Document Detail


Physcomitrella PpORS, basal to plant type III polyketide synthases in phylogenetic trees, is a very long chain 2'-oxoalkylresorcinol synthase.
MedLine Citation:
PMID:  23223578     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
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:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-12-07
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  288     ISSN:  1083-351X     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-01-28     Completed Date:  2013-04-02     Revised Date:  2014-01-28    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2767-77     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acyl Coenzyme A / 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:
0/Acyl Coenzyme A; 0/Recombinant Proteins; 79956-01-7/Polyketide Synthases
Comments/Corrections

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