The Enzyme Database

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EC 1.4.3.3     
Accepted name: D-amino-acid oxidase
Reaction: a D-amino acid + H2O + O2 = a 2-oxo carboxylate + NH3 + H2O2
For diagram of cephalosporin biosynthesis, click here
Other name(s): ophio-amino-acid oxidase; L-amino acid:O2 oxidoreductase; new yellow enzyme
Systematic name: D-amino-acid:oxygen oxidoreductase (deaminating)
Comments: A flavoprotein (FAD). Wide specificity for D-amino acids. Also acts on glycine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 9000-88-8
References:
1.  Dixon, M. and Kleppe, K. D-Amino acid oxidase. I. Dissociation and recombination of the haloenzyme. Biochim. Biophys. Acta 96 (1965) 357–367. [PMID: 14314378]
2.  Dixon, M. and Kleppe, K. D-Amino acid oxidase. II. Specificity, competitive inhibition and reaction sequence. Biochim. Biophys. Acta 96 (1965) 368–382.
3.  Dixon, M. and Kleppe, K. D-Amino acid oxidase. III. Effect of pH. Biochim. Biophys. Acta 96 (1965) 383–389. [PMID: 14314379]
4.  Massey, V., Palmer, G. and Bennett, R. The purification and some properties of D-amino acid oxidase. Biochim. Biophys. Acta 48 (1961) 1–9. [PMID: 13767909]
5.  Meister, A. and Wellner, D. Flavoprotein amino acid oxidase. In: Boyer, P.D., Lardy, H. and Myrbäck, K. (Eds), The Enzymes, 2nd edn, vol. 7, Academic Press, New York, 1963, pp. 609–648.
[EC 1.4.3.3 created 1961]
 
 


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