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Information on EC 2.7.8.7 - holo-[acyl-carrier-protein] synthase

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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 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 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
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Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
pptase, phosphopantetheinyl transferase, pptases, surfactin synthetase, phosphopantetheinyl transferases, 4'-phosphopantetheinyl transferase, mtppt, type ii fatty acid synthase system, sfp-type pptase, schppt, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
CoA-[4'-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier protein]
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