Activities | Families | Sequences | Fold types | References | Help
B6db references: nelpacf

type Journal Article
authors Schmidt, H.; Bode, R.; Birnbaum, D.
title A novel enzyme, L-lysine : pyruvate aminotransferase, catalyses the first step of lysine catabolism in Pichia guilliermondii
journal FEMS Microbiol. Lett.
Activity 2.6.1.71
sel selected
ui nelpacf
year (1988)
volume 49
pages 203-206
 
abstract Abstract A novel aminotransferase catalysing the first step of lysine catabolism, the oxidative transamination of the ϵ-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.
last changed 2009/05/19 15:45

B6db references