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1 protein previously reported to function as a lysophospholipase.
2 also recognized by antibodies to pancreatic lysophospholipase.
3 refer to as PLB2, encodes a phospholipase B/lysophospholipase.
4 shows no sequence similarities to any known lysophospholipases.
5 pase C were significantly overexpressed, and lysophospholipase 1, phospholipase A2, and phospholipase
11 line hydrolase, lipase, phospholipase A, and lysophospholipase A is as efficient as the wild-type str
13 secretion system, including phospholipase A, lysophospholipase A, and monoacylglycerol lipase, althou
14 e, lipase, phospholipase A, phospholipase C, lysophospholipase A, and tartrate-sensitive and tartrate
15 acid phosphatases, lipases, phospholipase C, lysophospholipase A, or protease grew normally at 25 deg
17 ivity-based protein profiling, we identified lysophospholipase A2 (LYPLA2) as a major enzyme responsi
18 ant lecithin:cholesterol acyltransferase and lysophospholipase activities in the mouse LLPL-transfect
19 olypeptide catalyzes phospholipase A1/A2 and lysophospholipase activities with distinct kinetic param
22 ter SDS-PAGE/silver-staining, possessed high lysophospholipase activity (50 micromol min(-1) mg(-1)),
23 donyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosp
27 uble deletion mutant is completely devoid of lysophospholipase activity toward the preferred substrat
28 LA2 activity of cPLA2 is able to inhibit its lysophospholipase activity with a similar IC50 to its PL
29 PLB2 resulted in the loss of 80% of cellular lysophospholipase activity, a plb1/plb2 double deletion
31 The CLC-depleted lysates retained their full lysophospholipase activity, and this activity could be b
32 n increase in total cellular phospholipase B/lysophospholipase activity, as well as the appearance of
33 The resulting mutant protein lost all of its lysophospholipase activity, even though it had the same
34 protein, initially reported to possess weak lysophospholipase activity, is still considered to be th
36 Purified cPLA(2)zeta exhibited much higher lysophospholipase and PLA(2) activity than cPLA(2)beta a
37 es but that it does interact with eosinophil lysophospholipases and known inhibitors of this lipolyti
39 Recent experimental evidence implicated the lysophospholipase, autotaxin (ATX), and its product, lys
40 t CLC protein is not one of the eosinophil's lysophospholipases but that it does interact with eosino
41 , is still considered to be the eosinophil's lysophospholipase, but it shows no sequence similarities
43 otaxin (ATX) is a secreted glycoprotein with lysophospholipase D (LPLD) activity that generates the b
46 perty of ATX was found to be mediated by its lysophospholipase D (lysoPLD) activity, which has been w
50 ation of LPC that is converted to LPA by the lysophospholipase D activity of autotaxin (ATX/lysoPLD).
51 sts and are also nanomolar inhibitors of the lysophospholipase D activity of autotaxin, the dominant
52 ntly ATX was shown to be responsible for the lysophospholipase D activity that generates lysophosphat
53 s LPA from lysophosphatidylcholine (LPC) via lysophospholipase D activity, but alternative enzymatic
54 was shown recently to be identical to serum lysophospholipase D activity, producing lysophosphatidic
57 levels in the vessel of both autotaxin, the lysophospholipase D enzyme responsible for generation of
58 ATX, NPP2) has recently been shown to be the lysophospholipase D responsible for synthesis of the bio
59 cant quantities of autotaxin (ATX; ENPP2), a lysophospholipase D that catalyzes the conversion of lys
64 cked LPA in inhibiting autotaxin, a secreted lysophospholipase D that produces LPA in biological flui
65 autotaxin (ATX), which is a secreted form of lysophospholipase D that produces lysophosphatidic acid
68 ospholipase (PLB1) is a secreted enzyme with lysophospholipase hydrolase and lysophospholipase transa
69 yme that demonstrates phospholipase B (PLB), lysophospholipase hydrolase and lysophospholipase transa
71 s act as both acyl-protein thioesterases and lysophospholipases in vitro, we demonstrate by transfect
72 -Leyden crystal (CLC) protein, or eosinophil lysophospholipase, is a characteristic protein of human
73 main-containing-3 (PNPLA3), neurocan (NCAN), lysophospholipase-like 1 (LYPLAL1), glucokinase regulato
76 phatidylcholine acyltransferase (LPCAT), and lysophospholipase (LYPLA) can contribute to the differen
79 suggesting that this enzyme may be a type of lysophospholipase (LysoPLA) with lysolecithin as its phy
80 y, does not act as an acceptor in either the lysophospholipase or the PLA2 reaction, but can affect e
83 ed enzyme alpha/beta-hydrolase 4 (Abh4) as a lysophospholipase/phospholipase B that selectively hydro
85 me of S. meliloti, we identified a potential lysophospholipase (SMc04041) and two predicted patatin-l
87 or 1 (LPAR1) or autotoxin (ATX), a secretory lysophospholipase that catalyzes LPA production, inhibit
90 may contribute to the total phospholipase B/lysophospholipase/transacylase activities of the cell.
91 recently discovered that a novel lipoprotein lysophospholipase, VolA, localizes on the surface of the
92 ly determine whether or not CLC protein is a lysophospholipase, we reassessed its enzymatic activity
93 es, comparable in size with human pancreatic lysophospholipase, which co-purifies in small quantities
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