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

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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.





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

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986606775101571

Affiliations: State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology, Shanghai 200237, P.R. China.

Publication date: February 1, 2006

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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