Document Detail


Identification of functionally important amino acids in a novel indigo-producing oxygenase from Rhodococcus sp. strain T104.
MedLine Citation:
PMID:  18404265     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A novel indigo-producing oxygenase gene, designated ipoA (1,197 bp) was characterized from Rhodococcus sp. strain T104. Three indigo-negative mutations (A58V, P59L, and G251D) were obtained through random mutagenesis using an E. coli mutator strain. Subsequent saturation mutagenesis resulted in the identification of nine and three amino acid substitutions that restore activity in the A58V and P59L mutants, respectively. Activity was not restored in the G251D mutation by any other amino acids. Interestingly, activity in the A58V mutant, where a methyl group is only replaced by an isopropyl side chain, is restored by a variety of amino acids, including polar ones. A molecular modeling study suggests that the residues at positions 58, 59, and 251 of the T104 IpoA enzyme are far from the active site, indicating that the mutations must alter the overall structure of the enzyme.
Authors:
Na Ra Kwon; Jong-Chan Chae; Ki Young Choi; Miyoun Yoo; Gerben J Zylstra; Young Min Kim; Beom Sik Kang; Eungbin Kim
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-04-11
Journal Detail:
Title:  Applied microbiology and biotechnology     Volume:  79     ISSN:  0175-7598     ISO Abbreviation:  Appl. Microbiol. Biotechnol.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-05-19     Completed Date:  2008-09-09     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  8406612     Medline TA:  Appl Microbiol Biotechnol     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  417-22     Citation Subset:  IM    
Affiliation:
Department of Biology, Yonsei University, Seoul, Korea.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Amino Acid Substitution
Bacterial Proteins / chemistry*,  genetics,  isolation & purification,  metabolism
Binding Sites
Indoles / chemistry,  metabolism*
Models, Molecular
Molecular Sequence Data
Mutagenesis, Site-Directed
Oxygenases / chemistry*,  genetics,  isolation & purification,  metabolism
Protein Structure, Tertiary
Rhodococcus / chemistry,  enzymology*,  genetics
Sequence Alignment
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Indoles; 482-89-3/indigo; EC 1.13.-/Oxygenases

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


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