生物化学
生物
乙酰辅酶A羧化酶
酰基载体蛋白
丙酮酸羧化酶
操纵子
基因
大肠杆菌
分子生物学
酶
作者
Pornpimon Kiatpapan,Hajime Kobayashi,Maki Sakaguchi,Hisayo Ono,Mitsuo Yamashita,Yoshinobu Kaneko,Yoshikatsu Murooka
标识
DOI:10.1128/aem.67.1.426-433.2001
摘要
Genes for subunits of acetyl coenzyme A carboxylase (ACC), which is the enzyme that catalyzes the first step in the synthesis of fatty acids in Lactobacillus plantarum L137, were cloned and characterized. We identified six potential open reading frames, namely, manB, fabH, accB, accC, accD, and accA, in that order. Nucleotide sequence analysis suggested that fabH encoded beta-ketoacyl-acyl carrier protein synthase III, that the accB, accC, accD, and accA genes encoded biotin carboxyl carrier protein, biotin carboxylase, and the beta and alpha subunits of carboxyltransferase, respectively, and that these genes were clustered. The organization of acc genes was different from that reported for Escherichia coli, for Bacillus subtilis, and for Pseudomonas aeruginosa. E. coli accB and accD mutations were complemented by the L. plantarum accB and accD genes, respectively. The predicted products of all five genes were confirmed by using the T7 expression system in E. coli. The gene product of accB was biotinylated in E. coli. Northern and primer extension analyses demonstrated that the five genes in L. plantarum were regulated polycistronically in an acc operon.
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