Document Detail


Streptomyces coelicolor RedP and FabH enzymes, initiating undecylprodiginine and fatty acid biosynthesis, exhibit distinct acyl-CoA and malonyl-acyl carrier protein substrate specificities.
MedLine Citation:
PMID:  22136753     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
RedP is proposed to initiate undecylprodiginine biosynthesis in Streptomyces coelicolor by condensing an acyl-CoA with malonyl-ACP, and is homologous to FabH which catalyzes the same reaction for initiation of fatty acid biosynthesis. Herein, we report the substrate specificities of RedP and FabH from assays using pairings of two acyl-CoA substrates (acetyl-CoA and isobutyryl-CoA) and two malonyl-ACP substrates (malonyl-RedQ and malonyl-FabC). RedP activity was observed only with a pairing of acetyl-CoA and malonyl-RedQ, consistent with its proposed role in initiating formation of acetyl CoA-derived prodiginines. Malonyl-FabC is not a substrate for RedP, indicating that ACP specificity is one of the factors that permit a separation between prodiginine and fatty acid biosynthetic processes. FabH demonstrated greater catalytic efficiency for isobutyryl-CoA in comparison to acetyl-CoA using malonyl-FabC, consistent with the observation that in streptomycetes, a broad mixture of fatty acids is synthesized, with those derived from branched chain acyl-CoA starter units predominating. Diminished FabH activity was also observed using malonyl-RedQ with the same preference for isobutyryl-CoA, completing biochemical and genetic evidence that in the absence of RedP this enzyme can produce branched alkyl chain prodiginines.
Authors:
Renu Singh; Sangjoon Mo; Galina Florova; Kevin A Reynolds
Related Documents :
1883713 - Distribution of a novel mycolic acid in species of the genus mycobacterium.
6874203 - Qualitative analysis of waste-water from ametryne production.
22396453 - Early parenteral nutrition evokes a phenotype of autophagy deficiency in liver and skel...
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2011-12-2
Journal Detail:
Title:  FEMS microbiology letters     Volume:  -     ISSN:  1574-6968     ISO Abbreviation:  -     Publication Date:  2011 Dec 
Date Detail:
Created Date:  2011-12-5     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7705721     Medline TA:  FEMS Microbiol Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Copyright Information:
© 2011 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.
Affiliation:
Department of Chemistry, Portland State University, Portland, Oregon, United States.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:

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


Previous Document:  Experimental study of a novel mechanical connector for sutureless open arterial anastomosis.
Next Document:  Pregnancy outcomes in adolescents in the UK and Ireland growing up with HIV.