Abstract
A novel aminotransferase catalysing the first step of lysine catabolism, the oxidative transamination of the ε{lunate}-group of L-lysine, was found and characterised in the yeast Pichia guilliermondii. The enzyme, L-lysine : pyruvate aminotransferase (Lys-AT), is strongly derepressed in cells grown on L-lysine as sole nitrogen source and its activity is highly specific for both L-lysine and pyruvate. We could successfully isolate a regulatory mutant which is unable to use lysine as sole nitrogen source based on its inability to derepress the Lys-AT. © 1988.
Author supplied keywords
Cite
CITATION STYLE
Schmidt, H., Bode, R., & Birnbaum, D. (1988). A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii. FEMS Microbiology Letters, 49(2), 203–206. https://doi.org/10.1111/j.1574-6968.1988.tb02716.x
Register to see more suggestions
Mendeley helps you to discover research relevant for your work.