Lysine degradation inCandida maltosa: occurrence of a novel enzyme, acetyl-CoA:L-lysine N-acetyltransferase

✍ Scribed by Heike Schmidt; Rüdiger Bode; Dieter Birnbaum

• Publisher: Springer
• Year: 1988
• Tongue: English
• Weight: 367 KB
• Volume: 150
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00407782

✦ Synopsis

The yeast Candida maltosa can utilize L-lysine as sole nitrogen and sole carbon source accompanied by accumulation of e-N-acetyl-L-lysine, indicating that lysine is metabolized by way of N-acetylated intermediates. A novel lysine acetyltransferase catalyzing the first step in this pathway, the N-acetylation of the e-amino group of L-lysine, was found in this yeast. The enzyme, acetyl-CoA: L-lysine N-acetyltransferase, is strongly induced in cells grown on L-lysine as sole carbon source. The enzyme is specific for both L-lysine and acetyl-CoA. The Km values are 10 mM for L-lysine and 0.33 mM for acetyl-CoA. The enzyme has a maximum activity at pH 8.1.