The Enzyme Database

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EC 2.7.8.7     
Accepted name: holo-[acyl-carrier-protein] synthase
Reaction: CoA-[4′-phosphopantetheine] + apo-[acyl-carrier protein] = adenosine 3′,5′-bisphosphate + holo-[acyl-carrier protein]
Other name(s): acyl carrier protein holoprotein (holo-ACP) synthetase; holo-ACP synthetase; coenzyme A:fatty acid synthetase apoenzyme 4′-phosphopantetheine transferase; holosynthase; acyl carrier protein synthetase; holo-ACP synthase; PPTase; AcpS; ACPS; acyl carrier protein synthase; P-pant transferase; CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase; CoA-[4′-phosphopantetheine]:apo-[acyl-carrier-protein] 4′-pantetheinephosphotransferase
Systematic name: CoA-[4′-phosphopantetheine]:apo-[acyl-carrier protein] 4′-pantetheinephosphotransferase
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 [3]. The enzyme from human can activate both the ACP domain of the human cytosolic multifunctional fatty acid synthase system (EC 2.3.1.85) and that associated with human mitochondria as well as peptidyl-carrier and acyl-carrier-proteins from prokaryotes [6]. Removal of the 4-phosphopantetheinyl moiety from holo-ACP is carried out by EC 3.1.4.14, [acyl-carrier-protein] phosphodiesterase.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37278-30-1
References:
1.  Elovson, J. and Vagelos, P.R. Acyl carrier protein. X. Acyl carrier protein synthetase. J. Biol. Chem. 243 (1968) 3603–3611. [PMID: 4872726]
2.  Prescott, D.J. and Vagelos, P.R. Acyl carrier protein. Adv. Enzymol. Relat. Areas Mol. Biol. 36 (1972) 269–311. [PMID: 4561013]
3.  Lambalot, R.H., Gehring, A.M., Flugel, R.S., Zuber, P., LaCelle, M., Marahiel, M.A., Reid, R., Khosla, C. and Walsh, C.T. A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3 (1996) 923–936. [DOI] [PMID: 8939709]
4.  Walsh, C.T., Gehring, A.M., Weinreb, P.H., Quadri, L.E.N. and Flugel, R.S. Post-translational modification of polyketide and nonribosomal peptide synthases. Curr. Opin. Chem. Biol. 1 (1997) 309–315. [DOI] [PMID: 9667867]
5.  Mootz, H.D., Finking, R. and Marahiel, M.A. 4′-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J. Biol. Chem. 276 (2001) 37289–37298. [DOI] [PMID: 11489886]
6.  Joshi, A.K., Zhang, L., Rangan, V.S. and Smith, S. Cloning, expression, and characterization of a human 4′-phosphopantetheinyl transferase with broad substrate specificity. J. Biol. Chem. 278 (2003) 33142–33149. [DOI] [PMID: 12815048]
[EC 2.7.8.7 created 1972, modified 2006]
 
 


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