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| Phospholipase C |
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Phospholipases can be divided into four groups depending on the position of the bond they hydrolyse on the phospholipid substrate: phospholipases A1, A2, C and D. ... |
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PLC
(Phospholipase C) |
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Degrading the phospholipid surfactant, which functions to reduce the surface tension so that the alveoli do not collapse completely when air leaves them during breathing. ... |
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| Phospholipase A2 |
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Two PLA2 enzymes (pat1 and pat2) have divergent evolutionary histories and discordant selective constraints, with pat2 deleted from most other non-TG rickettsiae genomes, while pat1 homologs are encoded in all sequenced Rickettsia genomes. Pat1 and Pat2 may be rvh T4SS substrates. ... |
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| Pld |
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Plays an important role in phagosomal escape. ... |
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| α-hemolysin |
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A paradigm for pore-forming toxins that utilize a β-barrel structure for channel formation. PDB code :7AHL. ... |
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| β-hemolysin |
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Tissue invasion. Sphingomyelinase, specifically cleaves sphingomyelin into phosphocholine and ceramide. ... |
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| δ-hemolysin |
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Capable of lysing erythrocytes and other mammalian cells, as well as subcellular structures. Forms α-helix with hydrophobic and hydrophilic domains on opposite sides and aggregates to form channels channels in the membrane. ... |
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| γ-hemolysin |
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Three protein (HlgA, HlgB, HlgC) are virtually identical in sequence to leukocidin component S and F, thus γ-hemolysin may act similarly to leukocidin. S component: HlgA, HlgC. F component: HlgB. ... |
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PVL
(Panton-Valentine leukocidin) |
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PVL, together with γ-hemolysin and other leukocidins such as LukE-LukD, belongs to the family of bicomponent synergohymenotropic toxins. Pore-forming toxin rich in β-sheet structures. ... |
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SE
(Staphylococcal enterotoxin) |
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Constitutes a family of eight single-chain polypeptides (26-28kDa, 228-239 amino acid residues) with a typical disulfide loop. Divided into two groups based on amino acid sequence homology: the first group consists of SEA,SEE, SED and SEH, and the second group including SEB, SEC, SEG. ... |
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