|
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 |
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