Document Detail

Priming type II polyketide synthases via a type II nonribosomal peptide synthetase mechanism.
MedLine Citation:
PMID:  16448095     Owner:  NLM     Status:  MEDLINE    
Benzoic acid priming of the enterocin and actinorhodin type II polyketide synthase complexes was accomplished in vitro via an unprecedented type II nonribosomal peptide synthetase-like mechanism involving the benzoate:acyl carrier protein (ACP) ligase EncN and the ACP EncC. The transfer of the aryl acid to the ACP is ATP-dependent, yet coenzyme A-independent, as characterized with radiolabeled substrates and protein mass spectrometry. Subsequent transport of the ACP-bound aryl group to the native enterocin and the aberrant actinorhodin ketosynthase chain length factor heterodimers was further demonstrated, thereby demonstrating the potential of this biocatalyst for engineering diverse aryl-primed aromatic polyketide agents.
Miho Izumikawa; Qian Cheng; Bradley S Moore
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Journal of the American Chemical Society     Volume:  128     ISSN:  0002-7863     ISO Abbreviation:  J. Am. Chem. Soc.     Publication Date:  2006 Feb 
Date Detail:
Created Date:  2006-02-01     Completed Date:  2006-04-03     Revised Date:  2014-09-10    
Medline Journal Info:
Nlm Unique ID:  7503056     Medline TA:  J Am Chem Soc     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1428-9     Citation Subset:  IM    
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MeSH Terms
Acyl Carrier Protein / chemistry,  metabolism
Anthraquinones / chemistry,  metabolism
Coenzyme A / chemistry,  metabolism
Naphthacenes / chemistry,  metabolism
Peptide Synthases / chemistry,  metabolism*
Polyketide Synthases / chemistry,  metabolism*
Grant Support
Reg. No./Substance:
0/Acyl Carrier Protein; 0/Anthraquinones; 0/Naphthacenes; 1397-77-9/actinorhodin; 146864-75-7/5838 DNI; 79956-01-7/Polyketide Synthases; EC 6.3.2.-/Peptide Synthases; EC 6.3.2.-/non-ribosomal peptide synthase; SAA04E81UX/Coenzyme A

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