The Enzyme Database

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EC 2.3.1.263     
Accepted name: 2-amino-4-oxopentanoate thiolase
Reaction: acetyl-CoA + D-alanine = CoA + (2R)-2-amino-4-oxopentanoate
Other name(s): AKPT; AKP thiolase; 2-amino-4-ketopentanoate thiolase
Systematic name: acetyl-CoA:D-alanine acetyltransferase
Comments: A pyridoxal 5′-phosphate enzyme. The enzyme, characterized from the bacterium Clostridium sticklandii, is part of a degradation pathway of ornithine. It is specific for acetyl-CoA and D-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Jeng, I.M., Somack, R. and Barker, H.A. Ornithine degradation in Clostridium sticklandii; pyridoxal phosphate and coenzyme A dependent thiolytic cleavage of 2-amino-4-ketopentanoate to alanine and acetyl coenzyme A. Biochemistry 13 (1974) 2898–2903. [PMID: 4407783]
2.  Fonknechten, N., Perret, A., Perchat, N., Tricot, S., Lechaplais, C., Vallenet, D., Vergne, C., Zaparucha, A., Le Paslier, D., Weissenbach, J. and Salanoubat, M. A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine. J. Bacteriol. 191 (2009) 3162–3167. [DOI] [PMID: 19251850]
[EC 2.3.1.263 created 2017]
 
 


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