organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.2; 301.15 K; cofactor NAD+

column_label: PMC full-text Table 3 row gammaGS under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 gammaGS row reports Km 72 uM, kcat 7 s^-1, kcat/Km 0.097 s^-1 uM^-1.

row_label: gammaGS

table_label: PMC Table 3, recombinant TcP5CDH-His6 kinetic parameters


substrate_name: NAD+

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

assay_conditions_summary: pH 7.2; 301.15 K; cofactor NADP+

column_label: PMC full-text Table 3 row NAD+ under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 NAD+ row reports Km 72.3 uM, kcat 7.5 s^-1, kcat/Km 0.103 s^-1 uM^-1.

row_label: NAD+

data_origin: experimental

substrate: NAD+

status: corrected

source: oed


substrate_name: NADP+

column_label: PMC full-text Table 3 row NADP+ under the recombinant TcP5CDH-His6 columns Km, kcat, and kcat/Km.

raw_value_unit_evidence: TcP5CDH-His6 NADP+ row reports Km 342 uM, kcat 1.2 s^-1, kcat/Km 0.003 s^-1 uM^-1.

row_label: NADP+

substrate: NADP+


organism: Homo sapiens

verification_status: unverified

kcat_over_km_origin: calculated

status: unverified


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S352A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 293.15 K; cofactor NAD+


substrate_name: NAD

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

assay_conditions_summary: cofactor NAD+

column_label: PMID 22516612 / PMC3372638 Results prose linked to Table S1; human wild-type ALDH4A1; NAD+ Km 100 uM.

normalized_value_unit_evidence: Human wild-type ALDH4A1 NAD+ Km normalized_value=0.1 normalized_unit=mM.

raw_value_unit_evidence: Human wild-type ALDH4A1; NAD+ Km raw_value=100 raw_unit=uM.

row_label: Human wild-type ALDH4A1, NAD+

substrate: NAD

status: verified

source: uniprot


organism: Thermus thermophilus

substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


enzyme_display_name: Malonyl CoA reductase (NADP)

organism: Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2)

substrate_name: malonyl-CoA (with 0.5 mM NADP)

assay_conditions_summary: cofactor NADPH

column_label: Full-text organism-specific properties paragraph reports M. sedula malonyl-CoA apparent Km 0.1 mM

raw_value_unit_evidence: Km raw_value=0.1 raw_unit=mM

row_label: Metallosphaera sedula partially purified native malonyl-CoA reductase

table_label: PMID 17041055 PMC full text

enzyme: Malonyl CoA reductase (NADP)

substrate: malonyl-CoA (with 0.5 mM NADP)


enzyme_display_name: Fatty acyl-CoA reductase 2, chloroplastic

organism: Arabidopsis thaliana

substrate_name: hexadecanoyl-CoA (at pH 7 and 30 degrees Celsius)

assay_conditions_summary: pH 7; buffer 100 mM potassium phosphate; cofactor CoA

column_label: Results prose under 'Kinetics of AtFAR2 utilizing C16:0-CoA and the effect of BSA on the enzyme activity' reports AtFAR2 had a Km value of 5.31 uM for C16:0-CoA; Figure 4A is the corresponding kinetics plot.

raw_value_unit_evidence: Km raw_value=5.31 raw_unit=uM

row_label: AtFAR2 / C16:0-CoA / hexadecanoyl-CoA

table_label: Figure 4A and Results prose: Kinetics of AtFAR2 utilizing C16:0-CoA


organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805)

substrate_name: oleoyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
alkane biosynthesis pathway
acyl-acyl carrier protein reductase
aldehyde decarbonylase

substrate: oleoyl-CoA


organism: Streptococcus pyogenes

substrate_name: succinate semialdehyde

smiles: O=CCCC(=O)O

proof_lines: complete uncompetitive substrate inhibition

substrate: succinate semialdehyde


source_db: brenda

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

proof_lines:
rat liver mitochondria
P5C dehydrogenase

source: brenda


organism: Mycobacterium tuberculosis

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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADP+

proof_lines: in the absence of Mg2+, at pH 7.5 and 37°C


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

proof_lines: with NADP+ as cosubstrate, in the absence of Mg2+, at pH 7.5 and 37°C

proof_lines: with NADP+ as cosubstrate, in the presence of 10 mM Mg2+, at pH 7.5 and 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+

proof_lines: in the presence of 10 mM Mg2+, at pH 7.5 and 37°C


proof_lines: steady-state parameter, 50 microM NADP+, at pH 7.5 and 37°C

proof_lines: steady-state parameter, 50 microM NADP+ and 10 mM Mg2+, at pH 7.5 and 37°C


substrate_name: Succinic semialdehyde

proof_lines: steady-state parameter, 200 microM succinic semialdehyde, at pH 7.5 and 37°C

proof_lines: steady-state parameter, 200 microM succinic semialdehyde and 10 mM Mg2+, at pH 7.5 and 37°C

proof_lines: partial substrate inhibition, pH 7.5 and 37°C

substrate: Succinic semialdehyde


organism: Klebsiella pneumoniae

assay_conditions_summary: pH 7.8; 303.15 K; cofactor NAD+


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADP+


enzyme_display_name: UniProt O57693

organism: Thermoproteus tenax

source_db: skid

source_license: CC BY-NC-ND 4.0

proof_lines:
Raw SKiD Env: Temp=45°C, pH=7
Raw SKiD Env: Temp=70°C, pH=7

enzyme: UniProt O57693

source: skid


substrate_name: D-glyceraldehyde 3-phosphate

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

proof_lines:
Raw SKiD Env: Temp=70°C, pH=7
Raw SKiD Env: Temp=45°C, pH=7

substrate: D-glyceraldehyde 3-phosphate


organism: Synechocystis sp. PCC 6803


organism: Trypanosoma brucei

substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
cytosolic enzyme
glyoxysomal enzyme

substrate: NADH


substrate_name: 3-phospho-D-glyceroyl phosphate

proof_lines:
glyoxysomal enzyme
cytosolic enzyme

substrate: 3-phospho-D-glyceroyl phosphate


organism: Escherichia coli

substrate_name: 2-oxoglutarate semialdehyde

substrate: 2-oxoglutarate semialdehyde


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NAD+


km_display: Not reported

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+


organism: Pseudomonas putida

proof_lines: apparent value, in 100 mM Tris-HCl, pH 8.5, at 25°C


proof_lines: apparent value, in 100 mM glycine-NaOH (pH 9.2), at 25°C


assay_conditions_summary: pH 9.2; 298.15 K; cofactor NAD+

proof_lines: apparent value, in the presence of benzaldehyde, 100 mM glycine-NaOH (pH 9.2), at 25°C


substrate_name: benzaldehyde

proof_lines: in 100 mM glycine-NaOH (pH 9.2), at 25°C

substrate: benzaldehyde


organism: Saccharomyces cerevisiae


enzyme_display_name: D-glyceraldehyde dehydrogenase (NADP+)

organism: Picrophilus oshimae

substrate_name: D-glyceraldehyde

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

enzyme: D-glyceraldehyde dehydrogenase (NADP+)

substrate: D-glyceraldehyde


assay_conditions_summary: pH 6.9; 331.15 K; cofactor NADP+


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: glycolaldehyde

smiles: C(C=O)O

substrate: glycolaldehyde


organism: Vibrio variabilis

sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature L249A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 313.15 K; cofactor NADP+

row_label: L249A / L-AHG columns

table_label: Table 2. Kinetic parameters of VvAHGD and its mutants against NADP+ and L-AHG


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S176A to reconstruct the assayed variant sequence.

column_label: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 mM^-1 s^-1.

normalized_value_unit_evidence: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 s^-1 mM^-1.

row_label: S176A / L-AHG columns


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S227A to reconstruct the assayed variant sequence.

row_label: S227A / L-AHG columns


sequence_variant_note: Resolved canonical sequence from rcsb_polymer_entity_6J75_1 and applied mutation signature S233A to reconstruct the assayed variant sequence.

row_label: S233A / L-AHG columns


assay_conditions_summary: pH 7; 313.15 K; buffer triplicate in 20 mM Tris-HCl; cofactor NADP+

column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / L-AHG

normalized_value_unit_evidence: Normalized evidence: kcat=58.29 s^-1; km=1.2 mM.

raw_value_unit_evidence: Kinetic parameters of VvAHGD and its mutants against the cofactor NADP+ and the substrate L-AHG; row Wild Type / L-AHG; Km 1.2 mM; kcat 58.29 s^-1; kcat/Km 48.58 mM^-1 s^-1. To measure kinetic parameters against L-AHG, reactions were conducted in triplicate in 20 mM Tris-HCl buffer (pH 7.0) using L-AHG over 0-4.4 mM and NADP+ fixed at 1.5 mM.

row_label: Wild Type / L-AHG


substrate_name: NADP+

row_label: L249A / NADP+ columns


row_label: S176A / NADP+ columns


row_label: S227A / NADP+ columns


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S233A to reconstruct the assayed variant sequence.


organism: Nitrosomonas europaea

substrate_name: L-Glyceraldehyde 3-phosphate

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADP+

proof_lines: pH 8.5, 30°C, recombinant enzyme, with NADP+

proof_lines: pH 8.5, 30°C, recombinant enzyme, with NAD+

substrate: L-Glyceraldehyde 3-phosphate


proof_lines: pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: NAD+


enzyme_display_name: farnesal dehydrogenase

organism: Persicaria minor

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

assay_conditions_summary: pH 9.5; 308.15 K; cofactor NAD+

enzyme: farnesal dehydrogenase


substrate_name: citral

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

substrate: citral


substrate_name: trans-cinnamaldehyde

substrate: trans-cinnamaldehyde


substrate_name: alpha-methyl-cinnamaldehyde

substrate: alpha-methyl-cinnamaldehyde


enzyme_display_name: Aldehyde dehydrogenase family 3 member A2

organism: Homo sapiens

substrate_name: hexanal

smiles: CCCCCC=O

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

substrate: hexanal


substrate_name: octanal

smiles: CCCCCCCC=O

enzyme: Aldehyde dehydrogenase family 3 member A2

substrate: octanal


substrate_name: decanal

smiles: CCCCCCCCCC=O

substrate: decanal


substrate_name: dodecanal

smiles: CCCCCCCCCCCC=O

substrate: dodecanal


substrate_name: tetradecanal

smiles: CCCCCCCCCCCCCC=O

substrate: tetradecanal


substrate_name: octadecanal

smiles: CCCCCCCCCCCCCCCCCC=O

substrate: octadecanal


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


organism: Thermoplasma acidophilum

assay_conditions_summary: pH 7; cofactor NAD+

proof_lines:
wild-type, pH 7.0, 50°C
wild type enzyme, at pH 7.0 and 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F34M/Y399C/S405N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F34M/Y399C/S405N, at pH 7.0 and 50°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F34M/S405N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F34M/S405N, at pH 7.0 and 50°C


assay_conditions_summary: pH 7; cofactor NADP+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S176A to reconstruct the assayed variant sequence.

raw_value_unit_evidence: Table 2 row S176A, L-AHG columns: Km 1.45 ± 0.11 mM; kcat 10.67 ± 0.68 s^-1; kcat/Km 7.36 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S227A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L249A to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; buffer triplicate in 20 mM Tris-HCl; cofactor NADP+

column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / L-AHG; kcat_over_km paper=48.58 s^-1 mM^-1; export=48.575 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=58.29 s^-1; km=1.2 mM; kcat_over_km=48.58 s^-1 mM^-1.


column_label: Journal of Molecular Biology 2020 Table 2, row label Wild Type / NADP+; kcat_over_km paper=209.36 s^-1 mM^-1; export=209.36363636363637 s^-1 mM^-1.

normalized_value_unit_evidence: Normalized evidence: kcat=69.09 s^-1; km=0.33 mM; kcat_over_km=209.36 s^-1 mM^-1.

raw_value_unit_evidence: Kinetic parameters of VvAHGD and its mutants against the cofactor NADP+ and the substrate L-AHG; row Wild Type / NADP+; Km 0.33 mM; kcat 69.09 s^-1; kcat/Km 209.36 mM^-1 s^-1. To measure kinetic parameters against NADP+, reactions were conducted in triplicate in 20 mM Tris-HCl buffer (pH 7.0) using NADP+ over 0-4.8 mM and L-AHG fixed at 3.52 mM.

row_label: Wild Type / NADP+


row_label: S233A / NADP+ columns


organism: Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828 / KAW 2/3)

substrate_name: glyceraldehyde (at pH 6.9 and 58 degrees Celsius)

proof_lines: kcat is 10 sec(-1) with glyceraldehyde as substrate, 12 sec(-1) with glyceraldehyde-3-phosphate as substrate, 20 sec(-1) with glycolaldehyde as substrate and 10 sec(-1) with NADP as substrate (at pH 6.9 and 58 degrees Celsius).


substrate_name: glyceraldehyde-3-phosphate (at pH 6.9 and 58 degrees Celsius)


substrate_name: glycolaldehyde (at pH 6.9 and 58 degrees Celsius)


substrate_name: NADP (at pH 6.9 and 58 degrees Celsius)

substrate: NADP (at pH 6.9 and 58 degrees Celsius)


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: glyceraldehyde-3-phosphate (at pH 7.9 and 58 degrees Celsius)

proof_lines: kcat is 26 sec(-1) with glyceraldehyde as substrate, 20 sec(-1) with glyceraldehyde-3-phosphate as substrate, 37 sec(-1) with glycolaldehyde as substrate and 25 sec(-1) with NADP as substrate (at pH 7.9 and 58 degrees Celsius).


enzyme_display_name: Vanillin dehydrogenase

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

substrate_name: vanillin in the presence of 0.5 mM NAD(+) (at pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 21.03 sec(-1) with vanillin as substrate in the presence of 0.5 mM NAD(+). kcat is 23.42 sec(-1) with 3,4-dihydroxybenzaldehyde as substrate in the presence of 0.5 mM NAD(+). kcat is 22.92 sec(-1) with 4-hydroxybenzaldehyde as subst

enzyme: Vanillin dehydrogenase


substrate_name: 3,4-dihydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: 4-hydroxybenzaldehyde in the presence of 0.5 mM NAD(+) (at pH 7.0)


substrate_name: NAD(+) in the presence of 1 mM vanillin

substrate: NAD(+) in the presence of 1 mM vanillin


substrate_name: NADP(+) in the presence of 1 mM vanillin


substrate_name: NAD (with G1P as effector)

sequence_variant_note: Mutation signature G1P/F6P could not be applied safely because the resolved sequence does not match the expected reference residue(s).

assay_conditions_summary: cofactor ADP

proof_lines: Km applies to a data set exhibiting Michaelis-Menten kinetics. When an enzyme does not exhibit Michaelis-Menten kinetics the binding affinity is simply expressed as S0.5 which corresponds to the observed substrate concentration for 0.5 x Vm

substrate: NAD (with G1P as effector)


substrate_name: D-glyceraldehyde

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N286H to reconstruct the assayed variant sequence.

substrate: D-glyceraldehyde


substrate_name: NADP+

sequence_source: multiple

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: pH and temperature not specified in the publication

source_databases_merged: brenda uniprot

substrate: NADP+


substrate_name: hexadecanal

smiles: CCCCCCCCCCCCCCCC=O

substrate: hexadecanal


substrate_name: farnesal

substrate: farnesal


substrate_name: D-glycerate

assay_conditions_summary: pH 6.9; cofactor NADP+

substrate: D-glycerate


column_label: Table 2 row Glyceraldehyde, T. acidophilum column: Km 0.2 mM; Kcat 26 s^-1; Kcat/Km 130 s^-1 mM^-1. Table 2 lines 195, 201, and 207: Glyceraldehyde row reports Km 0.2 mM, Kcat 26 s^-1, and Kcat/Km 130 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 0.2 mM; kcat 26 s^-1; kcat_over_km 130 s^-1*mM^-1

row_label: Glyceraldehyde, T. acidophilum column

table_label: Table 2


substrate_name: glycolaldehyde

smiles: O=CCO

column_label: Table 2 row Glycolaldehyde, T. acidophilum column: Km 12.3 mM; Kcat 37 s^-1; Kcat/Km 3 s^-1 mM^-1. Table 2 lines 197, 203, and 209: Glycolaldehyde row reports Km 12.3 mM, Kcat 37 s^-1, and Kcat/Km 3 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 12.3 mM; kcat 37 s^-1; kcat_over_km 3 s^-1*mM^-1

row_label: Glycolaldehyde, T. acidophilum column

substrate: glycolaldehyde


column_label: Table 2 row NADP+, T. acidophilum column: Km 0.36 mM; Kcat 25 s^-1; Kcat/Km 70 s^-1 mM^-1. Table 2 lines 198, 204, and 210: NADP+ row reports Km 0.36 mM, Kcat 25 s^-1, and Kcat/Km 70 s^-1 mM^-1 under T. acidophilum.

normalized_value_unit_evidence: km 0.36 mM; kcat 25 s^-1; kcat_over_km 70 s^-1*mM^-1

row_label: NADP+, T. acidophilum column


substrate_name: D-Glycerate

substrate: D-Glycerate


enzyme_display_name: L-2-aminoadipate reductase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

enzyme: L-2-aminoadipate reductase

substrate: NADPH


substrate_name: D-glyceraldehyde 3-phosphate

column_label: Table 3 row D-Ga3P reports kcat 1.0 +/- 0.2 min^-1, Km 2.20 +/- 0.10 mM, and kcat/Km 8 M^-1 s^-1

raw_value_unit_evidence: Table 3 D-Ga3P row in the D-Ga3P/NAD+ block: kcat 1.0 +/- 0.2 min^-1; Km 2.20 +/- 0.10 mM; kcat/Km 8 M^-1 s^-1

table_label: Table 3

substrate: D-glyceraldehyde 3-phosphate


substrate_name: L-Glyceraldehyde 3-phosphate

substrate: L-Glyceraldehyde 3-phosphate


substrate_name: NAD+

column_label: Table 3 row NAD+ reports kcat 1.0 +/- 0.2 min^-1, Km 0.40 +/- 0.03 mM, and kcat/Km 50 M^-1 s^-1

raw_value_unit_evidence: Table 3 NAD+ row in the D-Ga3P/NAD+ block: kcat 1.0 +/- 0.2 min^-1; Km 0.40 +/- 0.03 mM; kcat/Km 50 M^-1 s^-1

row_label: NAD+

substrate: NAD+


column_label: Table 3 row NADP+ reports kcat 0.80 +/- 0.01 min^-1, Km 0.23 +/- 0.01 mM, and kcat/Km 56 M^-1 s^-1

raw_value_unit_evidence: Table 3 NADP+ row in the D-Ga3P/NADP+ block: kcat 0.80 +/- 0.01 min^-1; Km 0.23 +/- 0.01 mM; kcat/Km 56 M^-1 s^-1

row_label: NADP+


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: with NAD+ as cosubstrate, at pH 8.0 and 30°C

proof_lines: with NADP+ as cosubstrate, at pH 8.0 and 30°C


organism: Picrophilus torridus

column_label: Table 2 row Glyceraldehyde, P. torridus column: Km 0.06 mM; Kcat 10 s^-1; Kcat/Km 167 s^-1 mM^-1. Table 2 lines 194-207: Glyceraldehyde row reports Km 0.06 mM, Kcat 10 s^-1, and Kcat/Km 167 s^-1 mM^-1 under P. torridus.

row_label: Glyceraldehyde, P. torridus column


column_label: Table 2 row Glycolaldehyde, P. torridus column: Km 11.1 mM; Kcat 20 s^-1; Kcat/Km 1.8 s^-1 mM^-1. Table 2 lines 197, 203, and 209: Glycolaldehyde row reports Km 11.1 mM, Kcat 20 s^-1, and Kcat/Km 1.8 s^-1 mM^-1 under P. torridus.

row_label: Glycolaldehyde, P. torridus column


column_label: Table 2 row NADP+, P. torridus column: Km 0.42 mM; Kcat 10 s^-1; Kcat/Km 24 s^-1 mM^-1. Table 2 lines 198, 204, and 210: NADP+ row reports Km 0.42 mM, Kcat 10 s^-1, and Kcat/Km 24 s^-1 mM^-1 under P. torridus.

normalized_value_unit_evidence: km 0.42 mM; kcat 10 s^-1; kcat_over_km 24 s^-1*mM^-1

row_label: NADP+, P. torridus column


proof_lines:
glyceraldehyde-3-phosphate
glycolaldehyde
glyceraldehyde dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F34M/S405N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 323.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F34M/Y399C/S405N to reconstruct the assayed variant sequence.


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

column_label: PDF page 6 Table 4 row Wildtype reports Km NAD+ = 22.7 mM, kcat NAD+ = 1.64 s^-1, and rounded kcat/Km NAD+ = 0.07 s^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized_value=1.64 normalized_unit=s^-1; Km normalized_value=22.7 normalized_unit=mM; kcat/Km table_normalized_value=0.07 normalized_unit=s^-1 mM^-1; CatLog computed ratio=0.0722466960352423.

row_label: Wildtype

table_label: Table 4: Cofactor Km- and kcat-values of key TaAlDH variants


proof_lines: Saccharomyces cerevisiae aminoadipate reductase


substrate_name: S-Carboxymethyl-L-cysteine

substrate: S-Carboxymethyl-L-cysteine


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: NADP (at 70 degrees Celsius)

column_label: Results prose states that S. solfataricus GAPN follows Michaelis-Menten kinetics for NADP+ and gives K_m 0.099 +/- 0.009 mM.

raw_value_unit_evidence: Km raw_value=0.099 +/- 0.009 raw_unit=mM

row_label: S. solfataricus GAPN / NADP+ Km

table_label: PMC full text PMID 15869466 S. solfataricus GAPN kinetic prose

substrate: NADP (at 70 degrees Celsius)


substrate_name: alpha-aminoadipate semialdehyde

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

substrate: alpha-aminoadipate semialdehyde


substrate_name: adipate

substrate: adipate


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


substrate_name: S-carboxymethyl-L-cysteine

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

substrate: S-carboxymethyl-L-cysteine


assay_conditions_summary: pH 8.8; 310.15 K; cofactor NADPH


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Pseudomonas sp.

substrate_name: Glutaric semialdehyde

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

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: Glutaric semialdehyde


assay_conditions_summary: cofactor NADP+


assay_conditions_summary: cofactor NAD+


enzyme_display_name: UniProt P0AFG8

substrate_name: thiamine diphosphate

enzyme: UniProt P0AFG8

substrate: thiamine diphosphate


substrate_name: pyruvate

substrate: pyruvate


organism: Pseudomonas aeruginosa


smiles: C(CS)O


substrate_name: propanal

smiles: CCC=O

substrate: propanal


organism: Escherichia coli

substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


organism: Vibrio sp. EJY3

assay_conditions_summary: pH 8

proof_lines:
VejAHGD
Km
pH 8.0


enzyme_display_name: retinal dehydrogenase

organism: Rattus norvegicus

substrate_name: benzaldehyde

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

enzyme: retinal dehydrogenase

substrate: benzaldehyde


substrate_name: octanal

substrate: octanal


proof_lines: microsomes, high-fate diet rats, pH and temperature not specified in the publication

proof_lines: microsomes, control rats, pH and temperature not specified in the publication


enzyme_display_name: Bifunctional protein PaaZ

organism: Escherichia coli (strain K12)

substrate_name: oxepin-CoA (at 22 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor CoA

proof_lines:
PaaZ
oxepin-CoA
hydrolytic ring cleavage

enzyme: Bifunctional protein PaaZ


substrate_name: malonate semialdehyde

substrate: malonate semialdehyde


substrate_name: CoA

assay_conditions_summary: cofactor CoA

substrate: CoA


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


enzyme_display_name: pyruvate dehydrogenase system

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

proof_lines: mutant Y177A, Hill coefficient 1.0, pH 7.0, 30°C

enzyme: pyruvate dehydrogenase system


proof_lines: wild-type, Hill coefficient 1.38, pH 7.0, 30°C


enzyme_display_name: glutamate-5-semialdehyde dehydrogenase

substrate_name: NADP+

enzyme: glutamate-5-semialdehyde dehydrogenase

substrate: NADP+


substrate_name: phosphate

substrate: phosphate


substrate_name: NADPH

substrate: NADPH


organism: Sus scrofa

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


smiles: CC(=O)SCCNC(=O)CCNC(=O)[O-]

assay_conditions_summary: pH 7.5; cofactor CoA

proof_lines: domestic pig, pH 7.5, temperature not specified in the publication


substrate_name: NAD+

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: NAD+


organism: Klebsiella pneumoniae

smiles: C(CO)C=O

assay_conditions_summary: pH 8; 318.15 K; cofactor NAD+


substrate_name: Isovaleraldehyde

smiles: CC(C)CC=O

substrate: Isovaleraldehyde


substrate_name: Valeraldehyde

smiles: CCCCC=O

substrate: Valeraldehyde


substrate_name: Butyraldehyde

smiles: CCCC=O

substrate: Butyraldehyde


proof_lines: pH 7.0, 37°C, mutant S271E of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S203A of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S271A of isoform PDH2


proof_lines: pH 7.0, 37°C, mutant S203E of isoform PDH2


organism: Ascaris suum

assay_conditions_summary: pH 7.4; 303.15 K; cofactor CoA


assay_conditions_summary: pH 7.4; 303.15 K; cofactor NAD+


organism: Lathyrus oleraceus

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


assay_conditions_summary: pH 7.6; 295.15 K; cofactor NAD+


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


organism: Arthrobacter sp. Cr-7

substrate_name: Isopyridoxal

substrate: Isopyridoxal


assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


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

organism: Pseudomonas sp. MA-1

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: pH 8.0, temperature not specified in the publication


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


organism: Solanum tuberosum

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA


substrate_name: pyruvate


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+


organism: Ricinus communis

substrate_name: coenzyme A

substrate: coenzyme A


substrate: pyruvate


organism: Bacillus subtilis

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


organism: Bos taurus

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Mn2+

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate, in presence of 2 mM Ca2+

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate, in presence of 2 mM Mn2+


proof_lines: pH 7.6, 30°C, overall reaction of complex


organism: Lactococcus lactis subsp. lactis

substrate_name: hydroxyethyl thiamine diphosphate

substrate: hydroxyethyl thiamine diphosphate


proof_lines: the complex displays cooperativity, Hill coefficient is 0.7, pH not specified in the publication, temperature not specified in the publication


assay_conditions_summary: pH 7.6; 303.15 K; cofactor CoA

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in presence of thiamine diphosphate

proof_lines: 2-oxoglutarate dehydrogenase complex, pH 7.6, 30°C, in absence of thiamine diphosphate


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NAD+


organism: Brassica oleracea


organism: Hordeum vulgare

assay_conditions_summary: pH 7.6; cofactor CoA

proof_lines: absence of malate, pH 7.6, temperature not specified in the publication

proof_lines: presence of 1 mM malate, pH 7.6, temperature not specified in the publication


assay_conditions_summary: pH 7.6; cofactor NAD+


organism: Escherichia coli

protein_accession_database: NCBI Protein

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

assay_conditions_summary: pH 8; 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.


assay_conditions_summary: pH 8; cofactor NADP+

proof_lines:
pH 8.0, 37°C, cofactor: NADP+
pH 8.0, 37°C, cofactor: NAD+


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

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: propionaldehyde

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


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+


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+


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+


organism: Mammalia

proof_lines: pyruvate dehydrogenase preparation with high activity


organism: Homo sapiens

proof_lines:
E1 component, pH 7.6, 30°C
pH 7.0, 37°C, isoform PDH2
pH 7.0, 37°C, isoform PDH1


organism: [Bacillus] caldolyticus


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


organism: Salmonella enterica subsp. enterica serovar Typhimurium

proof_lines: cooperativity is observed, Hill coefficient is 1.6, pH 7.6, 37°C


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


substrate_name: acetylphosphinate

substrate: acetylphosphinate


organism: Rhodospirillum rubrum

substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Pigeon


organism: Sus scrofa

proof_lines: domestic pig, pH 7.5, temperature not specified in the publication


organism: Dictyostelium discoideum


organism: Neurospora crassa

proof_lines:
similar values
pH 7.4, 30°C


substrate_name: lipoyl domain

proof_lines:
assay with whole enzyme complex
pH 8.0, 30°C

substrate: lipoyl domain


organism: Saccharomyces pastorianus

substrate_name: Unknown

proof_lines: assay with whole enzyme complex, competitive inhibition

substrate: Unknown


organism: Ricinus communis

assay_conditions_summary: cofactor NAD+

proof_lines: competitive inhibition vs. NAD+, whole enzyme complex

proof_lines: competitive inhibition vs. CoA, whole enzyme complex


organism: Lathyrus oleraceus

substrate_name: CoA

assay_conditions_summary: pH 7.6; 295.15 K; cofactor CoA

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

substrate: CoA


organism: Saccharomyces cerevisiae


enzyme_display_name: 2-oxoglutarate dehydrogenase system

organism: Urocitellus richardsonii

assay_conditions_summary: pH 7.8; 295.15 K; cofactor CoA

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

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

proof_lines: overall reaction, enzyme from euthermic animals, 5°C, pH 7.8

enzyme: 2-oxoglutarate dehydrogenase system


assay_conditions_summary: pH 7.8; 278.15 K; cofactor NAD+

proof_lines: overall reaction, enzyme from hibernating animals, 5°C, pH 7.8

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


assay_conditions_summary: pH 7.8; 303.15 K; cofactor CoA

proof_lines: S0.5 value, 0.15 M ionic strength, pH 7.8, 30°C

proof_lines: S0.5 value, 0.10 M ionic strength, pH 7.8, 30°C

proof_lines: S0.5 value, 0.05 M ionic strength, pH 7.8, 30°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

proof_lines: S0.5 value, Hill coefficient 0.4, pH 7.5, temperature not specified in the publication


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


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
component E1, pH 7.5, 37°C


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


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

organism: Thermus thermophilus

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


substrate_name: phosphate

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

substrate: phosphate


substrate_name: NADP+

assay_conditions_summary: pH 9.5; cofactor NADP+

substrate: NADP+


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H298T to reconstruct the assayed variant sequence.

proof_lines: mutant H298T, 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 H260E to reconstruct the assayed variant sequence.

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


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

normalized_value_unit_evidence: kcat normalized_value=0.076 normalized_unit=s^-1; Km normalized_value=16.3 normalized_unit=mM; kcat/Km normalized_value=0.0047 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=0.076 +/- 0.007 raw_unit=s^-1; Km raw_value=16.3 +/- 4.00 in Km (mM) raw_unit=mM; kcat/Km raw_value=0.0047 raw_unit=s^-1*mM^-1

row_label: none / 2-OV


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

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


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


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


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


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


substrate_name: NAD+

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


organism: Brassica oleracea


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


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


organism: Thermotoga maritima

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: Azotobacter vinelandii


organism: Aspergillus niger


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


organism: Oryctolagus cuniculus


organism: Komagataeibacter xylinus

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


organism: Homo sapiens


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.


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(+))

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


substrate_name: NADH (at pH 8.0)

substrate: NADH (at pH 8.0)


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

substrate_name: NADP(+)

substrate: NADP(+)


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(+).


organism: Thermus thermophilus

assay_conditions_summary: pH 9.5; 333.15 K; cofactor NADP+


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


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


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

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+


smiles: O=C(O)CCO

assay_conditions_summary: pH 8; 310.15 K; cofactor NADH

row_label: 3-Hydroxypropionic acid (footnote b) / NADH

table_label: Applied Microbiology and Biotechnology 2008 Table 4


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: benzaldehyde

assay_conditions_summary: pH 8; 310.15 K; cofactor NADP+

substrate: benzaldehyde


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: Isovaleraldehyde

smiles: CC(C)C=O

substrate: Isovaleraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: Valeraldehyde

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+

assay_conditions_summary: cofactor 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


organism: Azospirillum brasilense

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

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


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


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

smiles: CCCCCCC=O

enzyme: UniProt G3X982

substrate: Heptanal


substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: pentanal

smiles: CCCCC=O

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

smiles: CC=O

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


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+

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

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

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)

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

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


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


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

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_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)


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


smiles: CCCCC=O


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


substrate_name: ethyl vanillin

substrate: ethyl vanillin


substrate_name: acetaldehyde

smiles: CC=O

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

substrate: acetaldehyde


substrate_name: methylene blue

proof_lines: as electron acceptor under aerobic conditions

substrate: methylene blue