Information on EC - holo-[acyl-carrier-protein] synthase

for references in articles please use BRENDA:EC2.7.8.7
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IUBMB Comments
Requires Mg2+. All polyketide synthases, fatty-acid synthases and non-ribosomal peptide synthases require post-translational modification of their constituent acyl-carrier-protein (ACP) domains to become catalytically active. The inactive apo-proteins are converted into their active holo-forms by transfer of the 4'-phosphopantetheinyl moiety of CoA to the sidechain hydroxy group of a conserved serine residue in each ACP domain . The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes . Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC, [acyl-carrier-protein] phosphodiesterase.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
(FAS)ACP, 4'-phosphopantetheinyl transferase, 4'-PP transferase, 4-phosphopantetheinyl transferase, 4-phosphopantetheinyl transferase 1, AASDHPPT, AcpS, AcpT, acyl carrier protein holoprotein (holo-ACP) synthetase, acyl carrier protein synthase, more
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
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