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

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Passive modulation of blood-group antigens.

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

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

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kamiryo, T. Nishikawa, Y. Mishina, M. Numa, S. Terao, M.
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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	9
Volume Number	76
Language	English
Publisher	National Academy of Sciences
Publisher Date	1979-01-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Acetyl-CoA Carboxylase Metabolism Acyl Coenzyme A Candida Enzymology Coenzyme A Ligases Enzyme Repression Ligases Lipids Biosynthesis Genetics Lipid Metabolism Oxidation-Reduction Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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