Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp): Difference between revisions

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Jon Amoroso, Gitanjeli Prasad, Lawrence Sheringham Borketey, Carrie Morrison Penland

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	== Introduction ==		== Introduction ==

	'''Sfp''' is a 4'-phosphopantetheinyl (PPant) transferase endogenous to ''B. Subtilis'', first crystallized in 1999 [1]. The function of Sfp is to transfer a phosphopantetheinyl group from <scene name='Sfp/Coa_highlight/3'>coenzyme-A</scene> (CoA-SH) to the serine residue of peptides containing the sequence "DSL". Frequently this sequence is found in acyl- or peptidyl-carrier proteins in fatty acid synthases (FASs), polyketide synthases (PKSs), and nonribosomal peptide synthetases (NRPSs). This converts the inactive apo form peptide to the active holo form. The terminal thiol PPant prosthetic group acts as a point of covalent attachment between the peptide and the growing fatty acid, polyketide, or nonribosomal peptide.		'''Sfp''' is a 4'-phosphopantetheinyl (PPant) transferase endogenous to ''B. Subtilis'', first crystallized in 1999 [1]. The function of Sfp is to transfer a phosphopantetheinyl group from <scene name='Sfp/Coa_highlight/4'>coenzyme-A</scene> (CoA-SH) to the serine residue of peptides containing the sequence "DSL". Frequently this sequence is found in acyl- or peptidyl-carrier proteins in fatty acid synthases (FASs), polyketide synthases (PKSs), and nonribosomal peptide synthetases (NRPSs). This converts the inactive apo form peptide to the active holo form. The terminal thiol PPant prosthetic group acts as a point of covalent attachment between the peptide and the growing fatty acid, polyketide, or nonribosomal peptide.