Characterization of acetyl-CoA: l-lysine N6-acetyltransferase, which catalyses the first step of carbon catabolism from lysine in Saccharomyces cerevisiae
- 80 Downloads
- 3 Citations
Abstract
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°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.
Key words
Saccharomyces cerevisiae Acetyl-CoA l-Lysine N6 acetytransferase Lysine catabolismPreview
Unable to display preview. Download preview PDF.
References
- Gaillardin C, Fournier P, Sylvestre G, Heslot H (1976) Mutants of Saccharomycopsis lipolytica defective in lysine catabolism. J Bacteriol 125: 48–57Google Scholar
- Guengerich FP, Broquist HP (1976) Lysine catabolism in Rhizoctonia leguminicola and related fungi. J Bacteriol 126: 338–347Google Scholar
- Hammer T, Bode R, Birnbaum D (1991a) Occurrence of a novel yeast enzyme, l-lysine ε-dehydrogenase, which catalyses the first step of lysine catabolism in Candida albicans. J Gen Microbiol 137: 711–715Google Scholar
- Hammer T, Bode R, Schmidt H, Birnbaum D (1991b) Distribution of three lysine-catabolizing enzymes in various yeast species. J Basic Microbiol 31: 43–49Google Scholar
- Kohlhaw GB (1988) α-Isopropylmalate synthase from yeast. Methods Enzymol 166: 414–423Google Scholar
- Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680–685PubMedGoogle Scholar
- Large PJ, Robertson A (1991) The route of lysine breakdown in Candida tropicalis. FEMS Microbiol Lett 82: 209–214Google Scholar
- Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the Folin phenol reagent. J Biol Chem 193: 265–275Google Scholar
- Paik WK, Kim S (1964) Enzymic synthesis of ε-N-acetyl-l-lysine. Arch Biochem Biophys 108: 221–229Google Scholar
- Schmidt H, Bode R, Birnbaum D (1988a) A novel enzyme, l-lysine: pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii. FEMS Microbiol Lett 49: 203–206Google Scholar
- Schmidt H, Bode R, Birnbaum D (1988b) Lysine degradation in Candida maltosa: occurrence of a novel enzyme: acetyl-CoA: l-lysine N-acetyltransferase. Arch Microbiol 150: 215–218Google Scholar
- Tanaka H, Soda K (1974) Enzymatic N-acetylation of lysine analogs. Purification and properties of acetyl coenzyme A:S-(β-aminoethyl)-l-cysteine ε-N-acetyltransferase. J Biol Chem 249: 5285–5289Google Scholar
- Tanaka A, Ohishi N, Fukui S (1967) Studies on the formation of vitamins and their function in hydrocarbon fermentation. Production of vitamin B6 by Candida albicans in hydrocarbon medium. J Ferment Technol 45: 617–623Google Scholar
- Vogel HJ, Shimura Y (1971) Spectrophotometric determination of lysine. Methods Enzymol B 17: 228–229Google Scholar
- Walters LS, Thiselton MR (1953) Utilization of lysine by yeasts. J Inst Brew 59: 401–404Google Scholar