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Indexed by:期刊论文

Date of Publication:2012-06-01

Journal:BIOTECHNOLOGY LETTERS

Included Journals:SCIE、EI、PubMed

Volume:34

Issue:6

Page Number:1107-1113

ISSN No.:0141-5492

Key Words:C-C bond hydrolase; Esterase; Homology modeling; Molecular docking

Abstract: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.