Abstract
Site-directed mutagenesis was used to examine the roles of the conserved histidine, arginine and cysteine residues in acid phosphatase from Prevotella intermedia (PiACP). The replacement of histidine and arginine residues resulted in the elimination of the PiACP activity while the cysteine mutants retained activity. These results suggest that the histidine and arginine residues are essential for catalysis.
Keywords: prevotella intermedia acp, piacp, acid phosphatase, site-directed mutagenesis
Protein & Peptide Letters
Title: Kinetic and Site-Directed Mutagenesis Studies of Prevotella Intermedia Acid Phosphatase
Volume: 10 Issue: 1
Author(s): Xiaochi Chen, Toshihiro Ansai, Sailen Barik and Tadamichi Takehara
Affiliation:
Keywords: prevotella intermedia acp, piacp, acid phosphatase, site-directed mutagenesis
Abstract: Site-directed mutagenesis was used to examine the roles of the conserved histidine, arginine and cysteine residues in acid phosphatase from Prevotella intermedia (PiACP). The replacement of histidine and arginine residues resulted in the elimination of the PiACP activity while the cysteine mutants retained activity. These results suggest that the histidine and arginine residues are essential for catalysis.
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Cite this article as:
Chen Xiaochi, Ansai Toshihiro, Barik Sailen and Takehara Tadamichi, Kinetic and Site-Directed Mutagenesis Studies of Prevotella Intermedia Acid Phosphatase, Protein & Peptide Letters 2003; 10 (1) . https://dx.doi.org/10.2174/0929866033408282
DOI https://dx.doi.org/10.2174/0929866033408282 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
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