsius and pH 7)

smiles: C(C=O)O

proof_lines: higher affinities towards dihydroxyacetone, methylglyoxal, and glycolaldehyde than glycerol


substrate_name: methylglyoxal (at 25 degrees Celsius and pH 7)

smiles: CC(=O)C=O


organism: Geobacillus thermodenitrificans (strain NG80-2)

smiles: CCO

assay_conditions_summary: cofactor NADH

proof_lines: kcat is 638.69 sec(-1) for ethanol. kcat is 404.77 sec(-1) for acetaldehyde. kcat is 443.05 sec(-1) for NAD. kcat is 1645.74 sec(-1) for NADH. kcat is 43.90 sec(-1) for NADP.

substrate: ethanol


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


substrate_name: dihydroxyacetone phosphate

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

proof_lines: contralateral sensorineural hearing loss

substrate: dihydroxyacetone phosphate


proof_lines: PMID 287271 is a comment on a focal-disease paper, not a kinetics paper.


proof_lines:
adipose tissue
muscle
I6.5


organism: Pichia kudriavzevii

substrate_name: xylitol

substrate: xylitol


substrate_name: sorbitol

proof_lines: kcat is 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat i


substrate_name: NAD(+)


substrate_name: NADH


substrate_name: xylitol (at pH 10.0)

proof_lines: polyol substrates such as sorbitol, xylitol, or L-threitol


substrate_name: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

proof_lines: stereospecific oxidation of (2R,3R)-2,3-butanediol


substrate_name: D-fructose (at pH 7.1)


organism: Bos taurus

substrate_name: D-sorbitol (at pH 8.0)

proof_lines: kcat is 29 sec(-1) for D-sorbitol oxidation (at pH 8.0). kcat is 26 sec(-1) for xylitol oxidation (at pH 8.0). kcat is 21 sec(-1) for L-iditol oxidation (at pH 8.0). kcat is 22 sec(-1) for ribitol oxidation (at pH 8.0). kcat is 24 sec(-1) f

substrate: D-sorbitol (at pH 8.0)


substrate_name: xylitol (at pH 8.0)

substrate: xylitol (at pH 8.0)


substrate_name: L-threitol (at pH 8.0)

substrate: L-threitol (at pH 8.0)


substrate_name: D-fructose (at pH 7.4)

substrate: D-fructose (at pH 7.4)


substrate_name: D-ribulose (at pH 7.4)

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

substrate: D-ribulose (at pH 7.4)


substrate_name: NADH (at pH 7.4)

substrate: NADH (at pH 7.4)


proof_lines: Abstract-only context for bovine lens sorbitol dehydrogenase, EC 1.1.1.14, with polyol kinetics for xylitol and sorbitol.


proof_lines: kcat is 0.33 sec(-1) towards sorbitol for the reaction with sorbitol as substrate. kcat is 0.39 sec(-1) towards NAD(+) for the reaction with sorbitol as substrate.

substrate: sorbitol


substrate: NAD(+)


organism: Rattus norvegicus

proof_lines: The preserved abstract reports rat liver sorbitol dehydrogenase kinetics for NAD, sorbitol, NADH, and fructose.

proof_lines: kcat is 8 sec(-1) for sorbitol oxidation and 190 sec(-1) for D-fructose reduction.


substrate_name: D-fructose

substrate: D-fructose


substrate: NADH


organism: Ovis aries

substrate_name: xylitol (at pH 7.4)

proof_lines: kcat is 19.6 sec(-1) for D-sorbitol oxidation (at pH 7.4).

substrate: xylitol (at pH 7.4)


organism: Saccharolobus solfataricus

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

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH

proof_lines: Role of tryptophan 95 in substrate specificity and structural stability of Sulfolobus solfataricus alcohol dehydrogenase


organism: Thermus thermophilus HB27

sequence_source: NCBI RefSeq YP_003977.1 (identical replacement WP_011172461.1) cited in PMID 684583 for Thermus thermophilus HB27 adh_Tt

proof_lines: Molecular and biochemical characterization of an alcohol dehydrogenase from the thermophilic bacterium Thermus thermophilus HB27


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: alpha-tetralone

substrate: alpha-tetralone


proof_lines: Purification and characterization of a novel recombinant highly enantioselective short-chain NAD(H)-dependent alcohol dehydrogenase from Thermus thermophilus


substrate_name: methyl benzoylformate

substrate: methyl benzoylformate


substrate_name: alpha-tetralol

column_label: Table 4 row (+-)-alpha-Tetralol under kcat (s^-1) = 48.1 +/- 4.9 and Km (mM) = 5.3 +/- 0.6.

row_label: (+-)-alpha-Tetralol

substrate: alpha-tetralol


substrate_name: (S)-alpha-tetralol

row_label: (S)-(+)-alpha-Tetralol

substrate: (S)-alpha-tetralol


substrate_name: ethyl benzoylformate

sequence_source: NCBI RefSeq YP_003977.1 (identical replacement WP_011172461.1) cited in PMID 684583 for Thermus thermophilus HB27 adh_Tt; UniProt Q72LQ6 canonical sequence byte-identical (length 256). NCBI RefSeq YP_003977.1 (WP_011172461.1) cross-references UniProt Q72LQ6 (Thermus thermophilus HB27, 256 aa); cited in PMID 684583.

column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `Ethyl benzoylformate`: column 'kcat (s^-1)' = 50.1; column 'Km (mM)' = 1.0; column 'kcat/Km (s^-1 mM^-1)' = 50.1.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 50.1 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 50.1 s^(-1); the exported value is 50.1 s^(-1). Km: printed TABLE 4 cell 1.0 mM; the table already reports Km in mM, so no conversion is applied and the value is 1.0 mM; the exported value is 1.0 mM. kcat/Km: the paper PRINTS the kcat/Km cell 50.1 s^-1 mM^-1 for this substrate row; the table already reports kcat/Km in s^-1 mM^-1, so no conversion is applied and the value is 50.1 s^(-1)*mM^(-1); the exported value is 50.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `Ethyl benzoylformate`: kcat (s^-1) = 50.1; Km (mM) = 1.0; kcat/Km (s^-1 mM^-1) = 50.1.

row_label: TABLE 4, decoded plain-numeral transcription, substrate row `Ethyl benzoylformate`

substrate: ethyl benzoylformate


substrate_name: NADH

assay_conditions_summary: pH 10.5; 338.15 K; cofactor NADH

column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `NADH`: column 'kcat (s^-1)' = 52.4; column 'Km (mM)' = 0.035; column 'kcat/Km (s^-1 mM^-1)' = 1490.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 52.4 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 52.4 s^(-1); the exported value is 52.4 s^(-1). Km: printed TABLE 4 cell 0.035 mM; the table already reports Km in mM, so no conversion is applied and the value is 0.035 mM; the exported value is 0.0035 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1490 s^-1 mM^-1 for this substrate row; the table already reports kcat/Km in s^-1 mM^-1, so no conversion is applied and the value is 1490.0 s^(-1)*mM^(-1); the exported value is 14971.42857142857 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `NADH`: kcat (s^-1) = 52.4; Km (mM) = 0.035; kcat/Km (s^-1 mM^-1) = 1490.

row_label: TABLE 4, decoded plain-numeral transcription, substrate row `NADH`


organism: Scaptodrosophila lebanonensis

substrate_name: NAD+

substrate: NAD+


substrate_name: Cyclohexanol

substrate: Cyclohexanol


smiles: CC(C)CCCO


smiles: CC(C)O


smiles: CCCO


smiles: CCCCO


smiles: CC(C)CO


smiles: CCCCCO


substrate_name: ethanol

substrate: ethanol


smiles: CCCC(CCC)O


smiles: CCCCCCO


organism: Geobacillus stearothermophilus


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: tert-butanol

smiles: CC(C)(C)O

substrate: tert-butanol


smiles: C(CO)CO


smiles: CCC(C)O


substrate_name: 12-hydroxylauric acid methyl ester

assay_conditions_summary: pH 8

substrate: 12-hydroxylauric acid methyl ester


assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines:
ethanol Km 5.11 mM
Vmax 61.35 U/mg
ethanol + NAD+ -> acetaldehyde + NADH


assay_conditions_summary: pH 8; cofactor NADH


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


organism: Saccharomyces cerevisiae

substrate_name: furfural

sequence_source: Derived from UniProt P00330 (Saccharomyces cerevisiae ADH1) with the PMID 738991 double mutation S110P/Y295C applied.

substrate: furfural


sequence_source: UniProt P00330 (Saccharomyces cerevisiae ADH1), supported by the wild-type acetaldehyde kinetics reported in PMID 738991.


sequence_source: UniProt P00330 (Saccharomyces cerevisiae ADH1), supported by the wild-type furfural kinetics reported in PMID 738991.


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


sequence_source: UniProt P00330 (Saccharomyces cerevisiae ADH1), supported by the shared wild-type construct context in PMID 738991.


organism: Alligator mississippiensis

proof_lines: Basic features of class-I alcohol dehydrogenase


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


substrate_name: Hexanol

substrate: Hexanol


smiles: CCO


substrate_name: butanol

substrate: butanol


organism: Oenococcus oeni

assay_conditions_summary: pH 9; cofactor NAD+

proof_lines:
Oenococcus oeni Adh3
NAD+


assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
Oenococcus oeni Adh3
NADH

substrate: NADH


proof_lines:
Oenococcus oeni Adh3
acetaldehyde


assay_conditions_summary: pH 9

proof_lines:
Oenococcus oeni Adh3
ethanol


smiles: CC(CO)O


organism: Zea mays

sequence_source: NCBI RefSeq NP_001105409.2 (Zea mays alcohol dehydrogenase 1 / LOC542363, alias Adh1-1S)


organism: Mycobacterium sp.

sequence_source: UniProt W8VSK8 (ads1, Mycobacterium sp. B-009), cross-referenced to PMID 25082080 / BRENDA literature id 737865

assay_conditions_summary: pH 7; cofactor NAD+


substrate_name: Butanal

assay_conditions_summary: pH 7; cofactor NADH

substrate: Butanal


organism: Parageobacillus thermoglucosidasius

sequence_source: NCBI Protein GAJ43611.1 adhE full-length aldehyde dehydrogenase/alcohol dehydrogenase from Parageobacillus thermoglucosidasius NBRC 107763; cross-checked against PDB 3ZDR, which identifies the same bifunctional enzyme family and places the ADH domain at residues 457-867.


sequence_source: AdhE alcohol dehydrogenase domain residues 457-867, anchored by PDB 3ZDR chain A (engineered ADH-domain construct from Geobacillus/Parageobacillus thermoglucosidasius) and cross-checked against the corresponding residues 457-867 of NCBI Protein GAJ43611.1.

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


sequence_source: NCBI Protein GAJ43611.1 adhE full-length aldehyde dehydrogenase/alcohol dehydrogenase from Parageobacillus thermoglucosidasius NBRC 107763; cross-checked against PDB 3ZDR to distinguish wild-type full-length enzyme from the separate ADH-domain construct.


sequence_source: AdhE alcohol dehydrogenase domain residues 457-867, anchored by PDB 3ZDR chain A and cross-checked against the corresponding 457-867 region of NCBI Protein GAJ43611.1.


organism: Saccharomyces pastorianus

substrate_name: benzaldehyde

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

assay_conditions_summary: pH 7.3; cofactor NADH

substrate: benzaldehyde


substrate_name: p-Methoxybenzaldehyde

substrate: p-Methoxybenzaldehyde


substrate_name: p-methoxybenzyl alcohol

assay_conditions_summary: pH 7.3; cofactor NAD+

substrate: p-methoxybenzyl alcohol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Equus caballus

smiles: C(CCO)CN

proof_lines: BRENDA lists 4-amino-1-butanol as a horse liver ADH substrate for Equus caballus with Km 3.8 mM at pH 11.0 and 95% conversion.


smiles: C(CCCO)CCN

column_label: Table 1, Kinetic Parameters of HLADH Toward Amino Alcohols; row 6-amino-1-hexanolb; column KM, sub (mM): 6.71 +/- 1.48 mM. Footnote b = pH 9.

raw_value_unit_evidence: Km raw_value=6.71 raw_unit=mM; table reports 6.71 +/- 1.48 mM.


smiles: C(CCN)CCO

column_label: Table 1, Kinetic Parameters of HLADH Toward Amino Alcohols; row 5-amino-1-pentanolb; column KM, sub (mM): 29.6 +/- 16.9 mM. Footnote b = pH 9.

raw_value_unit_evidence: Km raw_value=29.6 raw_unit=mM; table reports 29.6 +/- 16.9 mM.


substrate_name: D-sorbitol (at pH 7.4)

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

substrate: D-sorbitol (at pH 7.4)


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: L-iditol 2-dehydrogenase

substrate_name: NADH

enzyme: L-iditol 2-dehydrogenase


substrate_name: D-xylitol

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

substrate: D-xylitol


substrate_name: D-sorbitol

substrate: D-sorbitol


substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-ribulose

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

substrate: D-ribulose


substrate_name: L-Threitol

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

proof_lines:
bovine lens sorbitol dehydrogenase
xylitol
sorbitol

substrate: L-Threitol


organism: Gallus gallus


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: L-arabinitol 4-dehydrogenase

organism: Meyerozyma caribbica

substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: PMID 27506274 abstract-only context for Meyerozyma caribbica 5XY2 xylitol dehydrogenase

proof_lines: broad polyol specificity with xylitol, d-sorbitol, ribitol, and l-arabitol

proof_lines: no preserved row-aligned excerpt for the NADP+ record

enzyme: L-arabinitol 4-dehydrogenase

substrate: NADP+


substrate_name: xylitol/ribitol/L-arabitol

assay_conditions_summary: pH 7

proof_lines: no preserved row-aligned excerpt for the xylitol/ribitol/L-arabitol record

substrate: xylitol/ribitol/L-arabitol


proof_lines: no preserved row-aligned excerpt for the D-sorbitol record


proof_lines: no preserved row-aligned excerpt for the NAD+ record


enzyme_display_name: L-xylulose reductase

organism: Neurospora crassa

substrate_name: xylitol

sequence_source: NCBI RefSeq XP_958988.2 / UniProt Q7S2T4 mapped from NCU09041 in PMID 17261518

proof_lines: Table 1 reports xylitol Km 1239 mM and kcat 334 min^-1 for Neurospora crassa L-xylulose reductase.

enzyme: L-xylulose reductase

substrate: xylitol


proof_lines: Table 1 reports D-ribulose Km 150 mM and kcat 7140 min^-1 for Neurospora crassa L-xylulose reductase.


substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 1; row NADPH; Km (mM) column.

normalized_value_unit_evidence: Km=0.0026 mM directly from Table 1.

raw_value_unit_evidence: Table 1 reports NADPH Km 0.0026 +/- 0.0005 mM.

row_label: NADPH

table_label: Table 1. Steady-state kinetics for N. crassa LXR

substrate: NADPH


column_label: Table 1; row NADP; Km (mM) column.

normalized_value_unit_evidence: Km=0.153 mM directly from Table 1.

raw_value_unit_evidence: Table 1 reports NADP Km 0.153 +/- 0.025 mM.

row_label: NADP


organism: Homo sapiens

substrate_name: D-xylulose

substrate: D-xylulose


substrate_name: L-erythrulose

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

substrate: L-erythrulose


enzyme_display_name: mannitol-1-phosphate 5-dehydrogenase

organism: Aspergillus fumigatus

substrate_name: D-mannitol 1-phosphate

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

assay_conditions_summary: pH 7.1; cofactor NAD+

column_label: Table 2 row Man-ol1P columns Ksubstrate (mM)=0.23+/-0.02, Kcofactor (mM)=0.75+/-0.09, kcat (s^-1)=8.5+/-0.4; prose reports Man-ol1P catalytic efficiency 3.8 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=0.23 mM; kcat normalized_value=8.5 s^-1; kcat/Km normalized_value=38 s^-1 mM^-1

raw_value_unit_evidence: Ksubstrate raw_value=0.23+/-0.02 raw_unit=mM; kcat raw_value=8.5+/-0.4 raw_unit=s^-1; catalytic efficiency raw_value=3.8 x 10^4 raw_unit=M^-1 s^-1

enzyme: mannitol-1-phosphate 5-dehydrogenase

substrate: D-mannitol 1-phosphate


substrate_name: D-fructose 6-phosphate

substrate: D-fructose 6-phosphate


column_label: Table 2 row Man-ol1P column Kcofactor (mM)=0.75+/-0.09; methods say NAD+ was varied with Man-ol1P held saturating.

normalized_value_unit_evidence: Km normalized_value=0.75 mM

raw_value_unit_evidence: Kcofactor raw_value=0.75+/-0.09 raw_unit=mM for NAD+ in Man-ol1P oxidation

row_label: Man-ol1P / Kcofactor


enzyme_display_name: D-arabinitol 4-dehydrogenase

organism: Candida tropicalis

assay_conditions_summary: cofactor NAD+

enzyme: D-arabinitol 4-dehydrogenase


substrate_name: D-arabinitol

substrate: D-arabinitol


organism: Trichoderma reesei

substrate_name: L-arabinitol

substrate: L-arabinitol


substrate_name: NAD+

substrate: NAD+


organism: Aspergillus niger


organism: Staphylococcus aureus

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

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: diacetyl

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

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

assay_conditions_summary: buffer Evidence used: the selected batch payload

proof_lines: mutant enzyme C138A, in 10 mM potassium phosphate buffer

substrate: diacetyl


organism: Erwinia sp.


organism: Pantoea ananatis


organism: Meyerozyma guilliermondii


organism: [Candida] arabinofermentans


organism: Ovis aries


substrate_name: D-xylitol

substrate: D-xylitol


organism: Malus domestica


organism: Gluconobacter oxydans

proof_lines: pH 7.0, 25°C, recombinant His-tagged enzyme


organism: Acinetobacter baylyi


organism: Eimeria tenella

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines:
cofactor NADH, 41°C, pH 7.5
cofactor NADPH, 41°C, pH 7.5


proof_lines: kcat is 1.6 sec(-1) with diacetyl as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11882650, PubMed:15103634). kcat is 0.65 sec(-1) with L-xylulose as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11882650). kcat is 0.48 sec(-


organism: Caenorhabditis elegans

substrate_name: L-(+) erythrulose (at 25 degrees Celsius)

proof_lines: The KM value for isatin is approximate as substrate saturation was not reached.


organism: Rattus norvegicus

proof_lines: kcat is 25 sec(-1) with diacetyl as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11882650). kcat is 39 sec(-1) with L-xylulose as substrate (at pH 7.0 and 25 degrees Celsius) (PubMed:11882650). kcat is 22 sec(-1) with 1,4-dibromo-2,


organism: Hypocrea jecorina (strain QM6a)


organism: Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7)


organism: Hypocrea jecorina

substrate_name: D-arabino-3-hexulose (at pH 8.6)

substrate: D-arabino-3-hexulose (at pH 8.6)


organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)


enzyme_display_name: Sorbitol dehydrogenase

proof_lines: kcat is 8 sec(-1) for sorbitol oxidation and 190 sec(-1) for D-fructose reduction.

enzyme: Sorbitol dehydrogenase


enzyme_display_name: NADH-dependent L-xylulose reductase

organism: Ambrosiozyma monospora

enzyme: NADH-dependent L-xylulose reductase


organism: Brochothrix thermosphacta

assay_conditions_summary: cofactor ATP


organism: Unknown

substrate_name: SPC_22969_Cell; SPC_1262_Cell

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

substrate: SPC_22969_Cell; SPC_1262_Cell


substrate_name: SPC_2078_Cell; SPC_37_Cell

substrate: SPC_2078_Cell; SPC_37_Cell


substrate_name: SPC_2156_Cell; SPC_37_Cell

substrate: SPC_2156_Cell; SPC_37_Cell


substrate_name: SPC_38_Cell; SPC_1374_Cell

substrate: SPC_38_Cell; SPC_1374_Cell


enzyme_display_name: inositol 2-dehydrogenase

organism: Bacillus subtilis

substrate_name: myo-inositol

sequence_variant_note: Resolved canonical sequence from uniprotkb:P26935 and applied mutation signature H176A to reconstruct the assayed variant sequence.

enzyme: inositol 2-dehydrogenase

substrate: myo-inositol


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26935 and applied mutation signature D172N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26935 and applied mutation signature Y235F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26935 and applied mutation signature Y233F 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.

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


sequence_variant_note: Resolved canonical sequence from uniprotkb:P26935 and applied mutation signature D179N to reconstruct the assayed variant sequence.


enzyme_display_name: shikimate dehydrogenase (NADP+)

organism: Toxoplasma gondii

substrate_name: shikimate

proof_lines: pH 8.8, temperature not specified in the publication

enzyme: shikimate dehydrogenase (NADP+)

substrate: shikimate


organism: Eucalyptus camaldulensis

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

proof_lines: pH 8.5, temperature not specified in the publication

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


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


organism: Aspergillus nidulans

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


substrate_name: myo-Inositol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D172N to reconstruct the assayed variant sequence.

substrate: myo-Inositol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D179N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H176A with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y233F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y235F to reconstruct the assayed variant sequence.


enzyme_display_name: glucuronate reductase

organism: Penicillium camemberti

substrate_name: D-galacturonate

enzyme: glucuronate reductase

substrate: D-galacturonate


substrate_name: NADH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

substrate: NADPH


substrate_name: D-Glucuronate

substrate: D-Glucuronate


enzyme_display_name: aldose reductase

organism: Homo sapiens

enzyme: aldose reductase


organism: Candida tenuis

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

smiles: NCC(F)(F)F


organism: Bos taurus


smiles: CC(F)CN


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 `3Br`: kcat (s^-1) = 15.6 +/- 4.1; Kaldehyde (mM) = 5.1 +/- 1.7; kcat/Kaldehyde (M^-1 s^-1) = 3066.

normalized_value_unit_evidence: kcat: printed cell 15.6 s^-1 -> 15.6 s^(-1) (unit already canonical); the exported value is 15.6 s^(-1). Km: printed Kaldehyde cell 5.1 mM -> 5.1 mM (unit already canonical); the exported value is 5.1 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 3066 M^-1 s^-1 for this substrate line -> 3.0660000000000003 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 3.058823529411765 s^(-1)*mM^(-1).

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

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


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `3Cl`: kcat (s^-1) = 13.9 +/- 0.6; Kaldehyde (mM) = 3.5 +/- 0.3; kcat/Kaldehyde (M^-1 s^-1) = 3957.

normalized_value_unit_evidence: kcat: printed cell 13.9 s^-1 -> 13.9 s^(-1) (unit already canonical); the exported value is 13.9 s^(-1). Km: printed Kaldehyde cell 3.5 mM -> 3.5 mM (unit already canonical); the exported value is 3.5 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 3957 M^-1 s^-1 for this substrate line -> 3.9570000000000003 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 3.9714285714285715 s^(-1)*mM^(-1).

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


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

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

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


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


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

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

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


organism: Debaryomyces nepalensis


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 `3-O-Methylglucose`: Km (mM) = 150; kcat (s^-1) = 0.06; 10^3 x kcat/Km (M^-1 s^-1) = 0.0004.

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

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

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


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

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

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


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4Cl`: kcat (s^-1) = 18.5 +/- 0.7; Kaldehyde (mM) = 1.8 +/- 0.2; kcat/Kaldehyde (M^-1 s^-1) = 10572.

normalized_value_unit_evidence: kcat: printed cell 18.5 s^-1 -> 18.5 s^(-1) (unit already canonical); the exported value is 18.5 s^(-1). Km: printed Kaldehyde cell 1.8 mM -> 1.8 mM (unit already canonical); the exported value is 1.8 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 10572 M^-1 s^-1 for this substrate line -> 10.572000000000001 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 10.277777777777777 s^(-1)*mM^(-1).

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


column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `4CN`: kcat (s^-1) = 17.2 +/- 1.1; Kaldehyde (mM) = 1.7 +/- 0.2; kcat/Kaldehyde (M^-1 s^-1) = 10131.

normalized_value_unit_evidence: kcat: printed cell 17.2 s^-1 -> 17.2 s^(-1) (unit already canonical); the exported value is 17.2 s^(-1). Km: printed Kaldehyde cell 1.7 mM -> 1.7 mM (unit already canonical); the exported value is 1.7 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 10131 M^-1 s^-1 for this substrate line -> 10.131 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 10.117647058823529 s^(-1)*mM^(-1).

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


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

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

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


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


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


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'; 9-cis-retinaldehyde column 'Km (uM)' = 0.7; 9-cis-retinaldehyde column 'kcat (min^-1)' = 0.9; 9-cis-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 1,300.

raw_value_unit_evidence: Table 1, row AKR1B10 K125L, 9-cis-retinaldehyde columns: Km = 0.7 uM; kcat = 0.9 min^-1; printed kcat/Km = 1,300 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'; 9-cis-retinaldehyde column 'Km (uM)' = 0.30; 9-cis-retinaldehyde column 'kcat (min^-1)' = 0.60; 9-cis-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 1,800.

raw_value_unit_evidence: Table 1, row AKR1B10 V301L, 9-cis-retinaldehyde columns: Km = 0.30 uM; kcat = 0.60 min^-1; printed kcat/Km = 1,800 mM^-1 min^-1.


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'; 9-cis-retinaldehyde column 'Km (uM)' = 0.7; 9-cis-retinaldehyde column 'kcat (min^-1)' = 0.9; 9-cis-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 1,300.

raw_value_unit_evidence: Table 1, row AKR1B10, 9-cis-retinaldehyde columns: Km = 0.7 uM; kcat = 0.9 min^-1; printed kcat/Km = 1,300 mM^-1 min^-1.


column_label: Table 1: Kinetic analysis for human AKRs and mutant enzymes using the BSA/HPLC method (PNAS 2007, vol. 104, no. 52), line 'AKR1B1'; 9-cis-retinaldehyde column 'Km (uM)' = 0.4; 9-cis-retinaldehyde column 'kcat (min^-1)' = 0.7; 9-cis-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 1,500.

raw_value_unit_evidence: Table 1, row AKR1B1, 9-cis-retinaldehyde columns: Km = 0.4 uM; kcat = 0.7 min^-1; printed kcat/Km = 1,500 mM^-1 min^-1.


substrate_name: Acetaldehyde

smiles: CC=O

substrate: Acetaldehyde


substrate_name: all-trans-Retinal

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'; all-trans-retinaldehyde column 'Km (uM)' = 0.15; all-trans-retinaldehyde column 'kcat (min^-1)' = 2; all-trans-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 13,100.

raw_value_unit_evidence: Table 1, row AKR1B10 K125L, all-trans-retinaldehyde columns: Km = 0.15 uM; kcat = 2 min^-1; printed kcat/Km = 13,100 mM^-1 min^-1.

substrate: all-trans-Retinal


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'; all-trans-retinaldehyde column 'Km (uM)' = 1; all-trans-retinaldehyde column 'kcat (min^-1)' = 3.5; all-trans-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 3,500.

raw_value_unit_evidence: Table 1, row AKR1B10 K125L/V301L, all-trans-retinaldehyde columns: Km = 1 uM; kcat = 3.5 min^-1; printed kcat/Km = 3,500 mM^-1 min^-1.


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'; all-trans-retinaldehyde column 'Km (uM)' = 0.6; all-trans-retinaldehyde column 'kcat (min^-1)' = 7.7; all-trans-retinaldehyde column 'kcat/Km (mM^-1 min^-1)' = 12,700.

raw_value_unit_evidence: Table 1, row AKR1B10 V301L, all-trans-retinaldehyde columns: Km = 0.6 uM; kcat = 7.7 min^-1; printed kcat/Km = 12,700 mM^-1 min^-1.


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

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

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


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

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

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


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: Benzaldehyde

column_label: Table 1 (PDF page 5 of 11, journal page 893), substrate row `BA`: kcat (s^-1) = 16.6 +/- 1.2; Kaldehyde (mM) = 15 +/- 2; kcat/Kaldehyde (M^-1 s^-1) = 1097.

normalized_value_unit_evidence: kcat: printed cell 16.6 s^-1 -> 16.6 s^(-1) (unit already canonical); the exported value is 16.6 s^(-1). Km: printed Kaldehyde cell 15 mM -> 15.0 mM (unit already canonical); the exported value is 15.0 mM. kcat/Km: the paper PRINTS the kcat/Kaldehyde cell 1097 M^-1 s^-1 for this substrate line -> 1.097 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 1.1066666666666667 s^(-1)*mM^(-1).

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

substrate: Benzaldehyde


substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: D-Galactose

substrate: D-Galactose


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 `D-Galactose`, AR column group: Km (mM) = 21.0; kcat (min^-1) = 222. Table III prints no kcat/Km cell.

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

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


substrate_name: D-Glucose

column_label: Table 2 (PDF page 4 of 7, journal page 36) 'Kinetic parameters for bovine lens aldehyde reductase', substrate row `D-Glucose`: Km (mM) = 120; kcat (s^-1) = 0.3; 10^3 x kcat/Km (M^-1 s^-1) = 0.0025.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1 is already the export unit s^(-1); the exported value is 0.3 s^(-1). Km: printed cell 120 mM is already the export unit mM; the exported value is 12.9 mM. kcat/Km: the printed efficiency cell 0.0025 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 0.0025 s^(-1)*mM^(-1); the exported value is 0.023255813953488372 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 `D-Glucose`: Km (mM) = 120; Vmax (umol/min per mg of enzyme) = 0.5; kcat (s^-1) = 0.3; 10^3 x kcat/Km (M^-1 s^-1) = 0.0025.

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

substrate: D-Glucose


organism: Sus scrofa


substrate_name: D-Glyceraldehyde

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table I (journal page 4365), substrate row `D-Glyceraldehyde`: kcat (min^-1) = 120; Km (mM) = 0.016; kcat/Km (M^-1 min^-1) = 7.5 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 120 min^-1 -> 120/60 = 2 s^-1, carried here at the export's stored precision as 2.0 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 2.0 s^(-1). Km: printed cell 0.016 mM -> 0.016 mM; the catalog holds 0.016 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 7.5 x 10^6 M^-1 min^-1 -> 7500000/(1000*60) = 125.0 s^(-1)*mM^(-1); the catalog holds 125.0 s^(-1)*mM^(-1), which equals the printed efficiency cell.

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

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

substrate: D-Glyceraldehyde


substrate_name: D-Glyceraldehyde 3-phosphate

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

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

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

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

substrate: D-Glyceraldehyde 3-phosphate


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

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

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

row_label: Table I, substrate row `Dihydroxyacetone`

substrate: Dihydroxyacetone


substrate_name: Dimethylglyoxal

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

substrate: Dimethylglyoxal


substrate_name: D-Lactaldehyde

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

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

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

substrate: D-Lactaldehyde


substrate_name: D-Lyxose

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: D-Lyxose


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

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

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

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

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

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


substrate_name: D-ribose

substrate: D-ribose


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


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.


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.


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


sequence_variant_note: Resolved canonical sequence from 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 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


substrate_name: Glucuronate

substrate: Glucuronate


substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

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