Document Detail


A bacterial homolog to the mitochondrial enoyl-CoA hydratase.
MedLine Citation:
PMID:  1743516     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A 257-amino acid (aa) open reading frame in the photosynthetic bacterium, Rhodobacter capsulatus, shows significant homology to the mitochondrial enoyl-CoA hydratase (290 aa). This similarity in size and sequence suggests that R. capsulatus oxidizes fatty acids using specific components, more like the mitochondrial system than the multifunctional component system of Escherichia coli.
Authors:
D L Beckman; R G Kranz
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Gene     Volume:  107     ISSN:  0378-1119     ISO Abbreviation:  Gene     Publication Date:  1991 Oct 
Date Detail:
Created Date:  1992-01-13     Completed Date:  1992-01-13     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  7706761     Medline TA:  Gene     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  171-2     Citation Subset:  IM    
Affiliation:
Department of Biology, Washington University, St. Louis, MO 63130.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/M59727;  M59728;  S68775;  S69445;  S69486;  S69499;  S69505;  S69519;  S69521;  X60194
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Enoyl-CoA Hydratase / genetics*
Mitochondria / enzymology
Molecular Sequence Data
Open Reading Frames / genetics
Rats
Rhodobacter capsulatus / enzymology*,  genetics
Sequence Homology, Nucleic Acid*
Grant Support
ID/Acronym/Agency:
BRSGS07 RR077054/RR/NCRR NIH HHS; GM 39106/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
EC 4.2.1.17/Enoyl-CoA Hydratase

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


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