Glycerol catabolism in Aspergillus nidulans

Autor: D.H.A. Hondmann, C.F.B. Witteveen, R. Busink, Jantien Visser
Rok vydání: 1991
Předmět:
Zdroj: Journal of general microbiology 137 (1991)
Journal of general microbiology, 137, 629-636
ISSN: 0022-1287
DOI: 10.1099/00221287-137-3-629
Popis: Glycerol is catabolized in Aspergillus nidulans by glycerol kinase and a mitochondrial FAD-dependent sn-glycerol 3-phosphate dehydrogenase. The levels of both enzymes are controlled by carbon catabolite repression and by specific induction. Biochemical and genetical analyses show that dihydroxyacetone and D-glyceraldehyde are converted into glycerol and then catabolized by the same pathway. D-Glyceraldehyde can be reduced by NADP(+)-dependent glycerol dehydrogenase or by alcohol dehydrogenase I, while dihydroxyacetone is only reduced by the first enzyme. Three new glycerol non-utilizing mutants have been found. These three mutations define three hitherto unknown loci, glcE, glcF and glcG. The mutation in glcG leads to a greatly decreased sn-glycerol-3-phosphate dehydrogenase activity.
Databáze: OpenAIRE