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UniProt functional annotation for Q8VPD4 | ||
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| UniProt code: Q8VPD4. |
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| Organism: | |
Rhodococcus opacus (Nocardia opaca). |
| Taxonomy: | |
Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus. |
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| Function: | |
Catalyzes an oxidative deamination of basic, hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme (Ref.1). Is active on most L-amino acid (39 on 43 tested) with the exception of L- Thr, L-Pro, and L-Gly (Ref.1). {ECO:0000269|Ref.1}. |
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| Catalytic activity: | |
Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 + NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179, ChEBI:CHEBI:59869; EC=1.4.3.2; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-asparagine + O2 = 2-oxosuccinamate + H2O2 + NH4(+); Xref=Rhea:RHEA:61224, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57735, ChEBI:CHEBI:58048; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-methionine + O2 = 4-methylsulfanyl-2-oxobutanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61236, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16723, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-phenylalanine + O2 = 3-phenylpyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61240, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18005, ChEBI:CHEBI:28938, ChEBI:CHEBI:58095; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-tyrosine + O2 = 3-(4-hydroxyphenyl)pyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61248, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:36242, ChEBI:CHEBI:58315; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-glutamine + O2 = 2-oxoglutaramate + H2O2 + NH4(+); Xref=Rhea:RHEA:61260, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16769, ChEBI:CHEBI:28938, ChEBI:CHEBI:58359; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-alanine + O2 = H2O2 + NH4(+) + pyruvate; Xref=Rhea:RHEA:61264, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:57972; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938, ChEBI:CHEBI:57427; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-lysine + O2 = 6-amino-2-oxohexanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:14437, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32551, ChEBI:CHEBI:58183; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-arginine + O2 = 5-guanidino-2-oxopentanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:51404, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:32682, ChEBI:CHEBI:58489; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-glutamate + O2 = 2-oxoglutarate + H2O2 + NH4(+); Xref=Rhea:RHEA:20728, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16810, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-cystine + O2 = (2R)-2-amino-2-carboxylatoethyl- disulfanyl-oxopropanoate + H2O2 + NH4(+); Xref=Rhea:RHEA:61284, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35491, ChEBI:CHEBI:144484; Evidence={ECO:0000269|Ref.1}; |
| Catalytic activity: | |
Reaction=H2O + L-serine + O2 = 3-hydroxypyruvate + H2O2 + NH4(+); Xref=Rhea:RHEA:61344, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17180, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; Evidence={ECO:0000269|Ref.1}; |
| Cofactor: | |
Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:17234209, ECO:0000269|Ref.1}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17234209, ECO:0000269|Ref.1}; |
| Biophysicochemical properties: | |
Kinetic parameters: KM=0.019 mM for L-Tyr {ECO:0000269|Ref.1}; KM=0.070 mM for L-Arg {ECO:0000269|Ref.1}; KM=0.026 mM for L-norleucine {ECO:0000269|Ref.1}; KM=0.034 mM for L-ornithine {ECO:0000269|Ref.1}; KM=0.022 mM for L-Phe {ECO:0000269|Ref.1}; KM=0.028 mM for L-Leu {ECO:0000269|Ref.1}; KM=0.039 mM for L-Met {ECO:0000269|Ref.1}; KM=0.026 mM for L-citrulline {ECO:0000269|Ref.1}; KM=0.028 mM for L-Asn {ECO:0000269|Ref.1}; KM=0.085 mM for L-Gln {ECO:0000269|Ref.1}; KM=0.274 mM for L-Ala {ECO:0000269|Ref.1}; KM=0.015 mM for L-Lys {ECO:0000269|Ref.1}; KM=5.11 mM for L-Ile {ECO:0000269|Ref.1}; KM=0.411 mM for L-Glu {ECO:0000269|Ref.1}; KM=3.73 mM for L-Val {ECO:0000269|Ref.1}; KM=1.36 mM for L-Ser {ECO:0000269|Ref.1}; Vmax=9.69 umol/min/mg enzyme toward L-Tyr {ECO:0000269|Ref.1}; Vmax=8.12 umol/min/mg enzyme toward L-Arg {ECO:0000269|Ref.1}; Vmax=7.55 umol/min/mg enzyme toward L-norleucine {ECO:0000269|Ref.1}; Vmax=7.48 umol/min/mg enzyme toward L-ornithine {ECO:0000269|Ref.1}; Vmax=6.97 umol/min/mg enzyme toward L-Phe {ECO:0000269|Ref.1}; Vmax=6.45 umol/min/mg enzyme toward L-Leu {ECO:0000269|Ref.1}; Vmax=6.43 umol/min/mg enzyme toward L-Met {ECO:0000269|Ref.1}; Vmax=5.47 umol/min/mg enzyme toward L-citrulline {ECO:0000269|Ref.1}; Vmax=5.37 umol/min/mg enzyme toward L-Asn {ECO:0000269|Ref.1}; Vmax=5.06 umol/min/mg enzyme toward L-Gln {ECO:0000269|Ref.1}; Vmax=4.27 umol/min/mg enzyme toward L-Ala {ECO:0000269|Ref.1}; Vmax=3.56 umol/min/mg enzyme toward L-Lys {ECO:0000269|Ref.1}; Vmax=2.84 umol/min/mg enzyme toward L-Ile {ECO:0000269|Ref.1}; Vmax=2.32 umol/min/mg enzyme toward L-Glu {ECO:0000269|Ref.1}; Vmax=1.93 umol/min/mg enzyme toward L-Val {ECO:0000269|Ref.1}; Vmax=4.36 umol/min/mg enzyme toward L-Ser {ECO:0000269|Ref.1}; pH dependence: Optimum pH is 8-9. {ECO:0000269|Ref.1}; |
| Subunit: | |
Homodimer; non-covalently linked. {ECO:0000269|Ref.1}. |
| Subcellular location: | |
Cytoplasm {ECO:0000305|Ref.1}. Note=Unexpectedly, is not secreted into the medium. {ECO:0000269|Ref.1}. |
| Ptm: | |
Predicted to be exported by the Tat system. {ECO:0000255|PROSITE- ProRule:PRU00648}. |
| Ptm: | |
Not glycosylated. {ECO:0000269|PubMed:17234209}. |
| Biotechnology: | |
Can be used for the preparation of D-amino acids by resolving racemic amino acid mixtures and for the production of alpha- keto acids. {ECO:0000305|Ref.1}. |
| Similarity: | |
Belongs to the flavin monoamine oxidase family. FIG1 subfamily. {ECO:0000305}. |
Annotations taken from UniProtKB at the EBI.