Search
Filter Results
- Resource Type
- Article1
- Book1
- Book Print1
- Journal1
- Result From
- Lane Catalog1
- PubMed1
- SearchWorks (biomedical subset) 1
-
Year
- Journal Title
- Proc Natl Acad Sci U S A1
Search Results
Sort by
- ArticleKamiryo T, Nishikawa Y, Mishina M, Terao M, Numa S.Proc Natl Acad Sci U S A. 1979 Sep;76(9):4390-4.Mutant strains of Candida lipolytica defective in acyl-CoA synthetase II [acid:CoA ligase (AMP-forming), EC 6.2.1.3] have been isolated. The mutants fail to grow on fatty acid as a sole carbon source but are capable of incorporating exogenous fatty acid into cellular lipids. This observation, together with our previous finding that mutant strains defective in acyl-CoA synthetase I cannot incorporate exogenous fatty acid into cellular lipids but are able to degrade fatty acid via beta-oxidation, indicates the presence of two functionally distinct long-chain acyl-CoA pools in the cell--i.e., one for lipid synthesis and the other for beta-oxidation. Unlike the wild-type and the revertant strains as well as the mutants lacking acyl-CoA synthetase II, the mutants defective in acyl-CoA synthetase I do not exhibit the repression of acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] by exogenous fatty acid. Measurement of the two long-chain acyl-CoA pools with the aid of appropriate mutant strains has indicated that the long-chain acyl-CoA to be utilized for lipid synthesis, but not that to be degraded via beta-oxidation, is involved in the repression of acetyl-CoA carboxylase.