Department of Biology and Chemistry, City University of Hong Kong, 83 Tat Chee Avenue, Kowloon, Hong Kong, PR China.
Bioorg Med Chem Lett. 2011 Nov 15;21(22):6667-73. doi: 10.1016/j.bmcl.2011.09.062. Epub 2011 Sep 21.
Glutaryl-CoA dehydrogenase catalyzes the oxidative decarboxylation of the γ-carboxylate of the substrate, glutaryl-CoA, to yield crotonyl-CoA and CO(2). The enzyme is a member of the acyl-CoA dehydrogenase (ACD) family of flavoproteins. In the present study, the catalytic properties of this enzyme, including its substrate specificity, isomerase activity, and interactions with inhibitors, were systematically studied. Our results indicated that the enzyme has its catalytic properties very similar to those of short-chain and medium-chain acyl-CoA dehydrogenase except its additional decarboxylation reaction. Therefore, the inhibitors of fatty acid oxidation targeting straight chain acyl-CoA dehydrogenase could also function as inhibitors for amino acid metabolism of lysine, hydroxylysine, and tryptophan.
谷氨酰辅酶 A 脱氢酶催化底物谷氨酰辅酶 A 的 γ-羧酸盐的氧化脱羧，生成巴豆酰辅酶 A 和 CO2。该酶是酰基辅酶 A 脱氢酶 (ACD) 家族黄素蛋白的成员。在本研究中，系统研究了该酶的催化特性，包括其底物特异性、异构酶活性以及与抑制剂的相互作用。我们的结果表明，该酶除了具有额外的脱羧反应外，其催化特性与短链和中链酰基辅酶 A 脱氢酶非常相似。因此，针对直链酰基辅酶 A 脱氢酶的脂肪酸氧化抑制剂也可以作为赖氨酸、羟赖氨酸和色氨酸氨基酸代谢的抑制剂。
