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acyl carrier protein metabolism

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 : PANTETHEINE-P moiety of : CO-A to the side chain hydroxy group of a conserved serine residue in each ACP domain. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC, : EG11095-MONOMER. The enzyme from E. coli has been characterized, and found not to be essential for growth. Its physiological role of is unknown .

from BIOCYC source record: ECO_PWY-6012
Type: pathway
Taxonomic scope
organism-specific biosystem
Escherichia coli

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