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Lysine degradation in Pichia guilliermondii: Characterization of a novel enzyme, L-lysine:pyruvate aminotransferase

✍ Scribed by H. Schmidt; DOZ. Dr. R. Bode; D. Birnbaum

Publisher: John Wiley and Sons
Year: 1987
Tongue: English
Weight: 390 KB
Volume: 27
Category: Article
ISSN: 0233-111X
DOI: 10.1002/jobm.3620271007

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✦ Synopsis

A novel aminotransferase catalyzing the oxidative transamination of the &-group of L-lysine was found in the yeast Pichiu guilliermondii. The enzyme, L-lysine: pyruvate aminotransferase, is strongly induced in cells grown on L-lysine as sole nitrogen source. The enzyme is highly specific for both ~-1ysine and pyruvate.

The &-values are 12 mM for L-lysine, 0.55 mM for pyruvate, und 40 PM for pyridoxal-5-phosphate. An apparent relative molecular weight of 90,000 was estimated by gel filtration. The enzyme has a maximum activity at pH 9.0 and a temperature optimum of 32 ' C.

') Dedicated to UDO TAUBENECK on the occasion of his 60 th birthday

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