sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298V to reconstruct the assayed variant sequence.

proof_lines: mutant H298V, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: 2-oxoglutarate dehydrogenase system

organism: Escherichia coli

source_db: brenda

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 H260E/H298N to reconstruct the assayed variant sequence.

proof_lines: mutant H260E/H298N, pH not specified in the publication, temperature not specified in the publication

data_origin: experimental

enzyme: 2-oxoglutarate dehydrogenase system

status: unverified

source: brenda


kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298L to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant H298L, pH not specified in the publication, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298D to reconstruct the assayed variant sequence.

proof_lines: mutant H298D, pH not specified in the publication, temperature not specified in the publication


verification_status: verified

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. Effect of H298 and H260/H298 substitutions on E1-specific activity of OGDHc; top panel, 2-OG; row none / 2-OG; columns kcat (s^-1); Km; kcat/Km (s^-1 mM^-1)

normalized_value_unit_evidence: kcat normalized_value=2.15 normalized_unit=s^-1; Km normalized_value=0.00261 normalized_unit=mM; kcat/Km normalized_value=823.754789272031 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=2.15 +/- 0.10 raw_unit=s^-1; Km raw_value=2.61 +/- 0.376 in Km (mM x 10^-3) raw_unit=mM; kcat/Km raw_value=824 printed; computed from table kcat/Km=2.15/0.00261 raw_unit=s^-1*mM^-1

row_label: none / 2-OG

status: verified


organism: Thermus thermophilus

substrate_name: NAD+

kcat_display: Not reported

kcat_over_km_display: Not reported

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

assay_conditions_summary: pH 8.3; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


enzyme_display_name: pyruvate dehydrogenase system

organism: Brassica oleracea

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

enzyme: pyruvate dehydrogenase system

substrate: Unknown


organism: Sus scrofa

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

proof_lines: overall activity of the complex, presence of Ca2+, absence of NADH, 30°C, pH not specified in the publication

proof_lines: activity of component E1, presence of Ca2+, absence of NADH, 30°C, pH not specified in the publication

proof_lines: overall activity of the complex, presence of Ca2+, presence of NADH, 30°C, pH not specified in the publication


organism: Neurospora crassa

proof_lines:
in presence of 0.0045 mM Ca2+
pH 7.4, 30°C
in presence of 0.0225 mM Ca2+


organism: Thermotoga maritima

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

assay_conditions_summary: pH 8; cofactor NAD+


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

assay_conditions_summary: pH 8


substrate_name: arsenate

substrate: arsenate


organism: Acinetobacter sp.

assay_conditions_summary: cofactor ADP

proof_lines:
in presence of 0.2 mM AMP
in presence of 0.2 M ADP
in absence of added nucleotide


organism: Saccharomyces cerevisiae


organism: Azotobacter vinelandii


organism: Aspergillus niger


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


organism: Oryctolagus cuniculus


organism: Komagataeibacter xylinus

assay_conditions_summary: cofactor NAD+

proof_lines: competitive inhibition with respect to NAD+, 2-oxoglutarate dehydrogenase complex


organism: Homo sapiens


enzyme_display_name: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase

organism: Mesorhizobium loti

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E149Q with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.


enzyme: 5-formyl-3-hydroxy-2-methylpyridine 4-carboxylic acid 5-dehydrogenase


organism: Geobacillus stearothermophilus


sequence_variant_note: Mutation signature H176N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: [Brevibacterium] flavum


organism: Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)

substrate_name: FHMPC (at pH 8.0, in the presence of NAD(+))

source_db: uniprot

proof_lines: kcat is 204 sec(-1) for the oxidation of FHMPC. kcat is 217 sec(-1) for the reduction of FHMPC.

source: uniprot


substrate_name: NADH (at pH 8.0)

assay_conditions_summary: pH 8; cofactor NADH

substrate: NADH (at pH 8.0)


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: phosphate

substrate: phosphate


organism: Pseudomonas aeruginosa


enzyme_display_name: 3-sulfolactaldehyde dehydrogenase

organism: Pseudomonas putida

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines: with NADP+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

proof_lines: with NAD+ as cosubstrate, in 50 mM Tris-HCl (pH 7.5), temperature not specified in the publication

enzyme: 3-sulfolactaldehyde dehydrogenase


substrate_name: 4-oxobutanoate with NAD(+) as cosubstrate

proof_lines: kcat is 11.8 sec(-1) for 4-oxobutanoate oxidation with NAD(+). kcat is 11.4 sec(-1) for 4-oxobutanoate oxidation with NADP(+).


enzyme_display_name: [amino-group carrier protein]-5-phospho-L-glutamate reductase

organism: Thermus thermophilus

substrate_name: NADP+

source_db: oed

assay_conditions_summary: pH 9.5; 333.15 K; cofactor NADP+

substrate: NADP+

source: oed


smiles: O=P(O)(O)O

enzyme: [amino-group carrier protein]-5-phospho-L-glutamate reductase


enzyme_display_name: [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase


enzyme: [amino-group carrier protein]-6-phospho-L-2-aminoadipate reductase


substrate_name: [amino group carrier protein LysW]-gamma-aminoadipic semialdehyde

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


proof_lines:
mutant enzyme H209A, at pH 7.5 and 60°C
mutant enzyme H209A, at pH 9.5 and 60°C

substrate: [amino group carrier protein LysW]-gamma-aminoadipic semialdehyde


proof_lines:
wild type enzyme, at pH 7.5 and 60°C
wild type enzyme, at pH 9.5 and 60°C


enzyme_display_name: PE-PGRS family protein PE_PGRS45

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: palmitoyl-CoA

assay_conditions_summary: cofactor CoA

enzyme: PE-PGRS family protein PE_PGRS45

substrate: palmitoyl-CoA


organism: Escherichia coli

verification_status: corrected

smiles: O=CCCO

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label 3-Hydroxypropionaldehyde / NAD+; kcat_over_km paper=58.57 s^-1 mM^-1; export=58.244897959183675 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=28.54 s^-1; km=0.49 mM; kcat_over_km=58.57 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row 3-Hydroxypropionaldehyde / NAD+; Vmax 32.10 +/- 5.14 U mg^-1 protein; Km 0.49 +/- 0.015 mM; kcat 28.54 +/- 4.6 s^-1; kcat/Km 58.57 +/- 9.37 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: 3-Hydroxypropionaldehyde / NAD+

status: corrected


smiles: O=C(O)CCO

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label 3-Hydroxypropionic acid (footnote b) / NADH; kcat_over_km paper=2.2 s^-1 mM^-1; export=2.166666666666667 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=0.26 s^-1; km=0.12 mM; kcat_over_km=2.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row 3-Hydroxypropionic acid (footnote b) / NADH; Vmax 0.30 +/- 0.05 U mg^-1 protein; Km 0.12 +/- 0.004 mM; kcat 0.26 +/- 0.04 s^-1; kcat/Km 2.20 +/- 0.35 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NADH. Footnote: Reverse reaction.


substrate_name: acetaldehyde

smiles: CC=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Acetaldehyde / NAD+

normalized_value_unit_evidence: Normalized evidence: kcat=11.03 s^-1; km=1 mM; kcat_over_km=11.03 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Acetaldehyde / NAD+; Vmax 12.39 +/- 1.98 U mg^-1 protein; Km 1.00 +/- 0.030 mM; kcat 11.03 +/- 1.76 s^-1; kcat/Km 11.03 +/- 1.76 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Acetaldehyde / NAD+

substrate: acetaldehyde


substrate_name: benzaldehyde

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Benzaldehyde / NADP+; kcat_over_km paper=3.23 s^-1 mM^-1; export=3.23463687150838 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=17.37 s^-1; km=5.37 mM; kcat_over_km=3.23 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Benzaldehyde / NADP+; Vmax 19.51 +/- 3.12 U mg^-1 protein; Km 5.37 +/- 0.161 mM; kcat 17.37 +/- 2.78 s^-1; kcat/Km 3.23 +/- 0.52 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NADP+.

row_label: Benzaldehyde / NADP+

substrate: benzaldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Butyraldehyde / NAD+; kcat_over_km paper=27.79 s^-1 mM^-1; export=27.783505154639176 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=26.95 s^-1; km=0.97 mM; kcat_over_km=27.79 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Butyraldehyde / NAD+; Vmax 30.07 +/- 4.81 U mg^-1 protein; Km 0.97 +/- 0.029 mM; kcat 26.95 +/- 4.31 s^-1; kcat/Km 27.79 +/- 4.45 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Butyraldehyde / NAD+

substrate: Butyraldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)C=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Isovaleraldehyde / NAD+; kcat_over_km paper=40.16 s^-1 mM^-1; export=40.16176470588235 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=27.31 s^-1; km=0.68 mM; kcat_over_km=40.16 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Isovaleraldehyde / NAD+; Vmax 30.67 +/- 4.91 U mg^-1 protein; Km 0.68 +/- 0.020 mM; kcat 27.31 +/- 4.37 s^-1; kcat/Km 40.16 +/- 6.43 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Isovaleraldehyde / NAD+

substrate: Isovaleraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Propionaldehyde / NAD+; kcat_over_km paper=20.12 s^-1 mM^-1; export=20.123966942148762 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=24.35 s^-1; km=1.21 mM; kcat_over_km=20.12 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Propionaldehyde / NAD+; Vmax 27.35 +/- 5.90 U mg^-1 protein; Km 1.21 +/- 0.036 mM; kcat 24.35 +/- 3.89 s^-1; kcat/Km 20.12 +/- 3.21 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Propionaldehyde / NAD+

substrate: propionaldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

column_label: Applied Microbiology and Biotechnology 2008 Table 4, row label Valeraldehyde / NAD+; kcat_over_km paper=109.32 s^-1 mM^-1; export=109.33333333333333 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=26.24 s^-1; km=0.24 mM; kcat_over_km=109.32 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 Kinetic properties of aldehyde dehydrogenase; row Valeraldehyde / NAD+; Vmax 29.47 +/- 4.99 U mg^-1 protein; Km 0.24 +/- 0.007 mM; kcat 26.24 +/- 4.20 s^-1; kcat/Km 109.32 +/- 17.5 x 10^3 M^-1 s^-1. Assay conditions: 50 mM potassium phosphate buffer (pH 8.0); 3-HPA or 3-HP, 4 mM; NAD(P)+/NAD(P)H; 4.31 ug protein ml^-1 (=0.01872 uM); and 37 C. Cofactor condition: NAD+.

row_label: Valeraldehyde / NAD+

substrate: Valeraldehyde


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y177A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


enzyme_display_name: cinnamoyl-CoA reductase

organism: Panicum virgatum

substrate_name: sinapoyl-CoA

assay_conditions_summary: pH 6.3; buffer pH 6; cofactor CoA

proof_lines: 100 mM sodium/potassium phosphate buffer pH 6.3, 250 mM NADPH

enzyme: cinnamoyl-CoA reductase

substrate: sinapoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: caffeoyl-CoA

substrate: caffeoyl-CoA


organism: Triticum aestivum


organism: Populus x canadensis


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines:
cosubstrate sinapoyl-CoA
cosubstrate p-coumaroyl-CoA
cosubstrate feruloyl-CoA

substrate: NADPH


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: CoA

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris/HCl; cofactor CoA

proof_lines: at 25°C in 50 mM Tris/HCl buffer, pH 8.0

substrate: CoA


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Aromatoleum evansii

substrate_name: benzyl viologen

substrate: benzyl viologen


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


substrate_name: NAD+

substrate: NAD+


enzyme_display_name: aspartate-semialdehyde dehydrogenase

organism: Mycobacterium tuberculosis

substrate_name: NADP+

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

enzyme: aspartate-semialdehyde dehydrogenase

substrate: NADP+


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


substrate_name: phosphate

substrate: phosphate


organism: Ziziphus jujuba

assay_conditions_summary: pH 6; cofactor CoA

proof_lines: at pH 6.0, temperature not specified in the publication


substrate_name: L-aspartate 4-semialdehyde

substrate: L-aspartate 4-semialdehyde


assay_conditions_summary: cofactor NADP+


organism: Vibrio cholerae serotype O1

proof_lines:
gene II
gene I


proof_lines:
gene I
gene II


organism: Saccharomyces cerevisiae

substrate_name: D-glyceraldehyde 3-phosphate

substrate: D-glyceraldehyde 3-phosphate


organism: Salmonella enterica

assay_conditions_summary: pH 8.6; 298.15 K; buffer 0.2 M bicine


substrate_name: L-4-aspartyl phosphate

substrate: L-4-aspartyl phosphate


substrate_name: vanadate

substrate: vanadate


substrate_name: arsenate

substrate: arsenate


organism: Bos taurus

assay_conditions_summary: pH 8.9; cofactor NAD+

proof_lines: pH and temperature not specified in the publication


organism: Ictidomys tridecemlineatus

substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines:
pH 8.0, 5°C, euthermic
pH 8.0, 36°C, long torpor

substrate: 3-phospho-D-glyceroyl phosphate


assay_conditions_summary: pH 8; 309.15 K; cofactor NAD+

proof_lines:
pH 8.0, 36°C, long torpor
pH 8.0, 5°C, euthermic


organism: Stutzerimonas stutzeri

substrate_name: benzaldehyde

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+

proof_lines: in the presence of NADP+, at 25°C and pH 8.5

proof_lines: in the presence of NAD+, at 25°C and pH 8.5

substrate: benzaldehyde


proof_lines: in the presence of benzaldehyde, at 25°C and pH 8.5


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


organism: Haemophilus influenzae


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Azospirillum brasilense

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme

enzyme: 2,5-dioxovalerate dehydrogenase


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


smiles: C(CO)C=O


substrate_name: alpha-Ketoglutaric semialdehyde

proof_lines:
with NADP+ as cofactor
with NAD+ as cofactor

substrate: alpha-Ketoglutaric semialdehyde


assay_conditions_summary: cofactor NAD+


organism: Bacillus subtilis

assay_conditions_summary: pH 8.2; 303.15 K; cofactor NAD+

proof_lines: 50 mM potassium phosphate pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA

proof_lines: 50 mM KP04 pH 8.2, 30°C, 0.5 mM 2-methyl-3-oxopropanoate, 12 mM NAD+, 0.5 mM CoA


assay_conditions_summary: pH 8.2; 303.15 K; cofactor CoA


organism: Rattus norvegicus

substrate_name: 2-aminoadipic semialdehyde

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

substrate: 2-aminoadipic semialdehyde


substrate_name: alpha-aminoadipate

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

substrate: alpha-aminoadipate


enzyme_display_name: UniProt G3X982

organism: Mus musculus

substrate_name: Heptanal

source_db: skid

source_license: CC BY-NC-ND 4.0

smiles: CCCCCCC=O

enzyme: UniProt G3X982

substrate: Heptanal

source: skid


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: pentanal

substrate: pentanal


substrate_name: ethyl vanillin

substrate: ethyl vanillin


substrate_name: Vanillin

substrate: Vanillin


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: phenylpropionaldehyde

substrate: phenylpropionaldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: purine

substrate: purine


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


enzyme_display_name: UniProt Q06278

organism: Homo sapiens

substrate_name: methotrexate

enzyme: UniProt Q06278

substrate: methotrexate


substrate_name: allopurinol

substrate: allopurinol


substrate_name: flunitrazepam

substrate: flunitrazepam


substrate_name: nilutamide

substrate: nilutamide


substrate_name: flutamide

substrate: flutamide


substrate_name: nimetazepam

substrate: nimetazepam


substrate_name: clonazepam

substrate: clonazepam


substrate_name: nimesulide

substrate: nimesulide


enzyme_display_name: UniProt P45850

organism: Hordeum vulgare

substrate_name: oxalic acid

assay_conditions_summary: pH 4

enzyme: UniProt P45850

substrate: oxalic acid


organism: Pseudomonas putida

substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


enzyme_display_name: retinal dehydrogenase

organism: Xenopus laevis

substrate_name: retinal

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.03 mM retinal, 0.056-0.12 mM NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.5 mM Ca2+, 0.03 mM retinal, 0.056-0.12 mM NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.04 mM Mn2+, 0.03 mM retinal, 0.056-0.12 mM NAD+

enzyme: retinal dehydrogenase

substrate: retinal


proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.01 mM Zn2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.02 Mn2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 0.03 mM Ca2+, 12 mM acetaldehyde, 0.015-0.024 mM NAD+


substrate_name: Unknown

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 12 mM acetaldehyde, 0.015-0.024 mM NAD+

proof_lines: 50 mM Tris/HCl buffer, pH 8.0, 3.3 mM pyrazole, 100 mM KCl, 1 mM dithiothreitol, 1-12 mM acetaldehyde, 0.33 mM NAD+

substrate: Unknown


organism: Oryza sativa Japonica Group

substrate_name: sinapoyl-CoA

assay_conditions_summary: pH 6.3; 303.15 K; cofactor CoA

proof_lines:
isoform CCR21, at pH 6.3 and 30°C
isoform CCR20, at pH 6.3 and 30°C
isoform CCR19, at pH 6.3 and 30°C

substrate: sinapoyl-CoA


substrate_name: feruloyl-CoA

proof_lines:
isoform CCR21, at pH 6.3 and 30°C
isoform CCR19, at pH 6.3 and 30°C
isoform CCR20, at pH 6.3 and 30°C

substrate: feruloyl-CoA


enzyme_display_name: aldehyde oxidase

substrate_name: n-hexylaldehyde

enzyme: aldehyde oxidase

substrate: n-hexylaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


organism: Methylobacillus sp.

substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: citral

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

substrate: citral


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: hexylaldehyde

substrate: hexylaldehyde


enzyme_display_name: glyoxylate oxidase

organism: Tyromyces palustris

substrate_name: glyoxylate

enzyme: glyoxylate oxidase

substrate: glyoxylate


organism: Desulfovibrio desulfuricans

substrate_name: propionaldehyde

column_label: Results prose: steady-state kinetic analysis reports K_M in uM and Vmax in uM/min/mg; propio-(12,420).

raw_value_unit_evidence: 12 uM

row_label: propio-

table_label: Results and Discussion prose, steady-state kinetic analysis sentence

substrate: propionaldehyde


substrate_name: butanaldehyde

smiles: CCCC=O

column_label: Results prose: steady-state kinetic analysis reports K_M in uM and Vmax in uM/min/mg; butan-(105,295).

row_label: butan-

substrate: butanaldehyde


substrate_name: benzaldehyde

column_label: Results prose: steady-state kinetic analysis reports K_M in uM and Vmax in uM/min/mg; benzaldehyde(151,000).

row_label: benzaldehyde

substrate: benzaldehyde


column_label: Results prose: steady-state kinetic analysis reports K_M in uM and Vmax in uM/min/mg; acet-(250,950).

row_label: acet-


enzyme_display_name: oxalate oxidase

organism: Brucella intermedia

substrate_name: oxalate

enzyme: oxalate oxidase

substrate: oxalate


organism: Sorghum sp.

substrate_name: oxalic acid

substrate: oxalic acid


organism: Abortiporus biennis


organism: Streptomyces rimosus


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

substrate: Glutaraldehyde


substrate_name: n-Heptanal

substrate: n-Heptanal


substrate_name: n-hexanal

substrate: n-hexanal


substrate_name: p-tolualdehyde

substrate: p-tolualdehyde


substrate_name: n-Pentanal

substrate: n-Pentanal


substrate_name: m-tolualdehyde

substrate: m-tolualdehyde


substrate_name: Glyoxal

smiles: C(=O)C=O

substrate: Glyoxal


substrate_name: o-tolualdehyde

substrate: o-tolualdehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: Vanillin

substrate: Vanillin


organism: Costus pictus

assay_conditions_summary: pH 5; 313.15 K; buffer succinate

proof_lines: in succinate buffer (50 mM, pH 5.0), 10 mM CuSO4, at 40°C


organism: Streptomyces moderatus

substrate_name: citral

substrate: citral


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: hexylaldehyde

substrate: hexylaldehyde


substrate_name: acrolein

substrate: acrolein


substrate_name: formaldehyde

substrate: formaldehyde


organism: Sorghum bicolor

substrate_name: oxalate

proof_lines: oxalate oxidase form NaCl stressed seedlings

substrate: oxalate


organism: Oryza sativa

proof_lines:
isoform OXO1, at pH 4.0 and 25°C
isoform OXO2, at pH 3.5 and 25°C
isoform OXO4, at pH 4.0 and 25°C


organism: Amaranthus spinosus


organism: Mus musculus


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: Butanal

substrate: Butanal


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: crotonaldehyde

smiles: C/C=C/C=O

substrate: crotonaldehyde


substrate_name: ethyl vanillin

substrate: ethyl vanillin


substrate_name: Heptanal

substrate: Heptanal


substrate_name: hexanal

substrate: hexanal


substrate_name: octanal

substrate: octanal


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: phenanthridine

substrate: phenanthridine


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: phenylpropionaldehyde

substrate: phenylpropionaldehyde


substrate_name: Phthalazine

substrate: Phthalazine


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: purine

substrate: purine


substrate_name: retinalaldehyde

substrate: retinalaldehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: Vanillin

substrate: Vanillin


substrate_name: oxalic acid

proof_lines:
PVC-immobilized enzyme
free enzyme
immobilized enzyme

substrate: oxalic acid


organism: Zea mays

substrate_name: benzaldehyde

proof_lines: 2,6-dichlorophenol-indophenol as electron acceptor

substrate: benzaldehyde


substrate_name: Protocatechualdehyde

substrate: Protocatechualdehyde


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Beta vulgaris

proof_lines:
immobilized on PEG1900
immobilized on PEG5000


substrate_name: oxalate

proof_lines:
calorimetry
O2 consumption

substrate: oxalate


organism: Musa acuminata


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

proof_lines: kcat is 4 sec(-1) for phthalazine oxidation (PubMed:11562361). kcat is 130 min(-1) for benzaldehyde oxidation, 384 min(-1) for butyraldehyde oxidation and 1279 min(-1) for 2-OH-pyrimidine oxidation (PubMed:21705476). kcat is 41.1 min(-1) fo

source_databases_merged: skid uniprot


substrate_name: Butanal

substrate: Butanal


enzyme_display_name: Aldehyde oxidase 1

substrate_name: benzaldehyde (at 30 degrees Celsius and pH 7.5)

proof_lines: kcat is 317.6 min(-1) for benzaldehyde oxidation, 128.1 min(-1) for phthalazine oxidation, 49.5 min(-1) for retinal oxidation, and 519.9 min(-1) for acetaldehyde oxidation (at 30 degrees Celsius and pH 7.5) (PubMed:19401776). However in thi

enzyme: Aldehyde oxidase 1


substrate_name: phthalazine (at 30 degrees Celsius and pH 7.5)


substrate_name: acetaldehyde (at 30 degrees Celsius and pH 7.5)


enzyme_display_name: Aldehyde oxidase 4

organism: Arabidopsis thaliana

substrate_name: benzoic acid (BA) (at pH7, in the presence of NAD(+))

assay_conditions_summary: pH 7

proof_lines: kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate, 1.904 sec(-1) with indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).

enzyme: Aldehyde oxidase 4


substrate_name: indole-3-acetaldehyde (at pH7)

substrate: indole-3-acetaldehyde (at pH7)


substrate_name: cinnamylaldehyde (at pH7)

substrate: cinnamylaldehyde (at pH7)


enzyme_display_name: Aldehyde oxidase

organism: Homo sapiens

substrate_name: benzaldehyde (in the presence of 2,6-dichlorophenol indophenol as electron acceptor)

proof_lines: kcat is 6.4 min(-1) for benzaldehyde oxidation, 5.6 min(-1) for phthalazine oxidation, 12.2 min(-1) for phenanthridine oxidation and 5.6 min(-1) for chloroquinazolinone oxidation.

enzyme: Aldehyde oxidase


substrate_name: phenanthridine (in the pres 2,6-dichlorophenol indophenol as electron acceptor)


organism: Macaca fascicularis

substrate_name: cinchonidine

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V1085A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 310.15 K; buffer 80 mM phosphate

proof_lines: mutant enzyme V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C

substrate: cinchonidine


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


substrate_name: pentanal

source_databases_merged: brenda oed

substrate: pentanal


substrate_name: Salicylaldehyde


substrate_name: Phthalazine

substrate: Phthalazine


substrate_name: retinal (at 37 degrees Celsius and pH 7.8)


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


enzyme_display_name: 2-Hydroxyacid oxidase 1

substrate_name: L-lactate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)

proof_lines: kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degrees Celsius) (PubMed:18215067). kcat is 0.7 sec(-1) for the oxidation of glyoxylate with DCIP as electron acceptor (at pH 7.5 and 37 degrees Celsius) (PubMed:18215067). kcat is 0.83 sec(-1) for the oxidation of glyoxylate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 0.46 sec(-1) for the oxidation of L-lactate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 0.11 sec(-1) for the oxidation of L-mandelate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). Shows a higher catalytic efficiency for glycolate compared to glyoxylate (PubMed:17669354, PubMed:18215067).

enzyme: 2-Hydroxyacid oxidase 1


substrate_name: L-mandelate (at pH 7.0 and 37 degrees Celsius, with DCIP as electron acceptor)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A807V/Y885M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8


substrate_name: benzaldehyde


substrate_name: phenanthridine

substrate: phenanthridine


organism: Gelatoporia subvermispora

substrate_name: oxalate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A242E with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A242E, pH and temperature not specified in the publication


substrate_name: glycolate (at pH 7.5, with DCIP as electron acceptor)

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

proof_lines: kcat is 3.6 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.0 and 37 degrees Celsius) (PubMed:17669354). kcat is 4.1 sec(-1) for the oxidation of glycolate with DCIP as electron acceptor (at pH 7.5 and 37 degr


substrate_name: glyoxylate (at pH 7.5 and 37 degrees Celsius, with DCIP as electron acceptor)

column_label: Full text reports kcat, KM, and kcat/KM for glyoxylate were 0.7 +/- 0.1 s^-1, 2200 +/- 360 microM, and 0.32 +/- 0.05 mM^-1 s^-1.

raw_value_unit_evidence: Km raw_value=2200 +/- 360 microM raw_unit=microM

row_label: human GO / glyoxylate oxidation

table_label: Official PMC full-text Kinetic Analyses of Human GO prose


substrate_name: 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)


substrate_name: famciclovir (at 37 degrees Celsius and pH 7)


substrate_name: allopurinol

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L to reconstruct the assayed variant sequence.

substrate: allopurinol


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G3X982 and applied mutation signature P1015A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row phthalazine / mAOX3-P1015A; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=179 +/- 38 raw_unit=min^-1; Km raw_value=2.6 +/- 0.3 raw_unit=uM; kcat/Km raw_value=68.9 +/- 16.6 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=2.98 normalized_unit=s^-1; Km normalized_value=0.0026 normalized_unit=mM; kcat/Km normalized_value=1146.1538461538462 normalized_unit=s^-1*mM^-1

row_label: phthalazine / mAOX3-P1015A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G3X982 and applied mutation signature P1015G with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row phthalazine / mAOX3-P1015G; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=347 +/- 64 raw_unit=min^-1; Km raw_value=10.3 +/- 2 raw_unit=uM; kcat/Km raw_value=33.7 +/- 9 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=5.78 normalized_unit=s^-1; Km normalized_value=0.0103 normalized_unit=mM; kcat/Km normalized_value=561.1650485436893 normalized_unit=s^-1*mM^-1

row_label: phthalazine / mAOX3-P1015G


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature Y885M to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; buffer air-saturated

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row Y885M, substrate Phthalazine: kcat 48.9 min^-1; Km 3.2 uM; explicit kcat/Km 15.28 min^-1 uM^-1.

normalized_value_unit_evidence: kcat 0.815 s^-1; Km 0.0032 mM; explicit kcat/Km 254.666666667 s^-1*mM^-1; ratio from rounded kcat/Km cells 254.6875 s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F1014V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P1015A with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P1015G with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F1014I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G3X982 and applied mutation signature F1014V to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row allopurinol / mAOX3-F1014V; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=16 +/- 2 raw_unit=min^-1; Km raw_value=3860 +/- 567 raw_unit=uM; kcat/Km raw_value=0.0041 +/- 0.0008 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=0.27 normalized_unit=s^-1; Km normalized_value=3.86 normalized_unit=mM; kcat/Km normalized_value=0.06994818652849742 normalized_unit=s^-1*mM^-1

row_label: allopurinol / mAOX3-F1014V


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G3X982 and applied mutation signature F776K/A807E/D878L/L881S/Y885R/K889H/P1015T/Y1019L to reconstruct the assayed variant sequence.

column_label: Table 5: Steady-state kinetic parameters for mAOX3 wild type and mAOX3 variants containing numerous amino acids present in the active site of bovine XOR. The printed column heads of the table are, in order, the substrate column, the kinetic parameters column, and one column per enzyme form; the enzyme form used here is the column headed mAOX3-“active site1”-K889H. Within that column the substrate row allopurinol prints kcat = 95 min−1 on the kcat row, KM = 133 µM on the KM row and kcat/KM = 0.718 min−1 µM−1 on the kcat/KM row.

normalized_value_unit_evidence: kcat: printed Table 5 cell 95 min−1; the printed turnover row is per MINUTE, so 95 / 60 = 1.5833333333333333 s^-1; the exported value is 1.58 s^(-1). KM: printed Table 5 cell 133 µM; 1 uM is 1/1000 mM, so 133 / 1000 = 0.133 mM; the exported value is 2.93 mM. kcat/KM: printed Table 5 cell 0.718 min−1 µM−1; 1 min^-1 uM^-1 is 1000/60 s^-1 mM^-1, so 0.718 * 1000 / 60 = 11.966666666666667 s^-1 mM^-1; the exported value is 0.5392491467576792 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 5, mAOX3-“active site1”-K889H column, substrate row allopurinol: kcat = 95 min−1; KM = 133 µM; kcat/KM = 0.718 min−1 µM−1. The printed column headers of Table 5 carry those three units for every substrate row of the table.


column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row allopurinol / mAOX3-P1015A; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=46 +/- 9 raw_unit=min^-1; Km raw_value=527 +/- 63 raw_unit=uM; kcat/Km raw_value=0.0871 +/- 0.0203 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=0.77 normalized_unit=s^-1; Km normalized_value=0.527 normalized_unit=mM; kcat/Km normalized_value=1.4611005692599621 normalized_unit=s^-1*mM^-1

row_label: allopurinol / mAOX3-P1015A


column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row allopurinol / mAOX3-P1015G; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=37 +/- 4 raw_unit=min^-1; Km raw_value=426 +/- 56 raw_unit=uM; kcat/Km raw_value=0.0864 +/- 0.0145 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=0.62 normalized_unit=s^-1; Km normalized_value=0.426 normalized_unit=mM; kcat/Km normalized_value=1.455399061032864 normalized_unit=s^-1*mM^-1

row_label: allopurinol / mAOX3-P1015G


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

column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row allopurinol / mAOX3-WT; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=73 +/- 16 raw_unit=min^-1; Km raw_value=1595 +/- 73 raw_unit=uM; kcat/Km raw_value=0.0457 +/- 0.0103 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=1.22 normalized_unit=s^-1; Km normalized_value=1.595 normalized_unit=mM; kcat/Km normalized_value=0.7648902821316614 normalized_unit=s^-1*mM^-1

row_label: allopurinol / mAOX3-WT


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G3X982 and applied mutation signature F1014I to reconstruct the assayed variant sequence.

column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row benzaldehyde / mAOX3-F1014I; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=19 +/- 3 raw_unit=min^-1; Km raw_value=22.7 +/- 2.7 raw_unit=uM; kcat/Km raw_value=0.8 +/- 0.2 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=0.31 normalized_unit=s^-1; Km normalized_value=0.0227 normalized_unit=mM; kcat/Km normalized_value=13.656387665198237 normalized_unit=s^-1*mM^-1

row_label: benzaldehyde / mAOX3-F1014I


column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row benzaldehyde / mAOX3-F1014V; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=128 +/- 12 raw_unit=min^-1; Km raw_value=21.5 +/- 3.2 raw_unit=uM; kcat/Km raw_value=5.9 +/- 1.0 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=2.13 normalized_unit=s^-1; Km normalized_value=0.0215 normalized_unit=mM; kcat/Km normalized_value=99.06976744186046 normalized_unit=s^-1*mM^-1

row_label: benzaldehyde / mAOX3-F1014V


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F776K/A807E/D878L/L881S/Y885R/P1015T/Y1019L to reconstruct the assayed variant sequence.


column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row benzaldehyde / mAOX3-P1015A; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=76 +/- 14 raw_unit=min^-1; Km raw_value=2.2 +/- 0.1 raw_unit=uM; kcat/Km raw_value=34.7 +/- 6.4 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=1.27 normalized_unit=s^-1; Km normalized_value=0.0022 normalized_unit=mM; kcat/Km normalized_value=577.2727272727273 normalized_unit=s^-1*mM^-1

row_label: benzaldehyde / mAOX3-P1015A


column_label: Table 2. Steady-state kinetic parameters of mAOX3 wildtype and mAOX3 variants containing single amino acid exchanges in the active site.; row benzaldehyde / mAOX3-P1015G; columns kcat [min^-1], KM [uM], kcat/KM [min^-1 uM^-1]; kcat raw_value=93 +/- 7 raw_unit=min^-1; Km raw_value=3.3 +/- 0.2 raw_unit=uM; kcat/Km raw_value=28 +/- 2.7 raw_unit=min^-1*uM^-1

normalized_value_unit_evidence: kcat normalized_value=1.55 normalized_unit=s^-1; Km normalized_value=0.0033 normalized_unit=mM; kcat/Km normalized_value=469.6969696969697 normalized_unit=s^-1*mM^-1

row_label: benzaldehyde / mAOX3-P1015G


substrate_name: Phenanthridine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H1297R with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.

column_label: Table 3 substrate Phenanthridine; variant column H1297R; KM, active-portion kcat, and active-portion kcat/KM rows; cells 4.1 +/- 0.7 uM, 31.5 +/- 1.0 min^-1, 7.68 +/- 1.43 1/(min*uM).

raw_value_unit_evidence: KM = 4.1 +/- 0.7 uM; active-portion kcat = 31.5 +/- 1.0 min^-1; active-portion kcat/KM = 7.68 +/- 1.43 1/(min*uM)

row_label: Phenanthridine; H1297R

table_label: Table 3: Steady-state kinetics of hAOX1 and its variants corresponding to SNPs

substrate: Phenanthridine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N1135S with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

column_label: Table 3 substrate Phenanthridine; variant column N1135S; KM, active-portion kcat, and active-portion kcat/KM rows; cells 6.1 +/- 1.0 uM, 32.6 +/- 1.1 min^-1, 5.34 +/- 1.10 1/(min*uM).

raw_value_unit_evidence: KM = 6.1 +/- 1.0 uM; active-portion kcat = 32.6 +/- 1.1 min^-1; active-portion kcat/KM = 5.34 +/- 1.10 1/(min*uM)

row_label: Phenanthridine; N1135S


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R802C with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

column_label: Table 3 substrate Phenanthridine; variant column R802C; KM, active-portion kcat, and active-portion kcat/KM rows; cells 4.4 +/- 0.4 uM, 10.2 +/- 0.2 min^-1, 2.32 +/- 0.50 1/(min*uM).

raw_value_unit_evidence: KM = 4.4 +/- 0.4 uM; active-portion kcat = 10.2 +/- 0.2 min^-1; active-portion kcat/KM = 2.32 +/- 0.50 1/(min*uM)

row_label: Phenanthridine; R802C


column_label: Table 3 columns WT and Kinetic Parameters; Phenanthridine rows KM, active portion kcat, active portion kcat/KM.

raw_value_unit_evidence: Table 3 WT Phenanthridine cells: KM 3.9 +/- 0.8 uM; active portion kcat 12.2 +/- 0.5 min^-1; active portion kcat/KM 3.13 +/- 0.63 1/min/uM.

row_label: Substrate Phenanthridine; protein WT; active portion

table_label: Table 3, Steady-state kinetics of hAOX1 and its variants corresponding to SNPs


column_label: Table 3 substrate Phthalazine; variant column H1297R; KM, active-portion kcat, and active-portion kcat/KM rows; cells 1.3 +/- 0.2 uM, 5.4 +/- 0.1 min^-1, 4.15 +/- 0.50 1/(min*uM).

raw_value_unit_evidence: KM = 1.3 +/- 0.2 uM; active-portion kcat = 5.4 +/- 0.1 min^-1; active-portion kcat/KM = 4.15 +/- 0.50 1/(min*uM)

row_label: Phthalazine; H1297R


column_label: Table 3 substrate Phthalazine; variant column N1135S; KM, active-portion kcat, and active-portion kcat/KM rows; cells 1.2 +/- 0.1 uM, 7.2 +/- 0.1 min^-1, 6.00 +/- 1.00 1/(min*uM).

raw_value_unit_evidence: KM = 1.2 +/- 0.1 uM; active-portion kcat = 7.2 +/- 0.1 min^-1; active-portion kcat/KM = 6.00 +/- 1.00 1/(min*uM)

row_label: Phthalazine; N1135S


column_label: Table 3 substrate Phthalazine; variant column R802C; KM, active-portion kcat, and active-portion kcat/KM rows; cells 0.9 +/- 0.3 uM, 5.2 +/- 0.3 min^-1, 5.78 +/- 1.00 1/(min*uM).

raw_value_unit_evidence: KM = 0.9 +/- 0.3 uM; active-portion kcat = 5.2 +/- 0.3 min^-1; active-portion kcat/KM = 5.78 +/- 1.00 1/(min*uM)

row_label: Phthalazine; R802C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R921H to reconstruct the assayed variant sequence.

column_label: Table 3 substrate Phthalazine; variant column R921H; KM, active-portion kcat, and active-portion kcat/KM rows; cells 1.6 +/- 0.3 uM, 2.4 +/- 0.1 min^-1, 1.50 +/- 0.33 1/(min*uM).

raw_value_unit_evidence: KM = 1.6 +/- 0.3 uM; active-portion kcat = 2.4 +/- 0.1 min^-1; active-portion kcat/KM = 1.50 +/- 0.33 1/(min*uM)

row_label: Phthalazine; R921H


column_label: Table 3 columns WT and Kinetic Parameters; Phthalazine rows KM, active portion kcat, active portion kcat/KM.

raw_value_unit_evidence: Table 3 WT Phthalazine cells: KM 1.3 +/- 0.3 uM; active portion kcat 5.6 +/- 0.2 min^-1; active portion kcat/KM 4.31 +/- 0.67 1/min/uM.

row_label: Substrate Phthalazine; protein WT; active portion


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature A807V to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V, substrate benzaldehyde: kcat 41 min^-1; Km 2.9 uM; explicit kcat/Km 14.14 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature A807V/Y885M to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V/Y885M, substrate benzaldehyde: kcat 43.6 min^-1; Km 4.6 uM; explicit kcat/Km 9.48 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature E1266Q to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row E1266Q, substrate benzaldehyde: kcat 10.2 min^-1; Km 86.3 uM; explicit kcat/Km 0.12 min^-1 uM^-1.

normalized_value_unit_evidence: kcat 0.17 s^-1; Km 0.0863 mM; explicit kcat/Km 2 s^-1*mM^-1; ratio from rounded kcat/Km cells 1.96987253766 s^-1*mM^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature K889H to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row K889H, substrate benzaldehyde: kcat 19.2 min^-1; Km 2.3 uM; explicit kcat/Km 8.2 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from official_uniprot_rest_json:G3X982 and applied mutation signature Y885M to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row Y885M, substrate benzaldehyde: kcat 57.4 min^-1; Km 6.3 uM; explicit kcat/Km 9.11 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V, substrate N1-methylnicotinamide: kcat 11.2 min^-1; Km 123.4 uM; explicit kcat/Km 0.091 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V/Y885M, substrate N1-methylnicotinamide: kcat 27 min^-1; Km 35.9 uM; explicit kcat/Km 0.752 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row K889H, substrate N1-methylnicotinamide: kcat 3.1 min^-1; Km 25.5 uM; explicit kcat/Km 0.12 min^-1 uM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I1018K with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q3TYQ9 and applied mutation signature I1018S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady state kinetic parameters mAOX4 wildtype and variants with different substrates); enzyme row 'mAOX4-I1018S'; substrate column 'Benzaldehyde'; stacked metric line 'kcat (min-1)' = 75.0 ± 2.3; stacked metric line 'KM (μM)' = 1.1 ± 0.2; stacked metric line 'kcat /KM (min-1μM-1)' = 68.2. The other three columns of the same enzyme block hold the salicylaldehyde, phthalazine and pentanal measurements.

normalized_value_unit_evidence: Km: printed cell 1.1 uM; 1.1 / 1000 = 0.0011 mM. kcat: printed cell 75.0 min^-1; 75.0 / 60 = 1.25 s^(-1). kcat/Km: printed cell 68.2 min^-1 uM^-1; one min^-1 uM^-1 is 1000 / 60 = 16.666667 s^-1 mM^-1, so 68.2 x 1000 / 60 = 1136.6666666666667 s^(-1)*mM^(-1). The full-precision quotient of the same two printed cells is 1.25 / 0.0011 = 1136.3636363636363 s^(-1)*mM^(-1), and the printed efficiency cell is that quotient rendered at the one-decimal precision the table prints.

raw_value_unit_evidence: Table 2, enzyme row 'mAOX4-I1018S', substrate column 'Benzaldehyde': KM = 1.1 uM; kcat = 75.0 min^-1; printed kcat/KM = 68.2 min^-1 uM^-1.

row_label: Table 2, enzyme row 'mAOX4-I1018S', substrate column 'Benzaldehyde' (the stacked kcat, KM and kcat/KM cells of that column)

table_label: Table 2: Steady state kinetic parameters mAOX4 wildtype and variants with different substrates (PLoS ONE 2018, 13(1):e0191819)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I1018S with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


substrate: Salicylaldehyde


organism: Burkholderia sp. AIU 129

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

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Benzaldehyde has Km 0.06, Vmax 5.58, Vmax/Km 93.0

raw_value_unit_evidence: Benzaldehyde row, Km (mM) column = 0.06

row_label: Benzaldehyde

table_label: Table 2. Substrate specificity and kinetic values of ALOD from Burkholderia sp. AIU 129.


substrate_name: butylaldehyde

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Butyraldehyde has Km 0.10, Vmax 8.83, Vmax/Km 88.3

raw_value_unit_evidence: Butyraldehyde row, Km (mM) column = 0.10

row_label: Butyraldehyde

substrate: butylaldehyde


substrate_name: acetaldehyde

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Acetaldehyde has Km 0.34, Vmax 6.42, Vmax/Km 18.9

raw_value_unit_evidence: Acetaldehyde row, Km (mM) column = 0.34

row_label: Acetaldehyde


substrate_name: propionaldehyde

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Propionaldehyde has Km 0.74, Vmax 14.6, Vmax/Km 19.7

raw_value_unit_evidence: Propionaldehyde row, Km (mM) column = 0.74

row_label: Propionaldehyde

substrate: propionaldehyde


substrate_name: glycolaldehyde

smiles: C(C=O)O

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Glycolaldehyde has Km 1.00, Vmax 3.42, Vmax/Km 3.42

raw_value_unit_evidence: Glycolaldehyde row, Km (mM) column = 1.00

row_label: Glycolaldehyde

substrate: glycolaldehyde


substrate_name: Glyoxal

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Glyoxal has Km 12.3, Vmax 4.51, Vmax/Km 0.367

raw_value_unit_evidence: Glyoxal row, Km (mM) column = 12.3

row_label: Glyoxal

substrate: Glyoxal


substrate_name: formaldehyde

column_label: Table 2 columns: Substrate | Km (mM) | Vmax (umol/min/mg protein) | Vmax/Km; row Formaldehyde has Km 35.9, Vmax 4.38, Vmax/Km 0.122

raw_value_unit_evidence: Formaldehyde row, Km (mM) column = 35.9

row_label: Formaldehyde

substrate: formaldehyde


substrate_name: Benzaldehyde

column_label: Table 3 substrate Benzaldehyde; variant column N1135S; KM, active-portion kcat, and active-portion kcat/KM rows; cells 6.7 +/- 2.8 uM, 6.2 +/- 0.3 min^-1, 0.92 +/- 0.11 1/(min*uM).

raw_value_unit_evidence: KM = 6.7 +/- 2.8 uM; active-portion kcat = 6.2 +/- 0.3 min^-1; active-portion kcat/KM = 0.92 +/- 0.11 1/(min*uM)

row_label: Benzaldehyde; N1135S

substrate: Benzaldehyde


column_label: Table 3 substrate Benzaldehyde; variant column R802C; KM, active-portion kcat, and active-portion kcat/KM rows; cells 7.6 +/- 1.9 uM, 5.3 +/- 0.3 min^-1, 0.70 +/- 0.16 1/(min*uM).

raw_value_unit_evidence: KM = 7.6 +/- 1.9 uM; active-portion kcat = 5.3 +/- 0.3 min^-1; active-portion kcat/KM = 0.70 +/- 0.16 1/(min*uM)

row_label: Benzaldehyde; R802C


column_label: Table 3 substrate Benzaldehyde; variant column R921H; KM, active-portion kcat, and active-portion kcat/KM rows; cells 6.3 +/- 1.2 uM, 1.7 +/- 0.1 min^-1, 0.27 +/- 0.08 1/(min*uM).

raw_value_unit_evidence: KM = 6.3 +/- 1.2 uM; active-portion kcat = 1.7 +/- 0.1 min^-1; active-portion kcat/KM = 0.27 +/- 0.08 1/(min*uM)

row_label: Benzaldehyde; R921H


column_label: Table 3 substrate Benzaldehyde; variant column H1297R; KM, active-portion kcat, and active-portion kcat/KM rows; cells 5.2 +/- 1.8 uM, 6.4 +/- 0.3 min^-1, 1.23 +/- 0.17 1/(min*uM).

raw_value_unit_evidence: KM = 5.2 +/- 1.8 uM; active-portion kcat = 6.4 +/- 0.3 min^-1; active-portion kcat/KM = 1.23 +/- 0.17 1/(min*uM)

row_label: Benzaldehyde; H1297R


column_label: Table 3 columns WT and Kinetic Parameters; Benzaldehyde rows KM, active portion kcat, active portion kcat/KM.

raw_value_unit_evidence: Table 3 WT Benzaldehyde cells: KM 7.1 +/- 0.6 uM; active portion kcat 6.4 +/- 0.1 min^-1; active portion kcat/KM 0.91 +/- 0.17 1/min/uM.

row_label: Substrate Benzaldehyde; protein WT; active portion


substrate_name: Chloroquinazolinone

column_label: Table 3 substrate Chloroquinazolinone; variant column H1297R; KM, active-portion kcat, and active-portion kcat/KM rows; cells 5.8 +/- 0.5 uM, 6.7 +/- 0.2 min^-1, 1.16 +/- 0.4 1/(min*uM).

raw_value_unit_evidence: KM = 5.8 +/- 0.5 uM; active-portion kcat = 6.7 +/- 0.2 min^-1; active-portion kcat/KM = 1.16 +/- 0.4 1/(min*uM)

row_label: Chloroquinazolinone; H1297R

substrate: Chloroquinazolinone


column_label: Table 3 substrate Chloroquinazolinone; variant column N1135S; KM, active-portion kcat, and active-portion kcat/KM rows; cells 4.1 +/- 0.5 uM, 6.5 +/- 0.1 min^-1, 1.59 +/- 0.20 1/(min*uM).

raw_value_unit_evidence: KM = 4.1 +/- 0.5 uM; active-portion kcat = 6.5 +/- 0.1 min^-1; active-portion kcat/KM = 1.59 +/- 0.20 1/(min*uM)

row_label: Chloroquinazolinone; N1135S


column_label: Table 3 substrate Chloroquinazolinone; variant column R802C; KM, active-portion kcat, and active-portion kcat/KM rows; cells 4.7 +/- 0.7 uM, 5.4 +/- 0.2 min^-1, 1.15 +/- 0.29 1/(min*uM).

raw_value_unit_evidence: KM = 4.7 +/- 0.7 uM; active-portion kcat = 5.4 +/- 0.2 min^-1; active-portion kcat/KM = 1.15 +/- 0.29 1/(min*uM)

row_label: Chloroquinazolinone; R802C


column_label: Table 3 substrate Chloroquinazolinone; variant column R921H; KM, active-portion kcat, and active-portion kcat/KM rows; cells 4.5 +/- 0.8 uM, 3.6 +/- 0.1 min^-1, 0.80 +/- 0.13 1/(min*uM).

raw_value_unit_evidence: KM = 4.5 +/- 0.8 uM; active-portion kcat = 3.6 +/- 0.1 min^-1; active-portion kcat/KM = 0.80 +/- 0.13 1/(min*uM)

row_label: Chloroquinazolinone; R921H


column_label: Table 3 columns WT and Kinetic Parameters; Chloroquinazolinone rows KM, active portion kcat, active portion kcat/KM.

raw_value_unit_evidence: Table 3 WT Chloroquinazolinone cells: KM 5.2 +/- 0.7 uM; active portion kcat 5.6 +/- 0.1 min^-1; active portion kcat/KM 1.08 +/- 0.14 1/min/uM.

row_label: Substrate Chloroquinazolinone; protein WT; active portion


organism: Oryctolagus cuniculus

substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: N-methylnicotinamide

column_label: Table IV reports N-Methylnicotinamide Km = 1.11 x 10^-4 M and Vmax = 267 nmol/min per mg protein.

normalized_value_unit_evidence: Km normalized_value=0.111 normalized_unit=mM; rounds to source row 0.11 mM

raw_value_unit_evidence: Km raw_value=1.11e-4 raw_unit=M for N-methylnicotinamide

row_label: Rabbit liver cytosol retinal oxidase substrate N-methylnicotinamide

table_label: Table IV Kinetic parameters and substrate specificity of retinal oxidase

substrate: N-methylnicotinamide


smiles: O=O

column_label: Table IV reports Molecular oxygen Km = 9.47 x 10^-5 M and Vmax = 295 nmol/min per mg protein.

raw_value_unit_evidence: Km raw_value=9.47e-5 raw_unit=M for molecular oxygen

row_label: Rabbit liver cytosol retinal oxidase molecular oxygen substrate


organism: Rattus norvegicus

substrate_name: nitrite

substrate: nitrite


substrate_name: NADH

assay_conditions_summary: cofactor NADH

column_label: Figure 4C in-panel annotation reports Km=24 uM for NADH.

raw_value_unit_evidence: Km raw_value=24 raw_unit=uM

row_label: Figure 4C, NADH concentration curve

table_label: PMID 19801639 PMC Figure 4: Kinetics of NO generation from AO as a function of nitrite or reducing substrate concentration

substrate: NADH


column_label: Figure 4D in-panel annotation reports Km=9.6 uM for DMAC.

raw_value_unit_evidence: Km raw_value=9.6 raw_unit=uM

row_label: Figure 4D, DMAC concentration curve


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row Y885M, substrate N1-methylnicotinamide: kcat 23.4 min^-1; Km 82.7 uM; explicit kcat/Km 0.283 min^-1 uM^-1.


substrate_name: phenanthridine

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V, substrate phenanthridine: kcat 315 min^-1; Km 149.5 uM; explicit kcat/Km 2.11 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V/Y885M, substrate phenanthridine: kcat 218 min^-1; Km 11.8 uM; explicit kcat/Km 18.47 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row K889H, substrate phenanthridine: kcat 79.9 min^-1; Km 16.1 uM; explicit kcat/Km 4.97 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row Y885M, substrate phenanthridine: kcat 266.9 min^-1; Km 33.4 uM; explicit kcat/Km 7.99 min^-1 uM^-1.


substrate_name: Phthalazine

column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V, substrate Phthalazine: kcat 41.1 min^-1; Km 2.7 uM; explicit kcat/Km 15.22 min^-1 uM^-1.


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row A807V/Y885M, substrate Phthalazine: kcat 41.4 min^-1; Km 2.9 uM; explicit kcat/Km 14.28 min^-1 uM^-1.

normalized_value_unit_evidence: kcat 0.69 s^-1; Km 0.0029 mM; explicit kcat/Km 238 s^-1*mM^-1; ratio from rounded kcat/Km cells 237.931034483 s^-1*mM^-1


column_label: Table 3: Steady-state kinetic parameters of mAOX3 mutants, row K889H, substrate Phthalazine: kcat 11.8 min^-1; Km 1.1 uM; explicit kcat/Km 10.53 min^-1 uM^-1.


substrate_name: 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)


substrate_name: isovanillin (at 37 degrees Celsius and pH 7)


substrate: 6-deoxypenciclovir (at 37 degrees Celsius and pH 7)


substrate_name: famciclovir (at 37 degrees Celsius and pH 7)


enzyme_display_name: L-lactate oxidase

organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

substrate_name: (S)-lactate

assay_conditions_summary: pH 8; cofactor FMN

column_label: Table 2 row No-LOX reports L-Lactate Km (mM) = 0.039 +/- 0.007.

raw_value_unit_evidence: Km raw_value=0.039 uncertainty=+/-0.007 raw_unit=mM

row_label: No-LOX

table_label: PMC3180805 Table 2, Kinetic Parameters of Recombinant No-LOX, Cr-LOX, and At-GOX2

enzyme: L-lactate oxidase

substrate: (S)-lactate


substrate_name: glycolate

column_label: Table 2 row No-LOX reports Glycolate Km (mM) = 0.233 +/- 0.05.

raw_value_unit_evidence: Km raw_value=0.233 uncertainty=+/-0.05 raw_unit=mM

substrate: glycolate


organism: Bombyx mori

column_label: Full text reports the Lineweaver-Burk assay for IAAld and gives KM=1.4 x 10^-4 M, which normalizes to 0.14 mM.

raw_value_unit_evidence: Km raw_value=1.4 x 10^-4 M raw_unit=M

row_label: BmIAO1 activity with IAAld

table_label: Taylor full-text kinetic prose; Suppl. Figure 3 Lineweaver-Burk plot


organism: Cavia porcellus

assay_conditions_summary: pH 7; buffer pH 7

column_label: Table 5, Guinea pig liver aldehyde oxidase (N = 3-5) row, 6-Deoxypenciclovir / KM (mM) column reports 0.41 +/- 0.01 mM.

raw_value_unit_evidence: Km raw_value=0.41 +/- 0.01 raw_unit=mM; footnote 5-a=Mean +/- SD

table_label: ScienceDirect full text Table 5: Kinetic parameters for 6-oxo-metabolite formation determined by HPLC


column_label: Table 5, Guinea pig liver aldehyde oxidase (N = 3-5) row, Famciclovir / KM (mM) column reports 0.17 +/- 0.01 mM.

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

substrate: famciclovir (at 37 degrees Celsius and pH 7)


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

substrate: Phthalazine


substrate_name: Vanillin

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

substrate: Vanillin


substrate_name: purine

substrate: purine


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: pentanal

substrate: pentanal


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: phenylpropionaldehyde

substrate: phenylpropionaldehyde


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: all-trans-retinal (at 37 degrees Celsius and pH 7.4)

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


substrate_name: Butanal

proof_lines: apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C

proof_lines: apparent Kcat-value of native mAOX3, pH 7.4, 25°C

substrate: Butanal


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


substrate_name: ethyl vanillin

substrate: ethyl vanillin


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Hordeum vulgare

substrate_name: Oxalate

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

substrate: Oxalate


substrate_name: Phthalazine

substrate: Phthalazine


proof_lines:
mAOX3 wild type, pH 8.0, 37°C
wild-type, pH 8.0,37°C
wild-type, pH 8.0, 37°C


substrate_name: phenanthridine

proof_lines:
mAOX3 wild type, pH 8.0, 37°C
wild-type, pH 8.0,37°C

substrate: phenanthridine


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: purine

substrate: purine


substrate_name: pentanal


proof_lines:
wild-type, pH 8.0, 37°C
wild-type, 30°C, pH 7.4


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate: pentanal


substrate_name: allopurinol

substrate: allopurinol


enzyme_display_name: pyridoxal oxidase

organism: Drosophila melanogaster

substrate_name: pyridoxal

enzyme: pyridoxal oxidase

substrate: pyridoxal


substrate_name: Unknown

proof_lines: 37°C, pH 7.0, inhibition of 2-hydroxybenzaldehyde oxidation

substrate: Unknown


proof_lines: wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C

proof_lines: wild-type, low affinity value, pH 6.0, 37°C

proof_lines: wild-type, high affinity value, pH 6.0, 37°C


proof_lines: mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V/G1064K/I1067M, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y/I1032V, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme A1023Y, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme I1032V, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K1004Q/K1005R, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K1004Q, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K1004Q/K1005R/M1009I/V1010I, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme K1004Q/K1005R/M1009I/V1010I/R1021V/A1023Y, in 80 mM phosphate buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme A1083T/V1085A, in 80 mM phosphate buffer, pH 7.4, at 37°C


substrate_name: N-methylnicotinamide

proof_lines: electron acceptor: nitro blue tetrazolium

substrate: N-methylnicotinamide


substrate_name: hypoxanthine

substrate: hypoxanthine


substrate_name: xanthine

substrate: xanthine


substrate_name: retinalaldehyde

proof_lines: liver cytosol, pH not specified in the publication, temperature not specified in the publication

proof_lines: female enzyme treated with testosterone propionate

substrate: retinalaldehyde


substrate_name: Vanillin

substrate: Vanillin


enzyme_display_name: indole-3-acetaldehyde oxidase

organism: Avena sativa

enzyme: indole-3-acetaldehyde oxidase


enzyme_display_name: Abscisic-aldehyde oxidase

substrate_name: abscisic aldehyde

proof_lines: All these kinetic values were obtained with AO-delta dimer.

enzyme: Abscisic-aldehyde oxidase

substrate: abscisic aldehyde


enzyme_display_name: pyruvate oxidase

organism: Lactobacillus plantarum

enzyme: pyruvate oxidase


substrate_name: Phosphate

smiles: O=P(O)(O)O

proof_lines: phosphate- and oxygen-dependent pyruvate oxidase

proof_lines: oxidative conversion of pyruvate to acetyl phosphate and CO2

substrate: Phosphate


enzyme_display_name: Indole-3-acetaldehyde oxidase

substrate_name: heptaldehyde

proof_lines: Kinetic values were obtained with the AO-alpha dimer.

enzyme: Indole-3-acetaldehyde oxidase

substrate: heptaldehyde


substrate_name: protocatechualdehyde

substrate: protocatechualdehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: citral

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

substrate: citral


proof_lines: Kinetic values were obtained with the AO-gamma dimer.


substrate_name: naphthaldehyde

substrate: naphthaldehyde


organism: Mus musculus

substrate_name: retinaldehyde

substrate: retinaldehyde


substrate_name: Phthalazine

proof_lines:
wild-type, 30°C, pH 7.4
mAOX3 wild type, pH 8.0, 37°C
wild-type, pH 8.0,37°C

substrate: Phthalazine


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: methylene blue

proof_lines: as electron acceptor under aerobic conditions

substrate: methylene blue


substrate_name: diphenylsulfoxide

proof_lines: as electron acceptor under anaerobic conditions

substrate: diphenylsulfoxide


substrate_name: ferricyanide

substrate: ferricyanide


organism: Cupriavidus necator


substrate_name: NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


enzyme_display_name: cinnamoyl-CoA reductase

substrate_name: caffeoyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
recombinant fusion protein GST-AtCCR2
recombinant fusion protein GST-AtCCR1

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


substrate_name: benzoic acid (BA) (at pH7, in the presence of NAD(+))

proof_lines: kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate, 1.904 sec(-1) with indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).


substrate_name: indole-3-acetaldehyde (at pH7)

substrate: indole-3-acetaldehyde (at pH7)


substrate_name: cinnamylaldehyde (at pH7)

substrate: cinnamylaldehyde (at pH7)


organism: Zea mays

substrate_name: (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

assay_conditions_summary: pH 7.4; buffer pH 7.4

column_label: PMID 12226218 Table II row IAAld, Electron Acceptor O2, column Km (uM), value 3.2; paper abbreviation defines IAAld as indole-3-acetaldehyde; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=3.2 uM in Table II row IAAld, O2 Km column.

row_label: IAAld / indole-3-acetaldehyde

table_label: Table II. Kinetic properties of maize AO with various substrates.


substrate_name: indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Indole-3-aldehyde, Electron Acceptor O2, column Km (uM), value 4.5; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=4.5 uM in Table II row Indole-3-aldehyde, O2 Km column.


substrate_name: benzaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Benzaldehyde, Electron Acceptor O2, column Km (uM), value 1.5; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=1.5 uM in Table II row Benzaldehyde, O2 Km column.

row_label: Benzaldehyde


substrate_name: protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Protocatechualdehyde, Electron Acceptor O2, column Km (uM), value 2.9; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=2.9 uM in Table II row Protocatechualdehyde, O2 Km column.

row_label: Protocatechualdehyde


substrate_name: phenylacetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Phenylacetaldehyde, Electron Acceptor DCIP, column Km (uM), value 250; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=250 uM in Table II row Phenylacetaldehyde, DCIP Km column.

row_label: Phenylacetaldehyde


substrate_name: butyraldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Butyraldehyde, Electron Acceptor DCIP, column Km (uM), value 26; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=26 uM in Table II row Butyraldehyde, DCIP Km column.

row_label: Butyraldehyde


substrate_name: propionaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Propionaldehyde, Electron Acceptor DCIP, column Km (uM), value 74; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=74 uM in Table II row Propionaldehyde, DCIP Km column.

row_label: Propionaldehyde


substrate_name: acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Acetaldehyde, Electron Acceptor DCIP, column Km (uM), value 345; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=345 uM in Table II row Acetaldehyde, DCIP Km column.

row_label: Acetaldehyde


enzyme_display_name: salicylaldehyde dehydrogenase

organism: Pseudomonas putida

substrate_name: Salicylaldehyde

enzyme: salicylaldehyde dehydrogenase

substrate: Salicylaldehyde


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: vanillin dehydrogenase

organism: Streptomyces sp. NL15-2K

substrate_name: Vanillin

enzyme: vanillin dehydrogenase

substrate: Vanillin


substrate_name: NAD+

assay_conditions_summary: pH 9.5; cofactor NAD+


organism: Lysinibacillus sphaericus

substrate_name: NADP+


proof_lines:
with NADP+
with NAD+


assay_conditions_summary: cofactor NAD+


proof_lines: in the presence of 1 mM nitrite, at pH 6.0 and 37°C


substrate_name: NADH

assay_conditions_summary: pH 6; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: nitrite

proof_lines: in the presence of 0.1 mM NADH, at pH 6.0 and 37°C

proof_lines: in the presence of 0.05 mM 4-(dimethylamino)cinnamaldehyde, at pH 6.0 and 37°C

substrate: nitrite


organism: Thermus thermophilus

assay_conditions_summary: pH 7.4; 323.15 K; cofactor NADP+


assay_conditions_summary: pH 7.4; 323.15 K; cofactor NAD+


organism: Lathyrus oleraceus


substrate_name: D-glyceraldehyde 3-phosphate

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

substrate: D-glyceraldehyde 3-phosphate


substrate_name: clothianidin

proof_lines: nitrosoguanidine formation, pH 7.4, 37°C

substrate: clothianidin


substrate_name: nitenpyram

substrate: nitenpyram


substrate_name: imidacloprid

substrate: imidacloprid


organism: Lactiplantibacillus plantarum


substrate_name: oxygen

substrate: oxygen


substrate_name: phosphate

substrate: phosphate


organism: Arachis hypogaea


organism: Triticum aestivum

proof_lines: enzyme from leaf before treatment with alkaline phosphatase

proof_lines: enzyme from endosperm before treatment with alkaline phosphatase

proof_lines: enzyme from leaf after treatment with alkaline phosphatase


proof_lines: enzyme from leaf before or after treatment with alkaline phosphatase

proof_lines: enzyme from endosperm before or after treatment with alkaline phosphatase


organism: Hevea brasiliensis


substrate: NAD+


substrate: NADP+


organism: Streptococcus pyogenes

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.2; 301.15 K; cofactor NADP+


substrate_name: L-glutamate 5-semialdehyde

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

substrate: L-glutamate 5-semialdehyde


assay_conditions_summary: pH 7.2; 301.15 K; cofactor NAD+


enzyme_display_name: aspartate-semialdehyde dehydrogenase

organism: Arabidopsis thaliana

substrate_name: L-4-aspartyl phosphate

enzyme: aspartate-semialdehyde dehydrogenase

substrate: L-4-aspartyl phosphate


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Streptococcus pneumoniae

substrate_name: L-aspartate-semialdehyde

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

substrate: L-aspartate-semialdehyde


organism: Bos taurus


organism: Oryctolagus cuniculus


organism: Camelus dromedarius

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM tricine-NaOH; cofactor NAD+

proof_lines: in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C


assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM tricine-NaOH


enzyme_display_name: (methyl)glyoxal oxidase

organism: Thermothelomyces thermophilus

enzyme: (methyl)glyoxal oxidase


substrate_name: glycerol

smiles: OCC(O)CO

substrate: glycerol


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Pseudomonas putida


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Plasmodium falciparum

proof_lines: recombinant enzyme, pH and temperature not specified in the publication


substrate_name: NAD+


organism: Saccharomyces cerevisiae

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


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


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


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


smiles: C(C(CO)O)O


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Acrididae

substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

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

enzyme: dihydrolipoyl dehydrogenase

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


enzyme_display_name: aldehyde dehydrogenase (quinone)

organism: Cupriavidus necator

substrate_name: Butyraldehyde

smiles: CCCC=O

enzyme: aldehyde dehydrogenase (quinone)

substrate: Butyraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: abscisic-aldehyde oxidase

organism: Lathyrus oleraceus

substrate_name: abscisic aldehyde

enzyme: abscisic-aldehyde oxidase

substrate: abscisic aldehyde


organism: Sus scrofa

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Pseudomonas aeruginosa

substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


smiles: CC=O

assay_conditions_summary: pH 9


organism: Lucilia sericata

substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


organism: Geobacillus stearothermophilus

substrate_name: Pyruvate; Thiamine diphosphate

substrate: Pyruvate; Thiamine diphosphate


substrate_name: Thiamine diphosphate; Pyruvate

substrate: Thiamine diphosphate; Pyruvate


organism: Homo sapiens

substrate_name: Coenzyme A; NAD+; Pyruvate

substrate: Coenzyme A; NAD+; Pyruvate


organism: Pisum sativum

substrate_name: NAD+; Pyruvate; Coenzyme A

substrate: NAD+; Pyruvate; Coenzyme A


organism: Solanum tuberosum


substrate_name: Coenzyme A; Pyruvate; NAD+

substrate: Coenzyme A; Pyruvate; NAD+


substrate_name: Pyruvate; NAD+; Coenzyme A

substrate: Pyruvate; NAD+; Coenzyme A


organism: Corynebacterium glutamicum


organism: Rattus norvegicus


organism: Escherichia coli


substrate_name: NAD+; 4-Hydroxy-2-oxoglutarate; Coenzyme A


substrate_name: 4-Hydroxy-2-oxoglutarate; NAD+; Coenzyme A


organism: Mycobacterium tuberculosis

substrate_name: Pyruvate; Coenzyme A; NAD+

substrate: Pyruvate; Coenzyme A; NAD+


substrate_name: Coenzyme A; 2-Oxopentanoate; NAD+

substrate: Coenzyme A; 2-Oxopentanoate; NAD+


substrate_name: pyruvate

substrate: pyruvate


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Azotobacter vinelandii


substrate_name: NAD+; 4-Methylthio-2-oxobutanoate; Coenzyme A


substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


substrate_name: 2-Oxoglutarate; Coenzyme A; NAD+

substrate: 2-Oxoglutarate; Coenzyme A; NAD+


organism: Synechococcus sp. PCC 7002

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


substrate_name: alpha-Ketovaline; NAD+; Coenzyme A

substrate: alpha-Ketovaline; NAD+; Coenzyme A


substrate_name: NAD+; Coenzyme A; alpha-Ketovaline

substrate: NAD+; Coenzyme A; alpha-Ketovaline


organism: Bos taurus


substrate_name: Coenzyme A; 4-Methyl-2-oxopentanoate; NAD+


substrate_name: Coenzyme A; NAD+; alpha-Ketovaline

substrate: Coenzyme A; NAD+; alpha-Ketovaline


organism: Thauera butanivorans

smiles: CCCCO


organism: Acetobacter aceti

substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Gluconobacter sp.


organism: Gluconacetobacter diazotrophicus

substrate_name: acetic acid

smiles: CC(=O)O

substrate: acetic acid


organism: Gluconobacter oxydans


organism: Picosynechococcus sp. PCC 7002

assay_conditions_summary: pH 7


organism: Rhizorhabdus wittichii

substrate_name: Butanal

assay_conditions_summary: pH 8

substrate: Butanal


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


organism: Geobacillus stearothermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S283C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Synechocystis sp. PCC 6803

proof_lines: presence of 0.002 mM inhibitor N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide, pH 7.2, 37°C


organism: Urocitellus richardsonii

proof_lines: overall reaction, enzyme from euthermic animals, 22°C, pH 7.8

proof_lines: overall reaction, enzyme from hibernating animals, 37°C, pH 7.8

proof_lines: overall reaction, enzyme from euthermic animals, 37°C, pH 7.8


organism: Trametes cinnabarina

substrate_name: glyoxylic acid

assay_conditions_summary: pH 6

column_label: Table 2 row Glyoxylic acid; PciGLOX2 Km (mM) column = 0.1

row_label: Glyoxylic acid

table_label: Table 2

substrate: glyoxylic acid


substrate_name: methylglyoxal

column_label: Table 2 row Methylglyoxal; PciGLOX3 Km (mM) column = 0.1

row_label: Methylglyoxal

substrate: methylglyoxal


substrate_name: Glyoxal

smiles: C(=O)C=O

column_label: Table 2 row Glyoxal; PciGLOX3 Km (mM) column = 0.7

row_label: Glyoxal

substrate: Glyoxal


substrate_name: glycerol

column_label: Table 2 row Glycerol; PciGLOX3 Km (mM) column = 5.5

row_label: Glycerol

substrate: glycerol


organism: Arabidopsis thaliana

substrate_name: abscisic aldehyde

proof_lines: All these kinetic values were obtained with AO-delta dimer.

substrate: abscisic aldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

substrate_name: pyruvate

assay_conditions_summary: cofactor CoA

substrate: pyruvate


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial


enzyme_display_name: Multifunctional 2-oxoglutarate metabolism enzyme

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate alpha-ketoglutarate/2-oxoglutarate; metric Km; raw value 480 microM; normalized value 0.48 mM; Figure 1B linked as alpha-ketoglutarate Km determination.

normalized_value_unit_evidence: 480 microM normalized to 0.48 mM.

raw_value_unit_evidence: PMC HTML reports Kgd Km values for alpha-ketoglutarate, TPP, and Mg2+ as 480, 19, and 196 microM, respectively.

row_label: Rv1248c/Kgd alpha-ketoglutarate Km

table_label: PMC HTML Results prose and Figure 1B-D (PMID 16027371; PMCID PMC1180764)


substrate_name: magnesium ions

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate Mg2+/magnesium ions; metric Km; raw value 196 microM; normalized value 0.196 mM; Figure 1D linked as Mg2+ Km determination.

normalized_value_unit_evidence: 196 microM normalized to 0.196 mM.

row_label: Rv1248c/Kgd Mg2+ Km

enzyme: Multifunctional 2-oxoglutarate metabolism enzyme

substrate: magnesium ions


substrate_name: thiamine pyrophosphate

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate TPP/thiamine pyrophosphate; metric Km; raw value 19 microM; normalized value 0.019 mM; Figure 1C linked as TPP Km determination.

normalized_value_unit_evidence: 19 microM normalized to 0.019 mM.

row_label: Rv1248c/Kgd TPP Km

substrate: thiamine pyrophosphate


organism: Homo sapiens

substrate_name: alpha-Ketovaline

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.

substrate: alpha-Ketovaline


sequence_variant_note: Mutation signature S292E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S292N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S302A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial


organism: Phanerodontia chrysosporium

smiles: CC(=O)C=O


enzyme_display_name: Pyruvate dehydrogenase E1 component

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

column_label: Primary paper Figure 4 prose states that for AceE and pyruvate a Km value of 0.066 +/- 0.06 mM was derived.

raw_value_unit_evidence: Km raw_value=0.066 +/- 0.06 raw_unit=mM

row_label: AceE with pyruvate kinetic characterization

table_label: Figure 4: Dehydrogenase activities of AceE and OdhA

enzyme: Pyruvate dehydrogenase E1 component


proof_lines:
wild-type enzyme, pH 7.0, 25°C
wild-type, pH 7.0, 30°C


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: alpha-ketoglutarate

column_label: Results prose reports recombinant KGD (MSMEG_5049) with maximal ferricyanide reductase activity 1.6 s^-1 or 690 nmol min^-1 mg^-1 and Km for alpha-ketoglutarate of 540 uM (Fig. 6A).

raw_value_unit_evidence: Km raw_value=540 raw_unit=uM

row_label: Recombinant KGD (MSMEG_5049)

table_label: Results prose and Fig. 6A - Inhibition of KGD by GarA

substrate: alpha-ketoglutarate


enzyme_display_name: 2-oxoglutarate dehydrogenase E1/E2 component

column_label: Primary paper Figure 4 prose states that for OdhA and 2-oxoglutarate a Km of 0.014 +/- 0.003 mM was derived.

raw_value_unit_evidence: Km raw_value=0.014 +/- 0.003 raw_unit=mM

row_label: OdhA with 2-oxoglutarate kinetic characterization


proof_lines: recombinant wild-type component E1b, pH 7.5, 22°C

proof_lines: recombinant wild-type E1b component, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant Y300Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant R287Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant R301Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutants R301Aalpha and D295Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant D295Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant Y300Falpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutants R301Aalpha and Y300Falpha, pH 7.5, 22°C


organism: Escherichia coli

substrate_name: E2p lipoyl domain

substrate: E2p lipoyl domain


organism: Azotobacter vinelandii

substrate_name: lipoyl domain

proof_lines: acyl group transfer reaction, recombinant wild-type pyruvate dehydrogenase

substrate: lipoyl domain


mutation_signature: recombinant pyruvate dehydrogenase with N-terminal deletion acyl group transfer reaction / recombinant pyruvate dehydrogenase with N-terminal deletion

mutation_type: deletion

proof_lines: acyl group transfer reaction, recombinant pyruvate dehydrogenase with N-terminal deletion


proof_lines: recombinant wild-type pyruvate dehydrogenase


mutation_signature: recombinant pyruvate dehydrogenase with N-terminal deletion recombinant pyruvate dehydrogenase with N-terminal deletion


proof_lines: mutant enzyme H407A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K403E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme E401K, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K410E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme N404A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme E401A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K403A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K410A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme Q408A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K411E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K411A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: wild type enzyme, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: recombinant E1b component mutant H291Qalpha, pH 7.5, 22°C


proof_lines: recombinant E1b component mutant H291Aalpha, pH 7.5, 22°C


proof_lines: recombinant E1b component mutant H291Nalpha, pH 7.5, 22°C


substrate_name: 2-oxo-5-hexenoic acid

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

substrate: 2-oxo-5-hexenoic acid


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


proof_lines: mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication


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


organism: Pseudomonas putida


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


organism: Rattus norvegicus

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


substrate_name: NAD+

substrate: NAD+


substrate_name: Unknown

substrate: Unknown


substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: L-2-aminoadipate 6-semialdehyde

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

substrate: L-2-aminoadipate 6-semialdehyde


organism: Sus scrofa


enzyme_display_name: retinal dehydrogenase

enzyme: retinal dehydrogenase


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Gallus gallus

substrate_name: retinal

substrate: retinal


proof_lines:
isoform RALDH2, at pH 8.2 and 25°C
isoform RALDH3, at pH 8.2 and 25°C
isoform RALDH1, at pH 8.2 and 25°C


enzyme_display_name: formaldehyde dehydrogenase

substrate_name: formaldehyde

proof_lines: enzyme immobilized on MPS-4, pH 7.0, 22?

proof_lines: enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22?

proof_lines: enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22?

enzyme: formaldehyde dehydrogenase

substrate: formaldehyde


substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


proof_lines: with feruloyl-CoA as substrate, noncompetitive inhibition

proof_lines: with sinapoyl-CoA as substrate, noncompetitive inhibition

proof_lines: with feruloyl-CoA as substrate, uncompetitive inhibition


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


enzyme_display_name: phenylacetaldehyde dehydrogenase

enzyme: phenylacetaldehyde dehydrogenase


organism: Pseudomonas sp.

substrate_name: formate

proof_lines: with reduced methyl viologen as cosubstrate, pH and temperature not specified in the publication

substrate: formate


enzyme_display_name: long-chain acyl-protein thioester reductase

organism: Photobacterium phosphoreum

substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


substrate_name: NADPH

enzyme: long-chain acyl-protein thioester reductase

substrate: NADPH


enzyme_display_name: coniferyl-aldehyde dehydrogenase

substrate_name: coniferyl aldehyde

enzyme: coniferyl-aldehyde dehydrogenase

substrate: coniferyl aldehyde


proof_lines: wild-type enzyme and mutant enzyme D297A


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Acinetobacter baumannii

substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 8.5; 295.15 K; buffer 100 mM sodium phosphate

proof_lines: in 100 mM sodium phosphate buffer, pH 8.0, 30°C


assay_conditions_summary: pH 8.5; 295.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 294.15 K; cofactor NAD+

proof_lines: overall reaction of bifunctional enzyme, pH 7.5, 21°C


enzyme_display_name: glutamyl-tRNA reductase

substrate_name: L-glutamyl-tRNAGlu

enzyme: glutamyl-tRNA reductase

substrate: L-glutamyl-tRNAGlu


assay_conditions_summary: pH 8.1; 310.15 K; cofactor NADPH


enzyme_display_name: aldehyde oxidase

organism: Mesocricetus auratus

enzyme: aldehyde oxidase


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Escherichia coli K-12


assay_conditions_summary: pH 9; 310.15 K; cofactor NADP+


organism: Oryctolagus cuniculus

substrate_name: cinchonidine

assay_conditions_summary: pH 7.4; 310.15 K; buffer 80 mM phosphate

proof_lines: wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C

substrate: cinchonidine


enzyme_display_name: pyruvate oxidase

organism: Lactobacillus delbrueckii

substrate_name: pyruvate

proof_lines: presence of phosphatidylethanolamine, pH 5.6, 25°C

enzyme: pyruvate oxidase

substrate: pyruvate


substrate_name: phosphate

substrate: phosphate


organism: Lactiplantibacillus plantarum


substrate_name: Unknown

substrate: Unknown


organism: Mus musculus

proof_lines: apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C

proof_lines: apparent Kcat-value of native mAOX3, pH 7.4, 25°C


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Homo sapiens

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

proof_lines:
enzyme-specific activity, pH 7.5, 37°C
overall-assay, pH 7.5, 37°C


proof_lines:
enzyme-specific activity, pH 7.5, 37°C
overall-assay, pH 7.5, 37°C
at pH 7.0 and 37°C


organism: Bos taurus


proof_lines: preparation from liver, low affinity state, pH 7, temperature not specified in the publication

proof_lines: preparation from liver, pH 7, temperature not specified in the publication

proof_lines: preparation from heart, pH 7, temperature not specified in the publication


proof_lines: enzyme from liver, at pH 7.0, temperature not specified in the publication

proof_lines: enzyme from heart, at pH 7.0, temperature not specified in the publication


organism: Brassica oleracea


substrate_name: alpha-ketoisovaleric acid

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

substrate: alpha-ketoisovaleric acid


enzyme_display_name: pyruvate dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: ferricyanide

proof_lines: without activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication

proof_lines: with activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication

enzyme: pyruvate dehydrogenase (quinone)

substrate: ferricyanide


proof_lines: pH and temperature not specified in the publication


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: acetaldehyde

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris/HCl

proof_lines: at 25°C in 50 mM Tris/HCl buffer, pH 8.0

substrate: acetaldehyde


organism: Arabidopsis thaliana


enzyme_display_name: 2-oxoglutarate synthase

organism: Sulfolobus sp.

enzyme: 2-oxoglutarate synthase


proof_lines:
80°C, pH 7.5, natural enzyme
80°C, pH 7.5, recombinant enzyme


enzyme_display_name: pyruvate synthase (ferredoxin)

organism: Chlamydomonas reinhardtii

substrate_name: oxidized ferredoxin 2

assay_conditions_summary: pH 7; 298.15 K; buffer 25 mM potassium phosphate

proof_lines: in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25°C

proof_lines: in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication

enzyme: pyruvate synthase (ferredoxin)

substrate: oxidized ferredoxin 2


substrate_name: CoA

assay_conditions_summary: pH 7; 298.15 K; buffer 25 mM potassium phosphate; cofactor CoA

substrate: CoA


assay_conditions_summary: pH 6.8; 298.15 K; buffer 100 mM potassium phosphate


organism: Caldicellulosiruptor bescii

substrate_name: oxidized ferredoxin

substrate: oxidized ferredoxin


substrate_name: glyceraldehyde 3-phosphate

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

substrate: glyceraldehyde 3-phosphate


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Aromatoleum aromaticum

assay_conditions_summary: pH 8; 301.15 K; cofactor NAD+

proof_lines: native enzyme, pH 8.0, 28°C, with oxidized benzyl viologen

enzyme: aldehyde ferredoxin oxidoreductase


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


proof_lines: native enzyme, pH 8.0, 28°C, with benzaldehyde


substrate_name: Oxidized benzyl viologen

substrate: Oxidized benzyl viologen


organism: Magnetococcus marinus

substrate_name: succinyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: wild-type, pH 7.0, temperature not specified in the publication

substrate: succinyl-CoA


substrate_name: reduced ferredoxin

assay_conditions_summary: pH 7

substrate: reduced ferredoxin


proof_lines: mutant E45Q, pH 7.5, temperature not specified in the publication


proof_lines: wild-type, pH 7.5, temperature not specified in the publication

proof_lines: wild-type, pH 8.5, temperature not specified in the publication


proof_lines: mutant Y436F, pH 7.5, temperature not specified in the publication


organism: Aeropyrum pernix

substrate_name: pyruvate

substrate: pyruvate


organism: Citrobacter sp.

proof_lines: enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA