Document Detail

Identification of ω-aminotransferase from Caulobacter crescentus and site-directed mutagenesis to broaden substrate specificity.
MedLine Citation:
PMID:  18239415     Owner:  NLM     Status:  MEDLINE    
A putative aminotransferase gene, cc3143 (aptA), from Caulobacter crescentus was screened by bioinformatical tools and overexpressed in E. coli, and the substrate specificity of the aminotransferase was investigated. AptA showed high activity for short-chain beta-amino acids. It showed the highest activity for 3-amino-n-butyric acid. It showed higher activity toward aromatic amines than aliphatic amines. The 3D model of the aminotransferase was constructed by homology modeling using a dialkylglycine decarboxylase PDB ID: 1DGE) as a template. Then, the aminotransferase was rationally redesigned to increase the activity for 3-amino- 3-phenylpropionic acid. The mutants N285A and V227G increased the relative activity for 3-amino-3-phenylpropionic acid to 3-amino-n-butyric acid by 11-fold and 3-fold, respectively, over that of wild type.
Bum-Yeol Hwang; Seung-Hyun Ko; Hyung-Yeon Park; Joo-Hyun Seo; Bon-Su Lee; Byung-Gee Kim
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of microbiology and biotechnology     Volume:  18     ISSN:  1017-7825     ISO Abbreviation:  J. Microbiol. Biotechnol.     Publication Date:  2008 Jan 
Date Detail:
Created Date:  2008-02-01     Completed Date:  2008-05-20     Revised Date:  2013-10-18    
Medline Journal Info:
Nlm Unique ID:  9431852     Medline TA:  J Microbiol Biotechnol     Country:  Korea (South)    
Other Details:
Languages:  eng     Pagination:  48-54     Citation Subset:  IM    
School of Chemical Engineering, and Institute for Molecular Biology and Genetics, Seoul National University, Seoul 151-742, Korea.
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MeSH Terms
Amino Acid Sequence
Amino Acids, Aromatic / metabolism
Caulobacter crescentus / enzymology*,  genetics
Computational Biology / methods
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed*
Structure-Activity Relationship
Substrate Specificity
Transaminases / chemistry,  genetics*,  metabolism*
Reg. No./Substance:
0/Amino Acids, Aromatic; EC 2.6.1.-/Transaminases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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