Post-translational modification of polyketide and nonribosomal peptide synthases.
The past year has witnessed a major advance in the study of polyketide and nonribosomal peptide biosynthesis with the identification of the phosphopantetheinyl transferase enzyme family, enzymes required to produce active, post-translationally modified polyketide and peptide synthases. Phosphopantetheinyl transferases required for fatty acid, peptide and siderophore biosynthesis have been characterized and a consensus sequence noted in order to facilitate future identification of additional proteins catalyzing phosphopantetheinyl transfer.
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. walsh@walsh.med.harvard.edu
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D005227:Fatty Acids / Q000096:biosynthesis; D009097:Multienzyme Complexes / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017855:Transferases (Other Substituted Phosphate Groups) / Q000378:metabolism*
D005227:Fatty Acids; D009097:Multienzyme Complexes; D010455:Peptides; D017855:Transferases (Other Substituted Phosphate Groups); C021364:holo-(acyl-carrier-protein) synthase