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


enzyme_display_name: (S)-mandelate dehydrogenase

organism: Pseudomonas putida

source_db: oed

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

mutation_type: substitution

data_origin: experimental

enzyme: (S)-mandelate dehydrogenase

status: unverified

source: oed


verification_status: corrected

mutation_signature: Unknown

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

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

status: corrected


kcat_over_km_origin: calculated


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.


enzyme_display_name: pyranose dehydrogenase (acceptor)

organism: Agaricus campestris

verification_status: verified

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)

enzyme: pyranose dehydrogenase (acceptor)

status: verified


substrate_name: D-galactose

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: 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


substrate_name: ferrocenium ion

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)

substrate: ferrocenium ion


substrate_name: D-Xylose

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

substrate: D-Xylose


substrate_name: lactose

substrate: lactose


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


organism: Agaricus xanthodermus

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)

row_label: Lactose


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


source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

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

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

source: brenda


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

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.


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

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.


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

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


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

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


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


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


enzyme_display_name: cellobiose dehydrogenase (acceptor)

organism: Phanerodontia chrysosporium

enzyme: cellobiose dehydrogenase (acceptor)


enzyme_display_name: UniProt Q3L245

source_db: skid

sequence_source: multiple

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

enzyme: UniProt Q3L245

source: skid


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)

source_db: uniprot

assay_conditions_summary: pH 5

enzyme: Pyranose dehydrogenase 1

source: uniprot


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

km_display: Not reported

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: cellobiose


substrate_name: Ethyl (S)-mandelate

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

substrate: Ethyl (S)-mandelate


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


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


substrate_name: Methyl (S)-mandelate

substrate: Methyl (S)-mandelate


organism: Rhodotorula graminis

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


organism: Escherichia coli

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

assay_conditions_summary: pH 7

proof_lines: KM for benzylalcohol is lower than 0.005 mM.

source_databases_merged: brenda uniprot

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

source_license: CC BY-NC-ND 4.0

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.


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

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


substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: mutant enzyme E149T/V178R/I200V, with trans-2-hexenal as cosubstrate, at pH 8.0 and 25°C

proof_lines: mutant enzyme E149T/V178R/I200V, with trans-2-nonenal as cosubstrate, at pH 8.0 and 25°C

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

substrate: NAD+


smiles: CCCCCCC=CC=O


substrate_name: hexanal

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

smiles: CCCCCC=O

source_databases_merged: brenda oed

substrate: hexanal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149T with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E149T, with hexanal as cosubstrate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E149D, with hexanal as cosubstrate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E149Q, with hexanal as cosubstrate, at pH 8.0 and 25°C


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E149N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E149N, with hexanal as cosubstrate, at pH 8.0 and 25°C


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

assay_conditions_summary: pH 7.4; 310.15 K; buffer 40 mM sodium phosphate

proof_lines: ALDH2, in 40 mM sodium phosphate buffer (pH 7.4), at 37°C


organism: Spinacia oleracea

substrate_name: Betaine aldehyde

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

substrate: Betaine aldehyde


enzyme_display_name: Aldehyde dehydrogenase family 3 member A2

proof_lines: kcat is 2.18 sec(-1) for decanal as substrate. kcat is 2.23 sec(-1) for dodecanal as substrate. kcat is 0.86 sec(-1) for tetradecanal as substrate. kcat is 0.95 sec(-1) for hexadecanal as substrate. kcat is 1.52 sec(-1) for octadecanal as s


substrate_name: octanal

smiles: CCCCCCCC=O

enzyme: Aldehyde dehydrogenase family 3 member A2

substrate: octanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: dodecanal

substrate: dodecanal


substrate_name: tetradecanal

smiles: CCCCCCCCCCCCCC=O

substrate: tetradecanal


substrate_name: octadecanal

smiles: CCCCCCCCCCCCCCCCCC=O

substrate: octadecanal


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Oryza sativa

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

proof_lines: isozyme BADH1, pH and temperature not specified in the publication


smiles: C(CN)C=O


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Rattus norvegicus


organism: Antirrhinum majus

proof_lines: kcat is 0.31 sec(-1) with benzaldehyde as substrate (PubMed:19292760). kcat is 2.08 sec(-1) with acetaldehyde as substrate (PubMed:19292760). kcat is 0.23 sec(-1) with phenylacetaldehyde as substrate (PubMed:19292760).


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


organism: Sinorhizobium meliloti

substrate_name: phosphonoacetaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N158A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: mutant enzyme N158A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C

substrate: phosphonoacetaldehyde


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E385A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E385A, with NAD+ in 50 mM HEPES, pH 7.5 supplemented with 10 mM MgSO4 for 5 min at 30°C


proof_lines: mutant enzyme N158A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C


proof_lines: mutant enzyme E385A, with phosphonoacetaldehyde as cosubstrate, at pH 7.5 and 30°C


organism: Ovis aries

assay_conditions_summary: cofactor NAD+

proof_lines:
reaction with propanal
reaction with butanal
cytoplasmic isoenzyme


substrate_name: propionaldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D80G with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

smiles: CCC=O

substrate: propionaldehyde


assay_conditions_summary: pH 7.5; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R475E with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R475Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

substrate: hexadecanal


substrate_name: farnesal

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

substrate: farnesal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature E103Q to reconstruct the assayed variant sequence.

smiles: C(CC=O)CN


substrate_name: NAD+

proof_lines: mutant enzyme E103Q, reaction with betaine aldehyde

proof_lines: mutant enzyme E103Q, reaction with 4-aminobutyraldehyde

substrate: NAD+


enzyme_display_name: Aldehyde dehydrogenase 1A1

organism: Oryctolagus cuniculus

smiles: CCCCCC(C=CC=O)O

enzyme: Aldehyde dehydrogenase 1A1


substrate_name: malonaldehyde

smiles: C(C=O)C=O

substrate: malonaldehyde


substrate_name: hexanal

substrate: hexanal


substrate_name: propanal

substrate: propanal


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H1A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines:
isozyme ALDH1A1
isozyme ALDH1A1 from brain


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H9A with inferred residue-numbering offset +7 to reconstruct the assayed variant sequence.


organism: Bos taurus

substrate_name: all-trans retinal

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

proof_lines: Has a much higher catalytic efficiency toward all-trans retinal.

substrate: all-trans retinal


organism: Craterostigma plantagineum

substrate_name: nonanal

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

substrate: nonanal


smiles: CC=O


organism: Loktanella sp.

proof_lines: pH 8.0, 22°C, recombinant wild-type enzyme


enzyme_display_name: Aldehyde dehydrogenase 1

organism: Tanacetum cinerariifolium

substrate_name: NAD(+)

assay_conditions_summary: cofactor NADP+

proof_lines: kcat is 0.11 sec(-1) with trans-chrysanthemal as substrate (in the presence of NAD(+)) (PubMed:29122986). kcat is 0.096 sec(-1) with trans-chrysanthemal as substrate (in the presence of NADP(+)) (PubMed:29122986). kcat is 0.09 sec(-1) with

enzyme: Aldehyde dehydrogenase 1

substrate: NAD(+)


substrate_name: NADP(+)

substrate: NADP(+)


organism: Homo sapiens


substrate_name: 9-cis retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal.


enzyme_display_name: Aldehyde dehydrogenase, cytosolic 1

proof_lines: The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal.

enzyme: Aldehyde dehydrogenase, cytosolic 1


substrate_name: benzaldehyde

substrate: benzaldehyde


enzyme_display_name: aldehyde dehydrogenase (NADP+)

organism: Acetobacter pasteurianus

substrate_name: NADP+

enzyme: aldehyde dehydrogenase (NADP+)

substrate: NADP+


enzyme_display_name: NAD/NADP-dependent betaine aldehyde dehydrogenase

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: NADP(+) (at pH 8.0 and 30 degrees Celsius)

proof_lines: kcat is 261 sec(-1) for the NADP-dependent oxidation of betaine aldehyde. kcat is 276 sec(-1) for the NAD-dependent oxidation of betaine aldehyde.


substrate_name: NAD(+) (at pH 8.0 and 30 degrees Celsius)

enzyme: NAD/NADP-dependent betaine aldehyde dehydrogenase


enzyme_display_name: aldehyde dehydrogenase (NAD(+))

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

enzyme: aldehyde dehydrogenase (NAD(+))


column_label: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / o-methoxy- (o-methoxybenzaldehyde), columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / o-methoxy- (o-methoxybenzaldehyde): kcat 22 min^-1 and Km 800 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.


column_label: Table 2 (Continued): Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Naphthaldehydes / 2-naphthaldehyde, columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2 (Continued): Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Naphthaldehydes / 2-naphthaldehyde: kcat 240 min^-1 and Km 8 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.

row_label: Naphthaldehydes / 2-naphthaldehyde


column_label: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / m-methoxy- (m-methoxybenzaldehyde), columns kcat (min-1) and Km (nM); kcat/Km is derived from those exact same-row same-column cells.

raw_value_unit_evidence: Table 2: Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes, row Benzaldehydes / m-methoxy- (m-methoxybenzaldehyde): kcat 350 min^-1 and Km 90 nM; the table prints no kcat/Km column, so kcat/Km is derived from those same-row same-column cells.


organism: Acinetobacter calcoaceticus

proof_lines:
reaction with heptanal
reaction with nonanal
reaction with pentanal


organism: Pseudomonas sp.

proof_lines: kcat is 8240 min(-1) with benzaldehyde and NAD as substrate. kcat is 2550 min(-1) with benzaldehyde and NADP as substrate.


organism: Macaca fascicularis

substrate_name: all-trans retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal.


substrate_name: Pentanal

smiles: CCCCC=O

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 pentanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 155: pentanal kcat 1370 min^-1 and Km 34 nM.

row_label: ALDH-2 pentanal

substrate: Pentanal


substrate_name: Phenylacetaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 phenylacetaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 233: phenylacetaldehyde kcat 1800 min^-1 and Km 29 nM.

row_label: ALDH-2 phenylacetaldehyde

substrate: Phenylacetaldehyde


substrate_name: p-Nitrobenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-nitrobenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 245: p-nitrobenzaldehyde kcat 430 min^-1 and Km 7 nM.

row_label: ALDH-2 p-nitrobenzaldehyde

substrate: p-Nitrobenzaldehyde


substrate_name: p-Tolualdehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-methylbenzaldehyde / p-tolualdehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 251: p-methylbenzaldehyde kcat 180 min^-1 and Km 17 nM.

substrate: p-Tolualdehyde


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 quinoline-3-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 383: quinoline-3-carboxaldehyde kcat 670 min^-1 and Km 330 nM.

row_label: ALDH-2 quinoline-3-carboxaldehyde


substrate_name: Salicylaldehyde

column_label: Table 2 row o-hydroxy- under Benzaldehydes gives columns K_m (nM) and kcat (min^-1); source salicylaldehyde is o-hydroxybenzaldehyde; kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 50 plus/minus 5; K_m 320000 plus/minus 40000 nM; kcat 590 plus/minus 70 min^-1

row_label: o-hydroxybenzaldehyde (salicylaldehyde)

table_label: ACS PDF Table 2 Continued - human liver ALDH-2 substrate specificity

substrate: Salicylaldehyde


substrate_name: trans-Cinnamaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 trans-cinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 224: trans-cinnamaldehyde kcat 150 min^-1 and Km 35 nM.

row_label: ALDH-2 trans-cinnamaldehyde

substrate: trans-Cinnamaldehyde


substrate_name: Veratraldehyde

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

column_label: Table 2  Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; journal page 4460, Table 2, Benzaldehydes block; row `3,4-dimethoxy- (veratraldehyde)`; column `Vm,rel (%)`; column `Km (nM)`; column `kcat (min-1)`; the row reads | 3,4-dimethoxy- (veratraldehyde) | Vm,rel (%) 7.2 +/- 0.4 | Km (nM) 330 +/- 60 | kcat (min-1) 85 +/- 7 |

normalized_value_unit_evidence: kcat: printed cell 85 min-1; 85.0 min-1 / 60 = 1.4166666666666667 s^-1, and the catalog kcat is 1.41666666666667 s^(-1), the same value at the catalog's own printed precision. Km: printed cell 330 nM; 330.0 nM / 1000000 = 0.00033 mM, which equals the catalog km exactly. kcat/Km: Table 1, Table 2 and Table 3 have no kcat/Km column and the paper prints no kcat/Km cell for this row, so the catalog kcat_over_km 4292.92929292929 s^(-1)*mM^(-1) can only be the full-precision quotient of this same row's own printed kcat and Km, 1.4166666666666667 / 0.00033 = 4292.929292929293.

raw_value_unit_evidence: journal page 4460, Table 2, Benzaldehydes block, row `3,4-dimethoxy- (veratraldehyde)`: Vm,rel and the two kinetic cells read | 3,4-dimethoxy- (veratraldehyde) | Vm,rel (%) 7.2 +/- 0.4 | Km (nM) 330 +/- 60 | kcat (min-1) 85 +/- 7 |. No kcat/Km cell is printed.

row_label: Table 2, Benzaldehydes block, row `3,4-dimethoxy-`

substrate: Veratraldehyde


substrate_name: decanal

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 decanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 159: decanal kcat 700 min^-1 and Km 22 nM.

row_label: ALDH-2 decanal

substrate: decanal


table_label: Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes

row_label: ALDH-2 quinoline-4-carboxaldehyde

column_label: kcat (min^-1), Km (nM), same-row ratio lock

raw_value_unit_evidence: Table 2 line 392: quinoline-4-carboxaldehyde kcat 280 min^-1 and Km 2800 nM.


column_label: Table 2 row phenanthrene-9-carboxaldehyde under Others gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 1.5 plus/minus 0.4; K_m 4 plus/minus 3 nM; kcat 18 plus/minus 6 min^-1


substrate_name: Heptanal

smiles: CCCCCCC=O

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 heptanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 157: heptanal kcat 1360 min^-1 and Km 27 nM.

row_label: ALDH-2 heptanal

substrate: Heptanal


substrate_name: Hexanal

smiles: CCCCCC=O

column_label: PMID 8605195 Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5); row ALDH-2 hexanal; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 156: hexanal kcat 1710 min^-1 and Km 30 nM.

row_label: ALDH-2 hexanal

substrate: Hexanal


substrate_name: Hydrocinnamaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 hydrocinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 227: hydrocinnamaldehyde kcat 740 min^-1 and Km 500 nM.

row_label: ALDH-2 hydrocinnamaldehyde

substrate: Hydrocinnamaldehyde


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 indole-3-acetaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 lines 424-425: indole-3-acetaldehyde kcat 560 min^-1 and Km 150 nM.

row_label: ALDH-2 indole-3-acetaldehyde


substrate_name: m-Methylbenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 m-methylbenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 254: m-methylbenzaldehyde kcat 270 min^-1 and Km 18 nM.

row_label: ALDH-2 m-methylbenzaldehyde

substrate: m-Methylbenzaldehyde


substrate_name: formaldehyde

smiles: C=O

column_label: PMID 8605195 Table 1; row ALDH-2 formaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 1 line 152: formaldehyde kcat 4050 min^-1 and Km 320000 nM.

row_label: ALDH-2 formaldehyde

table_label: Table 1. Substrate Specificity of ALDH-2 and ALDH-1 toward Aliphatic Aldehydes (pH 9.5)

substrate: formaldehyde


substrate_name: o-Methylbenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 o-methylbenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 278: o-methylbenzaldehyde kcat 165 min^-1 and Km 1300 nM.

row_label: ALDH-2 o-methylbenzaldehyde

substrate: o-Methylbenzaldehyde


substrate_name: o-Nitrobenzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 o-nitrobenzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 242: o-nitrobenzaldehyde kcat 74 min^-1 and Km 6.3 nM.

row_label: ALDH-2 o-nitrobenzaldehyde

substrate: o-Nitrobenzaldehyde


substrate_name: p-(dimethylamino)benzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 p-(dimethylamino)benzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 261: p-(dimethylamino)benzaldehyde kcat 140 min^-1 and Km 20 nM.

row_label: ALDH-2 p-(dimethylamino)benzaldehyde

substrate: p-(dimethylamino)benzaldehyde


substrate_name: p-(dimethylamino)cinnamaldehyde

column_label: PMID 8605195 Table 2; row ALDH-2 p-(dimethylamino)cinnamaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 221: p-(dimethylamino)cinnamaldehyde kcat 90 min^-1 and Km 5 nM.

row_label: ALDH-2 p-(dimethylamino)cinnamaldehyde

substrate: p-(dimethylamino)cinnamaldehyde


column_label: Table 2  Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; journal page 4461, Table 2 (Continued), Coumarin-4-carboxaldehydes block; row `6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde)`; column `Vm,rel (%)`; column `Km (nM)`; column `kcat (min-1)`; the row reads | 6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde) | Vm,rel (%) 5.0 +/- 0.5 | Km (nM) 690 +/- 100 | kcat (min-1) 59 +/- 7 |

normalized_value_unit_evidence: kcat: printed cell 59 min-1; 59.0 min-1 / 60 = 0.9833333333333333 s^-1, and the catalog kcat is 0.983333333333333 s^(-1), the same value at the catalog's own printed precision. Km: printed cell 690 nM; 690.0 nM / 1000000 = 0.00069 mM, which equals the catalog km exactly. kcat/Km: Table 1, Table 2 and Table 3 have no kcat/Km column and the paper prints no kcat/Km cell for this row, so the catalog kcat_over_km 1425.12077294686 s^(-1)*mM^(-1) can only be the full-precision quotient of this same row's own printed kcat and Km, 0.9833333333333333 / 0.00069 = 1425.1207729468594.

raw_value_unit_evidence: journal page 4461, Table 2 (Continued), Coumarin-4-carboxaldehydes block, row `6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde)`: Vm,rel and the two kinetic cells read | 6,7-dimethoxy- (6,7-dimethoxycoumarin-4-carboxaldehyde) | Vm,rel (%) 5.0 +/- 0.5 | Km (nM) 690 +/- 100 | kcat (min-1) 59 +/- 7 |. No kcat/Km cell is printed.

row_label: Table 2 (Continued), Coumarin-4-carboxaldehydes block, row `6,7-dimethoxy-`


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 6-(dimethylamino)-2-naphthaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 lines 321-322: 6-(dimethylamino)-2-naphthaldehyde kcat 37 min^-1 and Km 2.3 nM.


raw_value_unit_evidence: Table 2 line 396: 6-methoxy-2-quinolinone-4-carboxaldehyde kcat 59 min^-1 and Km 5400 nM.


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-acetoxycoumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 355: 7-acetoxy coumarin-4-carboxaldehyde kcat 65 min^-1 and Km 60 nM.


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-(dimethylamino)coumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 360: 7-(dimethylamino)coumarin-4-carboxaldehyde kcat 78 min^-1 and Km 62 nM.


column_label: Table 2 row 7-hydroxy- under Coumarin-4-carboxaldehydes gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 42 plus/minus 3; K_m 150000 plus/minus 20000 nM; kcat 500 plus/minus 40 min^-1


column_label: Table 2 row 7-methoxy-2-quinolinone-4- under Quinoline- and Quinolinonecarboxaldehydes gives columns K_m (nM) and kcat (min^-1); kcat/K_m is derived from these exact cells.

raw_value_unit_evidence: V_m rel 27 plus/minus 3; K_m 50000 plus/minus 10000 nM; kcat 320 plus/minus 40 min^-1


column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 7-methoxycoumarin-4-carboxaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 365: 7-methoxycoumarin-4-carboxaldehyde kcat 190 min^-1 and Km 280 nM.


substrate_name: alpha-Phenylpropionaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 alpha-phenylpropionaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 230: R-phenylpropionaldehyde kcat 910 min^-1 and Km 930 nM.

row_label: ALDH-2 alpha-phenylpropionaldehyde

substrate: alpha-Phenylpropionaldehyde


substrate_name: Benzaldehyde

column_label: PMID 8605195 Table 2. Substrate Specificity of ALDH-2 toward Aromatic and Fused Polycyclic Hydrocarbon and Heterocyclic Aldehydes; row ALDH-2 benzaldehyde; kcat and Km columns; kcat/Km locked from the same row.

raw_value_unit_evidence: Table 2 line 248: benzaldehyde kcat 350 min^-1 and Km 18 nM.

row_label: ALDH-2 benzaldehyde

substrate: Benzaldehyde


organism: Thermus thermophilus

substrate_name: propanal

column_label: The primary article states that ALDHTt530 has a KM of 2.76 mM when propanal was used.

raw_value_unit_evidence: Km raw_value=2.76 raw_unit=mM

row_label: ALDHTt530 with propanal

table_label: Discussion prose comparing ALDHTt530 propanal kinetic parameters

substrate: propanal


organism: Arabidopsis thaliana

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149T with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149T; kcat column raw 10.2 +/- 0.4; kcat/Km column raw 8.1 +/- 0.2; Km column raw 1262 +/- 38

normalized_value_unit_evidence: kcat normalized_value=10.2 normalized_unit=s^-1; kcat/Km normalized_value=8.0824088748019 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=8.1 +/- 0.2 s^-1 mM^-1; Km normalized_value=1.262 normalized_unit=mM from 1262 +/- 38 uM / 1000

raw_value_unit_evidence: kcat raw_value=10.2 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=8.1 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=1262 +/- 38 raw_unit=uM

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149T/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149T/I200G; kcat column raw 33.9 +/- 0.8; kcat/Km column raw 9.9 +/- 0.6; Km column raw 3418 +/- 187

normalized_value_unit_evidence: kcat normalized_value=33.9 normalized_unit=s^-1; kcat/Km normalized_value=9.91808074897601 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=9.9 +/- 0.6 s^-1 mM^-1; Km normalized_value=3.418 normalized_unit=mM from 3418 +/- 187 uM / 1000

raw_value_unit_evidence: kcat raw_value=33.9 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=9.9 +/- 0.6 raw_unit=s^-1 mM^-1; Km raw_value=3418 +/- 187 raw_unit=uM


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


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1I200G; kcat column raw 16.3 +/- 1.7; kcat/Km column raw 5.1 +/- 0.3; Km column raw 3218 +/- 54

normalized_value_unit_evidence: kcat normalized_value=16.3 normalized_unit=s^-1; kcat/Km normalized_value=5.06525792417651 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5.1 +/- 0.3 s^-1 mM^-1; Km normalized_value=3.218 normalized_unit=mM from 3218 +/- 54 uM / 1000

raw_value_unit_evidence: kcat raw_value=16.3 +/- 1.7 raw_unit=s^-1; kcat/Km raw_value=5.1 +/- 0.3 raw_unit=s^-1 mM^-1; Km raw_value=3218 +/- 54 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1I200V; kcat column raw 18.5 +/- 1.7; kcat/Km column raw 37.3 +/- 1.1; Km column raw 496 +/- 4

normalized_value_unit_evidence: kcat normalized_value=18.5 normalized_unit=s^-1; kcat/Km normalized_value=37.2983870967742 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=37.3 +/- 1.1 s^-1 mM^-1; Km normalized_value=0.496 normalized_unit=mM from 496 +/- 4 uM / 1000

raw_value_unit_evidence: kcat raw_value=18.5 +/- 1.7 raw_unit=s^-1; kcat/Km raw_value=37.3 +/- 1.1 raw_unit=s^-1 mM^-1; Km raw_value=496 +/- 4 raw_unit=uM


column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1; kcat column raw 17.2 +/- 1.6; kcat/Km column raw 40.9 +/- 1.2; Km column raw 421 +/- 23.5

normalized_value_unit_evidence: kcat normalized_value=17.2 normalized_unit=s^-1; kcat/Km normalized_value=40.855106888361 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=40.9 +/- 1.2 s^-1 mM^-1; Km normalized_value=0.421 normalized_unit=mM from 421 +/- 23.5 uM / 1000

raw_value_unit_evidence: kcat raw_value=17.2 +/- 1.6 raw_unit=s^-1; kcat/Km raw_value=40.9 +/- 1.2 raw_unit=s^-1 mM^-1; Km raw_value=421 +/- 23.5 raw_unit=uM


substrate_name: Nonanal

smiles: CCCCCCCCC=O

column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / Nonanal; kcat column raw 17.9 +/- 3.8; kcat/Km column raw 2166 +/- 37; Km column raw 8 +/- 2

normalized_value_unit_evidence: kcat normalized_value=17.9 normalized_unit=s^-1; kcat/Km normalized_value=2237.5 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=2166 +/- 37 s^-1 mM^-1; Km normalized_value=0.008 normalized_unit=mM from 8 +/- 2 uM / 1000

raw_value_unit_evidence: kcat raw_value=17.9 +/- 3.8 raw_unit=s^-1; kcat/Km raw_value=2166 +/- 37 raw_unit=s^-1 mM^-1; Km raw_value=8 +/- 2 raw_unit=uM

row_label: ALDH3H1 / Nonanal

substrate: Nonanal


smiles: CCC/C=C/C=O

column_label: Table 3. Kinetic properties related to substrate specificity of wild-type enzyme ALDH3H1 and triple mutant enzyme ALDH3H1E149T/V178R/I200V.; row ALDH3H1E149T/V178R/I200V / trans-2-Hexenal; kcat column raw 1.1 +/- 0.04; kcat/Km column raw 5.3 +/- 0.2; Km column raw 199 +/- 6

normalized_value_unit_evidence: kcat normalized_value=1.1 normalized_unit=s^-1; kcat/Km normalized_value=5.52763819095477 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5.3 +/- 0.2 s^-1 mM^-1; Km normalized_value=0.199 normalized_unit=mM from 199 +/- 6 uM / 1000

raw_value_unit_evidence: kcat raw_value=1.1 +/- 0.04 raw_unit=s^-1; kcat/Km raw_value=5.3 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=199 +/- 6 raw_unit=uM


column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / trans-2-Hexenal; kcat column raw 2.2 +/- 0.1; kcat/Km column raw 12.4 +/- 0.8; Km column raw 180 +/- 24

normalized_value_unit_evidence: kcat normalized_value=2.2 normalized_unit=s^-1; kcat/Km normalized_value=12.2222222222222 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=12.4 +/- 0.8 s^-1 mM^-1; Km normalized_value=0.18 normalized_unit=mM from 180 +/- 24 uM / 1000

raw_value_unit_evidence: kcat raw_value=2.2 +/- 0.1 raw_unit=s^-1; kcat/Km raw_value=12.4 +/- 0.8 raw_unit=s^-1 mM^-1; Km raw_value=180 +/- 24 raw_unit=uM

row_label: ALDH3H1 / trans-2-Hexenal


substrate_name: hexanal

column_label: Table 3, ALDH3H1 wild-type column. Kinetic properties related to substrate specificity.; row ALDH3H1 / Hexanal; kcat column raw 11.2 +/- 0.5; kcat/Km column raw 154 +/- 3; Km column raw 71 +/- 12

normalized_value_unit_evidence: kcat normalized_value=11.2 normalized_unit=s^-1; kcat/Km normalized_value=157.746478873239 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=154 +/- 3 s^-1 mM^-1; Km normalized_value=0.071 normalized_unit=mM from 71 +/- 12 uM / 1000

raw_value_unit_evidence: kcat raw_value=11.2 +/- 0.5 raw_unit=s^-1; kcat/Km raw_value=154 +/- 3 raw_unit=s^-1 mM^-1; Km raw_value=71 +/- 12 raw_unit=uM

row_label: ALDH3H1 / Hexanal

substrate: hexanal


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149D with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D; kcat column raw 10.7 +/- 0.8; kcat/Km column raw 24.3 +/- 1.1; Km column raw 441 +/- 40

normalized_value_unit_evidence: kcat normalized_value=10.7 normalized_unit=s^-1; kcat/Km normalized_value=24.2630385487528 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=24.3 +/- 1.1 s^-1 mM^-1; Km normalized_value=0.441 normalized_unit=mM from 441 +/- 40 uM / 1000

raw_value_unit_evidence: kcat raw_value=10.7 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=24.3 +/- 1.1 raw_unit=s^-1 mM^-1; Km raw_value=441 +/- 40 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149D/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D/I200G; kcat column raw 23.2 +/- 0.6; kcat/Km column raw 6.4 +/- 0.3; Km column raw 3651 +/- 125

normalized_value_unit_evidence: kcat normalized_value=23.2 normalized_unit=s^-1; kcat/Km normalized_value=6.35442344563133 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.4 +/- 0.3 s^-1 mM^-1; Km normalized_value=3.651 normalized_unit=mM from 3651 +/- 125 uM / 1000

raw_value_unit_evidence: kcat raw_value=23.2 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=6.4 +/- 0.3 raw_unit=s^-1 mM^-1; Km raw_value=3651 +/- 125 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149D/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149D/I200V; kcat column raw 12.4 +/- 0.4; kcat/Km column raw 12.5 +/- 0.6; Km column raw 991 +/- 82

normalized_value_unit_evidence: kcat normalized_value=12.4 normalized_unit=s^-1; kcat/Km normalized_value=12.5126135216953 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=12.5 +/- 0.6 s^-1 mM^-1; Km normalized_value=0.991 normalized_unit=mM from 991 +/- 82 uM / 1000

raw_value_unit_evidence: kcat raw_value=12.4 +/- 0.4 raw_unit=s^-1; kcat/Km raw_value=12.5 +/- 0.6 raw_unit=s^-1 mM^-1; Km raw_value=991 +/- 82 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N; kcat column raw 16.6 +/- 0.7; kcat/Km column raw 26.3 +/- 0.9; Km column raw 630 +/- 33.1

normalized_value_unit_evidence: kcat normalized_value=16.6 normalized_unit=s^-1; kcat/Km normalized_value=26.3492063492064 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=26.3 +/- 0.9 s^-1 mM^-1; Km normalized_value=0.63 normalized_unit=mM from 630 +/- 33.1 uM / 1000

raw_value_unit_evidence: kcat raw_value=16.6 +/- 0.7 raw_unit=s^-1; kcat/Km raw_value=26.3 +/- 0.9 raw_unit=s^-1 mM^-1; Km raw_value=630 +/- 33.1 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149N/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N/I200G; kcat column raw 26.9 +/- 2.1; kcat/Km column raw 6.5 +/- 0.2; Km column raw 4136 +/- 124

normalized_value_unit_evidence: kcat normalized_value=26.9 normalized_unit=s^-1; kcat/Km normalized_value=6.50386847195358 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.5 +/- 0.2 s^-1 mM^-1; Km normalized_value=4.136 normalized_unit=mM from 4136 +/- 124 uM / 1000

raw_value_unit_evidence: kcat raw_value=26.9 +/- 2.1 raw_unit=s^-1; kcat/Km raw_value=6.5 +/- 0.2 raw_unit=s^-1 mM^-1; Km raw_value=4136 +/- 124 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149N/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149N/I200V; kcat column raw 13.1 +/- 0.6; kcat/Km column raw 13.2 +/- 0.5; Km column raw 992 +/- 54.4

normalized_value_unit_evidence: kcat normalized_value=13.1 normalized_unit=s^-1; kcat/Km normalized_value=13.2056451612903 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=13.2 +/- 0.5 s^-1 mM^-1; Km normalized_value=0.992 normalized_unit=mM from 992 +/- 54.4 uM / 1000

raw_value_unit_evidence: kcat raw_value=13.1 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=13.2 +/- 0.5 raw_unit=s^-1 mM^-1; Km raw_value=992 +/- 54.4 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q70DU8 and applied mutation signature E149Q with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q; kcat column raw 12.7 +/- 0.8; kcat/Km column raw 14.3 +/- 0.7; Km column raw 886 +/- 110

normalized_value_unit_evidence: kcat normalized_value=12.7 normalized_unit=s^-1; kcat/Km normalized_value=14.334085778781 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=14.3 +/- 0.7 s^-1 mM^-1; Km normalized_value=0.886 normalized_unit=mM from 886 +/- 110 uM / 1000

raw_value_unit_evidence: kcat raw_value=12.7 +/- 0.8 raw_unit=s^-1; kcat/Km raw_value=14.3 +/- 0.7 raw_unit=s^-1 mM^-1; Km raw_value=886 +/- 110 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149Q/I200G to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q/I200G; kcat column raw 20.1 +/- 1.9; kcat/Km column raw 5 +/- 0.4; Km column raw 4059 +/- 130

normalized_value_unit_evidence: kcat normalized_value=20.1 normalized_unit=s^-1; kcat/Km normalized_value=4.9519586104952 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=5 +/- 0.4 s^-1 mM^-1; Km normalized_value=4.059 normalized_unit=mM from 4059 +/- 130 uM / 1000

raw_value_unit_evidence: kcat raw_value=20.1 +/- 1.9 raw_unit=s^-1; kcat/Km raw_value=5 +/- 0.4 raw_unit=s^-1 mM^-1; Km raw_value=4059 +/- 130 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E149Q/I200V to reconstruct the assayed variant sequence.

column_label: Table 1. Kinetic properties of recombinant ALDH3H1 and mutant enzymes.; row ALDH3H1E149Q/I200V; kcat column raw 11.4 +/- 0.6; kcat/Km column raw 6.1 +/- 0.1; Km column raw 1856 +/- 43

normalized_value_unit_evidence: kcat normalized_value=11.4 normalized_unit=s^-1; kcat/Km normalized_value=6.14224137931034 normalized_unit=s^-1*mM^-1 from same-row kcat and Km; printed efficiency=6.1 +/- 0.1 s^-1 mM^-1; Km normalized_value=1.856 normalized_unit=mM from 1856 +/- 43 uM / 1000

raw_value_unit_evidence: kcat raw_value=11.4 +/- 0.6 raw_unit=s^-1; kcat/Km raw_value=6.1 +/- 0.1 raw_unit=s^-1 mM^-1; Km raw_value=1856 +/- 43 raw_unit=uM


smiles: CCCCCC/C=C/C=O


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


enzyme_display_name: Aldehyde dehydrogenase family 3 member H1

substrate_name: propionaldehyde

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

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / propionaldehyde; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 propionaldehyde Km raw_value=510 raw_unit=uM

row_label: ALDH3H1 / propionaldehyde

substrate: propionaldehyde


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / hexanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 hexanal Km raw_value=71 raw_unit=uM

row_label: ALDH3H1 / hexanal

enzyme: Aldehyde dehydrogenase family 3 member H1


substrate_name: octanal

smiles: CCCCCCCC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / octanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 octanal Km raw_value=29 raw_unit=uM

row_label: ALDH3H1 / octanal

substrate: octanal


substrate_name: nonanal

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / nonanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 nonanal Km raw_value=8 raw_unit=uM

row_label: ALDH3H1 / nonanal

substrate: nonanal


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / dodecanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 dodecanal Km raw_value=5 raw_unit=uM

row_label: ALDH3H1 / dodecanal

substrate: dodecanal


smiles: CCCC=CC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / trans-2-hexenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 trans-2-hexenal Km raw_value=180 raw_unit=uM

row_label: ALDH3H1 / trans-2-hexenal


smiles: CCCCCCC=CC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / trans-2-nonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 trans-2-nonenal Km raw_value=3 raw_unit=uM

row_label: ALDH3H1 / trans-2-nonenal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3H1 / 4-hydroxynonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3H1 4-hydroxynonenal Km raw_value=40.3 raw_unit=uM

row_label: ALDH3H1 / 4-hydroxynonenal


substrate_name: NAD(+) (in the presence of hexanal as co-substrate)


enzyme_display_name: Aldehyde dehydrogenase family 3 member I1, chloroplastic

smiles: CCC=O

column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / propionaldehyde; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 propionaldehyde Km raw_value=8053 raw_unit=uM

row_label: ALDH3I1 / propionaldehyde


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / hexanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 hexanal Km raw_value=111 raw_unit=uM

row_label: ALDH3I1 / hexanal

enzyme: Aldehyde dehydrogenase family 3 member I1, chloroplastic


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / octanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 octanal Km raw_value=24 raw_unit=uM

row_label: ALDH3I1 / octanal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / nonanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 nonanal Km raw_value=7 raw_unit=uM

row_label: ALDH3I1 / nonanal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / dodecanal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 dodecanal Km raw_value=1.3 raw_unit=uM

row_label: ALDH3I1 / dodecanal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / trans-2-hexenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 trans-2-hexenal Km raw_value=151 raw_unit=uM

row_label: ALDH3I1 / trans-2-hexenal


column_label: Table 1. Kinetic properties of recombinant Arabidopsis ALDH3H1 and ALDH3I1 proteins; row ALDH3I1 / trans-2-nonenal; column(s) Km (uM)

raw_value_unit_evidence: Table 1 ALDH3I1 trans-2-nonenal Km raw_value=5.5 raw_unit=uM

row_label: ALDH3I1 / trans-2-nonenal