Characterization of acetyl-CoA:l-lysine N6-acetyltransferase, which catalyses the first step of carbon catabolism from lysine inSaccharomyces cerevisiae

✍ Scribed by Rüdiger Bode; Anja-Maria Thurau; Heike Schmidt

• Publisher: Springer
• Year: 1993
• Tongue: English
• Weight: 359 KB
• Volume: 160
• Category: Article
• ISSN: 0302-8933
• DOI: 10.1007/bf00252227

✦ Synopsis

The carbon catabolism of L-lysine starts in Saccharomyces cerevisiae with acetylation by an acetyl-CoA:L-lysine N6-acetyltransferase. The enzyme is strongly induced in cells grown on L-lysine as sole carbon source and has been purified about 530-fold. Its activity was specific for acetyl-CoA and, in addition to L-lysine, 5-hydroxylysine and thialysine act as acetyl acceptor. The following apparent Michaelis constants were determined: acetyl-CoA 0.8 mM, L-lysine 5.8 mM, DL-5-hydroxylysine, 2.8 mM, L-thialysine 100 mM. The enzyme had a maximum activity at pH 8.5 and 37 degrees C. Its molecular mass, estimated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis, was 52 kDa. Since the native molecular mass, determined by gel filtration, was 48 kDa, the enzyme is a monomer.