Holo-(acyl-carrier-protein) synthase

In enzymology and molecular biology, a holo-[acyl-carrier-protein] synthase (ACPS, EC 2.7.8.7) is an enzyme that catalyzes the chemical reaction:

CoA-[4'-phosphopantetheine] + apo-acyl carrier protein adenosine 3',5'-bisphosphate + holo-acyl carrier protein
phosphopantetheinyltransferase
holo-[acyl-carrier-protein] synthase trimer, Helicobacter pylori
Identifiers
EC no.2.7.8.7
CAS no.37278-30-1
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
ACPS
crystal structure of the 4'-phosphopantetheinyl transferase sfp-coenzyme a complex
Identifiers
SymbolACPS
PfamPF01648
InterProIPR008278
SCOP21qr0 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

This enzyme belongs to the family of transferases, specifically those transferring non-standard substituted phosphate groups. It is also known as 4'-phosphopantetheinyl transferase after the group it transfers.

Function

All ACPS enzymes known so far are evolutionally related to each other in a single superfamily of proteins. It transfers a 4'-phosphopantetheine (4'-PP) moiety from coenzyme A (CoA) to an invariant serine in an acyl carrier protein (ACP), a small protein responsible for acyl group activation in fatty acid biosynthesis. This post-translational modification renders holo-ACP capable of acyl group activation via thioesterification of the cysteamine thiol of 4'-PP.[1] This superfamily consists of two subtypes: the trimeric ACPS type such as E. coli ACPS and the monomeric Sfp (PCP-synthesizing) type such as B. subtilis SFP. Structures from both families are now known. The active site accommodates a magnesium ion. The most highly conserved regions of the protein are involved in binding the magnesium ion.[2][3]

Nomenclature

The systematic name of this enzyme class is CoA-[4'-phosphopantetheine]:apo-[acyl-carrier-protein] 4'-pantetheinephosphotransferase. Other names in common use, disregarding the synthetase/synthase spelling difference, include acyl carrier protein holoprotein synthetase, holo-ACP synthetase, coenzyme A:fatty acid synthetase apoenzyme 4'-phosphopantetheine, acyl carrier protein synthetase (ACPS), PPTase, acyl carrier protein synthase, P-pant transferase, and CoA:apo-[acyl-carrier-protein] pantetheinephosphotransferase.

Structural studies

As of late 2007, 8 structures have been solved for this class of enzymes, with PDB accession codes 1F7L, 1F7T, 1F80, 1FTE, 1FTF, 1FTH, 2JBZ, and 2JCA.

References

  1. Lambalot RH, Walsh CT (October 1995). "Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase". The Journal of Biological Chemistry. 270 (42): 24658–61. doi:10.1074/jbc.270.42.24658. PMID 7559576.
  2. Reuter K, Mofid MR, Marahiel MA, Ficner R (December 1999). "Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily". The EMBO Journal. 18 (23): 6823–31. doi:10.1093/emboj/18.23.6823. PMC 1171745. PMID 10581256.
  3. Marcella AM, Culbertson SJ, Shogren-Knaak MA, Barb AW (24 November 2017). "Structure, High Affinity, and Negative Cooperativity of the Escherichia coli Holo-(Acyl Carrier Protein):Holo-(Acyl Carrier Protein) Synthase Complex". Journal of Molecular Biology. 429 (23): 3763–3775. doi:10.1016/j.jmb.2017.10.015. PMID 29054754.

Further reading

This article incorporates text from the public domain Pfam and InterPro: IPR008278


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