Jäger W, Peters-Wendisch P G, Kalinowski J, Pühler A
Lehrstuhl für Genetik, Universität Bielefeld, Postfach 100131, D-33501 Bielefeld, Germany.
Arch Microbiol. 1996 Aug;166(2):76-82. doi: 10.1007/s002030050359.
Following the analysis of transposon Tn5432-induced mutants of Corynebacterium glutamicum ATCC 13032, a gene encoding a protein with a biotin-binding motif was cloned. The DNA sequence of this gene revealed an open reading frame encoding 591 amino acids with a calculated mol. mass of 63.4 kDa. The protein is composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein, that are highly similar to corresponding subunits from prokaryotic and eukaryotic biotin enzymes. Over 70% identity was found to a protein from Mycobacterium leprae proposed to be part of an acyl-CoA carboxylase. Since it was not possible to inactivate the C. glutamicum gene, the gene most likely encodes a subunit of the essential acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis.
在对转座子Tn5432诱导的谷氨酸棒杆菌ATCC 13032突变体进行分析之后，一个编码具有生物素结合基序蛋白的基因被克隆出来。该基因的DNA序列显示一个开放阅读框，编码591个氨基酸，计算分子量为63.4 kDa。该蛋白质由两个结构域组成，一个N端生物素羧化酶和一个C端生物素羧基载体蛋白，它们与原核和真核生物素酶的相应亚基高度相似。发现与麻风分枝杆菌中一种被认为是酰基辅酶A羧化酶一部分的蛋白质有超过70%的同一性。由于无法使谷氨酸棒杆菌基因失活，该基因很可能编码必需的乙酰辅酶A羧化酶的一个亚基，该酶催化脂肪酸合成中的关键步骤。
