A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii

18Citations
Citations of this article
3Readers
Mendeley users who have this article in their library.

This article is free to access.

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.

Cite

CITATION STYLE

APA

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.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free