Document Detail

A novel family of bacterial dioxygenases that catalyse the hydroxylation of free L-amino acids.
MedLine Citation:
PMID:  22448874     Owner:  NLM     Status:  Publisher    
L-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterised conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico selected IDO homologues belonging to the PF10014 were cloned and expressed in E. coli. L-methionine, L-leucine, L-isoleucine, and L-threonine were found to be catalysed by the investigated enzymes, producing L-methionine sulfoxide, 4-hydroxyleucine, 4-hydroxyisoleucine, and 4-hydroxythreonine, respectively. An investigation of enzyme kinetics suggested the existence of a novel subfamily of bacterial dioxygenases within the PF10014 family for which free L-amino acids could be accepted as in vivo substrates. A hypothesis regarding the physiological significance of hydroxylated L-amino acids is also discussed. © 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
Sergey V Smirnov; Pavel M Sokolov; Tomohiro Kodera; Masakazu Sugiyama; Makoto Hibi; Sakayu Shimizu; Kenzo Yokozeki; Jun Ogawa
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Publication Detail:
Type:  LETTER     Date:  2012-3-27
Journal Detail:
Title:  FEMS microbiology letters     Volume:  -     ISSN:  1574-6968     ISO Abbreviation:  -     Publication Date:  2012 Mar 
Date Detail:
Created Date:  2012-3-27     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
Ajinomoto-Genetika Research Institute, 1st Dorozhny pr. 1/1, Moscow, 117545, Russia.
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