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B6db references: 89335823

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
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

B6db references