Journal
FUNGAL GENETICS AND BIOLOGY
Volume 46, Issue 6-7, Pages 473-485Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.fgb.2009.03.004
Keywords
Acetyl-CoA hydrolase; CoA-transferase; Acetic acid detoxification; Succinyl-CoA; Physiological adaptation
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Funding
- Deutsche Forschungsgemeinschaft (DFG)
- Leibniz institute for Natural Product Research and Infection Biology e.V. (Hans Knoell Institute)
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Saccharomyces cerevisiae and Neurospora crassa mutants defective in the so-called acetyl-CoA hydrolases Ach1p and Acu-8, respectively, display a severe growth defect on acetate, which is most strongly pronounced under acidic conditions. Acetyl-CoA hydrolysis is an energy wasting process and therefore denoted as a biochemical conundrum. Acetyl-CoA hydrolases show high sequence identity to the CoA-transferase CoaT from Aspergillus nidulans. Therefore, we extensively re-characterised the yeast enzyme. Ach1p showed highest specific activity for the CoASH transfer front succinyl-CoA to acetate and only a minor acetyl-CoA-hydrolase activity. Complementation of an ach1 mutant with the coaT gene reversed the growth defect on acetate confirming the in vivo function of Ach1p as a CoA-transferase. Our results imply that Ach1p is involved in mitochondrial acetate detoxification by a CoASH transfer from succinyl-CoA to acetate. Thereby, Ach1p does not perform the energy wasting hydrolysis of acetyl-CoA but conserves energy by the detoxification of mitochondrial acetate. (C) 2009 Elsevier Inc. All rights reserved.
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