Holo-(acyl-carrier-protein) synthase

The correct title of this article is Holo-[acyl-carrier-protein] synthase. The substitution of any brackets is due to technical restrictions.

phosphopantetheinyltransferase
holo-[acyl-carrier-protein] synthase trimer, Helicobacter pylori
Identifiers
EC no.	2.7.8.7
CAS no.	37278-30-1
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
Search PMC articles PubMed articles NCBI proteins

ACPS
crystal structure of the 4'-phosphopantetheinyl transferase sfp-coenzyme a complex
Identifiers
Symbol	ACPS
Pfam	PF01648
InterPro	IPR008278
SCOP2	1qr0 / SCOPe / SUPFAM
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

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 ${\displaystyle \rightleftharpoons }$ adenosine 3',5'-bisphosphate + holo-acyl carrier protein

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.^{[ citation needed ]}

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

• Elovson J, Vagelos PR (July 1968). "Acyl carrier protein. X. Acyl carrier protein synthetase". The Journal of Biological Chemistry. 243 (13): 3603–11. doi: 10.1016/S0021-9258(19)34183-3 . PMID   4872726.
• Prescott DJ, Vagelos PR (1972). "Acyl carrier protein". Advances in Enzymology and Related Areas of Molecular Biology. Advances in Enzymology - and Related Areas of Molecular Biology. Vol. 36. pp. 269–311. doi:10.1002/9780470122815.ch8. ISBN   9780470122815. PMID   4561013.
• Lambalot RH, Gehring AM, Flugel RS, Zuber P, LaCelle M, Marahiel MA, Reid R, Khosla C, Walsh CT (November 1996). "A new enzyme superfamily - the phosphopantetheinyl transferases". Chemistry & Biology. 3 (11): 923–36. doi: 10.1016/S1074-5521(96)90181-7 . PMID   8939709.
• Walsh CT, Gehring AM, Weinreb PH, Quadri LE, Flugel RS (October 1997). "Post-translational modification of polyketide and nonribosomal peptide synthases". Current Opinion in Chemical Biology. 1 (3): 309–15. doi:10.1016/S1367-5931(97)80067-1. PMID   9667867.
• Mootz HD, Finking R, Marahiel MA (October 2001). "4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis". The Journal of Biological Chemistry. 276 (40): 37289–98. doi: 10.1074/jbc.M103556200 . PMID   11489886.
• Joshi AK, Zhang L, Rangan VS, Smith S (August 2003). "Cloning, expression, and characterization of a human 4'-phosphopantetheinyl transferase with broad substrate specificity". The Journal of Biological Chemistry. 278 (35): 33142–9. doi: 10.1074/jbc.M305459200 . PMID   12815048.

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