Amine oxidase (copper-containing)

From Wikipedia, the free encyclopedia

In enzymology, an amine oxidase (copper-containing) (EC 1.4.3.6) is an enzyme that catalyzes the chemical reaction

RCH₂NH₂ + H₂O + O₂ $\rightleftharpoons$ RCHO + NH₃ + H₂O₂

The 3 substrates of this enzyme are primary amines (RCH2NH2), H₂O, and O₂, whereas its 3 products are RCHO, NH₃, and H₂O₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). Other names in common use include diamine oxidase, diamino oxhydrase, histaminase, amine oxidase, monoamine oxidase, amine oxidase (pyridoxal containing), benzylamine oxidase, histamine deaminase, histamine oxidase, Cu-amine oxidase, amine oxygen oxidoreductase, diamine:O2 oxidoreductase (deaminating), semicarbazide-sensitive amine oxidase, and SSAO. This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta-alanine metabolism, and alkaloid biosynthesis ii. It has 2 cofactors: copper, and PQQ.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 51 structures have been solved for this class of enzymes, with PDB accession codes 1A2V, 1AV4, 1AVK, 1AVL, 1D6U, 1D6Y, 1D6Z, 1EKM, 1IQX, 1IQY, 1IU7, 1IVU, 1IVV, 1IVW, 1IVX, 1KSI, 1LVN, 1OAC, 1PU4, 1RJO, 1SIH, 1SII, 1SPU, 1TU5, 1UI7, 1UI8, 1US1, 1W2Z, 1W4N, 1W5Z, 1W6C, 1W6G, 1WMN, 1WMO, 1WMP, 2BT3, 2C10, 2C11, 2CFD, 2CFG, 2CFK, 2CFL, 2CFW, 2CG0, 2CG1, 2CWT, 2CWU, 2CWV, 2D1W, 2OOV, and 2OQE.

[edit] References

IUBMB entry for 1.4.3.6
BRENDA references for 1.4.3.6 (Recommended.)
PubMed references for 1.4.3.6
PubMed Central references for 1.4.3.6
Google Scholar references for 1.4.3.6
O (1984). "Microbial-production of pyrroloquinoline quinone". Agric. Biol. Chem. 48: 561–565.
AUGUSTINSSON KB, OLSSON B (1959). "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies". Biochem. J. 71: 477–84. PMID 13638253.
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 337-351.
BUFFONI F, BLASCHKO H (1964). "BENZYLAMINE OXIDASE AND HISTAMINASE: PURIFICATION AND CRYSTALLIZATION OF AN ENZYME FROM PIG PLASMA". Proc. R. Soc. Lond. B. Biol. Sci. 161: 153–67. PMID 14224405.
Haywood GW, Large PJ (1981). "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". Biochem. J. 199: 187–201. PMID 7337701.
McEwen CM Jr (1965). "Human plasma monoamine oxidase. 1. Purification and identification". J. Biol. Chem. 240: 2003–10. PMID 5888801.
Mondovi B, Costa MT, Agro AF, Rotilio G (1967). "Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase". Arch. Biochem. Biophys. 119: 373–81. doi:10.1016/0003-9861(67)90468-7. PMID 4964016.
Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part II. Purification and crystallisation of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 649–654.
Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 864–869.
Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 912–917.
Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 313-335.