Document Detail


Molecular cloning and expression of human carnitine octanoyltransferase: evidence for its role in the peroxisomal beta-oxidation of branched-chain fatty acids.
MedLine Citation:
PMID:  10486279     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
To study the putative role of human carnitine octanoyltransferase (COT) in the beta-oxidation of branched-chain fatty acids, we identified and cloned the cDNA encoding human COT and expressed it in the yeast Saccharomyces cerevisiae. Enzyme activity measurements showed that COT efficiently converts one of the end products of the peroxisomal beta-oxidation of pristanic acid, 4, 8-dimethylnonanoyl-CoA, to its corresponding carnitine ester. Production of the carnitine ester of this branched/medium-chain acyl-CoA within the peroxisome is required for its transport to the mitochondrion where further beta-oxidation occurs. In contrast, 4, 8-dimethylnonanoyl-CoA is not a substrate for carnitine acetyltransferase, another acyltransferase localized in peroxisomes, which catalyzes the formation of carnitine esters of the other products of pristanic acid beta-oxidation, namely acetyl-CoA and propionyl-CoA. Our results shed new light on the function of COT in fatty acid metabolism and point to a crucial role of COT in the beta-oxidation of branched-chain fatty acids.
Authors:
S Ferdinandusse; J Mulders; L IJlst; S Denis; G Dacremont; H R Waterham; R J Wanders
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Publication Detail:
Type:  Comparative Study; In Vitro; Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  263     ISSN:  0006-291X     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  1999 Sep 
Date Detail:
Created Date:  1999-10-21     Completed Date:  1999-10-21     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  213-8     Citation Subset:  IM    
Copyright Information:
Copyright 1999 Academic Press.
Affiliation:
Departments of Clinical Chemistry and Pediatrics, Emma Children's Hospital, Academic Medical Center, Amsterdam, 1100 DE, The Netherlands.
Data Bank Information
Bank Name/Acc. No.:
GENBANK/AF168793
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Base Sequence
Carnitine Acyltransferases / genetics*,  metabolism*
Cattle
Cloning, Molecular
DNA Primers / genetics
DNA, Complementary / genetics
Fatty Acids / metabolism*
Gene Expression
Humans
Microbodies / metabolism
Molecular Sequence Data
Oxidation-Reduction
Rats
Recombinant Proteins / genetics,  metabolism
Saccharomyces cerevisiae / genetics
Sequence Homology, Amino Acid
Species Specificity
Chemical
Reg. No./Substance:
0/DNA Primers; 0/DNA, Complementary; 0/Fatty Acids; 0/Recombinant Proteins; 1189-37-3/pristanic acid; EC 2.3.1.-/Carnitine Acyltransferases; EC 2.3.1.-/carnitine octanoyltransferase

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


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