Outer membrane phospholipase A1 (OMPLA) is an acyl hydrolase with a broad substrate specificity (EC:3.1.1.32.) from the bacterial outer membrane. It has been proposed that Ser164 is the active site of the protein (UniProt P00631) [1]
This integral membrane phospholipase was found in many Gram-negative bacteria and has a broad substrate specificity EC 3.1.1.32. The role of OMPLA has been most thoroughly studied in Escherichia coli, where it participates in the secretion of bacteriocins. Bacteriocin release is triggered by a lysis protein (bacteriocin release protein or BRP), followed by a phospholipase dependent accumulation of lysophospholipids and free fatty acids in the outer membrane.[2] The reaction products enhance the permeability of the outer membrane, which allows the semispecific secretion of bacteriocins. One speculative function of OMPLA is related to organic solvent tolerance in bacteria.
Structurally, it consists of a 12-stranded antiparallel beta-barrel with a convex and a flat side. The active site residues are exposed on the exterior of the flat face of the beta-barrel. The activity of the enzyme is regulated by reversible dimerisation. Dimer interactions occur exclusively in the membrane-embedded parts of the flat side of the beta-barrel, with polar residues embedded in an apolar environment forming the key interactions. The active site His and Ser residues are located at the exterior of the beta-barrel, at the outer leaflet side of the membrane. This location indicates that under normal conditions the substrate and the active site are physically separated, since in E. coli phospholipids are exclusively located in the inner leaflet of the outer membrane.[3]
^Horrevoets AJ, Verheij HM, de Haas GH (May 1991). "Inactivation of Escherichia coli outer-membrane phospholipase A by the affinity label hexadecanesulfonyl fluoride. Evidence for an active-site serine". European Journal of Biochemistry. 198 (1): 247–53. doi:10.1111/j.1432-1033.1991.tb16008.x. PMID 2040286.
OutermembranephospholipaseA1 (OMPLA) is an acyl hydrolase with a broad substrate specificity (EC:3.1.1.32.) from the bacterial outermembrane. It has...
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flow to inner medulla without affecting blood flow to outer medulla. V1Rs on the luminal membrane of the collecting duct limit the antidiuretic action...
RNU2-2: encoding protein RNA, U2 small nuclear 2 ROM1: retinal outer segment membrane protein 1 RPL27A: encoding protein 60S ribosomal protein L27a RPL36A:...
protein kinase C, which, in turn, activates phospholipase A2 (PLA2). PLA2 then modifies the integrin membrane glycoprotein IIb/IIIa, increasing its affinity...
phospholipids of cell membranes. It can be released from the membrane by the action of phospholipase A2, a peripheral membrane protein, which is activated...
two of them has no phenotypical effect. The G-proteins activate the phospholipase C PLCB4, which causes the TRP-channels TRPC6 and TRPC7 mediate to open...
(September 2000). "CAIR-1/BAG-3 forms an EGF-regulated ternary complex with phospholipase C-gamma and Hsp70/Hsc70". Oncogene. 19 (38): 4385–95. doi:10.1038/sj...
cellular responses by activating signaling pathways that include the: a) Phospholipase C/PI3K/AKT, b) Ras subfamily/ERK, c) Protein kinase C, d) IP3-induced...
includes GRM1 and GRM5 and these receptors have been shown to activate phospholipase C. Group II includes GRM2 and GRM3 while Group III includes GRM4, GRM6...
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