Document Detail

Identification of a novel mycobacterial 3-hydroxyacyl-thioester dehydratase, HtdZ (Rv0130), by functional complementation in yeast.
MedLine Citation:
PMID:  18375556     Owner:  NLM     Status:  MEDLINE    
We report on the identification of Mycobacterium tuberculosis HtdZ (Rv0130), representing a novel 3-hydroxyacyl-thioester dehydratase. HtdZ was picked up by the functional complementation of Saccharomyces cerevisiae htd2Delta cells lacking the dehydratase of mitochondrial type II fatty acid synthase. Mutant cells expressing HtdZ contained dehydratase activity, recovered their respiratory ability, and partially restored de novo lipoic acid synthesis.
Aner Gurvitz; J Kalervo Hiltunen; Alexander J Kastaniotis
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-03-28
Journal Detail:
Title:  Journal of bacteriology     Volume:  190     ISSN:  1098-5530     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2008 Jun 
Date Detail:
Created Date:  2008-05-16     Completed Date:  2008-07-03     Revised Date:  2011-04-06    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  4088-90     Citation Subset:  IM    
Section of Physiology of Lipid Metabolism, Institute of Physiology, Center for Physiology and Pathophysiology, Medical University of Vienna, Vienna, Austria.
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MeSH Terms
Bacterial Proteins / chemistry,  genetics,  metabolism*
Enoyl-CoA Hydratase / chemistry,  genetics,  metabolism*
Genetic Complementation Test
Mycobacterium tuberculosis / enzymology*,  genetics
Organisms, Genetically Modified
Oxygen Consumption / physiology
Saccharomyces cerevisiae / genetics,  metabolism*
Grant Support
P 19378-B03//Austrian Science Fund FWF; P 19399-B03//Austrian Science Fund FWF
Reg. No./Substance:
0/Bacterial Proteins; EC Hydratase

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