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Acyl carrier protein

Cofactor of both fatty acid and polyketide biosynthesis

Field	Value
Name	Acyl/peptidyl carrier protein
image	Act acp.png
caption	Streptomyces coelicolor actinorhodin polyketide synthase acyl carrier protein -
InterPro	IPR036736
Symbol	ACP-like_sf
SCOP	1nq4
CATH	1nq4
Pfam_clan	CL0314
Pfam	PF00550
PROSITE	PDOC00012

The acyl carrier protein (ACP) is a cofactor of both fatty acid and polyketide biosynthesis machinery. It is one of the most abundant proteins in cells of E. coli. In both cases, the growing chain is bound to the ACP via a thioester derived from the distal thiol of a 4'-phosphopantetheine moiety.

Structure

The ACPs are small negatively charged α-helical bundle proteins with a high degree of structural and amino acid similarity. The structures of a number of acyl carrier proteins have been solved using various NMR and crystallography techniques. The ACPs are related in structure and mechanism to the peptidyl carrier proteins (PCP) from nonribosomal peptide synthases.

Biosynthesis

Subsequent to the expression of the inactive apo ACP, the 4'-phosphopantetheine moiety is attached to a serine residue. This coupling is mediated by acyl carrier protein synthase (ACPS), a 4'-phosphopantetheinyl transferase. 4'-Phosphopantetheine is a prosthetic group of several acyl carrier proteins including the acyl carrier proteins (ACP) of fatty acid synthases, ACPs of polyketide synthases, the peptidyl carrier proteins (PCP), as well as aryl carrier proteins (ArCP) of nonribosomal peptide synthetases (NRPS).

References

Lawrence, Eleanor. "ACP".
(2014). "The Chain-Flipping Mechanism of ACP (Acyl Carrier Protein)-Dependent enzymes Appears Universal". [[Biochemical Journal]].
(June 2002). "X-ray crystallographic studies on butyryl-ACP reveal flexibility of the structure around a putative acyl chain binding site". [[Structure (journal).
(July 2008). "Acyl-carrier protein-phosphopantetheinyltransferase partnerships in fungal fatty acid synthases". [[ChemBioChem]].
(July 2001). "Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein". [[Biochemistry (journal).
(April 2000). "Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases". [[Structure (journal).

Info: Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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