A novel low-temperature-active beta-glucosidase from symbiotic Serratia sp TN49 reveals four essential positions for substrate accommodation

文献类型： 外文期刊

第一作者： Zhou, Junpei

作者： Zhou, Junpei;Zhang, Rui;Shi, Pengjun;Huang, Huoqing;Meng, Kun;Yuan, Tiezheng;Yang, Peilong;Yao, Bin;Zhou, Junpei

作者机构：

关键词： Longhorned beetle;Symbiotic Serratia sp.;Low-temperature-active beta-glucosidase;Gut;Ligand docking

期刊名称：APPLIED MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：4.813； 五年影响因子：4.697 ）

ISSN： 0175-7598

年卷期： 2011 年 92 卷 2 期

页码：

收录情况： SCI

摘要： A 2,373-bp full-length gene (bglA49) encoding a 790-residue polypeptide (BglA49) with a calculated mass of 87.8 kDa was cloned from Serratia sp. TN49, a symbiotic bacterium isolated from the gut of longhorned beetle (Batocera horsfieldi) larvae. The deduced amino acid sequence of BglA49 showed the highest identities of 80.1% with a conceptually translated protein from Pantoea sp. At-9b (EEW02556), 38.3% with the identified glycoside hydrolase (GH) family 3 beta-glucosidase from Clostridium stercorarium NCBI 11754 (CAB08072), and < 15.0% with the low-temperature-active GH 3 beta-glucosidases from Shewanella sp. G5 (ABL09836) and Paenibacillus sp. C7 (AAX35883). The recombinant enzyme (r-BglA49) was expressed in Escherichia coli and displayed the typical characteristics of low-temperature-active enzymes, such as low temperature optimum (showing apparent optimal activity at 35A degrees C), activity at low temperatures (retaining similar to 60% of its maximum activity at 20A degrees C and similar to 25% at 10A degrees C). Compared with the thermophilic GH 3 beta-glucosidase, r-BglA49 had fewer hydrogen bonds and salt bridges and less proline residues. These features might relate to the increased structure flexibility and higher catalytic activity at low temperatures of r-BglA49. The molecular docking study of four GH 3 beta-glucosidases revealed five conserved positions contributing to substrate accommodation, among which four positions of r-BglA49 (R192, Y228, D260, and E449) were identified to be essential based on site-directed mutagenesis analysis.

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