Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp): Difference between revisions
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== 4'-PHOSPHOPANTETHEINYL TRANSFERASE | == 4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp) == | ||
<StructureSection load='1qr0' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''> | <StructureSection load='1qr0' size='350' side='right' caption='Structure of HMG-CoA reductase (PDB entry [[1dq8]])' scene=''> | ||
== 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/ | '''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/5'>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 posttranslational modification 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 == | == Mechanism of Transfer == | ||
<scene name='Sfp/Sfp_mg/ | <scene name='Sfp/Sfp_mg/6'>Active site magnesium</scene> along with ATP are involved in the catalytic transformation of the apo proteins. | ||