文献类型：期刊文献

英文题名：Structure-based stabilization of an enzyme:: The case of penicillin acylase from Alcaligenes faecalis

作者：Wang, TW; Zhu, H; Ma, XY; Ma, YS; Wei, DZ

机构：[1]E China Univ Sci & Technol, State Key Lab Bioreactor Engn, New World Inst Biotechnol, Shanghai 200237, Peoples R China

年份：2006

卷号：13

期号：2

起止页码：177

外文期刊名：PROTEIN AND PEPTIDE LETTERS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000235725700013)】；

语种：英文

外文关键词：thermal stability; penicillin acylase; site-directed mutagenesis; homology modeling; double mutations

摘要：The modeled structure of penicillin acylase from Alcaligenes faecali (AFPGA) was constructed by comparative modeling with the Modeller program. Candidate positions that could be replaced with cysteine were estimated by scanning the modeled structure of AFPGA with the program MODIP (modeling disulfide bond in protein). The mutant Q3C/P751C had a higher optimum temperature by three degrees than that of the wild type AFPGA. The half life of the double mutant Q3C/P751C at 55 degrees C was increased by 50%. To our knowledge, this was the first structure-based genetic modification of AFPGA.