Document Detail

Arylamine N-acetyltransferase responsible for acetylation of 2-aminophenols in Streptomyces griseus.
MedLine Citation:
PMID:  17158669     Owner:  NLM     Status:  MEDLINE    
An arylamine N-acetyltransferase (NAT) responsible for the N acetylation of exogenous 3-amino-4-hydroxybenzoic acid in Streptomyces griseus was identified and characterized. This enzyme was distinct from other eukaryotic and bacterial NATs in that it acetylated various 2-aminophenol derivatives more effectively than it acetylated 5-aminosalicylic acid, and thus it may be involved in the metabolism of xenobiotic compounds.
Hirokazu Suzuki; Yasuo Ohnishi; Sueharu Horinouchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2006-12-08
Journal Detail:
Title:  Journal of bacteriology     Volume:  189     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2007 Mar 
Date Detail:
Created Date:  2007-02-15     Completed Date:  2007-03-28     Revised Date:  2013-06-06    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2155-9     Citation Subset:  IM    
Department of Biotechnology, Graduate School of Agriculture and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo 113-8657, Japan.
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MeSH Terms
Aminobenzoates / metabolism*
Aminophenols / metabolism*
Arylamine N-Acetyltransferase / genetics,  physiology*
Base Sequence
Escherichia coli / genetics
Molecular Sequence Data
Recombinant Proteins / biosynthesis
Streptomyces griseus / metabolism*
Substrate Specificity
Reg. No./Substance:
0/Aminobenzoates; 0/Aminophenols; 0/Hydroxybenzoates; 0/Recombinant Proteins; 1571-72-8/3-amino-4-hydroxybenzoic acid; 23RH73DZ65/2-aminophenol; EC N-Acetyltransferase

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