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.
Walsh
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Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115, USA. walsh@walsh.med.harvard.edu
Gehring
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Weinreb
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Quadri
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Flugel
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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