FLAVOPROTEINS IN FATTY ACID METABOLISM

脂肪酸代谢中的黄素蛋白

• 批准号: 3274042
• 负责人: Colin Thorpe
• 金额: $ 9.37万
• 依托单位: UNIVERSITY OF DELAWARE
• 依托单位国家: 美国
• 财政年份: 1979
• 资助国家: 美国
• 起止时间: 1979-07-01 至 1987-06-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/3274042
• 关键词: acyl coA dehydrogenases; affinity chromatography; chemical association; electron transport; enzyme structure; enzyme substrate complex; fatty acid metabolism; flavoproteins; gel filtration chromatography; kidney; ligands; oxidation reduction reaction; physical separation; spectrometry; stoichiometry

The overall objective of this research is to gain greater insight into the structure, mechanism of action and metabolic control of acyl-CoA dehydrogenases. Inactive derivatives of the pig kidney acyl-CoA dehydrogenase with iodoacetic acid and several dione reagents are under investigation to identify catalytically essential amino acid residues. Two mechanism based inhibitors of the enzyme, methylenecylcopropylacetyl-CoA and 3,4-pentadienoyl-CoA, are under investigation and preliminary results are suggestive of a mechanism of substrate dehydrogenation involving carbanion formation. The mechanism of stabilization of the red, anionic, seiquinone by acyl-CoA derivatives is under investigation. The results should aid in the interpretation of the mechanism of action of these acyl-CoA dehydrogenases. We will extend our preliminary studies on the reconstitution of pig kidney general acyl-CoA dehydrogenase using ring modified flavin analogs. Efforts will continue to develop a satisfactory purification scheme for pig kidney electron transferring flavoprotein.

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