Any feedback?
Please rate this page

BRENDA support

show all | hide all No of entries

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

for references in articles please use BRENDA:EC2.7.8.7
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
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.
Specify your search results
Select one or more organisms in this record: ?
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
pptase, phosphopantetheinyl transferase, surfactin synthetase, 4'-phosphopantetheinyl transferase, mtppt, type ii fatty acid synthase system, sfp-type pptase, schppt, holo-acyl carrier protein synthase, mtacps, more
CoA-[4'-phosphopantetheine] + an apo-[acyl-carrier protein] = adenosine 3',5'-bisphosphate + an [acyl-carrier protein]
show the reaction diagram