Open AccessA novel enzyme, L ‐lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii
Author(s) -
Schmidt H.,
Bode R.,
Birnbaum D.
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02716.x
Subject(s) - lysine , transamination , biochemistry , catabolism , enzyme , lysine decarboxylase , chemistry , biology , amino acid , putrescine , cadaverine
A novel aminotransferase catalysing the first step of lysine catabolism, the oxidative transamination of the ?‐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.