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PPTase, Phosphopantetheine transferase

Fig. 3. Phosphopantetheinylation of the acyl carrier protein (AGP) domain of a polyketide synthase. In order to be active, polyketide synthases must be post-translationally modified by a family of enzymes called phosphopantetheine transferases (PPTases). These enzymes transfer the 4 -phospho-pantetheine arm of Coenzyme A to an active site serine residue in the AGP... Fig. 3. Phosphopantetheinylation of the acyl carrier protein (AGP) domain of a polyketide synthase. In order to be active, polyketide synthases must be post-translationally modified by a family of enzymes called phosphopantetheine transferases (PPTases). These enzymes transfer the 4 -phospho-pantetheine arm of Coenzyme A to an active site serine residue in the AGP...
Despite the structural diversity of polyketides, the building blocks of these compounds are simple acyl-CoAs, and the biosynthetic logic is closely associated with that of fatty acid synthases (FASs) [9, 10]. In both polyketide and fatty acid biosynthesis, the growing chain is covalently tethered to an acyl carrier protein (ACP) via a phosphopantetheine (PPant) moiety. The PPant chain, derived from CoA, is attached post-translationaUy to a conserved serine residue on the npo-ACP by a phosphopantetheinyl transferase (PPTase), yielding the mature to-ACP (Scheme 1.1) [11,12],... [Pg.4]


See other pages where PPTase, Phosphopantetheine transferase is mentioned: [Pg.507]    [Pg.463]    [Pg.507]    [Pg.463]    [Pg.621]    [Pg.472]    [Pg.12]   
See also in sourсe #XX -- [ Pg.463 ]




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Phosphopantetheine

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