Anderson D H, Rodwell V W
Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907.
J Bacteriol. 1989 Dec;171(12):6468-72. doi: 10.1128/jb.171.12.6468-6472.1989.
The mva operon of Pseudomonas mevalonii encodes two enzymes that can convert internalized mevalonate into acetoacetate and acetyl-coenzyme A (CoA). The promoter-proximal gene of this operon is mvaA, the structural gene for 3-hydroxy-3-methylglutaryl (HMG)-CoA reductase (EC 1.1.1.88). The cloning, characterization, and expression of mvaA has been reported (M. J. Beach and V. W. Rodwell, J. Bacteriol. 171:2994-3001, 1989). We report here the nucleotide sequence of another gene of this operon, mvaB, its expression in Escherichia coli, and its identification as the structural gene for HMG-CoA lyase (EC 4.1.3.4). P. mevalonii HMG-CoA lyase is a cytosolic protein with 301 amino acid residues and a molecular weight of 31,600. This represents the first reported sequence of an HMG-CoA lyase from any source.
甲基营养型假单胞菌的mva操纵子编码两种酶，可将内化的甲羟戊酸转化为乙酰乙酸和乙酰辅酶A（CoA）。该操纵子中靠近启动子的基因是mvaA，即3-羟基-3-甲基戊二酰（HMG）-CoA还原酶（EC 1.1.1.88）的结构基因。mvaA的克隆、特性鉴定及表达已有报道（M. J. 比奇和V. W. 罗德韦尔，《细菌学杂志》171:2994 - 3001, 1989年）。我们在此报告该操纵子另一个基因mvaB的核苷酸序列、其在大肠杆菌中的表达以及其作为HMG-CoA裂解酶（EC 4.1.3.4）结构基因的鉴定。甲基营养型假单胞菌HMG-CoA裂解酶是一种胞质蛋白，有301个氨基酸残基，分子量为31,600。这是首次报道的来自任何来源的HMG-CoA裂解酶的序列。
