PMID: 8939709Nov 1, 1996Paper

A new enzyme superfamily - the phosphopantetheinyl transferases

Chemistry & Biology
R H LambalotC T Walsh

Abstract

All polyketide synthases, fatty acid synthases, and non-ribosomal peptide synthetases require posttranslational modification of their constituent acyl carrier protein domain(s) to become catalytically active. The inactive apoproteins are converted to their active holo-forms by posttranslational transfer of the 4'-phosphopantetheinyl (P-pant) moiety of coenzyme A to the sidechain hydroxyl of a conserved serine residue in each acyl carrier protein domain. The first P-pant transferase to be cloned and characterized was the recently reported Escherichia coli enzyme ACPS, responsible for apo to holo conversion of fatty acid synthase. Surprisingly, initial searches of sequence databases did not reveal any proteins with significant peptide sequence similarity with ACPS. Through refinement of sequence alignments that indicated low level similarity with the ACPS peptide sequence, we identified two consensus motifs shared among several potential ACPS homologs. This has led to the identification of a large family of proteins having 12-22 % similarity with ACPS, which are putative P-pant transferases. Three of these proteins, E. coli EntD and o195, and B. subtilis Sfp, have been overproduced, purified and found to have P-pant transferase a...Continue Reading

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Citations

Mar 14, 2007·Microbial Ecology·Torben MartensThorsten Brinkhoff
Sep 21, 2010·Applied Microbiology and Biotechnology·Xue GaoYi Tang
Jan 25, 2008·Journal of Industrial Microbiology & Biotechnology·L DuQ Wang
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