Cell-free extracts of Pseudomonas sp. strains KB 740 and K 172 both contained high levels of glutaryl-CoA dehydrogenase when grown anaerobically on benzoate or other aromatic compounds and with nitrate as electron acceptor. These aromatic compounds have in common benzoyl-CoA as the central aromatic
Purification of a novel enzyme involved in catechin degradation byCalvatia gigantea
β Scribed by M. Galiotou-Panayotou; P. Rodis; B. J. Macris; D. Stathakos
- Publisher
- Springer
- Year
- 1988
- Tongue
- English
- Weight
- 224 KB
- Volume
- 28
- Category
- Article
- ISSN
- 1432-0614
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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 ~-