|
type |
Journal Article |
authors |
Der Garabedian, P. A.; Vermeersch, J. J. |
title |
Lysine degradation in Candida. Characterization and probable role of L- norleucine-leucine, 4-aminobutyrate and delta-aminovalerate:2- oxoglutarate aminotransferases |
journal |
Biochimie |
Activity |
2.6.1.67 |
ui |
89335823 |
year |
(1989) |
volume |
71 |
number |
4 |
pages |
497-503. |
| |
keywords |
4-Aminobutyrate Transaminase/metabolism |
abstract |
Three enzymes partially purified that catalyze respectively the transamination of L-norleucine, 4-aminobutyrate and delta-aminovalerate with alpha-ketoglutarate as aminoacceptor were characterized and isolated from L-lysine adapted cell of Candida guilliermondii var. membranaefaciens. The transaminases have a maximum activity in the pH range of 7.8-8.5 and at 55 degrees C, 45 degrees C and 40 degrees C respectively. alpha-Ketoglutarate and to a lesser extent pyridoxal-5'- phosphate were effective protecting agents against rise in temperature. The enzymes exhibit absorption maximum at 280 nm, 330 nm and 410 nm. The fact that L-norleucine-leucine aminotransferase, 4-aminobutyrate aminotransferase and delta-aminovalerate aminotransferase are strongly induced by growing the yeast Candida on L-lysine suggests new hypothetic pathways for the catabolism of L-lysine where the main substrate of each aminotransferase could be an intermediary metabolite. |
last changed |
2002/11/20 18:18 |
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