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.
| Predicate | Object |
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| rdf:type | |
| rdfs:comment |
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.,
Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14.,
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.,
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.
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| rdfs:subClassOf | |
| skos:broaderTransitive | |
| uniprot:name |
4'-phosphopantetheinyl transferase,
ACPS,
Acyl carrier protein holoprotein (holo-ACP) synthetase,
Acyl carrier protein synthase,
Acyl carrier protein synthetase,
Alpha-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase,
Holo-ACP synthase,
Holo-ACP synthetase,
Holo-[acyl-carrier-protein] synthase,
Holosynthase,
L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase,
P-pant transferase,
PPTase
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| uniprot:activity |
CoA-(4'-phosphopantetheine) + apo-[acyl-carrier-protein] = adenosine 3',5'-bisphosphate + holo-[acyl-carrier-protein].
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| uniprot:cofactor |
Magnesium
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