The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver.
The purification and characterization of glutaryl-coenzyme A dehydrogenase from porcine and human liver.
复制标题
猪和人肝脏中戊二酰辅酶 A 脱氢酶的纯化和表征。
DOI：
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发表时间：
1986
影响因子：
4.8
通讯作者：
S. Goodman
中科院分区：
文献类型：
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作者：
A. Lenich;S. Goodman
戊二酰辅酶a脱氢酶是一种多功能酶，负责将戊二酰辅酶a脱氢和脱羧为巴豆酰辅酶a，已从猪肝线粒体中纯化了1680倍。纯化的猪酶亚基分子量为47,800，天然分子量为190,500。猪戊二酰辅酶a脱氢酶催化[1,5-14C]戊二酰辅酶a以1:1:1的比例转化为[14C]巴豆酰辅酶a和14CO2。猪酶的电子转移黄蛋白Km值为1.1 μ m，戊二酰辅酶a脱氢酶Km值为3.3 μ m，戊二酰辅酶a脱氢酶Km值为860 mol /min/mol，戊二酰辅酶a脱氢酶Km值为327 mol /min/mol。人戊二酰辅酶a脱氢酶已从人肝脏线粒体中纯化了1278倍。纯化的人酶亚基分子量为58,800，天然分子量为256,000。人戊二酰辅酶a脱氢酶与猪戊二酰辅酶a脱氢酶的双免疫扩散分析结果表明，人戊二酰辅酶a脱氢酶与猪戊二酰辅酶a脱氢酶具有部分同源性。
Glutaryl-CoA dehydrogenase, a multifunctional enzyme responsible for dehydrogenation and decarboxylation of glutaryl-CoA to crotonyl-CoA, has been purified 1,680-fold from porcine liver mitochondria. The purified porcine enzyme has a subunit molecular weight of 47,800 and a native molecular weight of 190,500. Porcine glutaryl-CoA dehydrogenase catalyzed the conversion of [1,5-14C]glutaryl-CoA to [14C] crotonyl-CoA and 14CO2 in a 1:1:1 ratio. The porcine enzyme has Km values for electron transfer flavoprotein and glutaryl-CoA of 1.1 and 3.3 microM, respectively, and turnover numbers of 860 mol of electron transfer flavoprotein/min/mol of glutaryl-CoA dehydrogenase and 327 mol of glutaryl-CoA/min/mol of glutaryl-CoA dehydrogenase. Human glutaryl-CoA dehydrogenase has been purified 1,278-fold from human liver mitochondria. The purified human enzyme has a subunit molecular weight of 58,800 and a native molecular weight of 256,000. Human glutaryl-CoA dehydrogenase showed a reaction of only partial identity when compared to porcine glutaryl-CoA dehydrogenase by Ouchterlony double immunodiffusion analysis using antiserum raised against and monospecific for porcine glutaryl-CoA dehydrogenase.