Glycerol catabolism in Aspergillus nidulans.
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.
Hondmann
D H
DH
Department of Genetics, Agricultural University, Wageningen, The Netherlands.
Busink
R
R
Witteveen
C F
CF
Visser
J
J
D000426:Alcohol Dehydrogenase / Q000378:metabolism; D001233:Aspergillus nidulans / Q000201:enzymology / Q000235:genetics / Q000254:growth & development / Q000378:metabolism*; D002244:Carbon / Q000378:metabolism; D005990:Glycerol / Q000378:metabolism*; D005991:Glycerol Kinase / Q000378:metabolism; D005993:Glycerolphosphate Dehydrogenase / Q000378:metabolism; D008928:Mitochondria / Q000201:enzymology; D009154:Mutation
D002244:Carbon; D005993:Glycerolphosphate Dehydrogenase; D000426:Alcohol Dehydrogenase; D005991:Glycerol Kinase; D005990:Glycerol