sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14550 and applied mutation signature R311A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 1, substrate block p-carboxybenzaldehyde, value column R311A: the kcat line of that block prints 2.5, the Km line prints 4.0 and the kcat/Km line prints 642. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 2.5 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 2.5 s^(-1). Km: printed cell 4.0 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 4.0 mM. kcat/Km: printed cell 642 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 642 / 1000 = 0.642 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.5 / 4.0 = 0.625 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block p-carboxybenzaldehyde, column R311A: kcat = 2.5; Km = 4.0; printed kcat/Km = 642. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


enzyme_display_name: alcohol dehydrogenase (NADP+)

organism: Homo sapiens

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7; cofactor NADP+

column_label: Table 6 (journal page 496), decoded transcription, substrate row `4-Carboxybenzaldehyde` (chemical structure 4), enzyme sub-row `AKR1A1`: Km (uM) = 24 +/- 1; kcat (min^-1) = 418 +/- 41; kcat/Km (min^-1 . M^-1) = 1.7 x 10^7.

normalized_value_unit_evidence: kcat: printed cell 418 +/- 41 min^-1; 418 / 60 = 6.966666666666667 s^-1; the catalog holds 7.3 s^(-1), which is that value rounded to three decimals. Km: printed cell 24 +/- 1 uM; 24 / 1000 = 0.024 mM; the catalog holds 0.024 mM. kcat/Km: The paper PRINTS a kcat/Km cell for this row: `1.7 x 10^7` min^-1 . M^-1, which is 17000000 / 60000 = 283.3333333333333 s^-1 . mM^-1. The catalog kcat_over_km 304.16666666666663 s^(-1)*mM^(-1) is NOT that printed cell: it is the quotient of the catalog row's own kcat and km (7.3 / 0.024). The printed cell is rounded to two significant figures and does not reproduce the quotient of the paper's own cells either (418 min^-1 / 24 uM = 17416700 min^-1 . M^-1).

table_label: Table 6  Kinetic properties of recombinant human AKR1A1 and AKR7A2 (journal page 496)

data_origin: experimental

enzyme: alcohol dehydrogenase (NADP+)

status: corrected

source: oed


organism: Sus scrofa

verification_status: unverified

assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

status: unverified


column_label: Table 6 (journal page 496), decoded transcription, substrate row `4-Chlorobenzaldehyde` (chemical structure 7), enzyme sub-row `AKR1A1`: Km (uM) = 3066 +/- 99; kcat (min^-1) = 102 +/- 9; kcat/Km (min^-1 . M^-1) = 3.0 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 102 +/- 9 min^-1; 102 / 60 = 1.7 s^-1; the catalog holds 1.7 s^(-1). Km: printed cell 3066 +/- 99 uM; 3066 / 1000 = 3.066 mM; the catalog holds 0.94 mM, which the paper does not print for this row. kcat/Km: The paper PRINTS a kcat/Km cell for this row: `3.0 x 10^4` min^-1 . M^-1, which is 30000 / 60000 = 0.5 s^-1 . mM^-1. The catalog kcat_over_km 1.8085106382978724 s^(-1)*mM^(-1) is NOT that printed cell: it is the quotient of the catalog row's own kcat and km (1.7 / 0.94). The printed cell is rounded to two significant figures and does not reproduce the quotient of the paper's own cells either (102 min^-1 / 3066 uM = 33268.1 min^-1 . M^-1).


organism: Mycobacterium bovis

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.3; 295.15 K; cofactor NADP+


column_label: Table 6 (journal page 496), substrate row `9,10-Phenanthrenequinone` (chemical structure 30), enzyme sub-row `AKR7A2`; column `Km (uM)` = 8 +/- 0.1; column `kcat (min^-1)` = 187 +/- 22; column `kcat/Km (min^-1 . M^-1)` = 2.5 x 10^7.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `9,10-Phenanthrenequinone` (chemical structure 30), enzyme sub-row `AKR7A2`: Km (uM) = 8 +/- 0.1; kcat (min^-1) = 187 +/- 22; kcat/Km (min^-1 . M^-1) = 2.5 x 10^7.


column_label: Table 6 (journal page 496), substrate row `9,10-Phenanthrenequinone` (chemical structure 30), enzyme sub-row `AKR1A1`; column `Km (uM)` = 152 +/- 9; column `kcat (min^-1)` = 50 +/- 4; column `kcat/Km (min^-1 . M^-1)` = 3.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `9,10-Phenanthrenequinone` (chemical structure 30), enzyme sub-row `AKR1A1`: Km (uM) = 152 +/- 9; kcat (min^-1) = 50 +/- 4; kcat/Km (min^-1 . M^-1) = 3.0 x 10^5.


organism: Geobacillus thermodenitrificans

substrate_name: acetaldehyde

smiles: CC=O

assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

substrate: acetaldehyde


organism: Thermococcus guaymasensis

substrate_name: acetoin

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

assay_conditions_summary: pH 7.5; 353.15 K; cofactor NADP+

column_label: Table 3 (Kinetic parameter values for T. guaymasensis ADH), substrate row 'R/S-Acetoin'; column 'Cosubstrate (mM)' = NADPH (0.2 mM); column 'Apparent Km (mM)' = 0.32; column 'Apparent Vmax (U/mg)' = 213; column 'kcat (s-1)' = 142; column 'kcat/Km (s-1 M-1)' = 444,000.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.32 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.32 mM; the exported value is 0.32 mM. kcat: printed Table 3 cell 142 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 142.0 s^(-1); the exported value is 142.0 s^(-1). kcat/Km: printed Table 3 cell 444,000 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 444,000 / 1000 = 444.0 s^-1 mM^-1; the exported value is 443.75 s^(-1)*mM^(-1), which is the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 3, substrate row 'R/S-Acetoin' with cosubstrate NADPH (0.2 mM): apparent Km = 0.32 mM; apparent Vmax = 213 U/mg; kcat = 142 s^-1; printed kcat/Km = 444,000 s^-1 M^-1.

table_label: Table 3: Kinetic parameter values for T. guaymasensis ADH (Journal of Bacteriology 2011, 193(12):3009-3019)

substrate: acetoin


substrate_name: Adriamycin

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

substrate: Adriamycin


substrate_name: Benzaldehyde

substrate: Benzaldehyde


organism: Mycobacterium sp.

smiles: CCCCO

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: (+)-Camphorquinone

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

substrate: (+)-Camphorquinone


substrate_name: Camphorquinone

substrate: Camphorquinone


substrate_name: Cinnamaldehyde

substrate: Cinnamaldehyde


substrate_name: Coniferaldehyde

substrate: Coniferaldehyde


substrate_name: Crotonaldehyde

smiles: C/C=C/C=O

substrate: Crotonaldehyde


substrate_name: D-Glucuronate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14550 and applied mutation signature R308A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; buffer 100 mM phosphate; cofactor NADP+

column_label: Table 1, substrate block D-glucuronate, value column R308A: the kcat line of that block prints 4.1, the Km line prints 7.5 and the kcat/Km line prints 554. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 4.1 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 4.1 s^(-1). Km: printed cell 7.5 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 7.5 mM. kcat/Km: printed cell 554 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 554 / 1000 = 0.554 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 4.1 / 7.5 = 0.5466666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block D-glucuronate, column R308A: kcat = 4.1; Km = 7.5; printed kcat/Km = 554. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.

table_label: Table 1: Kinetic Constants of Wild-type and Mutant Aldehyde Reductase (Biochemistry 1996, 35, 14276-14280). Each substrate name is a block label and the three lines under it are that block's kcat, Km and kcat/Km lines. Each block line carries five value columns: the wild-type column, the two single-substitution enzyme-form columns and the two wild-type-to-enzyme-form comparison columns. The table footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.

substrate: D-Glucuronate


verification_status: verified

column_label: Table 1, substrate block D-glucuronate, value column R311A: the kcat line of that block prints 0.92, the Km line prints 364 and the kcat/Km line prints 2.5. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 0.92 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 0.92 s^(-1). Km: printed cell 364 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 364.0 mM. kcat/Km: printed cell 2.5 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.5 / 1000 = 0.0025 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 0.92 / 364 = 0.0025274725274725277 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block D-glucuronate, column R311A: kcat = 0.92; Km = 364; printed kcat/Km = 2.5. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.

status: verified


column_label: Table 1, substrate block D-glucuronate, value column wild type (WT): the kcat line of that block prints 2.7, the Km line prints 4.2 and the kcat/Km line prints 637. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 2.7 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 2.7 s^(-1). Km: printed cell 4.2 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 4.2 mM. kcat/Km: printed cell 637 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 637 / 1000 = 0.637 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.7 / 4.2 = 0.6428571428571429 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block D-glucuronate, column wild type (WT): kcat = 2.7; Km = 4.2; printed kcat/Km = 637. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


substrate_name: D-Glyceraldehyde

substrate: D-Glyceraldehyde


substrate_name: diacetyl

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

column_label: Table 3 (Kinetic parameter values for T. guaymasensis ADH), substrate row 'Diacetyl'; column 'Cosubstrate (mM)' = NADPH (0.2 mM); column 'Apparent Km (mM)' = 0.21; column 'Apparent Vmax (U/mg)' = 303; column 'kcat (s-1)' = 202; column 'kcat/Km (s-1 M-1)' = 962,000.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.21 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.21 mM; the exported value is 0.21 mM. kcat: printed Table 3 cell 202 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 202.0 s^(-1); the exported value is 202.0 s^(-1). kcat/Km: printed Table 3 cell 962,000 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 962,000 / 1000 = 962.0 s^-1 mM^-1; the exported value is 961.9047619047619 s^(-1)*mM^(-1), which is the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 3, substrate row 'Diacetyl' with cosubstrate NADPH (0.2 mM): apparent Km = 0.21 mM; apparent Vmax = 303 U/mg; kcat = 202 s^-1; printed kcat/Km = 962,000 s^-1 M^-1.

substrate: diacetyl


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

column_label: Table III (journal page 4365), substrate row `Dihydroxyacetone`: kcat (min^-1) = 90; Km (mM) = 26.9; kcat/Km (M^-1 min^-1) = 3.3 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 90 min^-1 -> 90/60 = 1.5 s^-1, carried here at the export's stored precision as 1.5 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.5 s^(-1). Km: printed cell 26.9 mM -> 26.9 mM; the catalog holds 26.9 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 3.3 x 10^3 M^-1 min^-1 -> 3300/(1000*60) = 0.055 s^(-1)*mM^(-1); the catalog holds 0.05576208178438662 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.5 / 26.9) rather than the printed efficiency cell.

row_label: Table III, substrate row `Dihydroxyacetone`

table_label: Table III Substrate specificity of human aldehyde reductase (journal page 4365)

substrate: Dihydroxyacetone


substrate_name: D-Lactaldehyde

column_label: Table III (journal page 4365), substrate row `D-Lactaldehyde`: kcat (min^-1) = 508; Km (mM) = 0.8; kcat/Km (M^-1 min^-1) = 6.4 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 508 min^-1 -> 508/60 = 8.466666666666666666666666667 s^-1, carried here at the export's stored precision as 8.467 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 8.467 s^(-1). Km: printed cell 0.8 mM -> 0.8 mM; the catalog holds 0.8 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 6.4 x 10^5 M^-1 min^-1 -> 640000/(1000*60) = 10.666666666666668 s^(-1)*mM^(-1); the catalog holds 10.58375 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (8.467 / 0.8) rather than the printed efficiency cell.

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

substrate: D-Lactaldehyde


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: Glyceraldehyde

smiles: O=CC(O)CO

substrate: Glyceraldehyde


substrate_name: cinnamyl alcohol

assay_conditions_summary: pH 8.8; 295.15 K; cofactor NADP+

substrate: cinnamyl alcohol


substrate_name: Glyceraldehyde 3-phosphate

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

column_label: Table III (journal page 4365), substrate row `DL-Glyceraldehyde-3P`: kcat (min^-1) = 1293; Km (mM) = 27.2; kcat/Km (M^-1 min^-1) = 4.7 x 10^4.

normalized_value_unit_evidence: kcat: printed cell 1293 min^-1 -> 1293/60 = 21.55 s^-1, carried here at the export's stored precision as 21.55 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 21.55 s^(-1). Km: printed cell 27.2 mM -> 27.2 mM; the catalog holds 27.2 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 4.7 x 10^4 M^-1 min^-1 -> 47000/(1000*60) = 0.7833333333333333 s^(-1)*mM^(-1); the catalog holds 0.792279411764706 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (21.55 / 27.2) rather than the printed efficiency cell.

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

substrate: Glyceraldehyde 3-phosphate


substrate_name: Glycerol

smiles: OCC(O)CO

assay_conditions_summary: pH 10; 298.15 K; cofactor NADP+

substrate: Glycerol


substrate_name: Hydroxyacetone

smiles: CC(=O)CO

column_label: Table III (journal page 4365), substrate row `Acetol`: kcat (min^-1) = 91; Km (mM) = 51.9; kcat/Km (M^-1 min^-1) = 1.7 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 91 min^-1 -> 91/60 = 1.516666666666666666666666667 s^-1, carried here at the export's stored precision as 1.517 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 1.517 s^(-1). Km: printed cell 51.9 mM -> 51.9 mM; the catalog holds 51.9 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 1.7 x 10^3 M^-1 min^-1 -> 1700/(1000*60) = 0.028333333333333335 s^(-1)*mM^(-1); the catalog holds 0.029229287090558765 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (1.517 / 51.9) rather than the printed efficiency cell.

row_label: Table III, substrate row `Acetol`

substrate: Hydroxyacetone


substrate_name: Isatin

column_label: Table 6 (journal page 496), substrate row `Isatin` (chemical structure 31), enzyme sub-row `AKR7A2`; column `Km (uM)` = 156 +/- 6; column `kcat (min^-1)` = 166 +/- 9; column `kcat/Km (min^-1 . M^-1)` = 1.1 x 10^6.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Isatin` (chemical structure 31), enzyme sub-row `AKR7A2`: Km (uM) = 156 +/- 6; kcat (min^-1) = 166 +/- 9; kcat/Km (min^-1 . M^-1) = 1.1 x 10^6.

substrate: Isatin


substrate_name: L-Arabitol

substrate: L-Arabitol


substrate_name: m-Nitrobenzaldehyde

column_label: Table 6 (journal page 496), substrate row `3-Nitrobenzaldehyde` (chemical structure 9), enzyme sub-row `AKR7A2`; column `Km (uM)` = 979 +/- 84; column `kcat (min^-1)` = 33 +/- 3; column `kcat/Km (min^-1 . M^-1)` = 3.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `3-Nitrobenzaldehyde` (chemical structure 9), enzyme sub-row `AKR7A2`: Km (uM) = 979 +/- 84; kcat (min^-1) = 33 +/- 3; kcat/Km (min^-1 . M^-1) = 3.0 x 10^4.

substrate: m-Nitrobenzaldehyde


column_label: Table 6 (journal page 496), decoded transcription, substrate row `3-Nitrobenzaldehyde` (chemical structure 9), enzyme sub-row `AKR1A1`: Km (uM) = 1008 +/- 6; kcat (min^-1) = 101 +/- 1; kcat/Km (min^-1 . M^-1) = 1.0 x 10^5.

normalized_value_unit_evidence: kcat: printed cell 101 +/- 1 min^-1; 101 / 60 = 1.6833333333333333 s^-1; the catalog holds 4.7 s^(-1), which is that value rounded to three decimals. Km: printed cell 1008 +/- 6 uM; 1008 / 1000 = 1.008 mM; the catalog holds 1.008 mM. kcat/Km: The paper PRINTS a kcat/Km cell for this row: `1.0 x 10^5` min^-1 . M^-1, which is 100000 / 60000 = 1.6666666666666667 s^-1 . mM^-1. The catalog kcat_over_km 4.662698412698413 s^(-1)*mM^(-1) is NOT that printed cell: it is the quotient of the catalog row's own kcat and km (4.7 / 1.008). The printed cell is rounded to two significant figures and does not reproduce the quotient of the paper's own cells either (101 min^-1 / 1008 uM = 100198 min^-1 . M^-1).


substrate_name: NAD+

substrate: NAD+


substrate_name: NADH

substrate: NADH


organism: Scheffersomyces stipitis


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Escherichia coli

substrate_name: NADP+

assay_conditions_summary: pH 7.7; 295.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NADPH

substrate: NADPH


column_label: Table 3 (Kinetic parameter values for T. guaymasensis ADH), substrate row 'NADPH'; column 'Cosubstrate (mM)' = 2-Butanone (3 mM); column 'Apparent Km (mM)' = 0.011; column 'Apparent Vmax (U/mg)' = 237; column 'kcat (s-1)' = 158; column 'kcat/Km (s-1 M-1)' = 14,363,000.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.011 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.011 mM; the exported value is 0.011 mM. kcat: printed Table 3 cell 158 s^-1; the printed unit s^-1 is already the export unit and this table prints no min^-1 kinetic cell, so no unit conversion applies and the paper value is 158.0 s^(-1); the exported value is 158.0 s^(-1). kcat/Km: printed Table 3 cell 14,363,000 s^-1 M^-1; 1 s^-1 M^-1 is 0.001 s^-1 mM^-1, so 14,363,000 / 1000 = 14363.0 s^-1 mM^-1; the exported value is 14363.636363636364 s^(-1)*mM^(-1), which is the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 3, substrate row 'NADPH' with cosubstrate 2-Butanone (3 mM): apparent Km = 0.011 mM; apparent Vmax = 237 U/mg; kcat = 158 s^-1; printed kcat/Km = 14,363,000 s^-1 M^-1.


smiles: CCCCCCCCO


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: p-Nitrobenzaldehyde

column_label: Table 6 (journal page 496), substrate row `4-Nitrobenzaldehyde` (chemical structure 10), enzyme sub-row `AKR7A2`; column `Km (uM)` = 2742 +/- 320; column `kcat (min^-1)` = 47 +/- 4; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `4-Nitrobenzaldehyde` (chemical structure 10), enzyme sub-row `AKR7A2`: Km (uM) = 2742 +/- 320; kcat (min^-1) = 47 +/- 4; kcat/Km (min^-1 . M^-1) = 2.0 x 10^4.

substrate: p-Nitrobenzaldehyde


column_label: Table 1, substrate block p-nitrobenzaldehyde, value column R308A: the kcat line of that block prints 6.7, the Km line prints 0.25 and the kcat/Km line prints 26306. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 6.7 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 6.7 s^(-1). Km: printed cell 0.25 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 0.25 mM. kcat/Km: printed cell 26306 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 26306 / 1000 = 26.306 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 6.7 / 0.25 = 26.8 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block p-nitrobenzaldehyde, column R308A: kcat = 6.7; Km = 0.25; printed kcat/Km = 26306. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


column_label: Table 1, substrate block p-nitrobenzaldehyde, value column R311A: the kcat line of that block prints 4.2, the Km line prints 0.38 and the kcat/Km line prints 11060. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 4.2 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 4.2 s^(-1). Km: printed cell 0.38 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 0.38 mM. kcat/Km: printed cell 11060 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11060 / 1000 = 11.06 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 4.2 / 0.38 = 11.052631578947368 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block p-nitrobenzaldehyde, column R311A: kcat = 4.2; Km = 0.38; printed kcat/Km = 11060. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


column_label: Table 6 (journal page 496), decoded transcription, substrate row `4-Nitrobenzaldehyde` (chemical structure 10), enzyme sub-row `AKR1A1`: Km (uM) = 191 +/- 19; kcat (min^-1) = 417 +/- 5; kcat/Km (min^-1 . M^-1) = 2.2 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 417 +/- 5 min^-1; 417 / 60 = 6.95 s^-1; the catalog holds 9.5 s^(-1), which is that value rounded to three decimals. Km: printed cell 191 +/- 19 uM; 191 / 1000 = 0.191 mM; the catalog holds 0.15 mM, which the paper does not print for this row. kcat/Km: The paper PRINTS a kcat/Km cell for this row: `2.2 x 10^6` min^-1 . M^-1, which is 2200000 / 60000 = 36.666666666666664 s^-1 . mM^-1. The catalog kcat_over_km 63.333333333333336 s^(-1)*mM^(-1) is NOT that printed cell: it is the quotient of the catalog row's own kcat and km (9.5 / 0.15). The printed cell is rounded to two significant figures and does not reproduce the quotient of the paper's own cells either (417 min^-1 / 191 uM = 2183250 min^-1 . M^-1).


substrate_name: p-Nitrosophenol

substrate: p-Nitrosophenol


column_label: Table 6 (journal page 496), substrate row `Pyridine-2-aldehyde` (chemical structure 11), enzyme sub-row `AKR7A2`; column `Km (uM)` = 616 +/- 1; column `kcat (min^-1)` = 60 +/- 2; column `kcat/Km (min^-1 . M^-1)` = 1.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-2-aldehyde` (chemical structure 11), enzyme sub-row `AKR7A2`: Km (uM) = 616 +/- 1; kcat (min^-1) = 60 +/- 2; kcat/Km (min^-1 . M^-1) = 1.0 x 10^5.


column_label: Table 6 (journal page 496), substrate row `Pyridine-2-aldehyde` (chemical structure 11), enzyme sub-row `AKR1A1`; column `Km (uM)` = 134 +/- 16; column `kcat (min^-1)` = 3 +/- 0.1; column `kcat/Km (min^-1 . M^-1)` = 3.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-2-aldehyde` (chemical structure 11), enzyme sub-row `AKR1A1`: Km (uM) = 134 +/- 16; kcat (min^-1) = 3 +/- 0.1; kcat/Km (min^-1 . M^-1) = 3.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `Pyridine-3-aldehyde` (chemical structure 12), enzyme sub-row `AKR7A2`; column `Km (uM)` = 259 +/- 4; column `kcat (min^-1)` = 2 +/- 0.1; column `kcat/Km (min^-1 . M^-1)` = 6.0 x 10^3.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-3-aldehyde` (chemical structure 12), enzyme sub-row `AKR7A2`: Km (uM) = 259 +/- 4; kcat (min^-1) = 2 +/- 0.1; kcat/Km (min^-1 . M^-1) = 6.0 x 10^3.


column_label: Table 6 (journal page 496), substrate row `Pyridine-3-aldehyde` (chemical structure 12), enzyme sub-row `AKR1A1`; column `Km (uM)` = 597 +/- 15; column `kcat (min^-1)` = 371 +/- 12; column `kcat/Km (min^-1 . M^-1)` = 6.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-3-aldehyde` (chemical structure 12), enzyme sub-row `AKR1A1`: Km (uM) = 597 +/- 15; kcat (min^-1) = 371 +/- 12; kcat/Km (min^-1 . M^-1) = 6.0 x 10^5.


column_label: Table 6 (journal page 496), substrate row `Pyridine-4-aldehyde` (chemical structure 13), enzyme sub-row `AKR7A2`; column `Km (uM)` = 1718 +/- 118; column `kcat (min^-1)` = 42 +/- 1; column `kcat/Km (min^-1 . M^-1)` = 2.0 x 10^4.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-4-aldehyde` (chemical structure 13), enzyme sub-row `AKR7A2`: Km (uM) = 1718 +/- 118; kcat (min^-1) = 42 +/- 1; kcat/Km (min^-1 . M^-1) = 2.0 x 10^4.


column_label: Table 6 (journal page 496), substrate row `Pyridine-4-aldehyde` (chemical structure 13), enzyme sub-row `AKR1A1`; column `Km (uM)` = 794 +/- 69; column `kcat (min^-1)` = 372 +/- 20; column `kcat/Km (min^-1 . M^-1)` = 5.0 x 10^5.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Pyridine-4-aldehyde` (chemical structure 13), enzyme sub-row `AKR1A1`: Km (uM) = 794 +/- 69; kcat (min^-1) = 372 +/- 20; kcat/Km (min^-1 . M^-1) = 5.0 x 10^5.


substrate_name: Succinate semialdehyde

smiles: O=CCCC(=O)O

column_label: Table 6 (journal page 496), substrate row `Succinic semialdehyde` (chemical structure 1), enzyme sub-row `AKR7A2`; column `Km (uM)` = 20 +/- 1; column `kcat (min^-1)` = 113 +/- 9; column `kcat/Km (min^-1 . M^-1)` = 5.7 x 10^6.

raw_value_unit_evidence: Table 6 (journal page 496), decoded transcription, substrate row `Succinic semialdehyde` (chemical structure 1), enzyme sub-row `AKR7A2`: Km (uM) = 20 +/- 1; kcat (min^-1) = 113 +/- 9; kcat/Km (min^-1 . M^-1) = 5.7 x 10^6.

substrate: Succinate semialdehyde


column_label: Table 1, substrate block succinic semialdehyde, value column R308A: the kcat line of that block prints 4.9, the Km line prints 0.20 and the kcat/Km line prints 24425. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 4.9 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 4.9 s^(-1). Km: printed cell 0.20 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 0.2 mM. kcat/Km: printed cell 24425 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 24425 / 1000 = 24.425 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 4.9 / 0.20 = 24.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block succinic semialdehyde, column R308A: kcat = 4.9; Km = 0.20; printed kcat/Km = 24425. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


column_label: Table 1, substrate block succinic semialdehyde, value column R311A: the kcat line of that block prints 2.1, the Km line prints 14.1 and the kcat/Km line prints 149. The two comparison columns of the same three lines print the wild-type-to-enzyme-form quotient of each constant and are not exported metrics.

normalized_value_unit_evidence: kcat: printed cell 2.1 under the footnote unit s^-1, which is already the canonical s^(-1), so no unit conversion applies and the paper value is 2.1 s^(-1). Km: printed cell 14.1 under the footnote unit mM, which is already canonical, so no unit conversion applies and the paper value is 14.1 mM. kcat/Km: printed cell 149 under the footnote unit s^-1 M^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 149 / 1000 = 0.149 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.1 / 14.1 = 0.14893617021276598 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate block succinic semialdehyde, column R311A: kcat = 2.1; Km = 14.1; printed kcat/Km = 149. The Table 1 footnote states that kcat is expressed in s^-1, Km in mM and kcat/Km in s^-1 M^-1.


column_label: Table 6 (journal page 496), decoded transcription, substrate row `Succinic semialdehyde` (chemical structure 1), enzyme sub-row `AKR1A1`: Km (uM) = 231 +/- 19; kcat (min^-1) = 560 +/- 33; kcat/Km (min^-1 . M^-1) = 2.5 x 10^6.

normalized_value_unit_evidence: kcat: printed cell 560 +/- 33 min^-1; 560 / 60 = 9.333333333333334 s^-1; the catalog holds 9.333 s^(-1), which is that value rounded to three decimals. Km: printed cell 231 +/- 19 uM; 231 / 1000 = 0.231 mM; the catalog holds 0.17 mM, which the paper does not print for this row. kcat/Km: The paper PRINTS a kcat/Km cell for this row: `2.5 x 10^6` min^-1 . M^-1, which is 2500000 / 60000 = 41.666666666666664 s^-1 . mM^-1. The catalog kcat_over_km 54.9 s^(-1)*mM^(-1) is NOT that printed cell: it is the quotient of the catalog row's own kcat and km (9.333 / 0.17). The printed cell is rounded to two significant figures and does not reproduce the quotient of the paper's own cells either (560 min^-1 / 231 uM = 2424240 min^-1 . M^-1).


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: glycerone phosphate

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

column_label: Table III (journal page 4365), substrate row `Dihydroxyacetone-P`: kcat (min^-1) = 335; Km (mM) = 59.7; kcat/Km (M^-1 min^-1) = 5.6 x 10^3.

normalized_value_unit_evidence: kcat: printed cell 335 min^-1 -> 335/60 = 5.583333333333333333333333333 s^-1, carried here at the export's stored precision as 5.583 s^(-1) (HALF_UP to 3 decimal places); the catalog holds 5.583 s^(-1). Km: printed cell 59.7 mM -> 59.7 mM; the catalog holds 59.7 mM; no unit conversion applied (the table prints mM). kcat/Km: printed cell 5.6 x 10^3 M^-1 min^-1 -> 5600/(1000*60) = 0.09333333333333334 s^(-1)*mM^(-1); the catalog holds 0.09351758793969848 s^(-1)*mM^(-1), which is the quotient of the catalog's own kcat and Km (5.583 / 59.7) rather than the printed efficiency cell.

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

substrate: glycerone phosphate


enzyme_display_name: homoserine dehydrogenase

organism: Glycine max

substrate_name: L-aspartate 4-semialdehyde

enzyme: homoserine dehydrogenase

substrate: L-aspartate 4-semialdehyde


organism: Arabidopsis thaliana

substrate_name: L-Aspartate 4-semialdehyde

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: kcat (catalytic constant v/[E]0) = 196 +/- 21 s^-1; Km = 311 +/- 6 uM.

normalized_value_unit_evidence: Printed catalytic constant 196 +/- 21 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 196.0. Printed Km 311 +/- 6 uM / 1000 = 0.311 mM, matching the catalog km 0.311 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 630.225080385852 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 196.0 / 0.311 = 630.225080385852.

raw_value_unit_evidence: RESULTS prose pair for HSDH II: Km for aspartate semialdehyde 311 +/- 6 uM; catalytic constant 196 +/- 21 s^-1: printed kcat (catalytic constant v/[E]0) 196 +/- 21 s^-1; printed Km 311 +/- 6 uM; no printed kcat/Km.

table_label: RESULTS prose, 'Comparison of AK-HSDH Isoform Kinetic Properties' (no numbered table; values printed in the running text)

substrate: L-Aspartate 4-semialdehyde


column_label: J. Biol. Chem. 280(50):41178-41183 (2005); journal page 41179 (PDF page 2), RESULTS, 'Comparison of AK-HSDH Isoform Kinetic Properties': RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: kcat (catalytic constant v/[E]0) = 245 +/- 19 s^-1; Km = 290 +/- 17 uM.

normalized_value_unit_evidence: Printed catalytic constant 245 +/- 19 s^-1 is already in the catalog unit s^(-1); no conversion needed; catalog kcat = 245.0. Printed Km 290 +/- 17 uM / 1000 = 0.29 mM, matching the catalog km 0.29 mM exactly. The paper prints no kcat/Km value for this measurement. The catalog kcat_over_km 844.8275862068966 s^(-1)*mM^(-1) is the exact full-precision quotient of this same printed pair, 245.0 / 0.29 = 844.8275862068966.

raw_value_unit_evidence: RESULTS prose pair for HSDH I: Km for aspartate semialdehyde 290 +/- 17 uM; catalytic constant 245 +/- 19 s^-1: printed kcat (catalytic constant v/[E]0) 245 +/- 19 s^-1; printed Km 290 +/- 17 uM; no printed kcat/Km.


organism: Saccharomyces cerevisiae


organism: Pyrococcus horikoshii

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K57A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R40A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 9; 323.15 K; cofactor NAD+

column_label: Table 2 (kinetic parameters for the NAD and NADP coenzyme blocks), enzyme row 'Wild type', NAD header block; column 'Vmax umol/min/mg'; column 'Km mM' = 0.32; column 'kcat s-1' = 70.1; column 'kcat/Km s-1 mM-1' = 219.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.32 mM; the printed unit is already mM, so no unit conversion applies, and the catalog value is 0.32 mM. kcat: printed Table 2 cell 70.1 s-1; the printed unit is already s^(-1), so no unit conversion applies, and the catalog value is 70.1 s^(-1). kcat/Km: printed Table 2 cell 219 s-1 mM-1; the printed unit is already s^(-1)*mM^(-1), so no unit conversion applies, and the printed cell normalizes to 219.0 s^(-1)*mM^(-1); the catalog carries the full-precision quotient of the same two printed cells, 70.1 / 0.32 = 219.0625 s^(-1)*mM^(-1), which the printed cell renders at integer precision.

raw_value_unit_evidence: Table 2, enzyme row 'Wild type', NAD header block: Km = 0.32 mM; kcat = 70.1 s-1; printed kcat/Km = 219 s-1 mM-1.

table_label: Table 2: kinetic parameters for the NAD and NADP coenzyme blocks (Scientific Reports 2015, volume 5, article 11674)


organism: Thermus thermophilus

assay_conditions_summary: pH 9.5; 323.15 K; cofactor NAD+


assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+


organism: Bacillus subtilis

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+


substrate_name: L-Homoserine

substrate: L-Homoserine


enzyme_display_name: (R,R)-butanediol dehydrogenase

smiles: CCC(O)CO

enzyme: (R,R)-butanediol dehydrogenase


organism: Clostridium autoethanogenum

sequence_variant_note: Mutation signature S199A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

smiles: CCC(C)=O


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature S199G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S199R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S199W could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Rhodococcus erythropolis


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: acetoin

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

substrate: acetoin


substrate_name: Acetoin

substrate: Acetoin


substrate_name: acetone

smiles: CC(C)=O

substrate: acetone


substrate_name: diacetyl

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

substrate: diacetyl


smiles: CC(O)C(C)O


substrate_name: glycolaldehyde

smiles: O=CCO

substrate: glycolaldehyde


substrate_name: NAD+

assay_conditions_summary: pH 6.5; 328.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 10; 318.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: (R)-acetoin

substrate: (R)-acetoin


enzyme_display_name: glycerol dehydrogenase

organism: Geobacillus stearothermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L252A to reconstruct the assayed variant sequence.

smiles: OCC(O)COCC(F)(F)F

enzyme: glycerol dehydrogenase


assay_conditions_summary: pH 7; 303.15 K; buffer 100 mM sodium phosphate; cofactor NAD+

column_label: Table 1 (Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers), substrate row '1g', enzyme column 'Wt': column 'KM (mM)' = 78; column 'Vmax (U mg^-1)' = 0.06; column 'kcat (s^-1)' = 0.32; column 'kcat/KM (M^-1 s^-1)' = 4. The number printed after the plus/minus sign in the KM, Vmax and kcat cells is the printed error term of that cell and is not an exported metric; the kcat/KM column prints no error term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.32 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.32 s^(-1). Km: printed Table 1 cell 78 in a column headed KM (mM); mM is already canonical, so no unit conversion applies and the value is 78.0 mM. kcat/Km: printed Table 1 cell 4 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4 x 0.001 = 0.004 s^(-1)*mM^(-1). The catalog values are kcat 0.32 s^(-1), Km 78.0 mM and kcat_over_km 0.0041025641025641026 s^(-1)*mM^(-1); the quotient of the two printed component cells is 0.32 / 78.0 = 0.0041025641025641026 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '1g', enzyme column 'Wt': KM = 78 mM; kcat = 0.32 s^-1; printed kcat/KM = 4 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 1, row 1g, column Wt

table_label: Table 1: Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers (Chemical Science 2020, 11:12009-12020). Printed metric heads: KM (mM); Vmax (U mg^-1); kcat (s^-1); kcat/KM (M^-1 s^-1); each metric head prints two value columns, the left headed Wt, which is the wild-type column this record reads, and the right headed with the engineered enzyme name.


smiles: CCCCOCC(O)CO


smiles: CCOCC(O)CO


column_label: Table 1 (Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers), substrate row '1c', enzyme column 'Wt': column 'KM (mM)' = 13.4; column 'Vmax (U mg^-1)' = 0.036; column 'kcat (s^-1)' = 0.190; column 'kcat/KM (M^-1 s^-1)' = 14. The number printed after the plus/minus sign in the KM, Vmax and kcat cells is the printed error term of that cell and is not an exported metric; the kcat/KM column prints no error term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.190 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.19 s^(-1). Km: printed Table 1 cell 13.4 in a column headed KM (mM); mM is already canonical, so no unit conversion applies and the value is 13.4 mM. kcat/Km: printed Table 1 cell 14 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 14 x 0.001 = 0.014 s^(-1)*mM^(-1). The catalog values are kcat 0.19 s^(-1), Km 13.4 mM and kcat_over_km 0.01417910447761194 s^(-1)*mM^(-1); the quotient of the two printed component cells is 0.19 / 13.4 = 0.01417910447761194 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '1c', enzyme column 'Wt': KM = 13.4 mM; kcat = 0.190 s^-1; printed kcat/KM = 14 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 1, row 1c, column Wt


smiles: COCC(O)CO


column_label: Table 1 (Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers), substrate row '1b', enzyme column 'Wt': column 'KM (mM)' = 45; column 'Vmax (U mg^-1)' = 0.160; column 'kcat (s^-1)' = 0.84; column 'kcat/KM (M^-1 s^-1)' = 19. The number printed after the plus/minus sign in the KM, Vmax and kcat cells is the printed error term of that cell and is not an exported metric; the kcat/KM column prints no error term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.84 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.84 s^(-1). Km: printed Table 1 cell 45 in a column headed KM (mM); mM is already canonical, so no unit conversion applies and the value is 45.0 mM. kcat/Km: printed Table 1 cell 19 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 19 x 0.001 = 0.019 s^(-1)*mM^(-1). The catalog values are kcat 0.84 s^(-1), Km 45.0 mM and kcat_over_km 0.018666666666666665 s^(-1)*mM^(-1); the quotient of the two printed component cells is 0.84 / 45.0 = 0.018666666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '1b', enzyme column 'Wt': KM = 45 mM; kcat = 0.84 s^-1; printed kcat/KM = 19 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 1, row 1b, column Wt


column_label: Table 1 (Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers), substrate row '1h', enzyme column 'Wt': column 'KM (mM)' = 7; column 'Vmax (U mg^-1)' = 0.14; column 'kcat (s^-1)' = 0.7; column 'kcat/KM (M^-1 s^-1)' = 112. The number printed after the plus/minus sign in the KM, Vmax and kcat cells is the printed error term of that cell and is not an exported metric; the kcat/KM column prints no error term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.7 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.7 s^(-1). Km: printed Table 1 cell 7 in a column headed KM (mM); mM is already canonical, so no unit conversion applies and the value is 7.0 mM. kcat/Km: printed Table 1 cell 112 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 112 x 0.001 = 0.112 s^(-1)*mM^(-1). The catalog values are kcat 0.7 s^(-1), Km 7.0 mM and kcat_over_km 0.09999999999999999 s^(-1)*mM^(-1); the quotient of the two printed component cells is 0.7 / 7.0 = 0.09999999999999999 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '1h', enzyme column 'Wt': KM = 7 mM; kcat = 0.7 s^-1; printed kcat/KM = 112 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 1, row 1h, column Wt


smiles: CC(C)OCC(O)CO


smiles: CCCOCC(O)CO


organism: Klebsiella pneumoniae


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

substrate: Dihydroxyacetone


substrate_name: ethylene glycol

smiles: OCCO

substrate: ethylene glycol


substrate_name: glycerol

smiles: OCC(O)CO

substrate: glycerol


column_label: Table 1 (Michaelis-Menten steady-state parameters of the wild-type and the engineered glycerol dehydrogenase on different glyceryl ethers), substrate row '1a', enzyme column 'Wt': column 'KM (mM)' = 50; column 'Vmax (U mg^-1)' = 1.40; column 'kcat (s^-1)' = 7.4; column 'kcat/KM (M^-1 s^-1)' = 148. The number printed after the plus/minus sign in the KM, Vmax and kcat cells is the printed error term of that cell and is not an exported metric; the kcat/KM column prints no error term.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.4 in a column headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.4 s^(-1). Km: printed Table 1 cell 50 in a column headed KM (mM); mM is already canonical, so no unit conversion applies and the value is 50.0 mM. kcat/Km: printed Table 1 cell 148 in a column headed kcat/KM (M^-1 s^-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 148 x 0.001 = 0.148 s^(-1)*mM^(-1). The catalog values are kcat 7.4 s^(-1), Km 50.0 mM and kcat_over_km 0.14800000000000002 s^(-1)*mM^(-1); the quotient of the two printed component cells is 7.4 / 50.0 = 0.14800000000000002 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, substrate row '1a', enzyme column 'Wt': KM = 50 mM; kcat = 7.4 s^-1; printed kcat/KM = 148 in a column headed kcat/KM (M^-1 s^-1).

row_label: Table 1, row 1a, column Wt


substrate_name: Glycerol

substrate: Glycerol


assay_conditions_summary: pH 7.4; 308.15 K; cofactor NAD+


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Homo sapiens

substrate_name: dihydroxyacetone phosphate

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

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

substrate: dihydroxyacetone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R269A/N270A to reconstruct the assayed variant sequence.


organism: Oryctolagus cuniculus

substrate_name: sn-Glycerol 3-phosphate

smiles: O=P(O)(O)OCC(O)CO

assay_conditions_summary: pH 9; 295.15 K; cofactor NAD+

substrate: sn-Glycerol 3-phosphate


substrate_name: glycerone phosphate

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+

substrate: glycerone phosphate


source_db: uniprot

kcat_display: Not reported

kcat_over_km_display: Not reported

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

source: uniprot


enzyme_display_name: D-xylulose reductase

organism: Candida sp. (strain HA167)

substrate_name: D-Fructose

enzyme: D-xylulose reductase

substrate: D-Fructose


organism: Meyerozyma caribbica

substrate_name: D-sorbitol

substrate: D-sorbitol


substrate_name: D-Sorbitol

substrate: D-Sorbitol


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+


organism: Rhizomucor pusillus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D205A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D205A/I206R to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH


substrate_name: NADP+

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

substrate: NADP+


substrate_name: ribitol

substrate: ribitol


substrate_name: xylitol

substrate: xylitol


organism: Pichia kudriavzevii


organism: Scheffersomyces stipitis


organism: Torulaspora delbrueckii


substrate_name: L-Arabitol

substrate: L-Arabitol


organism: Weizmannia coagulans

substrate_name: NAD+

source_db: skid

source_license: CC BY-NC-ND 4.0

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

substrate: NAD+

source: skid


smiles: CC(CO)O


smiles: CCC(CO)O


smiles: C(C(CO)O)O


smiles: CC(C(C)O)O


substrate_name: pyruvate

substrate: pyruvate


substrate_name: NADH

substrate: NADH


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature D121N to reconstruct the assayed variant sequence.

smiles: CCC(O)CO


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature D121N/F245S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession_inactive_uniparc and applied mutation signature F245S 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.

assay_conditions_summary: cofactor NAD+

column_label: Table 2 row 1,2-butanediol, Native column, lists apparent K_m 3.0 mM; Table 3 row 1,2-butanediol, Native columns, lists kcat 120.5 s^-1 and kcat/K_m 40.0 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=3.0 normalized_unit=mM; kcat normalized_value=120.5 normalized_unit=s^-1; kcat/Km normalized_value=40.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.0 raw_unit=mM; kcat raw_value=120.5 raw_unit=s^-1; kcat/Km raw_value=40.0 raw_unit=mM^-1 s^-1

row_label: 1,2-butanediol / 1,2-butanediol; Native enzyme columns

table_label: Table 2. Kinetic properties of BcGDH and its altered forms with LDH activity; Table 3. kcat and kcat/Km of BcGDH and its altered forms with LDH activity on various substrates


column_label: Table 2 row 'd-1,2-propanediol' column Apparent Km (Native)=1.0 mM; Table 3 row 'd-1,2-propanediol' column kcat (Native)=92.0 s^-1; Table 3 row 'd-1,2-propanediol' column kcat/Km (Native)=92.0 mM^-1 s^-1

normalized_value_unit_evidence: Table 2 Km=1.0 mM; Table 3 kcat=92.0 s^-1; Table 3 kcat/Km=92.0 s^-1 mM^-1

raw_value_unit_evidence: Table 2 Km=1.0 mM; Table 3 kcat=92.0 s^-1; Table 3 kcat/Km=92.0 mM^-1 s^-1

table_label: Table 2 (Km) and Table 3 (kcat, kcat/Km)


column_label: Table 2 row d-2,3-butanediol, Native column, lists apparent K_m 17.0 mM; Table 3 row d-2,3-butanediol, Native columns, lists kcat 50.5 s^-1 and kcat/K_m 3.0 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=17.0 normalized_unit=mM; kcat normalized_value=50.5 normalized_unit=s^-1; kcat/Km normalized_value=3.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=17.0 raw_unit=mM; kcat raw_value=50.5 raw_unit=s^-1; kcat/Km raw_value=3.0 raw_unit=mM^-1 s^-1

row_label: d-2,3-butanediol / d-2,3-butanediol; Native enzyme columns


column_label: Table 2 row Glycerol, Native column, lists apparent K_m 4.0 mM; Table 3 row Glycerol, Native columns, lists kcat 117.5 s^-1 and kcat/K_m 30.0 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=4.0 normalized_unit=mM; kcat normalized_value=117.5 normalized_unit=s^-1; kcat/Km normalized_value=30.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.0 raw_unit=mM; kcat raw_value=117.5 raw_unit=s^-1; kcat/Km raw_value=30.0 raw_unit=mM^-1 s^-1

row_label: Glycerol / Glycerol; Native enzyme columns


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


column_label: Table 2 row Pyruvate, Native column, lists apparent K_m 207.0 mM; Table 3 row Pyruvate, Native columns, lists kcat 10.5 s^-1 and kcat/K_m 0.05 mM^-1 s^-1.

normalized_value_unit_evidence: Km normalized_value=207.0 normalized_unit=mM; kcat normalized_value=10.5 normalized_unit=s^-1; kcat/Km normalized_value=0.05 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=207.0 raw_unit=mM; kcat raw_value=10.5 raw_unit=s^-1; kcat/Km raw_value=0.05 raw_unit=mM^-1 s^-1

row_label: Pyruvate / Pyruvate; Native enzyme columns


organism: Heyndrickxia coagulans

source_db: brenda

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

source: brenda


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


assay_conditions_summary: pH 5.4; 328.15 K; cofactor NADH


assay_conditions_summary: pH 5.9; 328.15 K; cofactor NADH


assay_conditions_summary: pH 8.9; 328.15 K; cofactor NAD+


smiles: CCOCC(CO)O


smiles: CCCOCC(CO)O


smiles: CC(C)OCC(CO)O


smiles: C(C(COCC(F)(F)F)O)O


smiles: COCC(CO)O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L252A to reconstruct the assayed variant sequence.

smiles: CCCCOCC(CO)O


assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: glycerol

substrate: glycerol


smiles: CCC(C)O


smiles: CC(C)O


substrate_name: ethanol

smiles: CCO

substrate: ethanol


smiles: CCCO


substrate_name: ethylene glycol

smiles: C(CO)O

substrate: ethylene glycol


smiles: C(CCO)CO


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCO


smiles: CCCCCCCCO


organism: Clostridium butyricum

assay_conditions_summary: pH 9.1; 310.15 K; cofactor NADH


substrate_name: dihydroxyacetone

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

proof_lines:
pH 9.1, 37°C, wild-type enzyme
wild type enzyme, at pH 9.1 and 37°C

substrate: dihydroxyacetone


assay_conditions_summary: pH 9.7; 310.15 K; cofactor NAD+


smiles: C(C(CO)O)O


substrate_name: dihydroxyacetone phosphate

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

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

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

substrate: dihydroxyacetone phosphate


substrate_name: glycolaldehyde

km_display: Not reported

smiles: C(C=O)O

proof_lines:
wild type enzyme, at pH 7.5 and 25°C
wild-type enzyme, pH 7.5, 25°C

substrate: glycolaldehyde


organism: Cellulomonas sp.

smiles: CC(CO)O


smiles: C(C(CS)O)O


smiles: C(C(CCl)O)O


smiles: C(C(CBr)O)O


smiles: C(C(CO)O)N


smiles: CC(CN)O


organism: Klebsiella aerogenes

substrate_name: diacetyl

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

substrate: diacetyl


smiles: CC(C(C)O)O


smiles: CCC(C(C)O)O


substrate_name: Methyl pyruvate

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

substrate: Methyl pyruvate


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


substrate_name: methyl glyoxal

smiles: CC(=O)C=O

substrate: methyl glyoxal


organism: Klebsiella pneumoniae subsp. pneumoniae

smiles: C(CO)O


substrate_name: racemic 2,3-butanediol

substrate: racemic 2,3-butanediol


assay_conditions_summary: pH 8.6; 308.15 K; cofactor NAD+

proof_lines: Mg-GDH, pH 12.0, 45°C, recombinant enzyme


organism: Pichia membranifaciens

assay_conditions_summary: 298.15 K; cofactor NADH


assay_conditions_summary: 298.15 K; cofactor NAD+


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


smiles: C(C(CO)O)O


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: NAD+

substrate: NAD+


organism: Ceratitis capitata

substrate_name: sn-glycerol 3-phosphate

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

substrate: sn-glycerol 3-phosphate


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


substrate_name: NADH

substrate: NADH


organism: Eidolon helvum


substrate_name: glycerone phosphate

substrate: glycerone phosphate


assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+


organism: Homo sapiens

assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: pH 9; cofactor NAD+


assay_conditions_summary: pH 9


organism: Drosophila virilis


proof_lines: alpha-GPDHs, standard deviation 0.0041 mM


proof_lines: alpha-GPDHs, standard deviation 0.0215 mM


substrate_name: glycerol 3-phosphate

substrate: glycerol 3-phosphate


organism: Gallus gallus


organism: Rattus norvegicus


substrate_name: alpha-glycerol phosphate

substrate: alpha-glycerol phosphate


organism: Debaryomyces hansenii


organism: Spinacia oleracea


substrate_name: glycerol phosphate

substrate: glycerol phosphate


organism: Jaculus orientalis

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


organism: Trypanosoma brucei


organism: [Candida] sp. HA 167

substrate_name: sorbitol

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E154C to reconstruct the assayed variant sequence.

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

substrate: sorbitol


proof_lines: mutant E154C, kcat/Km (sorbitol): 1.5/Msec


organism: Meyerozyma caribbica

substrate_name: NADP+

assay_conditions_summary: pH 7; 303.15 K; cofactor NADP+

proof_lines: pH 7.0, 30°C, native enzyme, with xylitol

substrate: NADP+


substrate_name: L-arabitol

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

proof_lines:
pH 7.0, 30°C, native enzyme
pH 7.0, 30°C, recombinant enzyme

substrate: L-arabitol


substrate_name: D-sorbitol

substrate: D-sorbitol


assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

proof_lines: pH 7.0, 30°C, recombinant enzyme, with xylitol


organism: Saccharomyces cerevisiae

assay_conditions_summary: cofactor NAD+


substrate_name: D-xylulose

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

substrate: D-xylulose


substrate_name: xylitol

substrate: xylitol


organism: Blastobotrys adeninivorans

substrate_name: D-ribulose

substrate: D-ribulose


substrate_name: L-sorbose

substrate: L-sorbose


proof_lines:
35°C, pH 7.5, recombinant enzyme
35°C, pH 7.5, native enzyme


organism: Scheffersomyces shehatae


substrate_name: xylulose

substrate: xylulose


proof_lines:
25°C, pH 7.5, Tris-HCl
kcat/Km (sorbitol): 7800/Msec


proof_lines:
25°C, pH 7.5, Tris-HCl
25°C, pH 7.5, potassium phosphate


substrate_name: D-fructose

substrate: D-fructose


proof_lines:
25°C, pH 7.5, Tris-HCl
25°C, pH 7.5, potassium phosphate
25°C, pH 9.0


organism: Gluconobacter oxydans

assay_conditions_summary: pH 5; 308.15 K; cofactor NADH


substrate_name: NAD+

substrate: NAD+


organism: Escherichia coli

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

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

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


organism: Klebsiella pneumoniae

substrate_name: ethylene glycol

substrate: ethylene glycol


assay_conditions_summary: pH 7.4; 308.15 K; cofactor NAD+


organism: Pyrococcus furiosus

substrate_name: acetoin

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

substrate: acetoin


organism: Cynomys ludovicianus

substrate_name: NADH

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADH

proof_lines:
pH 7.5, 22°C, liver isozyme
pH 7.5, 5°C, liver isozyme
pH 7.5, 5°C, muscle isozyme

substrate: NADH


assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

proof_lines:
pH 8.5, 22°C, liver isozyme
pH 8.5, 5°C, liver isozyme
pH 8.5, 22°C, muscle isozyme


substrate_name: glycerone phosphate

proof_lines:
pH 7.5, 5°C, muscle isozyme
pH 7.5, 5°C, liver isozyme
pH 7.5, 22°C, muscle isozyme

substrate: glycerone phosphate


organism: Paenibacillus polymyxa

smiles: CC(CO)O


substrate_name: diacetyl

substrate: diacetyl


enzyme_display_name: alcohol dehydrogenase

organism: Homo sapiens

substrate_name: 16-Hydroxyhexadecanoic acid

smiles: O=C(O)CCCCCCCCCCCCCCCO

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

data_origin: curated

enzyme: alcohol dehydrogenase

substrate: 16-Hydroxyhexadecanoic acid


smiles: CCCCCCCCO


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: Ethanol

smiles: CCO

substrate: Ethanol


substrate_name: Glycol

smiles: OCCO

substrate: Glycol


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Saccharolobus solfataricus

smiles: CCCC(C)O

assay_conditions_summary: pH 10.5; buffer 0.1 M glycine-NaOH


smiles: CCC(CC)O


smiles: CCCCCCCO


smiles: CCOCCO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W95L/N249Y to reconstruct the assayed variant sequence.

smiles: CCC(C)O


smiles: CCCCCCO


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


smiles: CCCO


smiles: CCCCCO


substrate_name: ethanol

substrate: ethanol


smiles: CCCCO


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


assay_conditions_summary: pH 10.5; buffer assay context in 0.1 M glycine-NaOH


substrate_name: NAD+

assay_conditions_summary: pH 10.5; buffer assay context in 0.1 M glycine-NaOH; cofactor NAD+

substrate: NAD+


organism: Equus caballus

smiles: C(CCO)CN

proof_lines:
Raw SKiD Env: Temp=25°C, pH=9
Raw SKiD Env: Temp=25°C, pH=11
Raw SKiD Env: Temp=25°C, pH=7


proof_lines:
Raw SKiD Env: Temp=65°C, pH=-----
Raw SKiD Env: Temp=65°C, pH=10.5


proof_lines:
Raw SKiD Env: Temp=65°C, pH=-----
Raw SKiD Env: Temp=65°C, pH=10.5
Raw SKiD Env: Temp=55°C, pH=-----


proof_lines:
Raw SKiD Env: Temp=55°C, pH=-----
Raw SKiD Env: Temp=65°C, pH=-----
Raw SKiD Env: Temp=65°C, pH=10.5


proof_lines:
Raw SKiD Env: Temp=65°C, pH=-----
Raw SKiD Env: Temp=55°C, pH=-----
Raw SKiD Env: Temp=65°C, pH=10.5


proof_lines:
Raw SKiD Env: Temp=65°C, pH=10.5
Raw SKiD Env: Temp=55°C, pH=-----


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


smiles: C(CCN)CCO


smiles: C(CCCO)CCN


smiles: CCO


organism: Moraxella sp.


organism: Yarrowia lipolytica (strain CLIB 122 / E 150)

smiles: CCCCCCC(C)O

proof_lines: kcat is 1.05 sec(-1) with (S)-2-octanol as substrate and 3.42 sec(-1) for NAD(+). kcat is 0.56 sec(-1) for (2)-octanone.


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: glycerol

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

sequence_source: multiple

smiles: C(C(CO)O)O

proof_lines: The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation).

source_databases_merged: skid uniprot

substrate: glycerol


organism: Thermotoga maritima

substrate_name: NADH

substrate: NADH


proof_lines:
Raw SKiD Env: Temp=50°C, pH=7.4
Raw SKiD Env: Temp=50°C, pH=7.9


organism: Escherichia coli (strain K12)

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

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


organism: Oryctolagus cuniculus

proof_lines:
adipose tissue
muscle
I6.5


substrate_name: glycerone phosphate

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

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W54L with inferred residue-numbering offset -9 to reconstruct the assayed variant sequence.

smiles: CC(C)CCO


smiles: CCC(C)O


smiles: CC(C)O


smiles: CC(C)CCCO


substrate_name: Pentanol

smiles: CCCCCO

substrate: Pentanol


substrate_name: Hexanol

smiles: CCCCCCO

substrate: Hexanol


substrate_name: Propanol

smiles: CCCO

substrate: Propanol


substrate_name: butanol

smiles: CCCCO

substrate: butanol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


substrate_name: ethanol

substrate: ethanol


substrate_name: NADP+

assay_conditions_summary: pH 8.8; cofactor NADP+

substrate: NADP+


smiles: CC(C(C)O)O


assay_conditions_summary: pH 8.8; cofactor NAD+


organism: Thermus thermophilus

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

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 `4-Methoxybenzyl alcohol`: column 'kcat (s^-1)' = 1.6; column 'Km (mM)' = 61.0; column 'kcat/Km (s^-1 mM^-1)' = 0.026.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 1.6 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 1.6 s^(-1); the exported value is 1.6 s^(-1). Km: printed TABLE 4 cell 61.0 mM; the table already reports Km in mM, so no conversion is applied and the value is 61.0 mM; the exported value is 61.0 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.026 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 0.026 s^(-1)*mM^(-1); the exported value is 0.026 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `4-Methoxybenzyl alcohol`: kcat (s^-1) = 1.6; Km (mM) = 61.0; kcat/Km (s^-1 mM^-1) = 0.026.

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

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

substrate: 4-methoxybenzyl alcohol


assay_conditions_summary: pH 6


substrate_name: alpha-tetralone

column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `alpha-Tetralone`: column 'kcat (s^-1)' = 7.70; column 'Km (mM)' = 5.8; column 'kcat/Km (s^-1 mM^-1)' = 1.3.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 7.70 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 7.7 s^(-1); the exported value is 7.7 s^(-1). Km: printed TABLE 4 cell 5.8 mM; the table already reports Km in mM, so no conversion is applied and the value is 5.8 mM; the exported value is 5.8 mM. kcat/Km: the paper PRINTS the kcat/Km cell 1.3 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 1.3 s^(-1)*mM^(-1); the exported value is 1.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `alpha-Tetralone`: kcat (s^-1) = 7.70; Km (mM) = 5.8; kcat/Km (s^-1 mM^-1) = 1.3.

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

substrate: alpha-tetralone


column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `1-Indanone`: column 'kcat (s^-1)' = 8.30; column 'Km (mM)' = 27.6; column 'kcat/Km (s^-1 mM^-1)' = 0.30.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 8.30 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 8.3 s^(-1); the exported value is 8.3 s^(-1). Km: printed TABLE 4 cell 27.6 mM; the table already reports Km in mM, so no conversion is applied and the value is 27.6 mM; the exported value is 27.6 mM. kcat/Km: the paper PRINTS the kcat/Km cell 0.30 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 0.3 s^(-1)*mM^(-1); the exported value is 0.3 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `1-Indanone`: kcat (s^-1) = 8.30; Km (mM) = 27.6; kcat/Km (s^-1 mM^-1) = 0.30.

row_label: TABLE 4, decoded plain-numeral transcription, substrate row `1-Indanone`


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


substrate_name: methylbenzoylformate

substrate: methylbenzoylformate


substrate_name: methyl oxo(phenyl)acetate

column_label: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `MBF`: column 'kcat (s^-1)' = 38.1; column 'Km (mM)' = 2.7; column 'kcat/Km (s^-1 mM^-1)' = 14.1.

normalized_value_unit_evidence: kcat: printed TABLE 4 cell 38.1 s^-1; the table already reports kcat in s^-1, so no conversion is applied and the value is 38.1 s^(-1); the exported value is 38.1 s^(-1). Km: printed TABLE 4 cell 2.7 mM; the table already reports Km in mM, so no conversion is applied and the value is 2.7 mM; the exported value is 2.7 mM. kcat/Km: the paper PRINTS the kcat/Km cell 14.1 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 14.1 s^(-1)*mM^(-1); the exported value is 14.1 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 4 'Steady-state kinetic constants of ADH_Tt', substrate row `MBF`: kcat (s^-1) = 38.1; Km (mM) = 2.7; kcat/Km (s^-1 mM^-1) = 14.1.

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

substrate: methyl oxo(phenyl)acetate


substrate_name: alpha-tetralol

substrate: alpha-tetralol


substrate_name: (S)-alpha-tetralol

substrate: (S)-alpha-tetralol


substrate_name: ethyl oxo(phenyl)acetate

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 oxo(phenyl)acetate


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 1490.0 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`


substrate_name: (S)-(+)-alpha-tetralol

substrate: (S)-(+)-alpha-tetralol


substrate_name: NADPH

assay_conditions_summary: pH 6.1; cofactor NADPH

substrate: NADPH


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


assay_conditions_summary: pH 6.1; cofactor NADH

substrate: NADH


substrate_name: NAD+

substrate: NAD+


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: CCC(CC)O


substrate_name: methanol

smiles: CO

substrate: methanol


smiles: CCCC(C)O


assay_conditions_summary: pH 9.2; cofactor NAD+


smiles: CCO


assay_conditions_summary: pH 7.5; cofactor NADH


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: benzylalcohol

substrate: benzylalcohol


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


substrate_name: benzyl alcohol

substrate: benzyl alcohol


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


substrate_name: benzaldehyde

substrate: benzaldehyde


assay_conditions_summary: cofactor NADH


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


assay_conditions_summary: cofactor NAD+


organism: Sulfolobus acidocaldarius

assay_conditions_summary: pH 8


assay_conditions_summary: pH 5; cofactor NADH


assay_conditions_summary: pH 8; cofactor NAD+


substrate_name: cycloheptanol

substrate: cycloheptanol


substrate_name: methyl benzoylformate

substrate: methyl benzoylformate


substrate_name: methyl o-chlorobenzoylformate

substrate: methyl o-chlorobenzoylformate


substrate_name: (R)-alpha-tetralol

substrate: (R)-alpha-tetralol


substrate_name: isatin

substrate: isatin


substrate_name: Butyl alcohol

substrate: Butyl alcohol


substrate_name: hexyl alcohol

substrate: hexyl alcohol


substrate_name: Propyl alcohol

substrate: Propyl alcohol


substrate_name: ethanol

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


smiles: CCCCCCC(C)O


smiles: CCCC(=O)C


substrate_name: acetone

substrate: acetone


smiles: CCC(=O)CC


substrate_name: Isopropanol

smiles: CC(C)O

substrate: Isopropanol


smiles: CCC(C)O


organism: Coturnix coturnix

substrate_name: Cyclohexanol

substrate: Cyclohexanol


smiles: C(CCCCCC(=O)[O-])CCCCCO


smiles: CCCCCCCCO


substrate_name: benzyl alcohol

substrate: benzyl alcohol


smiles: CCCCCO


substrate_name: NAD+

substrate: NAD+


smiles: CCCCO


substrate_name: NADH

substrate: NADH


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


organism: Rattus norvegicus

assay_conditions_summary: pH 10


smiles: CC=CCO


assay_conditions_summary: pH 10; cofactor NAD+


substrate_name: m-nitrobenzaldehyde

substrate: m-nitrobenzaldehyde


substrate_name: Butanal

substrate: Butanal


organism: Corynebacterium glutamicum R

substrate_name: propanal

assay_conditions_summary: pH 7

substrate: propanal


substrate_name: propanone

smiles: CC(=O)C

substrate: propanone


substrate_name: methanol

smiles: CO

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: n-Propanol

smiles: CCCO

substrate: n-Propanol


substrate_name: n-Pentanal

smiles: CCCCC=O

substrate: n-Pentanal


substrate_name: n-butanol

substrate: n-butanol


assay_conditions_summary: pH 5


substrate_name: benzil

substrate: benzil


substrate_name: ethyl benzoylformate

substrate: ethyl benzoylformate


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: Methylorubrum extorquens


smiles: CC(CO)O


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Geobacillus stearothermophilus


substrate_name: iso-propanol

smiles: CC(C)O

substrate: iso-propanol


organism: Brevibacterium sp.


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: ethylene glycol

smiles: C(CO)O

substrate: ethylene glycol


substrate_name: tryptophol

substrate: tryptophol


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


smiles: C(CCCCCCCC(=O)[O-])CCCCCCCO


organism: Sphingomonas sp. A1

substrate_name: D-arabitol

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

substrate: D-arabitol


substrate_name: D-ribonate

substrate: D-ribonate


substrate_name: D-sorbitol

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

substrate: D-sorbitol


substrate_name: D-talonate

substrate: D-talonate


substrate_name: D-altronate

substrate: D-altronate


organism: Thermococcus kodakarensis

substrate_name: NAD+

assay_conditions_summary: pH 9; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 9; cofactor NADP+

substrate: NADP+


substrate_name: acetoin

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

assay_conditions_summary: pH 6

substrate: acetoin


substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 9


smiles: CC(C(C)O)O


organism: Mesocricetus auratus

substrate_name: all-trans retinol

substrate: all-trans retinol


organism: Yokenella sp.


smiles: CC=CCO


assay_conditions_summary: pH 8; cofactor NADP+


substrate_name: benzaldehyde

substrate: benzaldehyde


smiles: CC=CC=O


substrate_name: NADPH

assay_conditions_summary: pH 6.5; cofactor NADPH

substrate: NADPH


organism: Megalodesulfovibrio gigas


substrate_name: ethanol

smiles: CCO

substrate: ethanol


smiles: CCCO


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: benzyl alcohol

substrate: benzyl alcohol


assay_conditions_summary: pH 7; cofactor NAD+


organism: Homo sapiens

substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: all-trans-retinol

substrate: all-trans-retinol


assay_conditions_summary: pH 7.5; cofactor NAD+


smiles: C(CCCCCC(=O)[O-])CCCCCO


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: n-Hexanol

smiles: CCCCCCO

substrate: n-Hexanol


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: methylcrotonyl alcohol

substrate: methylcrotonyl alcohol


organism: Sporotrichum pulverulentum


assay_conditions_summary: cofactor NADH


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Rhodococcus ruber


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: acetophenone

substrate: acetophenone


substrate_name: capronaldehyde

smiles: CCCCCC=O

substrate: capronaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


organism: Zea mays

sequence_variant_note: Mutation signature H1S 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: Saccharomyces cerevisiae

substrate_name: propanal

smiles: CCC=O

substrate: propanal


smiles: C=O


substrate_name: furfural

assay_conditions_summary: pH 7; cofactor NADH

substrate: furfural


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


organism: Aspergillus nidulans

substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: NADH

substrate: NADH


substrate_name: ethanol

substrate: ethanol


smiles: CC(C)O


organism: Drosophila simulans


smiles: CCC(C)O


organism: Pyrobaculum calidifontis

smiles: C(CCO)CO


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

substrate: Glutaraldehyde


substrate_name: Propanol

substrate: Propanol


substrate_name: Hexanol

substrate: Hexanol


assay_conditions_summary: pH 7.7; cofactor NAD+


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


assay_conditions_summary: pH 7.7; cofactor NADH


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


organism: Zymomonas mobilis


substrate_name: NAD+

substrate: NAD+


organism: Thermus sp.


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: cyclohexanone

substrate: cyclohexanone


organism: Acetobacter pasteurianus


assay_conditions_summary: pH 8.5; cofactor NAD+


organism: Crocus sativus

assay_conditions_summary: pH 8.5; cofactor NADH


organism: Rattus norvegicus


organism: Leifsonia sp.


substrate_name: phenyl trifluoromethyl ketone

assay_conditions_summary: pH 7

substrate: phenyl trifluoromethyl ketone


organism: Meyerozyma guilliermondii


organism: Hordeum vulgare


organism: Chlamydomonas moewusii


organism: Euglena gracilis

assay_conditions_summary: pH 9; buffer bis-Tris propane; cofactor NAD+


assay_conditions_summary: pH 9; buffer bis-Tris propane


substrate_name: Isopropanol

substrate: Isopropanol


substrate_name: Isopentanol

smiles: CC(C)CCO

substrate: Isopentanol


organism: Magnusiomyces capitatus

assay_conditions_summary: pH 6


assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 6; cofactor NADH


assay_conditions_summary: pH 8


organism: Oryza sativa


substrate_name: p-Methoxybenzaldehyde

assay_conditions_summary: pH 7.3; cofactor NADH

substrate: p-Methoxybenzaldehyde


substrate_name: p-methoxybenzyl alcohol

assay_conditions_summary: pH 7.3; cofactor NAD+

substrate: p-methoxybenzyl alcohol


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Homo sapiens

substrate_name: Vanillyl alcohol

assay_conditions_summary: pH 10

substrate: Vanillyl alcohol


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: NADH

assay_conditions_summary: pH 7.5; cofactor NADH

substrate: NADH


organism: Mesocricetus auratus


assay_conditions_summary: cofactor NAD+


substrate_name: butanol

substrate: butanol


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Moraxella sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A25Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; cofactor NAD+


substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


organism: Equus caballus

assay_conditions_summary: cofactor NADH


substrate_name: 5beta-cholanic acid-3-one

substrate: 5beta-cholanic acid-3-one


organism: Sus scrofa


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


substrate_name: mevaldate

substrate: mevaldate


organism: Mus musculus

substrate_name: Hexanol

substrate: Hexanol


organism: Citrobacter sp. S-77

substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: Saccharolobus solfataricus


smiles: CCCCCO


substrate_name: 12-Hydroxydodecanoic acid

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

substrate: 12-Hydroxydodecanoic acid


organism: Saccharomyces cerevisiae


substrate_name: Unknown

substrate: Unknown


organism: Arabidopsis thaliana


organism: Kluyveromyces marxianus


substrate_name: glycolaldehyde

smiles: C(C=O)O

assay_conditions_summary: pH 7; cofactor NADH

substrate: glycolaldehyde


organism: Ogataea angusta

assay_conditions_summary: pH 9


substrate_name: NAD+

substrate: NAD+


organism: Triticum turgidum


organism: Oryctolagus cuniculus


organism: Triticum monococcum


substrate_name: allyl alcohol

smiles: C=CCO

substrate: allyl alcohol


substrate_name: crotyl alcohol

smiles: CC=CCO

substrate: crotyl alcohol


organism: Brassica napus


organism: Petroselinum crispum


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Oncorhynchus mykiss


organism: Pseudomonas aeruginosa


organism: Klebsiella oxytoca


assay_conditions_summary: pH 10.5; cofactor NAD+


organism: Escherichia coli

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

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


organism: Priestia megaterium

assay_conditions_summary: pH 9; 298.15 K; cofactor NAD+


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


organism: Klebsiella pneumoniae


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


organism: Chlamydomonas reinhardtii

substrate_name: dihydroxyacetone phosphate

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

substrate: dihydroxyacetone phosphate


substrate_name: NADH

substrate: NADH


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


organism: Apis mellifera


assay_conditions_summary: buffer MOPS

proof_lines: in MOPS buffer, 0.33 mM in Tris-histidine


organism: Candida tropicalis


substrate_name: xylitol

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

substrate: xylitol


organism: Urocitellus richardsonii

assay_conditions_summary: pH 8; 278.15 K; cofactor NAD+

proof_lines: pH 7.5, 22°C, euthermic G3PDH enzyme and hibernation G3PDH enzyme


substrate_name: sn-glycerol 3-phosphate

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

proof_lines: enzyme from hibernating animal, at pH 7.5 and 22°C

substrate: sn-glycerol 3-phosphate


organism: Saccharomyces kudriavzevii


organism: Ovis aries

substrate_name: D-sorbitol

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

substrate: D-sorbitol


organism: Rhizobium etli

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+


organism: Spathaspora passalidarum

assay_conditions_summary: pH 9; 308.15 K; cofactor NAD+


organism: Fusarium oxysporum


substrate_name: D-xylitol

substrate: D-xylitol


organism: Pachysolen tannophilus


organism: Scheffersomyces stipitis

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

assay_conditions_summary: cofactor NADP+

proof_lines: mutant D207A/I208R/F209S: kcat/Km (NAD+): 181 l/min/mmol, kcat/Km (NADP+): 0.65 l/min/mmol


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

proof_lines: mutant S96C/S99C/Y102C/D207A/I208R/F209S: kcat/Km (NADP+): 10700 l/min/mmol


organism: Picrophilus oshimae

substrate_name: ethanol

substrate: ethanol


organism: Meyerozyma guilliermondii


assay_conditions_summary: pH 8.2; 295.15 K; cofactor NAD+


organism: Homo sapiens

substrate_name: methanol

smiles: CO

substrate: methanol


organism: Carboxydothermus hydrogenoformans

substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


organism: Scyliorhinus canicula

substrate_name: Octanol

smiles: CCCCCCCCO

substrate: Octanol


organism: Equus caballus

substrate_name: p-nitrophenyl octanoate

substrate: p-nitrophenyl octanoate


organism: Bacillus subtilis

smiles: CCO


substrate_name: benzyl alcohol

assay_conditions_summary: pH 10

substrate: benzyl alcohol


organism: Flavobacterium frigidimaris


organism: Hafnia alvei


organism: Pseudomonas aeruginosa

substrate_name: ethylene glycol

smiles: C(CO)O

substrate: ethylene glycol


organism: Devosia riboflavina


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


organism: [Candida] sp.

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Thermoplasma acidophilum

assay_conditions_summary: pH 5


organism: Thermomicrobium roseum


organism: Mus musculus

substrate_name: Unknown

assay_conditions_summary: pH 7.4; buffer 0.1 M Na-K phosphate

substrate: Unknown


organism: Glycine max


organism: Saccharomyces cerevisiae

substrate_name: phenylglyoxylic acid

substrate: phenylglyoxylic acid


organism: Paenibacillus polymyxa

smiles: CC(C(C)O)O


organism: Bacillus sp. (in: firmicutes)


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Bacillus thuringiensis serovar kurstaki


organism: Salmonella enterica

smiles: CC(CCO)O


organism: Klebsiella pneumoniae


substrate_name: glycerol

proof_lines:
pH 10.0, 30°C, free enzyme
pH 10.0, 30°C, immobilized enzyme
pH 7.4, 35°C

substrate: glycerol


organism: Cellulomonas sp.


substrate_name: dihydroxyacetone

substrate: dihydroxyacetone


organism: Klebsiella pneumoniae subsp. pneumoniae

assay_conditions_summary: pH 12; 318.15 K; cofactor NAD+

proof_lines: wild-type Zn-GDH, pH 12.0, 45°C, recombinant enzyme


substrate_name: NADH

assay_conditions_summary: pH 11; 310.15 K; cofactor NADH

proof_lines: recombinant chimeric enzyme GDH-NOX, pH 11.0, 37°C

substrate: NADH


organism: Coturnix japonica

substrate_name: alpha-glycerophosphate

proof_lines: testes liver

substrate: alpha-glycerophosphate


organism: Arthrobacter sp.


organism: Torulaspora delbrueckii

substrate_name: xylitol

substrate: xylitol


organism: Scheffersomyces stipitis


organism: Cavia porcellus

substrate_name: D-xylulose

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

substrate: D-xylulose


organism: Gluconobacter oxydans

substrate_name: D-sorbitol

substrate: D-sorbitol


organism: Serratia marcescens


organism: [Candida] sp. HA 167


enzyme_display_name: UniProt P00326

organism: Homo sapiens

enzyme: UniProt P00326


enzyme_display_name: UniProt P08319

enzyme: UniProt P08319


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH7

substrate_name: 12-OH-dodecanoic acid (with 0.1 M sodium phosphate at pH 7.5)

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


enzyme_display_name: Alcohol dehydrogenase class-P

organism: Arabidopsis thaliana

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

enzyme: Alcohol dehydrogenase class-P


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: 10-hydroxy-decanoate (at pH 8)

smiles: OCCCCCCCCCC(=O)O

assay_conditions_summary: pH 8

substrate: 10-hydroxy-decanoate (at pH 8)


enzyme_display_name: Alcohol dehydrogenase class-3

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

proof_lines: kcat is 1351 min(-1) with S-hydroxymethylglutathione as substrate (at pH 8 and 25 degrees Celsius). kcat is 6 min(-1) with farnesol as substrate (at pH 7.5 and 25 degrees Celsius). kcat is 324 min(-1) with cinnamylalcohol as substrate (at p

enzyme: Alcohol dehydrogenase class-3


enzyme_display_name: Alcohol dehydrogenase

organism: Moraxella sp. (strain TAE123)

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

enzyme: Alcohol dehydrogenase


organism: Pisum sativum

substrate_name: 12-OH-dodecanoic acid (at pH 10)

proof_lines: kcat is 190 min(-1) with octanol as substrate (at pH 10). kcat is 110 min(-1) with 12-OH-dodecanoic acid as substrate (at pH 10). kcat is 380 min(-1) with S-hydroxymethylglutathione as substrate (at pH 8).

substrate: 12-OH-dodecanoic acid (at pH 10)


enzyme_display_name: Alcohol dehydrogenase 2

organism: Yarrowia lipolytica (strain CLIB 122 / E 150)

proof_lines: kcat is 1.05 sec(-1) with (S)-2-octanol as substrate and 3.42 sec(-1) for NAD(+). kcat is 0.56 sec(-1) for (2)-octanone.

enzyme: Alcohol dehydrogenase 2


organism: Thermotoga maritima

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

assay_conditions_summary: pH 7.4; 323.15 K; cofactor NAD+


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 V44A/K157N to reconstruct the assayed variant sequence.

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


proof_lines: mutant enzyme V44A/ K157N, at pH 7.4 and 50°C


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


proof_lines: mutant enzyme V44A/K157G, at pH 7.4 and 50°C


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

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 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


proof_lines: mutant enzyme I154A/K157G, at pH 7.4 and 50°C


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


proof_lines: mutant enzyme V44A/I154A/K157G, at pH 7.4 and 50°C


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


proof_lines: mutant enzyme V44A/ I154A, at pH 7.4 and 50°C


enzyme_display_name: UniProt Q9WYQ4

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

enzyme: UniProt Q9WYQ4


enzyme_display_name: Glycerol dehydrogenase

organism: Escherichia coli (strain K12)

proof_lines: The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation).

enzyme: Glycerol dehydrogenase


organism: Oryctolagus cuniculus

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH

proof_lines:
muscle
I6.5
adipose tissue


enzyme_display_name: Glycerol-3-phosphate dehydrogenase [NAD(+)] 2, chloroplastic


enzyme_display_name: Glycerol-3-phosphate dehydrogenase [NAD(+)] 1, chloroplastic


enzyme_display_name: Sorbitol dehydrogenase

organism: Rattus norvegicus

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

enzyme: Sorbitol dehydrogenase


organism: Providencia stuartii

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


organism: Unknown

substrate_name: SPC_37_Cell; SPC_56_Cell

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

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

substrate: SPC_37_Cell; SPC_56_Cell


organism: Zea mays


assay_conditions_summary: cofactor NADH


substrate_name: SPC_37_Cell; SPC_1303_Cell

substrate: SPC_37_Cell; SPC_1303_Cell


organism: Dunaliella viridis

proof_lines:
recombinant isozyme GDH2
isozyme GPDH2
recombinant isozyme GDH1


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
isozyme GPDH1
recombinant isozyme GDH1
recombinant isozyme GDH2

substrate: NADPH


substrate_name: SPC_37_Cell; SPC_2033_Cell

substrate: SPC_37_Cell; SPC_2033_Cell


enzyme_display_name: L-xylulose reductase

organism: Cavia porcellus

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

enzyme: L-xylulose reductase


column_label: Table II (journal page 17888), decoded transcription, substrate row `1,4-Dibromo-2,3-butanedione`, Human column group: Km (mM) = 0.006; kcat (s^-1) = 0.48; kcat/Km (s^-1 mM^-1) = 80.

normalized_value_unit_evidence: kcat: printed cell 0.48 s^-1 -> 0.48 s^(-1); the catalog holds 0.48 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 0.006 mM -> 0.006 mM; the catalog holds 0.006 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: The paper PRINTS the kcat/Km cell `80` s^-1 mM^-1 for this row and column; it equals the catalog kcat_over_km 80.0 s^(-1)*mM^(-1) exactly (it is also the exact quotient 0.48 / 0.006 of this row's own printed kcat and Km).

table_label: Table II (journal page 17888) 'Substrate specificitiy for carbonyl compounds of rodent and human DCXRs'


organism: Mesocricetus auratus


organism: Mus musculus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K153M with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S136A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y149F to reconstruct the assayed variant sequence.


column_label: Table II (journal page 17888), decoded transcription, substrate row `1-Phenyl-1,2-propanedione`, Guinea pig column group: Km (mM) = 0.074; kcat (s^-1) = 23; kcat/Km (s^-1 mM^-1) = 311.

normalized_value_unit_evidence: kcat: printed cell 23 s^-1 -> 23.0 s^(-1); the catalog holds 23.0 s^(-1); no unit conversion applied (the paper prints s^-1 directly). Km: printed cell 0.074 mM -> 0.074 mM; the catalog holds 0.074 mM; no unit conversion applied (the paper prints mM directly). kcat/Km: The paper PRINTS the kcat/Km cell `311` s^-1 mM^-1 for this row and column. The catalog stores 310.81081081081084 s^(-1)*mM^(-1), which is the exact full-precision quotient 23 / 0.074 of this row's own printed kcat and Km; rounded to the printed cell's precision it is exactly `311`, so the only difference between the printed cell and the catalog number is printed precision (the paper reports kcat/Km to three significant figures).


organism: Homo sapiens