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词条 Zinc-dependent phospholipase C
释义

  1. References

{{Pfam_box
| Symbol = Zn_dep_PLPC
| Name = Zinc dependent phospholipase C
| image =1olp_opm.png
| width =220
| caption =Alpha toxin of Clostridium showing the zinc dependent phospholipase domain in red and the PLAT domain in yellow
| Pfam= PF00882
| InterPro= IPR001531
| PROSITE= PDOC00357
| SMART=
| SCOP = 1ah7
| TCDB =
| OPM family= 81
| OPM protein= 1olp
| CDD = cd11009
| PDB=
}}

In molecular biology, zinc-dependent phospholipases C is a family of bacterial phospholipases C enzymes, some of which are also known as alpha toxins.

Bacillus cereus contains a monomeric phospholipase C {{EC number|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.

name="PUB00018111">{{cite journal |vauthors =Bateman A, Sandford R |title=The PLAT domain: a new piece in the PKD1 puzzle |journal=Curr. Biol. |volume=9 |issue=16 |pages= R588–90|year=1999 |pmid=10469604 |doi=10.1016/S0960-9822(99)80380-7}}[5]

References

1. ^{{cite journal |vauthors =Nakamura S, Yamada A, Tsukagoshi N, Udaka S, Sasaki T, Makino S, Little C, Tomita M, Ikezawa H |title=Nucleotide sequence and expression in Escherichia coli of the gene coding for sphingomyelinase of Bacillus cereus |journal=Eur. J. Biochem. |volume=175 |issue=2 |pages=213–220 |year=1988 |pmid=2841128 |doi=10.1111/j.1432-1033.1988.tb14186.x}}
2. ^{{cite journal |vauthors =Titball RW, Rubidge T, Hunter SE, Martin KL, Morris BC, Shuttleworth AD, Anderson DW, Kelly DC |title=Molecular cloning and nucleotide sequence of the alpha-toxin (phospholipase C) of Clostridium perfringens |journal=Infect. Immun. |volume=57 |issue=2 |pages=367–376 |year=1989 |pmid=2536355 |pmc=313106}}
3. ^{{cite journal |vauthors =Kocks C, Dramsi S, Ohayon H, Geoffroy C, Mengaud J, Cossart P, Vazquez-Boland JA |title=Nucleotide sequence of the lecithinase operon of Listeria monocytogenes and possible role of lecithinase in cell-to-cell spread |journal=Infect. Immun. |volume=60 |issue=1 |pages=219–230 |year=1992 |pmid=1309513 |pmc=257526}}
4. ^{{cite journal |vauthors =Titball RW, Rubidge T |title=The role of histidine residues in the alpha toxin of Clostridium perfringens |journal=FEMS Microbiol. Lett. |volume=56 |issue=3 |pages=261–265 |year=1990 |pmid=2111259 |doi=10.1111/j.1574-6968.1988.tb03188.x}}
5. ^{{cite journal |vauthors =Ponting CP, Hofmann K, Bork P |title=A latrophilin/CL-1-like GPS domain in polycystin-1 |journal=Curr. Biol. |volume=9 |issue=16 |pages=R585–8 |date=August 1999 |pmid=10469603 |doi= 10.1016/S0960-9822(99)80379-0|url=http://linkinghub.elsevier.com/retrieve/pii/S0960-9822(99)80379-0}}
{{InterPro content|IPR001531}}{{Esterases}}{{Enzymes}}{{Portal bar|Molecular and Cellular Biology|border=no}}{{DEFAULTSORT:Zinc Dependent Phospholipase C}}{{membrane-protein-stub}}

4 : EC 3.1.4|Protein domains|Peripheral membrane proteins|Zinc proteins

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