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Zinc dependent phospholipase C

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Title: Zinc dependent phospholipase C  
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Subject: Tubulin, DNA glycosylase, Phosphoinositide phospholipase C, Vitamin K epoxide reductase, Signal peptide peptidase, M protein (Streptococcus)
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Zinc dependent phospholipase C

Zinc dependent phospholipase C
Clostridium showing the zinc dependent phospholipase domain in red and the PLAT domain in yellow
Symbol Zn_dep_PLPC
Pfam InterPro PROSITE PDOC00357
SCOP SUPERFAMILY OPM superfamily OPM protein 1olp
CDD cd11009

Zinc-dependent prokaryotic phospholipases C is a family of bacterial phospholipases C, some of which are also known as alpha toxins.

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]


This article incorporates text from the IPR001531

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