Song S, Steinbüchel A
Biology Institute, Hebei Academy of Sciences, Shijazhuang 050051, China.
Wei Sheng Wu Xue Bao. 2001 Aug;41(4):402-7.
An esterase-positive clone was isolated by screening a genomic library of Ralstonia eutropha CH34 constructed in Escherichia coli S17-1 with top agar containing alpha-naphtyl acetate and Fast Blue RR. A gne encoding esterase activity, estA was subcloned from this clone. Nucleotide sequencing of estA showed that it was a 825 bp open reading frame, encoding an esterase EstA, composed of 275 amino acids with a predicted molecular mass of 30,785 D. Homology analysis revealed that EstA exhibited significant amino acid similarity with the enzymes involved in the meta-cleavage pathway in the metaboleism of aromatic acid compounds.
通过用含有α-萘基乙酸和固蓝RR的顶层琼脂筛选在大肠杆菌S17-1中构建的真养产碱菌CH34基因组文库，分离出一个酯酶阳性克隆。从该克隆中亚克隆出一个编码酯酶活性的基因estA。estA的核苷酸测序表明，它是一个825 bp的开放阅读框，编码一种酯酶EstA，由275个氨基酸组成，预测分子量为30785 D。同源性分析表明，EstA与芳香酸化合物代谢中参与间位裂解途径的酶具有显著的氨基酸相似性。
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