4'-phosphopantetheinyl transferase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
ACPS
PDB 1qr0 EBI.jpg
crystal structure of the 4'-phosphopantetheinyl transferase sfp-coenzyme a complex
Identifiers
Symbol ACPS
Pfam PF01648
InterPro IPR008278
SCOP 1qr0
SUPERFAMILY 1qr0

In molecular biology, the 4'-phosphopantetheinyl transferase superfamily of proteins transfer 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 ACPS type such as E. coli ACPS and the Sfp type such as B. subtilis SFP. The structure of the Sfp type is known,[2] which shows the active site accommodates a magnesium ion. The most highly conserved regions of the protein are involved in binding the magnesium ion.

References[edit]

  1. ^ Lambalot RH, Walsh CT (October 1995). "Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase". J. Biol. Chem. 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". EMBO J. 18 (23): 6823–31. doi:10.1093/emboj/18.23.6823. PMC 1171745. PMID 10581256. 

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