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


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Thermothelomyces myriococcoides

substrate_name: 2,6-dichlorophenol indophenol

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

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.

data_origin: experimental

enzyme: cellobiose dehydrogenase (acceptor)

substrate: 2,6-dichlorophenol indophenol

status: unverified

source: oed


smiles: O=O

mutation_type: substitution


organism: Phanerodontia chrysosporium

substrate_name: cellobiose

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -3, so it is treated as a source-provided variant sequence.

substrate: cellobiose


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M685Y with inferred residue-numbering offset +18 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -13, so it is treated as a source-provided variant sequence.


substrate_name: lactose

substrate: lactose


proof_lines:
Phanerochaete chrysosporium
PcCDH
cellobiose dehydrogenase


enzyme_display_name: alkan-1-ol dehydrogenase (acceptor)

organism: Ensifer sp. AS08

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H465A to reconstruct the assayed variant sequence.

smiles: OCCO

enzyme: alkan-1-ol dehydrogenase (acceptor)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N90A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


organism: Thermothelomyces fergusii

substrate_name: D-glucose

source_db: brenda

substrate: D-glucose

source: brenda


assay_conditions_summary: pH 5


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: triiodide ion

smiles: I[I-]I

substrate: triiodide ion


organism: Homo sapiens

substrate_name: GHB

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

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

column_label: Results prose reports apparent Km values of 0.17 mmol/L and 1.2 mmol/L for GHB and 2-KG respectively; Table 1 lists GHB human liver 0.2 x 10^-3 mol/L, consistent with the rounded prose value.

raw_value_unit_evidence: Km raw_value=0.17 raw_unit=mmol/L

row_label: GHB / Human liver

table_label: Results prose and Table 1: apparent Km values

substrate: GHB

status: verified

source: uniprot


substrate_name: SSA

column_label: Results prose reports apparent Km values of 0.04 mmol/L and 0.12 mmol/L for SSA and D-2-HG respectively; Table 1 lists SSA human liver 0.4 x 10^-4 mol/L, equal to 0.04 mM.

raw_value_unit_evidence: Km raw_value=0.04 raw_unit=mmol/L

row_label: SSA / Human liver

substrate: SSA


enzyme_display_name: UniProt Q3L245

organism: Leucoagaricus meleagris

substrate_name: L-arabinose

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q3L245

substrate: L-arabinose

source: skid


substrate_name: maltose

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=8.5

substrate: maltose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: maltotriose

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: maltotriose


substrate_name: L-sorbose

substrate: L-sorbose


substrate_name: methyl-alpha-D-glucopyranoside

substrate: methyl-alpha-D-glucopyranoside


substrate_name: D-sorbose

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

substrate: D-sorbose


substrate_name: xylobiose

substrate: xylobiose


enzyme_display_name: Pyranose dehydrogenase

organism: Agaricus bisporus

substrate_name: D-glucose (with 1,4-benzoquinone as electron acceptor)

enzyme: Pyranose dehydrogenase


substrate_name: D-cellobiose (with 1,4-benzoquinone as electron acceptor)


substrate_name: L-arabinose (with 1,4-benzoquinone as electron acceptor)


substrate_name: sucrose (with 1,4-benzoquinone as electron acceptor)


substrate_name: 1,4-benzoquinone (with D-glucose as substrate)


enzyme_display_name: (S)-mandelate dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: (S)-Mandelate

enzyme: (S)-mandelate dehydrogenase

substrate: (S)-Mandelate


substrate_name: ferricyanide


organism: Chaetomium sp.

substrate_name: cellobiose


organism: Irpex lacteus


organism: Rattus norvegicus

substrate_name: GHB

assay_conditions_summary: pH 7

column_label: Printed page 16878, Table X, gamma-hydroxybutyrate row, Km(app) column: 3.0 x 10^-4 M.

normalized_value_unit_evidence: 3.0 x 10^-4 M = 0.3 mM; exact match to the current row.

raw_value_unit_evidence: Km(app) = 3.0 x 10^-4 M for gamma-hydroxybutyrate.

row_label: gamma-hydroxybutyrate

table_label: Table X


substrate_name: SSA


organism: Termitomyces sp. OE 147

substrate_name: maltose

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

proof_lines:
cellobiose
pH 5.0
cellulose degradation


organism: Cerrena unicolor

proof_lines:
cellobiose
ferricytochrome c
DCIP


substrate_name: lactose

proof_lines:
lactose
DCIP
cytochrome c


substrate_name: benzyl viologen

proof_lines:
cellobiose oxidase
substrate specificity
Phanerodontia chrysosporium

substrate: benzyl viologen


enzyme_display_name: 2-oxo-acid reductase

organism: Proteus mirabilis

substrate_name: carboxamido-methyl viologen

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

enzyme: 2-oxo-acid reductase

substrate: carboxamido-methyl viologen


substrate_name: D-ribonate

substrate: D-ribonate


substrate_name: galactarate

substrate: galactarate


substrate_name: D-galactonate

substrate: D-galactonate


substrate_name: D-gulonate

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

substrate: D-gulonate


substrate_name: Lactobionate

substrate: Lactobionate


substrate_name: D-lactate

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

substrate: D-lactate


substrate_name: L-arabinuronate

substrate: L-arabinuronate


substrate_name: D-glucarate

substrate: D-glucarate


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Macropsalliota meleagris

substrate_name: D-galactose

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

enzyme: pyranose dehydrogenase (acceptor)

substrate: D-galactose


substrate_name: D-mannose

substrate: D-mannose


substrate_name: cellobiose

substrate: cellobiose


substrate_name: ferrocenium ion

proof_lines: mutant enzyme N75G/N175Q, at pH 7.5 and 30°C

substrate: ferrocenium ion


proof_lines: mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N75G/N252Q, at pH 7.5 and 30°C


proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 8.5 and 30°C


substrate_name: D-sorbose

substrate: D-sorbose


substrate_name: D-trehalose

substrate: D-trehalose


substrate_name: sucrose

substrate: sucrose


substrate_name: D-maltoheptaose

substrate: D-maltoheptaose


substrate_name: D-maltopentaose

substrate: D-maltopentaose


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


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: L-fucose

substrate: L-fucose


assay_conditions_summary: pH 4; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 4.0 and 30°C


substrate_name: lactose

assay_conditions_summary: pH 8.5; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C

substrate: lactose


proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 8.5 and 30°C


substrate_name: D-glucose

substrate: D-glucose


proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 4.0 and 30°C


proof_lines: wild type enzyme, with D-glucose as cosubstrate, at pH 7.4 and 30°C


assay_conditions_summary: pH 7.4; 303.15 K; cofactor FAD

proof_lines: mutant enzyme H103Y, with D-glucose as cosubstrate, at pH 7.4 and 30°C


substrate_name: L-sorbose

proof_lines: with ferrocenium ion as cosubstrate, pH and temperature not specified in the publication

substrate: L-sorbose


substrate_name: xylobiose

substrate: xylobiose


substrate_name: maltose

assay_conditions_summary: pH 7.5; 303.15 K; buffer phosphate

proof_lines: isoform PDH3, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

proof_lines: isoform PDH2, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

proof_lines: recombinant enzyme, with 0.4 mM ferricenium ion as the electron acceptor, at 30°C in phosphate buffer, pH 7.5

substrate: maltose


substrate_name: methyl-alpha-D-glucopyranoside

proof_lines: isoform PDH1, with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

substrate: methyl-alpha-D-glucopyranoside


assay_conditions_summary: pH 4; 303.15 K; buffer phosphate

proof_lines: isoform PDH3, with D-glucose as cosubstrate, at pH 4.0 and 30°C

proof_lines: isoform PDH2, with D-glucose as cosubstrate, at pH 4.0 and 30°C

proof_lines: recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 2.0


proof_lines: isoform PDH1, with D-glucose as cosubstrate, at pH 4.0 and 30°C


substrate_name: maltotriose

substrate: maltotriose


substrate_name: D-xylose

substrate: D-xylose


enzyme_display_name: (R)-pantolactone dehydrogenase (flavin)

organism: Nocardia asteroides

substrate_name: (R)-pantolactone

enzyme: (R)-pantolactone dehydrogenase (flavin)

substrate: (R)-pantolactone


substrate_name: D-xylobiose

substrate: D-xylobiose


proof_lines: mutant enzyme N75G/N175Q, at pH 7.5 and 30°C


substrate_name: D-mannose

substrate: D-mannose


proof_lines: mutant enzyme N75G/N175Q/N252Q, at pH 7.5 and 30°C


proof_lines: wild type enzyme, with ferrocenium ion as cosubstrate, at pH 8.5 and 30°C


substrate_name: cellobiose

substrate: cellobiose


proof_lines: mutant enzyme N75G/N252Q, at pH 7.5 and 30°C


proof_lines: mutant enzyme N175Q/N252Q, at pH 7.5 and 30°C


organism: Escherichia coli

substrate_name: (S)-Mandelate

proof_lines: chitosan-immobilized enzyme, at pH 3.4 and 45°C

substrate: (S)-Mandelate


substrate_name: D-allose

substrate: D-allose


substrate_name: D-galactose

substrate: D-galactose


substrate_name: ferricenium ion

substrate: ferricenium ion


substrate_name: D-Mannose

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

substrate: D-Mannose


substrate_name: D-Xylose

substrate: D-Xylose


organism: Chlorophyllum rhacodes

substrate_name: D-glucose

proof_lines: 25°C, ferricenium ion as electron acceptor

substrate: D-glucose


substrate_name: L-arabinose

substrate: L-arabinose


organism: Agaricus xanthodermus

source_databases_merged: brenda uniprot


substrate_name: ferricenium hexafluorophosphate

substrate: ferricenium hexafluorophosphate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: D-arabinose

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

proof_lines: at 30°C with 0.4 mM ferricenium as electron acceptor

substrate: D-arabinose


substrate_name: gentiobiose

substrate: gentiobiose


substrate_name: D-maltotriose

substrate: D-maltotriose


organism: Pseudomonas putida

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

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

proof_lines: pH 7.5, 20°C, MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach


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


smiles: CCCCC(C(=O)[O-])O


smiles: CCCC(C(=O)[O-])O


smiles: CCCCCCC(C(=O)[O-])O


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


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


substrate_name: 2-hydroxybutanoate (at pH 7.5 and 20 degrees Celsius)

proof_lines: kcat is 290 sec(-1) with (S)-mandelate as substrate and DCPIP as electron acceptor (at pH 7.5 and 20 degrees Celsius) (PubMed:10493804). kcat is 0.5 sec(-1) with 2-hydroxyoctanoate as substrate and DCPIP as electron acceptor (at pH 7.5 and


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R165G/R277K to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R277G could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme R277G, at 20°C, in 0.1 M potassium phosphate, pH 7.5


sequence_variant_note: Mutation signature R165K/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +1, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


proof_lines: mutant enzyme R277K, at 20°C, in 0.1 M potassium phosphate, pH 7.5


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R277L to reconstruct the assayed variant sequence.


verification_status: corrected

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

column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `DCIP (pH 4)` the AxPDH group prints Km 0.09, kcat 7.65 and kcat/Km 85.0.

normalized_value_unit_evidence: kcat: printed Table 4 cell 7.65 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 7.65 s^(-1). Km: printed cell 0.09 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.09 mM. kcat/Km: printed cell 85.0 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 85.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 7.65 / 0.09 = 85.0 s^-1 mM^-1, against the printed efficiency cell 85.0.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `DCIP (pH 4)`, AxPDH column group: Km = 0.09 mM; kcat = 7.65 s-1; kcat/Km = 85.0 mM-1 s-1.

row_label: Table 4, substrate row `DCIP (pH 4)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)

table_label: Table 4: Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. (Biomolecules 2013, 3(3):535-552)

status: corrected


column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `1,4-BQ (pH 4)` the AxPDH group prints Km 3.25, kcat 12.89 and kcat/Km 4.0.

normalized_value_unit_evidence: kcat: printed Table 4 cell 12.89 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 12.89 s^(-1). Km: printed cell 3.25 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 3.25 mM. kcat/Km: printed cell 4.0 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 4.0 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 12.89 / 3.25 = 3.9661538461538464 s^-1 mM^-1, against the printed efficiency cell 4.0.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `1,4-BQ (pH 4)`, AxPDH column group: Km = 3.25 mM; kcat = 12.89 s-1; kcat/Km = 4.0 mM-1 s-1.

row_label: Table 4, substrate row `1,4-BQ (pH 4)`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)


assay_conditions_summary: pH 7.5; 303.15 K; buffer the standard activity assay: 50 mM sodium phosphate

column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `D-glucose` the AxPDH group prints Km 0.49, kcat 13.02 and kcat/Km 26.6.

normalized_value_unit_evidence: kcat: printed Table 3 cell 13.02 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 13.02 s^(-1). Km: printed cell 0.49 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.49 mM. kcat/Km: printed cell 26.6 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 26.6 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 13.02 / 0.49 = 26.57142857142857 s^-1 mM^-1, against the printed efficiency cell 26.6.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `D-glucose`, AxPDH column group: Km = 0.49 mM; kcat = 13.02 s-1; kcat/Km = 26.6 mM-1 s-1.

row_label: Table 3, substrate row `D-glucose`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)

table_label: Table 3: Apparent kinetic constants for selected electron donors determined at 30 °C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor. (Biomolecules 2013, 3(3):535-552)


column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `L-arabinose` the AxPDH group prints Km 4.16, kcat 22.90 and kcat/Km 5.5.

normalized_value_unit_evidence: kcat: printed Table 3 cell 22.90 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 22.9 s^(-1). Km: printed cell 4.16 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 4.16 mM. kcat/Km: printed cell 5.5 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 5.5 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 22.9 / 4.16 = 5.504807692307692 s^-1 mM^-1, against the printed efficiency cell 5.5.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `L-arabinose`, AxPDH column group: Km = 4.16 mM; kcat = 22.90 s-1; kcat/Km = 5.5 mM-1 s-1.

row_label: Table 3, substrate row `L-arabinose`, AxPDH column group (Km, kcat and kcat/Km for AxPDH)


substrate_name: lactose

proof_lines: with ferrocenium ion as cosubstrate, at pH 7.5 and 30°C

substrate: lactose


assay_conditions_summary: pH 5; buffer phosphate

proof_lines: recombinant enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0

proof_lines: native enzyme, with 25 mM D-glucose as cosubstrate, at 30°C in phosphate buffer, pH 5.0


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

assay_conditions_summary: pH 7.5; 293.15 K; buffer 0.1 M potassium phosphate

proof_lines: in 0.1 M potassium phosphate buffer, pH 7.5 at 20°C

source_databases_merged: brenda skid uniprot


proof_lines: pH 7.5, chimeric mutant of (S)-mandelate dehydrogenase with membrane anchoring loop replaced by a portion of glycolate oxidase from spinach

proof_lines: pH 7.5, 20°C, mutant enzyme MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with 205 residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach


sequence_source: multiple

proof_lines: pH 7.5, (S)-mandelate dehydrogenase with residues 2-4 deleted

proof_lines: pH 7.5, (S)-mandelate dehydrogenase with 17 residues deleted at the carboxy terminus


proof_lines: pH 7.5, 20°C, cosubstrate: 2,6-dichloroindophenol, wild-type enzyme


organism: Rhodotorula graminis

proof_lines: pH 7.5, 25°C, electron acceptor: 2,6-dichloroindophenol

proof_lines: pH 7.5, 25°C, electron acceptor: cytochrome c

proof_lines: pH 7.5, 25°C, electron acceptor: ferricyanide


organism: Agaricus campestris

column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `L-arabinose` the AcPDH group prints Km 4.23, kcat 3.05 and kcat/Km 0.7.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.05 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 3.05 s^(-1). Km: printed cell 4.23 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 4.23 mM. kcat/Km: printed cell 0.7 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 0.7 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 3.05 / 4.23 = 0.7210401891252954 s^-1 mM^-1, against the printed efficiency cell 0.7.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `L-arabinose`, AcPDH column group: Km = 4.23 mM; kcat = 3.05 s-1; kcat/Km = 0.7 mM-1 s-1.

row_label: Table 3, substrate row `L-arabinose`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


column_label: Table 3 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `Lactose` the AcPDH group prints Km 53.16, kcat 3.12 and kcat/Km 0.1.

normalized_value_unit_evidence: kcat: printed Table 3 cell 3.12 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 3.12 s^(-1). Km: printed cell 53.16 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 53.16 mM. kcat/Km: printed cell 0.1 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 0.1 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 3.12 / 53.16 = 0.058690744920993236 s^-1 mM^-1, against the printed efficiency cell 0.1.

raw_value_unit_evidence: Table 3 (electron donors), substrate row `Lactose`, AcPDH column group: Km = 53.16 mM; kcat = 3.12 s-1; kcat/Km = 0.1 mM-1 s-1.

row_label: Table 3, substrate row `Lactose`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 °C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor. Enzyme column group 'AcPDH'; substrate row 'D-glucose'; column 'Km [mM]' = 0.35; column 'kcat [s-1]' = 4.10; column 'kcat/Km [mM-1 s-1]' = 11.7.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.35, header unit mM; already millimolar, no conversion; the exported value is 0.35 mM. kcat: printed Table 3 cell 4.10, header unit s^-1; no conversion; the exported value is 5.23 s^(-1). kcat/Km: printed Table 3 cell 11.7, header unit mM^-1 s^-1, which is the export's own ratio unit; no conversion; the exported value is 14.942857142857145 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, enzyme column group 'AcPDH', substrate row 'D-glucose': Km = 0.35 mM; kcat = 4.10 s^-1; printed kcat/Km = 11.7 mM^-1 s^-1.


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 °C with 25 mM D-glucose as the electron donor. Enzyme column group 'AcPDH'; substrate row 'DCIP (pH 4)'; column 'Km [mM]' = 0.11; column 'kcat [s-1]' = 10.56; column 'kcat/Km [mM-1 s-1]' = 96.0.

normalized_value_unit_evidence: Km: printed Table 4 cell 0.11, header unit mM; already millimolar, no conversion; the exported value is 0.00011 mM. kcat: printed Table 4 cell 10.56, header unit s^-1; no conversion; the exported value is 10.56 s^(-1). kcat/Km: printed Table 4 cell 96.0, header unit mM^-1 s^-1, which is the export's own ratio unit; no conversion; the exported value is 96000.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 4, enzyme column group 'AcPDH', substrate row 'DCIP (pH 4)': Km = 0.11 mM; kcat = 10.56 s^-1; printed kcat/Km = 96.0 mM^-1 s^-1.


column_label: Table 4 carries two column groups, `AcPDH` and `AxPDH`, each with the column heads `Km [mM]`, `kcat [s-1]` and `kcat/Km [mM-1 s-1]`. In the substrate row `1,4-BQ (pH 4)` the AcPDH group prints Km 0.12, kcat 34.82 and kcat/Km 302.8.

normalized_value_unit_evidence: kcat: printed Table 4 cell 34.82 s-1; the table header prints s-1, which is the export unit s^(-1), so no conversion is applied and the paper value is 34.82 s^(-1). Km: printed cell 0.12 mM; the table header prints mM, which is the export unit, so no conversion is applied and the paper value is 0.12 mM. kcat/Km: printed cell 302.8 mM-1 s-1; mM^-1 s^-1 is identical to the export unit s^(-1)*mM^(-1), so no conversion is applied and the paper value is 302.8 s^(-1)*mM^(-1). Closure disclosure: the quotient of this row's own printed component cells is 34.82 / 0.12 = 290.1666666666667 s^-1 mM^-1, against the printed efficiency cell 302.8.

raw_value_unit_evidence: Table 4 (electron acceptors), substrate row `1,4-BQ (pH 4)`, AcPDH column group: Km = 0.12 mM; kcat = 34.82 s-1; kcat/Km = 302.8 mM-1 s-1.

row_label: Table 4, substrate row `1,4-BQ (pH 4)`, AcPDH column group (Km, kcat and kcat/Km for AcPDH)


km_display: Not reported


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H274G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H274G, in presence of 20 mM imidazole


smiles: O=O


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81D to reconstruct the assayed variant sequence.

source_databases_merged: brenda oed


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81V to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxybutyrate. Cells read: kcat cell 0.10 ± 0.01 s-1 and Km cell 32.0 ± 3.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.10 ± 0.01 s-1 equals the exported kcat 0.1 s^(-1) with no unit conversion; Km 32.0 ± 3.5 mM equals the exported km 32.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.003 s-1 mM-1; the exported ratio 0.003125 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxybutyrate: kcat 0.10 ± 0.01 s-1 = 0.1 s^(-1) (no conversion); Km 32.0 ± 3.5 mM = 32.0 mM (no conversion); kcat/Km 0.003125 s^-1 mM^-1 = 0.1 / 32.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxybutyrate	0.10 ± 0.01	32.0 ± 3.5	0.003	0.37 ± 0.03	4.4 ± 1.0	0.08 | the line's leading label is wtMDH | 2-hydroxybutyrate

row_label: wtMDH | 2-hydroxybutyrate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 20°C, mutant enzyme, G81A/MDH-GOX2, a chimeric mutant of (S)-mandelate dehydrogenase with residues 177-215 replaced by residues 176-195 of glycolate oxidase from spinach and a G81A mutation in MDH


proof_lines:
pH 7.5, 20°C, mutant enzyme G81A
mutant G81A
mutant G81A of chimera MDH-GOX2


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyhexanoate. Cells read: kcat cell 0.34 ± 0.02 s-1 and Km cell 4.9 ± 0.4 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.34 ± 0.02 s-1 equals the exported kcat 0.34 s^(-1) with no unit conversion; Km 4.9 ± 0.4 mM equals the exported km 4.9 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.07 s-1 mM-1; the exported ratio 0.06938775510204082 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyhexanoate: kcat 0.34 ± 0.02 s-1 = 0.34 s^(-1) (no conversion); Km 4.9 ± 0.4 mM = 4.9 mM (no conversion); kcat/Km 0.06938775510204082 s^-1 mM^-1 = 0.34 / 4.9.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyhexanoate	0.34 ± 0.02	4.9 ± 0.4	0.07	0.19 ± 0.008	1.4 ± 0.2	0.14 | the line's leading label is wtMDH | 2-hydroxyhexanoate

row_label: wtMDH | 2-hydroxyhexanoate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyvalerate. Cells read: kcat cell 0.36 ± 0.01 s-1 and Km cell 15.3 ± 1.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.36 ± 0.01 s-1 equals the exported kcat 0.36 s^(-1) with no unit conversion; Km 15.3 ± 1.5 mM equals the exported km 15.3 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.024 s-1 mM-1; the exported ratio 0.023529411764705882 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyvalerate	0.36 ± 0.01	15.3 ± 1.5	0.024	0.27 ± 0.02	6.4 ± 1.0	0.04 | the line's leading label is wtMDH | 2-hydroxyvalerate

row_label: wtMDH | 2-hydroxyvalerate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyoctanoate. Cells read: kcat cell 0.5 ± 0.06 s-1 and Km cell 0.8 ± 0.1 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.5 ± 0.06 s-1 equals the exported kcat 0.5 s^(-1) with no unit conversion; Km 0.8 ± 0.1 mM equals the exported km 0.8 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.63 s-1 mM-1; the exported ratio 0.625 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyoctanoate: kcat 0.5 ± 0.06 s-1 = 0.5 s^(-1) (no conversion); Km 0.8 ± 0.1 mM = 0.8 mM (no conversion); kcat/Km 0.625 s^-1 mM^-1 = 0.5 / 0.8.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyoctanoate	0.5 ± 0.06	0.8 ± 0.1	0.63	0.26 ± 0.01	0.14 ± 0.01	1.9 | the line's leading label is wtMDH | 2-hydroxyoctanoate

row_label: wtMDH | 2-hydroxyoctanoate


sequence_variant_note: Resolved canonical sequence from multiple and applied mutation signature G81S to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxyisocaproate. Cells read: kcat cell 0.8 ± 0.05 s-1 and Km cell 4.3 ± 0.2 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.8 ± 0.05 s-1 equals the exported kcat 0.8 s^(-1) with no unit conversion; Km 4.3 ± 0.2 mM equals the exported km 4.3 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.19 s-1 mM-1; the exported ratio 0.186046511627907 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxyisocaproate: kcat 0.8 ± 0.05 s-1 = 0.8 s^(-1) (no conversion); Km 4.3 ± 0.2 mM = 4.3 mM (no conversion); kcat/Km 0.186046511627907 s^-1 mM^-1 = 0.8 / 4.3.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxyisocaproate	0.8 ± 0.05	4.3 ± 0.2	0.19	0.48 ± 0.02	1.6 ± 0.1	0.3 | the line's leading label is wtMDH | 2-hydroxyisocaproate

row_label: wtMDH | 2-hydroxyisocaproate


column_label: Table: Table 3:  wtMDH and the Gly81 Mutants:  Activities with Oxygen as the Electron Acceptor and Redox Potentialsa Printed line read: wtMDH. Cells read: kcat cell 1.2 ± 0.7 s-1 and Km cell 3.2 ± 1.9 mM. Both cells were read from the single printed wtMDH line of this table; the remaining printed cells on that line (kox, Kd(O2), redox potential) were not used. kcat 1.2 ± 0.7 s-1 equals the exported kcat 1.2 s^(-1) with no unit conversion; Km 3.2 ± 1.9 mM equals the exported km 3.2 mM with no unit conversion. This table prints no kcat/Km cell, so the exported ratio is recorded only as the quotient of this line's own two printed cells. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

raw_value_unit_evidence: Table 3:  wtMDH and the Gly81 Mutants:  Activities with Oxygen as the Electron Acceptor and Redox Potentialsa | printed line: wtMDH	1.2 ± 0.7	3.2 ± 1.9	2.5 ± 0.9	2.3 ± 0.9	−91 ± 4 | the line's leading label is wtMDH

row_label: wtMDH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature G81S to reconstruct the assayed variant sequence.


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 2-hydroxy-3-butynoate. Cells read: kcat cell 3.9 ± 0.1 s-1 and Km cell 22.0 ± 1.5 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 3.9 ± 0.1 s-1 equals the exported kcat 3.9 s^(-1) with no unit conversion; Km 22.0 ± 1.5 mM equals the exported km 22.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.177 s-1 mM-1; the exported ratio 0.17727272727272728 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 2-hydroxy-3-butynoate: kcat 3.9 ± 0.1 s-1 = 3.9 s^(-1) (no conversion); Km 22.0 ± 1.5 mM = 22.0 mM (no conversion); kcat/Km 0.17727272727272728 s^-1 mM^-1 = 3.9 / 22.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 2-hydroxy-3-butynoate	3.9 ± 0.1	22.0 ± 1.5	0.177	14.8 ±0.6	4.3 ± 0.5	3.4 | the line's leading label is wtMDH | 2-hydroxy-3-butynoate

row_label: wtMDH | 2-hydroxy-3-butynoate


substrate_name: Phenyllactate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81A to reconstruct the assayed variant sequence.

substrate: Phenyllactate


column_label: Table: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa Printed line read: wtMDH | 3-phenyllactate. Cells read: kcat cell 0.52 ± 0.01 s-1 and Km cell 2.0 ± 0.1 mM. The printed row carries two enzyme column groups; only the wtMDH group's cells were read. The second group's cells on the same line were not used for any value here. kcat 0.52 ± 0.01 s-1 equals the exported kcat 0.52 s^(-1) with no unit conversion; Km 2.0 ± 0.1 mM equals the exported km 2.0 mM with no unit conversion. The same line also prints a separately rounded ratio cell 0.26 s-1 mM-1; the exported ratio 0.26 s^-1 mM^-1 is the quotient of this line's own printed kcat and Km cells and rounds back to that printed cell at the cell's own precision, so the two agree and no correction is warranted. No value here is taken from another printed line, another enzyme column group, another table, or another paper.

normalized_value_unit_evidence: Printed line wtMDH | 3-phenyllactate: kcat 0.52 ± 0.01 s-1 = 0.52 s^(-1) (no conversion); Km 2.0 ± 0.1 mM = 2.0 mM (no conversion); kcat/Km 0.26 s^-1 mM^-1 = 0.52 / 2.0.

raw_value_unit_evidence: Table 2:  Comparison of Substrate Specificity of wtMDH and G81Aa | printed line: 3-phenyllactate	0.52 ± 0.01	2.0 ± 0.1	0.26	0.15 ± 0.002	0.37 ± 0.02	0.4 | the line's leading label is wtMDH | 3-phenyllactate

row_label: wtMDH | 3-phenyllactate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G81V to reconstruct the assayed variant sequence.


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


raw_value_unit_evidence: Table 2 reports 2-hydroxyvalerate row, wtMDH columns: kcat (0.36 +/- 0.01) s^-1, Km (15.3 +/- 1.5) mM, kcat/Km 0.024 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 2-hydroxyvalerate row / wtMDH columns

table_label: Table 2 / Comparison of Substrate Specificity of wtMDH and G81A


raw_value_unit_evidence: Table 2 reports 4-chloromandelate row, wtMDH columns: kcat (334 +/- 6) s^-1, Km (0.27 +/- 0.04) mM, kcat/Km 1237 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 4-chloromandelate row / wtMDH columns


substrate_name: Indoleglycolate

substrate: Indoleglycolate


raw_value_unit_evidence: Table 2 reports indoleglycolate row, wtMDH columns: kcat (122 +/- 14) s^-1, Km (0.40 +/- 0.03) mM, kcat/Km 305 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: indoleglycolate row / wtMDH columns


substrate_name: Indolelactate

substrate: Indolelactate


raw_value_unit_evidence: Table 2 reports 3-indolelactate row, wtMDH columns: kcat (1.0 +/- 0.01) s^-1, Km (0.9 +/- 0.1) mM, kcat/Km 1.1 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: 3-indolelactate row / wtMDH columns


substrate_name: Mandelate

substrate: Mandelate


raw_value_unit_evidence: Table 2 reports mandelate row, wtMDH columns: kcat (350 +/- 10) s^-1, Km (0.24 +/- 0.02) mM, kcat/Km 1458 s^-1 mM^-1. Uncertainty values are numeric uncertainty, not plus/minus assay conditions.

row_label: mandelate row / wtMDH columns


substrate_name: (S)-Mandelate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R165E to reconstruct the assayed variant sequence.

substrate: (S)-Mandelate


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature R165G/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +9, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature R165K/R277G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature R165K/R277K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R277G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R277K 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.


column_label: ScienceDirect article HTML, Table 2; row 2,6-Dichloroindophenol (2 e-) (pH 4); Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=0.06 mM; kcat=57.6 s^-1; printed kcat/Km=958 s^-1 mM^-1; exported kcat/Km=960.0000000000001 s^-1 mM^-1.

row_label: 2,6-Dichloroindophenol (2 e-) (pH 4)

table_label: Table 2


substrate_name: cellobiose

column_label: ScienceDirect article HTML, Table 2; row Cellobiose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=2.45 mM; kcat=24.63 s^-1; printed kcat/Km=10 s^-1 mM^-1; exported kcat/Km=10.461224489795917 s^-1 mM^-1. Exported kcat=25.63 s^-1 but Table 2 prints 24.63 s^-1.

row_label: Cellobiose

substrate: cellobiose


substrate_name: D-galactose

column_label: ScienceDirect article HTML, Table 2; row d-Galactose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=4.19 mM; kcat=28.7 s^-1; printed kcat/Km=6.9 s^-1 mM^-1; exported kcat/Km=6.849642004773269 s^-1 mM^-1.

row_label: d-Galactose

substrate: D-galactose


column_label: ScienceDirect article HTML, Table 2; row d-Glucose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=1.54 mM; kcat=33.7 s^-1; printed kcat/Km=22 s^-1 mM^-1; exported kcat/Km=21.883116883116884 s^-1 mM^-1.

row_label: d-Glucose


substrate_name: ferrocenium ion

substrate: ferrocenium ion


substrate_name: D-Xylose

column_label: ScienceDirect article HTML, Table 2; row d-Xylose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=4.75 mM; kcat=36.9 s^-1; printed kcat/Km=7.8 s^-1 mM^-1; exported kcat/Km=7.768421052631578 s^-1 mM^-1.

row_label: d-Xylose

substrate: D-Xylose


column_label: ScienceDirect article HTML, Table 2; row Lactose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=40.51 mM; kcat=15.95 s^-1; printed kcat/Km=0.4 s^-1 mM^-1; exported kcat/Km=0.3937299432238953 s^-1 mM^-1.

row_label: Lactose


substrate_name: maltose

column_label: ScienceDirect article HTML, Table 2; row Maltose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=2.16 mM; kcat=27.26 s^-1; printed kcat/Km=13 s^-1 mM^-1; exported kcat/Km=12.62037037037037 s^-1 mM^-1.

row_label: Maltose

substrate: maltose


substrate_name: raffinose

column_label: ScienceDirect article HTML, Table 2; row Raffinose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=10.79 mM; kcat=19.61 s^-1; printed kcat/Km=1.8 s^-1 mM^-1; exported kcat/Km=1.8174235403151067 s^-1 mM^-1.

row_label: Raffinose

substrate: raffinose


substrate_name: D-Mannose

column_label: ScienceDirect article HTML, Table 2; row d-Mannose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=109.1 mM; kcat=13.31 s^-1; printed kcat/Km=0.1 s^-1 mM^-1; exported kcat/Km=0.12199816681943172 s^-1 mM^-1.

row_label: d-Mannose

substrate: D-Mannose


column_label: ScienceDirect article HTML, Table 2; row 1,4-Benzoquinone (2 e-) (pH 4); Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=0.566 mM; kcat=44.2 s^-1; printed kcat/Km=78 s^-1 mM^-1; exported kcat/Km=78.09187279151945 s^-1 mM^-1.

row_label: 1,4-Benzoquinone (2 e-) (pH 4)


substrate_name: L-Arabinose

column_label: ScienceDirect article HTML, Table 2; row l-Arabinose; Km, kcat, and kcat/Km columns. Table label: Apparent kinetic constants of recAbPDH for electron acceptors with 25 mM D-glucose at respective pH and for mono-, di- and tri-saccharides with 0.2 mM ferrocenium hexafluorophosphate at pH 7.5.

normalized_value_unit_evidence: normalized Table 2 values: Km=1.33 mM; kcat=29.6 s^-1; printed kcat/Km=22 s^-1 mM^-1; exported kcat/Km=22.25563909774436 s^-1 mM^-1.

row_label: l-Arabinose

substrate: L-Arabinose


column_label: Table 2 row 2-hydroxy-3-butynoate under wtMDH columns gives kcat 3.9 +/- 0.1 s^-1, Km 22.0 +/- 1.5 mM, and explicit kcat/Km 0.177 s^-1 mM^-1.

normalized_value_unit_evidence: Export has kcat=3.9 s^-1, Km=22.0 mM, kcat/Km=0.17727272727272728 s^-1*mM^-1; explicit paper column normalizes to kcat/Km=0.177 s^-1*mM^-1.

table_label: Table 2: Comparison of Substrate Specificity of wtMDH and G81A


column_label: Table 2 row 2-hydroxybutyrate under wtMDH columns gives kcat 0.10 +/- 0.01 s^-1, Km 32.0 +/- 3.5 mM, and explicit kcat/Km 0.003 s^-1 mM^-1.

normalized_value_unit_evidence: Export has kcat=0.1 s^-1, Km=32.0 mM, kcat/Km=0.003125 s^-1*mM^-1; explicit paper column normalizes to kcat/Km=0.003 s^-1*mM^-1.


smiles: CCCCC(O)C(=O)[O-]


column_label: Table 2 row 2-hydroxyhexanoate under wtMDH columns gives kcat 0.34 +/- 0.02 s^-1, Km 4.9 +/- 0.4 mM, and explicit kcat/Km 0.07 s^-1 mM^-1.

normalized_value_unit_evidence: Export has kcat=0.34 s^-1, Km=4.9 mM, kcat/Km=0.06938775510204082 s^-1*mM^-1; explicit paper column normalizes to kcat/Km=0.07 s^-1*mM^-1.


column_label: Table 2 row 2-hydroxyisocaproate under wtMDH columns gives kcat 0.8 +/- 0.05 s^-1, Km 4.3 +/- 0.2 mM, and explicit kcat/Km 0.19 s^-1 mM^-1.

normalized_value_unit_evidence: Export has kcat=0.8 s^-1, Km=4.3 mM, kcat/Km=0.186046511627907 s^-1*mM^-1; explicit paper column normalizes to kcat/Km=0.19 s^-1*mM^-1.


smiles: CCCCCCC(O)C(=O)[O-]


column_label: Table 2 row 2-hydroxyoctanoate under wtMDH columns gives kcat 0.5 +/- 0.06 s^-1, Km 0.8 +/- 0.1 mM, and explicit kcat/Km 0.63 s^-1 mM^-1.

normalized_value_unit_evidence: Export has kcat=0.5 s^-1, Km=0.8 mM, kcat/Km=0.625 s^-1*mM^-1; explicit paper column normalizes to kcat/Km=0.63 s^-1*mM^-1.


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row DCIP (pH 4); AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.11, 10.56, 96.0

normalized_value_unit_evidence: Km=0.11 mM; kcat=10.56 s^-1; kcat/Km=96.0 s^-1 mM^-1 (explicit table value)

row_label: DCIP (pH 4)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row D-galactose; AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 7.13, 5.23, 0.7

normalized_value_unit_evidence: Km=7.13 mM; kcat=5.23 s^-1; kcat/Km=0.7 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AcPDH / D-galactose: Km=7.13 mM; kcat=5.23 s^-1; kcat/Km=0.7 mM^-1 s^-1

row_label: D-galactose


substrate_name: D-glucose

column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row D-glucose; AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.35, 4.10, 11.7

normalized_value_unit_evidence: Km=0.35 mM; kcat=4.10 s^-1; kcat/Km=11.7 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AcPDH / D-glucose: Km=0.35 mM; kcat=4.10 s^-1; kcat/Km=11.7 mM^-1 s^-1

row_label: D-glucose

substrate: D-glucose


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row Fc+PF6 (pH 8.5); AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 1.19, 19.92, 16.7

normalized_value_unit_evidence: Km=1.19 mM; kcat=19.92 s^-1; kcat/Km=16.7 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row D-xylose; AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 4.19, 6.37, 1.5

normalized_value_unit_evidence: Km=4.19 mM; kcat=6.37 s^-1; kcat/Km=1.5 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AcPDH / D-xylose: Km=4.19 mM; kcat=6.37 s^-1; kcat/Km=1.5 mM^-1 s^-1

row_label: D-xylose


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row 1,4-BQ (pH 4); AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.12, 34.82, 302.8

normalized_value_unit_evidence: Km=0.12 mM; kcat=34.82 s^-1; kcat/Km=302.8 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row L-arabinose; AcPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 4.23, 3.05, 0.7

normalized_value_unit_evidence: Km=4.23 mM; kcat=3.05 s^-1; kcat/Km=0.7 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AcPDH / L-arabinose: Km=4.23 mM; kcat=3.05 s^-1; kcat/Km=0.7 mM^-1 s^-1

row_label: L-arabinose


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row DCIP (pH 4); AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.09, 7.65, 85.0

normalized_value_unit_evidence: Km=0.09 mM; kcat=7.65 s^-1; kcat/Km=85.0 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row D-glucose; AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.49, 13.02, 26.6

normalized_value_unit_evidence: Km=0.49 mM; kcat=13.02 s^-1; kcat/Km=26.6 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AxPDH / D-glucose: Km=0.49 mM; kcat=13.02 s^-1; kcat/Km=26.6 mM^-1 s^-1


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row Fc+PF6 (pH 8.5); AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 0.03, 22.07, 735.7

normalized_value_unit_evidence: Km=0.03 mM; kcat=22.07 s^-1; kcat/Km=735.7 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row Lactose; AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 293.84, 24.65, 0.1

normalized_value_unit_evidence: Km=293.84 mM; kcat=24.65 s^-1; kcat/Km=0.1 s^-1 mM^-1 (explicit table value)


column_label: Table 4. Apparent kinetic constants for selected electron acceptors determined at 30 C with 25 mM D-glucose as the electron donor; row 1,4-BQ (pH 4); AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 3.25, 12.89, 4.0

normalized_value_unit_evidence: Km=3.25 mM; kcat=12.89 s^-1; kcat/Km=4.0 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row D-xylose; AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 1.44, 29.16, 20.3

normalized_value_unit_evidence: Km=1.44 mM; kcat=29.16 s^-1; kcat/Km=20.3 s^-1 mM^-1 (explicit table value)


column_label: Table 3. Apparent kinetic constants for selected electron donors determined at 30 C with 0.2 mM ferrocenium hexafluorophosphate as the electron acceptor; row L-arabinose; AxPDH columns Km (mM), kcat (s^-1), kcat/Km (mM^-1 s^-1); cells 4.16, 22.90, 5.5

normalized_value_unit_evidence: Km=4.16 mM; kcat=22.90 s^-1; kcat/Km=5.5 s^-1 mM^-1 (explicit table value)

raw_value_unit_evidence: AxPDH / L-arabinose: Km=4.16 mM; kcat=22.90 s^-1; kcat/Km=5.5 mM^-1 s^-1


column_label: Table 2; row label: (R,S)-3-phenyllactate; metric column: KM (mM); raw value: 2.0 +/- 0.1; raw unit: mM; normalized value: 2.0; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 2.0 mM

raw_value_unit_evidence: Table 2 KM column reports 2.0 +/- 0.1 mM for (R,S)-3-phenyllactate.

table_label: Table 2: Relative Steady-State Kinetic Parameters at pH 7.5 for MDH with Alternate Substrates

source_databases_merged: brenda skid


column_label: Table 2; row label: (R,S)-2-hydroxyisocaproate; metric column: KM (mM); raw value: 4.3 +/- 0.2; raw unit: mM; normalized value: 4.3; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 4.3 mM

raw_value_unit_evidence: Table 2 KM column reports 4.3 +/- 0.2 mM for (R,S)-2-hydroxyisocaproate.


column_label: Table 2; row label: (R,S)-2-hydroxyisovalerate; metric column: KM (mM); raw value: 9.5 +/- 1.7; raw unit: mM; normalized value: 9.5; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 9.5 mM

raw_value_unit_evidence: Table 2 KM column reports 9.5 +/- 1.7 mM for (R,S)-2-hydroxyisovalerate.


column_label: Table 2; row label: (R,S)-2-hydroxyvalerate; metric column: KM (mM); raw value: 15.3 +/- 1.5; raw unit: mM; normalized value: 15.3; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 15.3 mM

raw_value_unit_evidence: Table 2 KM column reports 15.3 +/- 1.5 mM for (R,S)-2-hydroxyvalerate.


substrate_name: (R,S)-2-hydroxy-3-butynoic acid

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

column_label: Table 2; row label: (R,S)-2-hydroxy-3-butynoate; metric column: KM (mM); raw value: 22.0 +/- 1.5; raw unit: mM; normalized value: 22.0; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 22.0 mM

raw_value_unit_evidence: Table 2 KM column reports 22.0 +/- 1.5 mM for (R,S)-2-hydroxy-3-butynoate.

substrate: (R,S)-2-hydroxy-3-butynoic acid


column_label: Table 2; row label: (R,S)-2-hydroxybutyrate; metric column: KM (mM); raw value: 32.0 +/- 3.5; raw unit: mM; normalized value: 32.0; normalized unit: mM; assay condition: 100 mM potassium phosphate buffer pH 7.5 at 20 C with 100 uM DCPIP, 1 mM PMS, and 1 mg/mL BSA; Table 2 footnote states assay conditions were as in Table 1.

normalized_value_unit_evidence: Km 32.0 mM

raw_value_unit_evidence: Table 2 KM column reports 32.0 +/- 3.5 mM for (R,S)-2-hydroxybutyrate.


organism: Leucoagaricus meleagris

sequence_variant_note: Mutation signature H103Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Official EuropePMC PDF text extraction lines 412-430: Table 3; AmPDH row DCIP (pH 4); columns Km, kcat, kcat/Km; cells 0.14 mM, 40.7 s^-1, 290.7 mM^-1 s^-1.

raw_value_unit_evidence: Table 3 AmPDH DCIP (pH 4) row cells report Km 0.14 mM, kcat 40.7 s^-1, and kcat/Km 290.7 mM^-1 s^-1.

row_label: AmPDH; DCIP (pH 4)

table_label: Table 3 apparent kinetic constants for selected electron acceptors


column_label: Table 3 keeps recombinant and native rows distinct; no exact single row gives 15.1 / 0.61 / 24.754.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 15.1 s^-1; Km 0.55 mM; kcat/Km 25.5 s^-1 mM^-1.

row_label: Native AmPDH / 2-chloro-1,4-benzoquinone

table_label: Table 3. Apparent kinetic constants of recombinant and native AmPDH for several electron acceptors


substrate_name: ferricenium ion

column_label: Table 3 row Fc+PF6- under recombinant AmPDH gives Km 0.22, kcat 203, kcat/Km 923.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 203.0 s^-1; Km 0.22 mM; kcat/Km 923 s^-1 mM^-1.

row_label: Recombinant AmPDH / ferricenium hexafluorophosphate (Fc+PF6-)

substrate: ferricenium ion


substrate_name: lactose

column_label: Table 2 separates recombinant and native lactose rows; no row gives exported 41.0 / 128.0 exactly.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 39.6 s^-1; Km 134.0 mM; kcat/Km 0.29 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 native AmPDH lactose: Km 134 +/- 6.3 mM; kcat 39.6 +/- 0.8 s^-1; kcat/Km 0.29 M^-1 s^-1. Recombinant lactose row: Km 113.94 +/- 7.48 mM; kcat 31.9 +/- 8.4 s^-1; kcat/Km 0.28.

row_label: Native AmPDH / Lactose

table_label: Table 2. Apparent kinetic constants of recombinant and native AmPDH produced for several electron donors

substrate: lactose


column_label: Table 2 has no D-xylose row with kcat 62.4 or kcat/Km 32.33.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 43.4 s^-1; Km 1.93 mM; kcat/Km 22.9 s^-1 mM^-1.

row_label: Native AmPDH / D-xylose


organism: Phanerodontia chrysosporium


proof_lines:
Raw SKiD Env: Temp=30°C, pH=2
Raw SKiD Env: Temp=30°C, pH=3
Raw SKiD Env: Temp=30°C, pH=4

source_databases_merged: skid uniprot


proof_lines:
Raw SKiD Env: Temp=30°C, pH=5
Raw SKiD Env: Temp=30°C, pH=-----


enzyme_display_name: Pyranose dehydrogenase 1

substrate_name: 2,5-dichloro-1,4-benzoquinone (at pH 5.0 with D-glucose as substrate)

enzyme: Pyranose dehydrogenase 1


substrate_name: methyl-1,4-benzoquinone (at pH 8.0 with D-glucose as substrate)

assay_conditions_summary: pH 8


enzyme_display_name: glucose-fructose oxidoreductase

organism: Zymomonas mobilis

substrate_name: gluconolactone

enzyme: glucose-fructose oxidoreductase

substrate: gluconolactone


substrate_name: sorbitol

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

substrate: sorbitol


substrate_name: D-fructose

substrate: D-fructose


substrate_name: cellobiose


substrate_name: Ethyl (S)-mandelate

substrate: Ethyl (S)-mandelate


proof_lines: ethyl and methyl esters of (S)-mandelic acid are substrates for MDH


substrate_name: Methyl (S)-mandelate

substrate: Methyl (S)-mandelate


substrate_name: ferricyanide

column_label: PMC article prose metric sentence gives kcat for ferricyanide as 550 s-1 at 25 C

normalized_value_unit_evidence: PMC article prose kcat normalized_value=550 normalized_unit=s^-1

raw_value_unit_evidence: PMC article prose: artificial (ferricyanide, kcat=550 s-1 at 25 degrees C)

row_label: ferricyanide artificial electron acceptor sentence

table_label: PMC article prose

substrate: ferricyanide


substrate_name: (S)-Mandelate

proof_lines:
Pseudomonas putida
(S)-mandelate dehydrogenase
benzoylformate

substrate: (S)-Mandelate


enzyme_display_name: gluconate 2-dehydrogenase (acceptor)

organism: Gluconobacter oxydans

substrate_name: D-gluconate

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

enzyme: gluconate 2-dehydrogenase (acceptor)

substrate: D-gluconate


enzyme_display_name: glycerol dehydrogenase (acceptor)

substrate_name: glycerol

smiles: C(C(CO)O)O

proof_lines:
membrane fraction
solubilized enzyme

enzyme: glycerol dehydrogenase (acceptor)

substrate: glycerol


substrate_name: meso-erythritol

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

substrate: meso-erythritol


substrate_name: D-arabitol

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

substrate: D-arabitol


organism: Amycolatopsis methanolica

substrate_name: isobutanol (at pH 6.3 and 30 degrees Celsius)

smiles: CC(C)CO


substrate_name: butanol (at pH 6.3 and 30 degrees Celsius)

smiles: CCCCO


substrate_name: propanol (at pH 6.3 and 30 degrees Celsius)

smiles: CCCO


substrate_name: formaldehyde (at pH 6.3 and 30 degrees Celsius)

smiles: C=O


substrate_name: 2-methoxyethanol (at pH 6.3 and 30 degrees Celsius)

smiles: COCCO


substrate_name: NDMA (at pH 6.3 and 30 degrees Celsius)

smiles: CN(C)N=O

substrate: NDMA (at pH 6.3 and 30 degrees Celsius)


substrate_name: ethyleneglycol (at pH 6.3 and 30 degrees Celsius)

smiles: C(CO)O


substrate_name: ethanol (at pH 6.3 and 30 degrees Celsius)

smiles: CCO


substrate_name: propan-2-ol (at pH 6.3 and 30 degrees Celsius)

smiles: CC(C)O


substrate_name: glycerol (at pH 6.3 and 30 degrees Celsius)


substrate_name: methanol (at pH 6.3 and 30 degrees Celsius)

smiles: CO


substrate_name: ethanolamine (at pH 6.3 and 30 degrees Celsius)

smiles: C(CO)N


substrate_name: CTP

assay_conditions_summary: cofactor ATP

proof_lines: presence of ATP, pH not specified in the publication, temperature not specified in the publication

substrate: CTP


substrate_name: GTP

proof_lines: presence of dTTP, pH not specified in the publication, temperature not specified in the publication

substrate: GTP


substrate_name: UTP

substrate: UTP


substrate_name: ATP

proof_lines: presence of dGTP, pH not specified in the publication, temperature not specified in the publication

substrate: ATP


substrate_name: Unknown

ki_unit: mM

proof_lines: substrate ATP, pH not specified in the publication, temperature not specified in the publication

proof_lines: substrate GTP, pH not specified in the publication, temperature not specified in the publication

substrate: Unknown


enzyme_display_name: alcohol dehydrogenase (azurin)

proof_lines:
isoform ADH IIB, pH 8.0
isoform ADH IIG, pH 8.0

enzyme: alcohol dehydrogenase (azurin)


smiles: CC(CO)O

proof_lines:
isoform ADH IIG, pH 8.0
isoform ADH IIB, pH 8.0


substrate_name: glycerol


substrate_name: ethanol

substrate: ethanol


enzyme_display_name: hydroxyacid-oxoacid transhydrogenase

organism: Rattus norvegicus

substrate_name: Succinic semialdehyde

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

enzyme: hydroxyacid-oxoacid transhydrogenase

substrate: Succinic semialdehyde


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


enzyme_display_name: NDMA-dependent alcohol dehydrogenase

organism: Rhodococcus erythropolis

substrate_name: 4-methylheptan-3-ol (when NDMA is the electron acceptor)

sequence: MKTKAAVLFETHKPFEIVELEL

wild_type_sequence: MKTKAAVLFETHKPFEIVELEL

smiles: CCCC(C)C(CC)O

proof_lines: The lower limit of the determination of KM with NDMA as electron acceptor was 0.001 mM. KM was even lower for hexan-1-ol, pentan-1-ol, and citronellol.

enzyme: NDMA-dependent alcohol dehydrogenase


substrate_name: 1-phenylethanol (when NDMA is the electron acceptor)


substrate_name: 1-phenylpropan-1-ol (when NDMA is the electron acceptor)


substrate_name: 1-phenylpropan-2-ol (when NDMA is the electron acceptor)


substrate_name: 1-phenylbutan-2-ol (when NDMA is the electron acceptor)


substrate_name: cyclohexanol (when NDMA is the electron acceptor)


substrate_name: propane-1,2-diol (when NDMA is the electron acceptor)


substrate_name: propane-1,3-diol (when NDMA is the electron acceptor)

smiles: C(CO)CO


substrate_name: 3-butene-1,2-diol (when NDMA is the electron acceptor)

smiles: C=CC(CO)O


substrate_name: pentane-1,2-diol (when NDMA is the electron acceptor)

smiles: CCCC(CO)O


substrate_name: 1-phenylethane-1,2-diol (when NDMA is the electron acceptor)


substrate_name: formaldehyde (when NDMA is the electron acceptor)


substrate_name: acetaldehyde (when veratryl alcohol is the electron donor)

smiles: CC=O


substrate_name: benzaldehyde (when veratryl alcohol is the electron donor)


substrate_name: 2-phenylpropionaldehyde (when veratryl alcohol is the electron donor)


substrate_name: 3-phenylpropionaldehyde (when veratryl alcohol is the electron donor)


substrate_name: 3-phenylbutyraldehyde (when veratryl alcohol is the electron donor)


substrate_name: glyoxal (when veratryl alcohol is the electron donor)

smiles: C(=O)C=O


substrate_name: methylglyoxal (when veratryl alcohol is the electron donor)

smiles: CC(=O)C=O


substrate_name: phenylglyoxal (when veratryl alcohol is the electron donor)


substrate_name: hydroxyacetone (when veratryl alcohol is the electron donor)

smiles: CC(=O)CO


substrate_name: cyclohexanone (when veratryl alcohol is the electron donor)


substrate_name: NDMA (when veratryl alcohol is the electron donor)

smiles: CN(C)N=O


enzyme_display_name: alcohol dehydrogenase (nicotinoprotein)

smiles: CCCCO

proof_lines: KM for benzylalcohol is lower than 0.005 mM.

enzyme: alcohol dehydrogenase (nicotinoprotein)


smiles: CCCO


substrate_name: ethanol

smiles: CCO


smiles: CCC(C)O


smiles: CC(C)O


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: soluble quinoprotein glucose dehydrogenase

organism: Acinetobacter calcoaceticus

substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T416V/T417V with inferred residue-numbering offset -17 to reconstruct the assayed variant sequence.

substrate: D-glucose


sequence_variant_note: Mutation signature D340F/Y418F could not be applied safely because the resolved sequence does not match the expected reference residue(s).

enzyme: soluble quinoprotein glucose dehydrogenase


sequence_variant_note: Mutation signature D340F/Y418I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: ethanol (when NDMA is the electron acceptor)


substrate_name: propan-1-ol (when NDMA is the electron acceptor)


substrate_name: butan-1-ol (when NDMA is the electron acceptor)


substrate_name: heptan-1-ol (when NDMA is the electron acceptor)

smiles: CCCCCCCO


substrate_name: octan-1-ol (when NDMA is the electron acceptor)

smiles: CCCCCCCCO


substrate_name: 2-propen-1-ol (when NDMA is the electron acceptor)

smiles: C=CCO


substrate_name: isobutanol (when NDMA is the electron acceptor)

smiles: CC(C)CO


substrate_name: 3-methylbutan-1-ol (when NDMA is the electron acceptor)

smiles: CC(C)CCO


substrate_name: benzyl alcohol (when NDMA is the electron acceptor)


substrate_name: 4-hydroxybenzyl alcohol (when NDMA is the electron acceptor)


substrate_name: vanillyl alcohol (when NDMA is the electron acceptor)


substrate_name: veratryl alcohol (when NDMA is the electron acceptor)


substrate_name: 2-phenylethanol (when NDMA is the electron acceptor)


substrate_name: 2-phenylpropan-1-ol (when NDMA is the electron acceptor)


substrate_name: 3-phenylpropan-1-ol (when NDMA is the electron acceptor)


substrate_name: cinnamyl alcohol (when NDMA is the electron acceptor)


substrate_name: coniferyl alcohol (when NDMA is the electron acceptor)


substrate_name: 2-phenylbutan-1-ol (when NDMA is the electron acceptor)


substrate_name: propan-2-ol (when NDMA is the electron acceptor)


substrate_name: butan-2-ol (when NDMA is the electron acceptor)


substrate_name: pentan-2-ol (when NDMA is the electron acceptor)

smiles: CCCC(C)O


substrate_name: hexan-2-ol (when NDMA is the electron acceptor)

smiles: CCCCC(C)O


substrate_name: heptan-2-ol (when NDMA is the electron acceptor)

smiles: CCCCCC(C)O


substrate_name: octan-2-ol (when NDMA is the electron acceptor)

smiles: CCCCCCC(C)O


substrate_name: 3-methylheptan-4-ol (when NDMA is the electron acceptor)

smiles: CCCC(C(C)CC)O


substrate_name: D-glucose


substrate_name: lactose

proof_lines: electron transfer mediator: N,N'-dimethyl-4,4'-azopyridinium methyl sulfate, pH 8.0, temperature not specified in the publication

proof_lines: electron transfer mediator: 1-(N,N-dimethylamine)-4-(4-morpholine)benzene, pH 8.0, temperature not specified in the publication

proof_lines: electron transfer mediator: N,N'-dimethyl-4,4'-azopyridinium methyl sulfate, pH 7.0, temperature not specified in the publication

substrate: lactose


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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

column_label: Table 2. Kinetic properties of the d-2HG-pyruvate transhydrogenase activity of Dld2 and Dld3, Table 2 / d-2HG / Dld2: Km=74 uM.

raw_value_unit_evidence: Km=74 uM

row_label: Table 2 / d-2HG / Dld2


substrate_name: (R)-lactate

column_label: Table 1. Kinetic properties of the d-2HG and d-lactate dehydrogenase activities of Dld2 and Dld3, Table 1 / d-Lactate / Dld2: Km=5215 uM.

row_label: Table 1 / d-Lactate / Dld2

substrate: (R)-lactate


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

column_label: Table 2. Kinetic properties of the d-2HG-pyruvate transhydrogenase activity of Dld2 and Dld3, Table 2 / d-2HG / Dld3: Km=111 uM.

raw_value_unit_evidence: Km=111 uM

row_label: Table 2 / d-2HG / Dld3


substrate_name: pyruvate

column_label: Table 2. Kinetic properties of the d-2HG-pyruvate transhydrogenase activity of Dld2 and Dld3, Table 2 / Pyruvate / Dld3: Km=450 uM.

raw_value_unit_evidence: Km=450 uM

row_label: Table 2 / Pyruvate / Dld3

substrate: pyruvate


column_label: Table 1. Kinetic properties of the d-2HG and d-lactate dehydrogenase activities of Dld2 and Dld3, Table 1 / d-Lactate / Dld3: Km=533 uM.

raw_value_unit_evidence: Km=533 uM

row_label: Table 1 / d-Lactate / Dld3


sequence_variant_note: Mutation signature N462H could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: D-galactose

substrate: D-galactose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N452T to reconstruct the assayed variant sequence.


substrate_name: D-lactose

substrate: D-lactose


substrate_name: D-maltose

substrate: D-maltose


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


sequence_variant_note: Mutation signature N428C could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Arabidopsis thaliana

substrate_name: (R)-2-hydroxyglutarate (with DCIP as acceptor molecule)

proof_lines: Very low activity toward D-lactate, D-2-hydroxybutyrate and meso-tartrate. Does not efficiently use cytochrome c as electron acceptor and is not able to transfer electrons to NAD or NADP.


organism: Niallia circulans

substrate_name: S-adenosyl-L-methionine

proof_lines:
pH 8.0, 28°C
pH 8.0, 28°C, EDTA-treated enzyme
Raw SKiD Env: Temp=28°C, pH=8

substrate: S-adenosyl-L-methionine


enzyme_display_name: D-2-hydroxyglutarate dehydrogenase

organism: Stutzerimonas stutzeri (strain A1501)

substrate_name: D-2-hydroxyglutarate (at pH 7.4 and 37 degrees Celsius)

proof_lines: kcat is 7.9 sec(-1) with D-2-hydroxyglutarate as substrate and DCIP as the electron acceptor (at pH 7.4 and 37 degrees Celsius). kcat is 13.0 sec(-1) with D-2-hydroxyglutarate as substrate and electron transfer flavoprotein (ETF) as the ele

enzyme: D-2-hydroxyglutarate dehydrogenase


organism: Pantoea ananatis (strain AJ13355)


organism: Escherichia coli (strain K12)

column_label: Results state: The apparent Km value for D-2-HGA was 83 microM for D2HGDHEc and 208 microM for D2HGDHPa; Table 2 lists D2HGDH (YdiJ) E. coli Km(D-2-HGA) 83 +/- 5 microM.

raw_value_unit_evidence: Km raw_value=83 raw_unit=microM

row_label: D2HGDH (YdiJ) E. coli with D-2-HGA / (R)-2-hydroxyglutarate

table_label: PMC full-text PMID 36144368 / Table 2 and Results paragraph


substrate_name: D-malate (at pH 7.4 and 30 degrees Celsius)

column_label: Table 2 lists D2HGDH of P. stutzeri with D-Malate Km 3.61 +/- 0.14 mM.

raw_value_unit_evidence: Km raw_value=3.61 +/- 0.14 raw_unit=mM

row_label: D2HGDH of P. stutzeri / D-Malate

table_label: Table 2, Steady-state kinetic parameters of D2HGDH toward different substrates


proof_lines: recombinant wild-type with R4-tail, pH 7.0

proof_lines: heterodimer wild-type/mutant H168Q, pH 7.0


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E277K with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.


substrate_name: D-xylose

substrate: D-xylose


organism: Homo sapiens

column_label: Supplementary Table S1 row D-2-HG WT, column Km (mM), reports 0.12+0.01.

raw_value_unit_evidence: Km raw_value=0.12+0.01 raw_unit=mM

row_label: D-2-HG WT

table_label: Supplementary Table S1


substrate_name: D-malate

column_label: Supplementary Table S1 row D-MAL WT, column Km (mM), reports 0.17+/-0.01.

raw_value_unit_evidence: Km raw_value=0.17+/-0.01 raw_unit=mM

row_label: D-MAL WT

substrate: D-malate


substrate_name: D-lactate

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

column_label: Supplementary Table S1 row D-LAC WT, column Km (mM), reports 0.15+/-0.05.

raw_value_unit_evidence: Km raw_value=0.15+/-0.05 raw_unit=mM

row_label: D-LAC WT

substrate: D-lactate


organism: Agaricus bisporus

substrate_name: D-mannose

proof_lines: with ferrocenium ion as electron acceptor, in 100 mM sodium phosphate pH 7.5, at 30°C

substrate: D-mannose


substrate_name: raffinose

substrate: raffinose


substrate_name: L-arabinose

substrate: L-arabinose


proof_lines: with D-glucose as cosubstrate, in 100 mM sodium acetate pH 4.0, at 30°C


proof_lines: with D-glucose as cosubstrate, in 100 mM sodium phosphate pH 7.5, at 30°C


substrate_name: ferrocenium ion

substrate: ferrocenium ion


organism: Pseudomonas aeruginosa

substrate_name: coenzyme Q1

substrate: coenzyme Q1


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


substrate_name: ferricyanide

substrate: ferricyanide


substrate_name: Unknown

substrate: Unknown


organism: Xanthomonas citri pv. viticola (strain LMG 965 / NCPPB 2475 / ICMP 3867 / CFBP 7660)

substrate_name: D-2-hydroxyglutarate (at pH 7.4 and 25 degrees Celsius)

column_label: Table 1, enzyme A0A077SBA9, substrate D-2-hydroxyglutarate, KM column cell 0.08 +/- 0.01 x 10^-3 M.

normalized_value_unit_evidence: KM normalized_value=0.08 normalized_unit=mM from 0.08 x 10^-3 M.

raw_value_unit_evidence: Table 1 A0A077SBA9 D-2-hydroxyglutarate cells: KM raw_value=0.08 +/- 0.01 x 10^-3 raw_unit=M; kcat raw_value=5.957 raw_unit=s^-1; kcat/KM raw_value=7.29 x 10^4 raw_unit=M^-1 s^-1.

row_label: A0A077SBA9 D-2-hydroxyglutarate row

table_label: PMC8491902 Table 1


substrate_name: D-malate (at pH 7.4 and 25 degrees Celsius)

column_label: Table 1, enzyme A0A077SBA9, substrate D-malate, KM column cell 5.03 +/- 1.38 x 10^-3 M.

normalized_value_unit_evidence: KM normalized_value=5.03 normalized_unit=mM from 5.03 x 10^-3 M.

raw_value_unit_evidence: Table 1 A0A077SBA9 D-malate cells: KM raw_value=5.03 +/- 1.38 x 10^-3 raw_unit=M; kcat raw_value=0.039 raw_unit=s^-1; kcat/KM raw_value=7.78 raw_unit=M^-1 s^-1.

row_label: A0A077SBA9 D-malate row


enzyme_display_name: alcohol oxidase

organism: [Candida] sp.

substrate_name: methanol

smiles: CO

enzyme: alcohol oxidase

substrate: methanol


substrate_name: ethanol

smiles: CCO

substrate: ethanol


organism: Rhodococcus jostii

substrate_name: D-glucose 6-phosphate

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

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

proof_lines: kcat above 0.047 s-1, mutant enzyme R282Q, at pH 7.5 and 25°C

proof_lines: Km above 100 mM, mutant enzyme R282Q, at pH 7.5 and 25°C

substrate: D-glucose 6-phosphate


proof_lines:
pH 8.0, 28°C
Raw SKiD Env: Temp=28°C, pH=8


enzyme_display_name: (S)-2-hydroxy-acid oxidase

organism: Spinacia oleracea

substrate_name: glycerate

enzyme: (S)-2-hydroxy-acid oxidase

substrate: glycerate


enzyme_display_name: UniProt Q92UV7

organism: Sinorhizobium meliloti

substrate_name: glyceraldehyde 3-phosphate

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

enzyme: UniProt Q92UV7

substrate: glyceraldehyde 3-phosphate


substrate_name: phosphonoacetaldehyde

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.5
Raw SKiD Env: Temp=30°C, pH=-----

substrate: phosphonoacetaldehyde


enzyme_display_name: UniProt Q72KD3

organism: Thermus thermophilus

substrate_name: propanal

smiles: CCC=O

enzyme: UniProt Q72KD3

substrate: propanal


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Acetobacter pasteurianus

substrate_name: acetaldehyde

smiles: CC=O

enzyme: aldehyde dehydrogenase (NADP+)

substrate: acetaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


enzyme_display_name: UniProt G7VCG0

organism: Pyrobaculum ferrireducens

substrate_name: propionaldehyde

enzyme: UniProt G7VCG0

substrate: propionaldehyde


substrate_name: glyceraldehyde

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

substrate: glyceraldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


enzyme_display_name: UniProt P30838

enzyme: UniProt P30838


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


enzyme_display_name: UniProt Q13WK4

organism: Paraburkholderia xenovorans LB400

substrate_name: Valeraldehyde

smiles: CCCCC=O

enzyme: UniProt Q13WK4

substrate: Valeraldehyde


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


enzyme_display_name: UniProt P17202

proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P17202


enzyme_display_name: UniProt Q9L4P8

organism: Staphylococcus aureus

substrate_name: NADP+

enzyme: UniProt Q9L4P8

substrate: NADP+


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


organism: Saccharomyces cerevisiae

column_label: Table 2. Kinetic properties of the d-2HG-pyruvate transhydrogenase activity of Dld2 and Dld3, Table 2 / d-2HG / Dld3: Km=111 uM; kcat=4.0 s^-1; kcat/Km=3.6 x 10^4 s^-1 M^-1.


substrate_name: pyruvate

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

column_label: Table 2. Kinetic properties of the d-2HG-pyruvate transhydrogenase activity of Dld2 and Dld3, Table 2 / Pyruvate / Dld3: Km=450 uM; kcat=4.9 s^-1; kcat/Km=1.2 x 10^4 s^-1 M^-1.

substrate: pyruvate


enzyme_display_name: glucose 1-dehydrogenase (PQQ, quinone)

organism: Pseudomonas putida

substrate_name: ubiquinone

proof_lines: Km below 0.0002 mM, native enzyme, at pH 7.5 and 28°C

enzyme: glucose 1-dehydrogenase (PQQ, quinone)

substrate: ubiquinone


substrate_name: D-glucose

proof_lines:
recombinant enzyme, at pH 7.5 and 28°C
native enzyme, at pH 7.5 and 28°C

substrate: D-glucose


enzyme_display_name: aldehyde dehydrogenase [NAD(P)+]

organism: Equus caballus

substrate_name: pentanal

enzyme: aldehyde dehydrogenase [NAD(P)+]

substrate: pentanal


substrate_name: acetaldehyde

proof_lines:
isoenzyme F2
isoenzyme F1

substrate: acetaldehyde


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: isopentanal

substrate: isopentanal


substrate_name: propanal

substrate: propanal


substrate_name: Chloroacetaldehyde

smiles: C(C=O)Cl

substrate: Chloroacetaldehyde


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


substrate_name: formaldehyde

substrate: formaldehyde


enzyme_display_name: betaine-aldehyde dehydrogenase

organism: Aspergillus nidulans

substrate_name: glycine betaine aldehyde

proof_lines: mutant enzyme G1036A/Y1178F, at pH 7.5 and 30°C

enzyme: betaine-aldehyde dehydrogenase

substrate: glycine betaine aldehyde


substrate_name: N,N-dimethylglycine

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

substrate: N,N-dimethylglycine


proof_lines: mutant enzyme Y1178F, at pH 7.5 and 30°C


substrate_name: glycine betaine

substrate: glycine betaine


substrate_name: Unknown

proof_lines: wild type enzyme, competing against glycine betaine, at pH 7.5 and 30°C

proof_lines: wild type enzyme, competing against glycine betaine aldehyde, at pH 7.5 and 30°C

substrate: Unknown


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


substrate_name: Undecanal

smiles: CCCCCCCCCCC=O

substrate: Undecanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: tridecanal

smiles: CCCCCCCCCCCCC=O

substrate: tridecanal


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: Heptanal

substrate: Heptanal


substrate_name: Butanal

substrate: Butanal


smiles: CCC=O


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: Valeraldehyde

substrate: Valeraldehyde


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: Isovaleraldehyde

substrate: Isovaleraldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Sulfurisphaera tokodaii

substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


assay_conditions_summary: pH 8; 353.15 K; cofactor NAD+

proof_lines: pH and temperature not specified in the publication


assay_conditions_summary: pH 8; 353.15 K; cofactor NADP+


organism: Oryza sativa

smiles: C(CN)C=O

proof_lines: isozyme BADH2, pH and temperature not specified in the publication


smiles: C[N+](C)(C)CCCC=O


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


organism: Pseudomonas aeruginosa

substrate_name: Tetradecanal

smiles: CCCCCCCCCCCCCC=O

substrate: Tetradecanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


enzyme_display_name: aldehyde dehydrogenase (NAD+)

organism: Euglena gracilis

substrate_name: propanal

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

proof_lines: 100 mM Na2HPO4, pH 7.4, 100 mM NaCl, 1 mM NAD+, 25°C

enzyme: aldehyde dehydrogenase (NAD+)

substrate: propanal


organism: Bacillus cereus

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

proof_lines: mutant enzyme C300S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C


proof_lines: wild type enzyme, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C


substrate_name: all-trans-retinal

proof_lines: with NAD+ as cosubstrate, at pH 7.0 and 37°C

substrate: all-trans-retinal


proof_lines: mutant enzyme E194S, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C


proof_lines: mutant enzyme E457V, with all-trans-retinal as cosubstrate, at pH 7.0 and 37°C


organism: Ctenopharyngodon idella


assay_conditions_summary: pH 9.5; cofactor NAD+

proof_lines:
reaction with acetaldehyde, at pH 9.5
reaction with acetaldehyde, at pH 7.5


enzyme_display_name: aldehyde dehydrogenase [NAD(P)(+)]

column_label: Table 1. Kinetic parameters for aldehyde substrates of BcALDH in oxidation activity using NAD+ as a cosubstrate; row Acetaldehyde; Km column raw 95 +/- 4 uM; kcat column raw 11 +/- 0.4 min^-1; kcat/Km column raw 111 +/- 4 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.095 normalized_unit=mM; kcat normalized_value=0.183 normalized_unit=s^-1; kcat/Km normalized_value=1.9263157894736842 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=95 +/- 4 raw_unit=uM; kcat raw_value=11 +/- 0.4 raw_unit=min^-1; kcat/Km raw_value=111 +/- 4 raw_unit=mM^-1 min^-1

row_label: Acetaldehyde

enzyme: aldehyde dehydrogenase [NAD(P)(+)]


column_label: Table 1. Kinetic parameters for aldehyde substrates of BcALDH in oxidation activity using NAD+ as a cosubstrate; row all-trans-retinal -> all-trans-retinoic acid; Km column raw 7 +/- 0.1 uM; kcat column raw 0.28 +/- 0.03 min^-1; kcat/Km column raw 40 +/- 0.2 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.007 normalized_unit=mM; kcat normalized_value=0.0047 normalized_unit=s^-1; kcat/Km normalized_value=0.6714285714285715 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=7 +/- 0.1 raw_unit=uM; kcat raw_value=0.28 +/- 0.03 raw_unit=min^-1; kcat/Km raw_value=40 +/- 0.2 raw_unit=mM^-1 min^-1


column_label: Table 1. Kinetic parameters for aldehyde substrates of BcALDH in oxidation activity using NAD+ as a cosubstrate; row Benzaldehyde; Km column raw 200 +/- 4 uM; kcat column raw 13 +/- 0.1 min^-1; kcat/Km column raw 65 +/- 1 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.2 normalized_unit=mM; kcat normalized_value=0.217 normalized_unit=s^-1; kcat/Km normalized_value=1.085 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=200 +/- 4 raw_unit=uM; kcat raw_value=13 +/- 0.1 raw_unit=min^-1; kcat/Km raw_value=65 +/- 1 raw_unit=mM^-1 min^-1

row_label: Benzaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C300S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E194S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E457V to reconstruct the assayed variant sequence.


column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NAD+ oxidation; Km column raw 4.0 +/- 0.2 uM; kcat column raw 0.10 +/- 0.01 min^-1; kcat/Km column raw 25 +/- 0.1 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.004 normalized_unit=mM; kcat normalized_value=0.0017 normalized_unit=s^-1; kcat/Km normalized_value=0.425 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.0 +/- 0.2 raw_unit=uM; kcat raw_value=0.10 +/- 0.01 raw_unit=min^-1; kcat/Km raw_value=25 +/- 0.1 raw_unit=mM^-1 min^-1

row_label: NAD+ oxidation


organism: Mammalia

smiles: CCCCCCC=CC=O


smiles: CCCCCC=CC=O


smiles: CCCCCC(C=CC=O)O

proof_lines: in the cytosolic extracts of the ALDH3A1-transfected HCE cells


smiles: CCCC=CC=O


organism: Homo sapiens


organism: Bacillus licheniformis

smiles: CC(C)CC=O

assay_conditions_summary: pH 7; 310.15 K; buffer 50 mM potassium phosphate; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C

proof_lines: with NAD+ as cosubstrate, in 50 mM potassium phosphate buffer (pH 7.0), 1 mM dithiothreitol, at 37°C


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


organism: Mus musculus


proof_lines: with DL-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C

proof_lines: with acetaldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C

proof_lines: with Dl-glyceraldehyde as cosubstrate, in 50 mM Tris/HCl, at pH 8.0 and 80°C


substrate_name: DL-glyceraldehyde 3-phosphate

substrate: DL-glyceraldehyde 3-phosphate


substrate_name: DL-glyceraldehyde

substrate: DL-glyceraldehyde


substrate_name: NADP+

substrate: NADP+


organism: Pyrobaculum ferrireducens

substrate_name: glyceraldehyde

substrate: glyceraldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


enzyme_display_name: benzaldehyde dehydrogenase (NADP+)

organism: Acinetobacter baylyi

column_label: Table 2 row 4-Hydroxy benzaldehyde, columns Km app (uM), kcat app (s^-1), and kcat app/Km app (s^-1 M^-1).

normalized_value_unit_evidence: Table 2 normalized central values: Km=0.006 mM; kcat=4.0 s^-1; kcat/Km=660 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row 4-Hydroxy benzaldehyde: Km=6 (1.8) uM; kcat=4.0 (0.4) s^-1; kcat/Km=6.6 x 10^5 s^-1 M^-1.

row_label: 4-Hydroxy benzaldehyde

table_label: Table 2, Apparent kinetic constants Km app and kcat app for 4-hydroxy benzaldehyde dehydrogenase

enzyme: benzaldehyde dehydrogenase (NADP+)


substrate_name: benzaldehyde

column_label: Table 2 row Benzaldehyde, columns Km app (uM), kcat app (s^-1), and kcat app/Km app (s^-1 M^-1).

normalized_value_unit_evidence: Table 2 normalized central values: Km=0.029 mM; kcat=4.6 s^-1; kcat/Km=160 s^-1 mM^-1.

substrate: benzaldehyde


substrate_name: NAD+

proof_lines:
apparent Kcat
apparent KM

substrate: NAD+


column_label: Table 2 row 3-Methoxy 4-hydroxy benzaldehyde (vanillin), columns Km app (uM), kcat app (s^-1), and kcat app/Km app (s^-1 M^-1).

normalized_value_unit_evidence: Table 2 normalized central values: Km=0.044 mM; kcat=18 s^-1; kcat/Km=410 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row 3-Methoxy 4-hydroxy benzaldehyde (vanillin): Km=44 (5.6) uM; kcat=18 (0.8) s^-1; kcat/Km=4.1 x 10^5 s^-1 M^-1.


column_label: Table 2 row 3,4-dihydroxy benzaldehyde, columns Km app (uM), kcat app (s^-1), and kcat app/Km app (s^-1 M^-1).

normalized_value_unit_evidence: Table 2 normalized central values: Km=0.037 mM; kcat=25 s^-1; kcat/Km=680 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row 3,4-dihydroxy benzaldehyde: Km=37 (2.1) uM; kcat=25 (0.1) s^-1; kcat/Km=6.8 x 10^5 s^-1 M^-1.

row_label: 3,4-dihydroxy benzaldehyde


organism: Avena sativa


substrate_name: beta-NAD+

assay_conditions_summary: pH 8.7; cofactor NAD+

substrate: beta-NAD+


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


organism: Proteus vulgaris

smiles: CCC=O


substrate_name: isopentanal

substrate: isopentanal


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Oryctolagus cuniculus


organism: Rattus norvegicus

substrate_name: p-nitrobenzaldehyde

proof_lines:
native enzyme
isoenzyme ALDH-II
membrane-bound isoenzyme ALDH

substrate: p-nitrobenzaldehyde


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

proof_lines:
native enzyme
isoenzyme ALDH-II
isoenzyme ALDH-I

substrate: Glutaraldehyde


organism: Equus caballus

proof_lines:
isoenzyme F2
isoenzyme F1


proof_lines:
isoenzyme F1
isoenzyme F2


organism: Gluconobacter oxydans


organism: Thermoplasma acidophilum

substrate_name: D-glyceraldehyde

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

proof_lines: pH 7.3, temperature not specified in the publication, wild-type enzyme

substrate: D-glyceraldehyde


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

proof_lines: pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I


proof_lines: pH 7.3, temperature not specified in the publication, mutant D176S/S206K/M262I/W271Y/W275V


proof_lines: reaction with benzaldehyde, enzyme from stomach mucosa

proof_lines: reaction with benzaldehyde, enzyme from adenocarcinoma cell line


substrate_name: 3-acetylpyridine adenine dinucleotide

proof_lines:
isoenzyme E1
isoenzyme E2

substrate: 3-acetylpyridine adenine dinucleotide


substrate_name: 3-pyridinealdehyde adenine dinucleotide

proof_lines:
isoenzyme E2
isoenzyme E1

substrate: 3-pyridinealdehyde adenine dinucleotide


proof_lines:
reaction with acetaldehyde
isoenzyme F1
isoenzyme F2


proof_lines:
reaction with acetaldehyde
isoenzyme F2
isoenzyme F1


organism: Pseudomonas fluorescens


organism: Cylindrocarpon didymum

substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


organism: Zoysia tenuifolia


smiles: C(CC=O)CN


substrate_name: NAD+; H2O; Propanal

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

proof_lines:
membrane-bound isoenzyme ALDH
native enzyme

substrate: NAD+; H2O; Propanal


organism: Cytophaga sp.

assay_conditions_summary: pH 10


assay_conditions_summary: pH 10; cofactor NAD+


proof_lines: in the absence of Alda-1, at pH 7.4 and 25°C

proof_lines: in the presence of 0.01 mM Alda-1, at pH 7.4 and 25°C


proof_lines:
isozyme ALDH1A1 from liver
isozyme ALDH1A1 from brain


substrate_name: H2O; NAD+; Acetaldehyde

assay_conditions_summary: pH 7.4; 310.15 K; buffer pH 7; cofactor NAD+

proof_lines: 50 mM sodium phosphate buffer pH 7.4, 1 mM NAD+, 37°C

substrate: H2O; NAD+; Acetaldehyde


organism: Limulus polyphemus


substrate_name: NADP+

substrate: NADP+


organism: Homo sapiens

smiles: CC=O

assay_conditions_summary: pH 9.5; 298.15 K; buffer 0.1 M sodium diphosphate; cofactor NAD+

proof_lines:
enzyme form ALDH-1, pH 9.5
enzyme form ALDH-2, pH 9.5
major component of enzyme E3


assay_conditions_summary: pH 7.4; cofactor NAD+

proof_lines: enzyme from promotion phase of hepatocarcinogenesis


substrate_name: glycolaldehyde

smiles: C(C=O)O

proof_lines:
isoenzyme I
isoenzyme II
isoenzyme 2, pH 7.4

substrate: glycolaldehyde


proof_lines:
enzyme ALDH-2
enzyme ALDH-1
isoenzyme I


organism: Ipomoea batatas


substrate_name: methylglyoxal

smiles: CC(=O)C=O

proof_lines: minor component of enzyme form E3, pH 7.4

substrate: methylglyoxal


substrate_name: propanal

proof_lines:
native enzyme, pH 7.4
native enzyme, pH 9.0
native enzyme

substrate: propanal


substrate_name: NADP+; H2O; Acetaldehyde

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

substrate: NADP+; H2O; Acetaldehyde


organism: Mus musculus

substrate_name: muconaldehyde

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

assay_conditions_summary: cofactor NADPH

substrate: muconaldehyde


organism: Lycium ruthenicum

proof_lines: pH 8.0, 30°C, recombinant isozyme LrAMADH1


organism: Sphingopyxis macrogoltabida

substrate_name: n-dodecanal

smiles: CCCCCCCCCCCC=O

assay_conditions_summary: pH 8; 309.15 K; buffer pH8

proof_lines: 50 mM potassium phosphate buffer pH8.0, 1 mM CaCl2, 36°C

substrate: n-dodecanal


substrate_name: NAD+; Benzaldehyde; H2O

proof_lines:
isoenzyme E1
isoenzyme E2

substrate: NAD+; Benzaldehyde; H2O


enzyme_display_name: Aldehyde dehydrogenase

organism: Paenarthrobacter nicotinovorans

substrate_name: NADP(+)

proof_lines: kcat is 0.38 sec(-1) with formaldehyde as substrate. kcat is 0.75 sec(-1) with acetaldehyde as substrate. kcat is 1.2 sec(-1) with propionaldehyde as substrate. kcat is 1.35 sec(-1) with glyceraldehyde as substrate. kcat is 0.65 sec(-1) wit

enzyme: Aldehyde dehydrogenase

substrate: NADP(+)


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: glyceraldehyde

substrate: glyceraldehyde


substrate_name: butyraldehyde

substrate: butyraldehyde


substrate_name: glutaraldehyde

substrate: glutaraldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149T/V178R/I200V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8

proof_lines: mutant enzyme E149T/V178R/I200V, at pH 8.0 and 25°C