Open AccessInvolvement of long-chain acyl coenzyme A for lipid synthesis in repression of acetyl-coenzyme A carboxylase in Candida lipolytica.
Author(s) -
Tatsuyuki Kamiryo,
Yoshiyuki Nishikawa,
Masayoshi Mishina,
Mineko Terao,
Shosaku Numa
Publication year - 1979
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.76.9.4390
Subject(s) - acetyl coa carboxylase , coenzyme a , biochemistry , dna ligase , pyruvate carboxylase , mutant , fatty acid , fatty acid synthesis , acyl coa , biology , enzyme , beta oxidation , acyl carrier protein , biosynthesis , gene , reductase
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.