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

Tianwen Wang; Hu Zhu; Xingyuan Ma; Yushu Ma; Dongzhi Wei

doi:10.2174/092986606775101571

ISSN: 0929-8665
E-ISSN: 1875-5305

Structure-Based Stabilization of an Enzyme: The Case of Penicillin Acylase from Alcaligenes faecalis
Authors: Tianwen Wang¹, Hu Zhu², Xingyuan Ma³, Yushu Ma⁴ and Dongzhi Wei⁵
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¹ State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China. ² State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China. ³ State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China. ⁴ State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China. ⁵ State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China.
Source: Protein and Peptide Letters, Volume 13, Issue 2, Feb 2006, p. 177 - 183
DOI: https://doi.org/10.2174/092986606775101571
- Available online: 01 Feb 2006

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.

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2006-02-01

2025-05-20

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Article Type: Research Article

Keyword(s): Double mutations; Homology modeling; Penicillin acylase; Site-directed mutagenesis; Thermal stability

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

Abstract

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