| Physcomitrella PpORS, basal to plant type III polyketide synthases in phylogenetic trees, is a very long chain 2'-oxoalkylresorcinol synthase. | |
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MedLine Citation:
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PMID: 23223578 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The plant type III polyketide synthases (PKSs), which produce diverse secondary metabolites with different biological activities, have successfully co-evolved with land plants. To gain insight into the roles that ancestral type III PKSs played during the early evolution of land plants, we cloned and characterized PpORS from the moss Physcomitrella. PpORS has been proposed to closely resemble the most recent common ancestor of the plant type III PKSs. PpORS condenses a very long chain fatty acyl-CoA with four molecules of malonyl-CoA and catalyzes decarboxylative aldol cyclization to yield the pentaketide 2'-oxoalkylresorcinol. Therefore, PpORS is a 2'-oxoalkylresorcinol synthase. Structure modeling and sequence alignments identified a unique set of amino acid residues (Gln(218), Val(277), and Ala(286)) at the putative PpORS active site. Substitution of the Ala(286) to Phe apparently constricted the active site cavity, and the A286F mutant instead produced triketide alkylpyrones from fatty acyl-CoA substrates with shorter chain lengths. Phylogenetic analysis and comparison of the active sites of PpORS and alkylresorcinol synthases from sorghum and rice suggested that the gramineous enzymes evolved independently from PpORS to have similar functions but with distinct active site architecture. Microarray analysis revealed that PpORS is exclusively expressed in nonprotonemal moss cells. The in planta function of PpORS, therefore, is probably related to a nonprotonemal structure, such as the cuticle. |
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Authors:
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Sun Young Kim; Che C Colpitts; Gertrud Wiedemann; Christina Jepson; Mehrieh Rahimi; Jordan R Rothwell; Adam D McInnes; Mitsuyasu Hasebe; Ralf Reski; Brian T Sterenberg; Dae-Yeon Suh |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-12-07 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 288 ISSN: 1083-351X ISO Abbreviation: J. Biol. Chem. Publication Date: 2013 Jan |
Date Detail:
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Created Date: 2013-01-28 Completed Date: 2013-04-02 Revised Date: 2013-04-16 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 2767-77 Citation Subset: IM |
Affiliation:
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Department of Chemistry and Biochemistry, University of Regina, Regina, Saskatchewan S4S 0A2, Canada. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Acyl Coenzyme A
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chemistry Binding Sites Bryopsida / metabolism* Catalysis Catalytic Domain Cloning, Molecular Expressed Sequence Tags Gene Expression Regulation, Enzymologic Kinetics Models, Chemical Mutagenesis, Site-Directed Mutation Oligonucleotide Array Sequence Analysis Phylogeny Polyketide Synthases / chemistry, metabolism* Protein Binding Recombinant Proteins / chemistry |
| Chemical | |
Reg. No./Substance:
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0/Acyl Coenzyme A; 0/Recombinant Proteins; 79956-01-7/Polyketide Synthases |
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