| 词条 | 4'-phosphopantetheinyl transferase |
| 释义 |
| Symbol = ACPS | Name = ACPS | image = PDB 1qr0 EBI.jpg | width = | caption = crystal structure of the 4'-phosphopantetheinyl transferase sfp-coenzyme a complex | Pfam = PF01648 | Pfam_clan = | InterPro = IPR008278 | SMART = | PROSITE = | MEROPS = | SCOP = 1qr0 | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} 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. References1. ^{{cite journal | vauthors = Lambalot RH, Walsh CT | title = Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase | journal = J. Biol. Chem. | volume = 270 | issue = 42 | pages = 24658–61 |date=October 1995 | pmid = 7559576 | doi = 10.1074/jbc.270.42.24658| url = }} {{InterPro content|IPR008278}}2. ^{{cite journal | vauthors = Reuter K, Mofid MR, Marahiel MA, Ficner R | title = Crystal structure of the surfactin synthetase-activating enzyme sfp: a prototype of the 4'-phosphopantetheinyl transferase superfamily | journal = EMBO J. | volume = 18 | issue = 23 | pages = 6823–31 |date=December 1999 | pmid = 10581256 | pmc = 1171745 | doi = 10.1093/emboj/18.23.6823 | url = }} 1 : Protein families |
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