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:1.4.3.4
Description:Monoamine oxidase.
Alternative Name: Tyramine oxidase.
Tyraminase.
Amine oxidase (flavin-containing).
Amine oxidase.
Adrenaline 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 1.4.3.4
BRENDA Enzyme Link: BRENDA 1.4.3.4
KEGG Enzyme Link: KEGG1.4.3.4
BioCyc Enzyme Link: BioCyc 1.4.3.4
ExPASy Enzyme Link: ExPASy1.4.3.4
EC2PDB Enzyme Link: EC2PDB 1.4.3.4
ExplorEnz Enzyme Link: ExplorEnz 1.4.3.4
PRIAM enzyme-specific profiles Link: PRIAM 1.4.3.4
IntEnz Enzyme Link: IntEnz 1.4.3.4
MEDLINE Enzyme Link: MEDLINE 1.4.3.4
MSA:

1.4.3.4;

Phylogenetic Tree:

1.4.3.4;

Uniprot:
M-CSA:
RHEA:26414 a secondary aliphatic amine + H2O + O2 = a primary amine + an aldehyde + H2O2
RULE(radius=1) [*:1]-[NH;+0:2]-[CH2;+0:3]-[*:4].[O;H0;+0:5]=[O;H0;+0:6].[OH2;+0:7]>>[*:4]-[CH;+0:3]=[O;H0;+0:7].[*:1]-[NH2;+0:2].[OH;+0:5]-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B.De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A2005 Sep 616129825
Structure and mechanism of monoamine oxidase.Edmondson DE, Mattevi A, Binda C, Li M, Hubálek F2004 Aug15279562