Document Detail

Improving the acidic stability of a methyl parathion hydrolase by changing basic residues to acidic residues.
MedLine Citation:
PMID:  22350335     Owner:  NLM     Status:  Publisher    
The acidic stability of a methyl parathion hydrolase (Ochr-MPH) was improved by selectively changing basic amino acids to acidic ones. Mutation sites were selected based on the position-specific amino acid replacement probabilities (more than or equal to 0.2) and the entropy of each site (more than or equal to 0.8). Three mutants (K208E, K277D, and K208E/K277D) were more stable than the wild-type (WT). Their half-lives at pH 5.0 were 64, 68, 65 min, respectively, whereas that of WT was 39 min. The acidic stability of proteins may therefore be improved by changing selected basic amino acid residues to acidic ones.
Lu Huang; Ping Wang; Jian Tian; Huachen Jiang; Ningfeng Wu; Peilong Yang; Bin Yao; Yunliu Fan
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-2-21
Journal Detail:
Title:  Biotechnology letters     Volume:  -     ISSN:  1573-6776     ISO Abbreviation:  -     Publication Date:  2012 Feb 
Date Detail:
Created Date:  2012-2-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8008051     Medline TA:  Biotechnol Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, Beijing, 100081, People's Republic of China,
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