枯草芽孢杆菌α-酮戊二酸脱氢酶复合体的遗传学
Genetics of the alpha-ketoglutarate dehydrogenase complex of Bacillus subtilis.
作者信息
Hoch J A, Coukoulis H J
出版信息
J Bacteriol. 1978 Jan;133(1):265-9. doi: 10.1128/jb.133.1.265-269.1978.
Abstract
The enzymatic defects in a number of Bacillus subtilis mutants of the alpha-ketoglutarate dehydrogenase complex lacking activity have been investigated. Mutants in the citK locus, as well as a series of deletions of unknown length covering the citK locus, are deficient in E1 of the complex, alpha-ketoglutarate dehydrogenase, but have normal activities of E2, dehydrolipoyl transsuccinylase, and E3, lipoamide dehydrogenase. The citK mutants and the citL22 mutant show in vitro complementation of alpha-ketoglutarate dehydrogenase complex activity. The citL22 mutant is severely deficient in lipoamide dehydrogenase activity, and, as a result, lacks activity for both the alpha-ketoglutarate and the pyruvate dehydrogenase complexes. Thus, the E3 components of both complexes are identical. The citL22 mutation maps between ura and metC on the chromosome.
摘要
对一些缺乏活性的α-酮戊二酸脱氢酶复合体的枯草芽孢杆菌突变体中的酶缺陷进行了研究。citK基因座中的突变体，以及一系列覆盖citK基因座但长度未知的缺失突变体，复合体的E1（α-酮戊二酸脱氢酶）存在缺陷，但E2（二氢硫辛酰转琥珀酰酶）和E3（硫辛酰胺脱氢酶）具有正常活性。citK突变体和citL22突变体在体外表现出α-酮戊二酸脱氢酶复合体活性的互补。citL22突变体的硫辛酰胺脱氢酶活性严重缺乏，因此，α-酮戊二酸和丙酮酸脱氢酶复合体均缺乏活性。因此，这两种复合体的E3成分是相同的。citL22突变位于染色体上ura和metC之间。
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