Structure-Based Stabilization of an Enzyme: The Case of Penicillin Acylase from Alcaligenes faecalis

Title: Structure-Based Stabilization of an Enzyme: The Case of Penicillin Acylase from Alcaligenes faecalis

Volume: 13 Issue: 2

Author(s): Tianwen Wang, Hu Zhu, Xingyuan Ma, Yushu Ma and Dongzhi Wei

Affiliation:

Keywords: Thermal stability, Penicillin acylase, Site-directed mutagenesis, Homology modeling, Double mutations

Abstract: 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°C was increased by 50%. To our knowledge, this was the first structure-based genetic modification of AFPGA.

Cite this article as:

Wang Tianwen, Zhu Hu, Ma Xingyuan, Ma Yushu and Wei Dongzhi, Structure-Based Stabilization of an Enzyme: The Case of Penicillin Acylase from Alcaligenes faecalis, Protein & Peptide Letters 2006; 13 (2) . https://dx.doi.org/10.2174/092986606775101571