Document Detail

The multifunctional protein in peroxisomal beta-oxidation: structure and substrate specificity of the Arabidopsis thaliana protein MFP2.
MedLine Citation:
PMID:  20463021     Owner:  NLM     Status:  MEDLINE    
Plant fatty acids can be completely degraded within the peroxisomes. Fatty acid degradation plays a role in several plant processes including plant hormone synthesis and seed germination. Two multifunctional peroxisomal isozymes, MFP2 and AIM1, both with 2-trans-enoyl-CoA hydratase and l-3-hydroxyacyl-CoA dehydrogenase activities, function in mouse ear cress (Arabidopsis thaliana) peroxisomal beta-oxidation, where fatty acids are degraded by the sequential removal of two carbon units. A deficiency in either of the two isozymes gives rise to a different phenotype; the biochemical and molecular background for these differences is not known. Structure determination of Arabidopsis MFP2 revealed that plant peroxisomal MFPs can be grouped into two families, as defined by a specific pattern of amino acid residues in the flexible loop of the acyl-binding pocket of the 2-trans-enoyl-CoA hydratase domain. This could explain the differences in substrate preferences and specific biological functions of the two isozymes. The in vitro substrate preference profiles illustrate that the Arabidopsis AIM1 hydratase has a preference for short chain acyl-CoAs compared with the Arabidopsis MFP2 hydratase. Remarkably, neither of the two was able to catabolize enoyl-CoA substrates longer than 14 carbon atoms efficiently, suggesting the existence of an uncharacterized long chain enoyl-CoA hydratase in Arabidopsis peroxisomes.
Susan Arent; Caspar E Christensen; Valerie E Pye; Allan Nørgaard; Anette Henriksen
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2010-05-12
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  285     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-26     Completed Date:  2010-09-14     Revised Date:  2011-08-02    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  24066-77     Citation Subset:  IM    
Protein Chemistry Group, Carlsberg Laboratory, Gamle Carlsberg Vej 10, DK-2500 Valby, Denmark.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Arabidopsis / enzymology*
Arabidopsis Proteins / chemistry*,  metabolism
Crystallography, X-Ray / methods
Fatty Acids / chemistry
Gene Expression Regulation, Plant*
Models, Biological
Oxygen / chemistry*
Peroxisomes / chemistry*
Protein Binding
Protein Conformation
Protein Isoforms
Protein Structure, Tertiary
Substrate Specificity
Reg. No./Substance:
0/Arabidopsis Proteins; 0/Fatty Acids; 0/MFP2 protein, Arabidopsis; 0/Protein Isoforms; 7782-44-7/Oxygen

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

Previous Document:  Structural basis of fatty acid substrate binding to cyclooxygenase-2.
Next Document:  Pro-tumorigenic effects of miR-31 loss in mesothelioma.