Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp): Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
== 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/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. | '''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 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/6'>Active site magnesium</scene> | <scene name='Sfp/Sfp_mg/6'>Active site magnesium</scene> along with ATP are involved in the catalytic transformation of the apo proteins. | ||