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

Revision as of 20:20, 10 October 2012

4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP4'-PHOSPHOPANTETHEINYL TRANSFERASE SFP

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 (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.

Mechanism of Transfer

Biochemical Applications

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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

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	== Mechanism of Transfer ==		== Mechanism of Transfer ==
	<scene name='Sfp/Sfp_mg/2'>Active site magnesium</scene>		<scene name='Sfp/Sfp_mg/4'>Active site magnesium</scene>