Regulation of enzymes by fatty acyl coenzyme A. Site-specific binding of fatty acyl coenzyme A by citrate synthase--a spin-labeling study.

作者: Gary L. Powell , Anthony V. Caggiano

DOI: 10.1016/S0021-9258(17)30144-8

关键词:

摘要: 4.1.3.7) at about the same concentration as did palmitoyl-CoA. Competitive binding studies show acetyl-CoA and ATP to displace 6- 16-doxylstearoyl-CoA from citrate synthase but little while oxalacetate NADPH compete very effectively. These may suggest by fatty acyl-CoA sites apart site. The differential displacement argues against of a general nucleotide spectrum 6-doxylstearoyl-CoA in presence high concentrations was for an immobilized spin label; under conditions mobile. spectral differences were interpreted terms specific site which portion acyl chain proximal thioester methyl end allowed greater motional freedom. Phospholipid vesicles included label not that 6doxylstearoyl-CoA excess support above interpretation. A model on with provision interaction biological membrane is presented. Site-specific provides strong physiological role regulation analogy other related enzymes lipid metabolism.

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