Structural highlights
Function
PGPB_ECOLI Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Also has undecaprenyl pyrophosphate phosphatase activity, required for the biosynthesis of the lipid carrier undecaprenyl phosphate. Can also use lysophosphatidic acid (LPA) and phosphatidylglycerophosphate as substrates. The pattern of activities varies according to subcellular location, PGP phosphatase activity is higher in the cytoplasmic membrane, whereas PA and LPA phosphatase activities are higher in the outer membrane. Activity is independent of a divalent cation ion and insensitive to inhibition by N-ethylmaleimide.[1] [2] [3] [4]
References
- ↑ El Ghachi M, Derbise A, Bouhss A, Mengin-Lecreulx D. Identification of multiple genes encoding membrane proteins with undecaprenyl pyrophosphate phosphatase (UppP) activity in Escherichia coli. J Biol Chem. 2005 May 13;280(19):18689-95. Epub 2005 Mar 18. PMID:15778224 doi:http://dx.doi.org/M412277200
- ↑ Touze T, Blanot D, Mengin-Lecreulx D. Substrate specificity and membrane topology of Escherichia coli PgpB, an undecaprenyl pyrophosphate phosphatase. J Biol Chem. 2008 Jun 13;283(24):16573-83. doi: 10.1074/jbc.M800394200. Epub 2008, Apr 14. PMID:18411271 doi:http://dx.doi.org/10.1074/jbc.M800394200
- ↑ Lu YH, Guan Z, Zhao J, Raetz CR. Three phosphatidylglycerol-phosphate phosphatases in the inner membrane of Escherichia coli. J Biol Chem. 2011 Feb 18;286(7):5506-18. doi: 10.1074/jbc.M110.199265. Epub 2010 , Dec 9. PMID:21148555 doi:http://dx.doi.org/10.1074/jbc.M110.199265
- ↑ Dillon DA, Wu WI, Riedel B, Wissing JB, Dowhan W, Carman GM. The Escherichia coli pgpB gene encodes for a diacylglycerol pyrophosphate phosphatase activity. J Biol Chem. 1996 Nov 29;271(48):30548-53. PMID:8940025
