点击次数：

论文类型：期刊论文

发表时间：2012-06-01

发表刊物：BIOTECHNOLOGY LETTERS

收录刊物：SCIE、EI、PubMed

卷号：34

期号：6

页面范围：1107-1113

ISSN号：0141-5492

关键字：C-C bond hydrolase; Esterase; Homology modeling; Molecular docking

摘要：A C-C hydrolase gene (bphD (LA-4) ) from strain Dyella ginsengisoli LA-4 was cloned and expressed in Escherichia coli BL21 (DE3). BphD(LA-4) together with another hydrolase MfphA(LA-4), which derived from the same strain, possessed esterase activities. p-Nitrophenyl butyrate was the best substrate for both enzymes. BphD(LA-4) had high catalytic efficiency to p-nitrophenyl benzoate, whereas MfphA(LA-4) had no activity. Homology modeling and docking studies demonstrated that the proper hydrogen bond interaction was important for the reactivity of specific substrate.