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2.3.1.263 |
Description |
2-amino-4-oxopentanoate thiolase |
Alternative names |
AKPT; AKP thiolase; 2-amino-4-ketopentanoate thiolase |
Catalyzed reaction |
acetyl-CoA + D-alanine = CoA + (2R)-2-amino-4-oxopentanoate |
Cofactor |
Pyridoxal-phosphate. |
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 |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 2.3.1.263
BRENDA (activities) 2.3.1.263
KEGG (pathways) 2.3.1.263
PLPMDB (PLP mutants) 2.3.1.263
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References |
Fonknechten N1, Perret A, Perchat N, Tricot S, Lechaplais C, Vallenet D, Vergne C, Zaparucha A, Le Paslier D, Weissenbach J, Salanoubat M (2009) A conserved gene cluster rules anaerobic oxidative degradation of L-ornithine J Bacteriol 191 3162-7. Jeng IM, Somack R, Barker HA. (1974) 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 2898-903. Articles on 2.3.1.263 |
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last changed |
2018/02/13 18:10 |
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