title: Characterization of acetyl-CoA: L-lysine N6-acetyltransferase, which catalyses the first step of carbon catabolism from lysine in Saccharomyces cerevisiae.
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 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.
authors.affiliation: Institut für Genetik und Biochemie, Fachrichtung Biologie, Ernst-Moritz-Arndt-Universität Greifswald, Germany.
authors.forename: R
authors.initials: R
authors.lastname: Bode
authors.forename: A M
authors.initials: AM
authors.lastname: Thurau
authors.forename: H
authors.initials: H
authors.lastname: Schmidt
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000096:biosynthesis / Q000737:chemistry* / Q000302:isolation & purification; D002850:Chromatography, Gel; D004790:Enzyme Induction; D006863:Hydrogen-Ion Concentration; D008239:Lysine / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology; D012441:Saccharomyces cerevisiae / Q000201:enzymology*; D013379:Substrate Specificity; D013696:Temperature; D013997:Time Factors
chemical_list: D008670:Metals; D000123:Acetyltransferases; C084723:acetyl-CoA - lysine N6-acetyltransferase; D008239:Lysine