Enzyme

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     1. Oxidoreductases
        1.4 Acting on the CH-NH2 group of donors
            1.4.3 With oxygen as acceptor
ID:1.4.3.21
Description:Primary-amine oxidase.
Alternative Name: Copper amine oxidase.
CAO.
Benzylamine oxidase.
Amine oxidase (copper-containing).
Amine oxidase.
Cath: 1.10.405.10; 1.20.5.1360; 3.10.450.40; 3.30.457.10; 3.50.50.60; 3.90.660.10; 2.70.98.20; 3.10.129.10;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.4.3.21
BRENDA Enzyme Link: BRENDA 1.4.3.21
KEGG Enzyme Link: KEGG1.4.3.21
BioCyc Enzyme Link: BioCyc 1.4.3.21
ExPASy Enzyme Link: ExPASy1.4.3.21
EC2PDB Enzyme Link: EC2PDB 1.4.3.21
ExplorEnz Enzyme Link: ExplorEnz 1.4.3.21
PRIAM enzyme-specific profiles Link: PRIAM 1.4.3.21
IntEnz Enzyme Link: IntEnz 1.4.3.21
MEDLINE Enzyme Link: MEDLINE 1.4.3.21
MSA:

1.4.3.21;

Phylogenetic Tree:

1.4.3.21;

Uniprot:
M-CSA:
RHEA:35107 3-nitrotyramine + H2O + O2 = 4-hydroxy-3-nitrophenylacetaldehyde + H2O2 + NH4(+)
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH2;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]-[CH;+0:2]=[O;H0;+0:6].[NH3;+0:3].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Escherichia coli NsrR regulates a pathway for the oxidation of 3-nitrotyramine to 4-hydroxy-3-nitrophenylacetate.Rankin LD, Bodenmiller DM, Partridge JD, Nishino SF, Spain JC, Spiro S2008 Sep18658270

RHEA:25265 2-phenylethylamine + H2O + O2 = 2-phenylacetaldehyde + H2O2 + NH4(+)
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH2;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]-[CH;+0:2]=[O;H0;+0:6].[NH3;+0:3].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Visualization of dioxygen bound to copper during enzyme catalysis.Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE1999 Nov 2610576737

RHEA:16153 an aliphatic amine + H2O + O2 = an aldehyde + H2O2 + NH4(+)
RULE(radius=1) [*:1]-[CH2;+0:2]-[NH2;+0:3].[O;H0;+0:4]=[O;H0;+0:5].[OH2;+0:6]>>[*:1]-[CH;+0:2]=[O;H0;+0:6].[NH3;+0:3].[OH;+0:4]-[OH;+0:5]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini.Lee Y, Sayre LM1998 Jul 319677370
Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone.Wilce MC, Dooley DM, Freeman HC, Guss JM, Matsunami H, McIntire WS, Ruggiero CE, Tanizawa K, Yamaguchi H1997 Dec 239405045
Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects.Lyles GA1996 Mar8920635
Cloning and molecular analysis of the pea seedling copper amine oxidase.Tipping AJ, McPherson MJ1995 Jul 147622512
Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source.Haywood GW, Large PJ1981 Oct 17337701
Crystal structure of the human vascular adhesion protein-1: unique structural features with functional implications.Airenne TT, Nymalm Y, Kidron H, Smith DJ, Pihlavisto M, Salmi M, Jalkanen S, Johnson MS, Salminen TA2005 Aug16046623
Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do.O'Sullivan J, Unzeta M, Healy J, O'Sullivan MI, Davey G, Tipton KF2004 Jan14697905
Probing the catalytic mechanism of Escherichia coli amine oxidase using mutational variants and a reversible inhibitor as a substrate analogue.Saysell CG, Tambyrajah WS, Murray JM, Wilmot CM, Phillips SE, McPherson MJ, Knowles PF2002 Aug 111985492
Tissue activity and cellular localization of human semicarbazide-sensitive amine oxidase.Andrés N, Lizcano JM, Rodríguez MJ, Romera M, Unzeta M, Mahy N2001 Feb11156689
Mammalian Cu-containing amine oxidases (CAOs): new methods of analysis, structural relationships, and possible functions.Houen G199910668504