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. 1979 Sep;76(9):4390–4394. doi: 10.1073/pnas.76.9.4390

Involvement of long-chain acyl coenzyme A for lipid synthesis in repression of acetyl-coenzyme A carboxylase in Candida lipolytica.

T Kamiryo, Y Nishikawa, M Mishina, M Terao, S Numa
PMCID: PMC411580  PMID: 41242

Abstract

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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