Each of these proteins is a zinc-dependent enzyme, binding 3 zinc ions per molecule.[4] The enzymes catalyse the conversion of phosphatidylcholine and water to 1,2-diacylglycerol and choline phosphate.[1][2][4]
In Bacillus cereus, there are nine residues known to be involved in binding the zinc ions: 5 His, 2 Asp, 1 Glu and 1 Trp. These residues are all conserved in the Clostridium alpha-toxin.
Some examples of this enzyme contain a C-terminal sequence extension that contains a PLAT domain which is thought to be involved in membrane localisation.[5][6]
Referencesedit
^ abNakamura S, Yamada A, Tsukagoshi N, Udaka S, Sasaki T, Makino S, Little C, Tomita M, Ikezawa H (1988). "Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus". Eur. J. Biochem. 175 (2): 213–220. doi:10.1111/j.1432-1033.1988.tb14186.x. PMID 2841128.
^ abTitball RW, Rubidge T, Hunter SE, Martin KL, Morris BC, Shuttleworth AD, Anderson DW, Kelly DC (1989). "Molecular cloning and nucleotide sequence of the alpha-toxin (phospholipase C) of Clostridium perfringens". Infect. Immun. 57 (2): 367–376. doi:10.1128/IAI.57.2.367-376.1989. PMC313106. PMID 2536355.
^Kocks C, Dramsi S, Ohayon H, Geoffroy C, Mengaud J, Cossart P, Vazquez-Boland JA (1992). "Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread". Infect. Immun. 60 (1): 219–230. doi:10.1128/IAI.60.1.219-230.1992. PMC257526. PMID 1309513.
^ abTitball RW, Rubidge T (1990). "The role of histidine residues in the alpha toxin of Clostridium perfringens". FEMS Microbiol. Lett. 56 (3): 261–265. doi:10.1111/j.1574-6968.1988.tb03188.x. PMID 2111259.
^Bateman A, Sandford R (1999). "The PLAT domain: a new piece in the PKD1 puzzle". Curr. Biol. 9 (16): R588–90. doi:10.1016/S0960-9822(99)80380-7. PMID 10469604. S2CID 15018010.
^Ponting CP, Hofmann K, Bork P (August 1999). "A latrophilin/CL-1-like GPS domain in polycystin-1". Curr. Biol. 9 (16): R585–8. doi:10.1016/S0960-9822(99)80379-0. PMID 10469603. S2CID 17252179.
This article incorporates text from the public domain Pfam and InterPro: IPR001531
zinc, dependent, phospholipase, molecular, biology, zinc, dependent, phospholipases, family, bacterial, phospholipases, enzymes, some, which, also, known, alpha, toxins, zinc, dependent, phospholipase, calpha, toxin, clostridium, showing, zinc, dependent, phos. In molecular biology zinc dependent phospholipases C is a family of bacterial phospholipases C enzymes some of which are also known as alpha toxins Zinc dependent phospholipase CAlpha toxin of Clostridium showing the zinc dependent phospholipase domain in red and the PLAT domain in yellowIdentifiersSymbolZn dep PLPCPfamPF00882InterProIPR001531PROSITEPDOC00357SCOP21ah7 SCOPe SUPFAMOPM superfamily81OPM protein1olpCDDcd11009Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryBacillus cereus contains a monomeric phospholipase C EC 3 1 4 3 PLC of 245 amino acid residues Although PLC prefers to act on phosphatidylcholine it also shows weak catalytic activity with sphingomyelin and phosphatidylinositol 1 Sequence studies have shown the protein to be similar both to alpha toxin from Clostridium perfringens and Clostridium bifermentans a phospholipase C involved in haemolysis and cell rupture 2 and to lecithinase from Listeria monocytogenes which aids cell to cell spread by breaking down the 2 membrane vacuoles that surround the bacterium during transfer 3 Each of these proteins is a zinc dependent enzyme binding 3 zinc ions per molecule 4 The enzymes catalyse the conversion of phosphatidylcholine and water to 1 2 diacylglycerol and choline phosphate 1 2 4 In Bacillus cereus there are nine residues known to be involved in binding the zinc ions 5 His 2 Asp 1 Glu and 1 Trp These residues are all conserved in the Clostridium alpha toxin Some examples of this enzyme contain a C terminal sequence extension that contains a PLAT domain which is thought to be involved in membrane localisation 5 6 References edit a b Nakamura S Yamada A Tsukagoshi N Udaka S Sasaki T Makino S Little C Tomita M Ikezawa H 1988 Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus Eur J Biochem 175 2 213 220 doi 10 1111 j 1432 1033 1988 tb14186 x PMID 2841128 a b Titball RW Rubidge T Hunter SE Martin KL Morris BC Shuttleworth AD Anderson DW Kelly DC 1989 Molecular cloning and nucleotide sequence of the alpha toxin phospholipase C of Clostridium perfringens Infect Immun 57 2 367 376 doi 10 1128 IAI 57 2 367 376 1989 PMC 313106 PMID 2536355 Kocks C Dramsi S Ohayon H Geoffroy C Mengaud J Cossart P Vazquez Boland JA 1992 Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell to cell spread Infect Immun 60 1 219 230 doi 10 1128 IAI 60 1 219 230 1992 PMC 257526 PMID 1309513 a b Titball RW Rubidge T 1990 The role of histidine residues in the alpha toxin of Clostridium perfringens FEMS Microbiol Lett 56 3 261 265 doi 10 1111 j 1574 6968 1988 tb03188 x PMID 2111259 Bateman A Sandford R 1999 The PLAT domain a new piece in the PKD1 puzzle Curr Biol 9 16 R588 90 doi 10 1016 S0960 9822 99 80380 7 PMID 10469604 S2CID 15018010 Ponting CP Hofmann K Bork P August 1999 A latrophilin CL 1 like GPS domain in polycystin 1 Curr Biol 9 16 R585 8 doi 10 1016 S0960 9822 99 80379 0 PMID 10469603 S2CID 17252179 This article incorporates text from the public domain Pfam and InterPro IPR001531 Portal nbsp Biology nbsp This membrane protein related article is a stub You can help Wikipedia by expanding it vte Retrieved from https en wikipedia org w index php title Zinc dependent phospholipase C amp oldid 1171105644, wikipedia, wiki, book, books, library,
