编码两种具有相反立体特异性的恶臭假单胞菌卤代烷酸脱卤酶的操纵子的克隆与部分测序
Cloning and partial sequencing of an operon encoding two Pseudomonas putida haloalkanoate dehalogenases of opposite stereospecificity.
作者信息
Barth P T, Bolton L, Thomson J C
机构信息
Biotechnology Department, ICI Pharmaceuticals, Macclesfield, Cheshire, United Kingdom.
出版信息
J Bacteriol. 1992 Apr;174(8):2612-9. doi: 10.1128/jb.174.8.2612-2619.1992.
Abstract
We have cloned fragments of DNA (up to 13 kb), from Pseudomonas putida AJ1, that code for two stereospecific haloalkanoate dehalogenases. These enzymes are highly specific for D and L substrates. The two genes, designated hadD and hadL, have been isolated and independently expressed in Escherichia coli and P. putida hosts by using broad-host-range vectors. They are closely adjacent and inducible in what appears to be an operon with an upstream open reading frame of unknown function. Nucleotide sequence determination of hadD predicts a mature, cytoplasmic protein of 300 amino acid residues (molecular weight of 33,601). This has no significant homology with the L-specific haloalkanoate dehalogenases from Pseudomonas sp. strain CBS3 (B. Schneider, R. Muller, R. Frank, and F. Lingens, J. Bacteriol. 173:1530-1535, 1991) nor with any other known DNA or protein sequences.
摘要
我们从恶臭假单胞菌AJ1中克隆出了DNA片段（长达13 kb），这些片段编码两种立体特异性卤代烷酸脱卤酶。这些酶对D型和L型底物具有高度特异性。已分离出两个基因，分别命名为hadD和hadL，并通过使用广宿主范围载体在大肠杆菌和恶臭假单胞菌宿主中独立表达。它们紧密相邻，且在一个似乎带有功能未知的上游开放阅读框的操纵子中是可诱导的。hadD的核苷酸序列测定预测其成熟的胞质蛋白由300个氨基酸残基组成（分子量为33,601）。这与来自假单胞菌属菌株CBS3的L特异性卤代烷酸脱卤酶（B. 施奈德、R. 米勒、R. 弗兰克和F. 林根斯，《细菌学杂志》173:1530 - 1535，1991）以及任何其他已知的DNA或蛋白质序列均无显著同源性。
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