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Serine esterase inhibitors

SERINE DEHYDRATASE SERINE DEHYDRATASE SERINE DEHYDROGENASE Serine esterase inhibitor, irreversible, PHENYLMETHYLSULFONYL FLUORIDE SERINE HYDROXYMETHYLTRANSFERASE SERINE PALMITOYLTRANSFERASE Serine protease inhibitor, irreversible, PHENYLMETHYLSULFONYL FLUORIDE Serine proteinase inhibitor,... [Pg.780]

Like pancreatic lipase, this enzyme is clearly dependent on a lipid/water interface for maximal activity, where it also may reach a very high catalytic rale, Abo like pancreatic lipase, it is not inhibited by serine esterase inhibitors like DFP orPMSF. [Pg.200]

In this connection, it is noteworthy that some cellular proteins, including hoimones and other secretory polypeptides, are produced by limited cleavage of precursors. The proteases involved are not fully characterized, but seem to be located on membrane-bound structures (1J, 27, 28), have optimiim activities at neutral to slightly alkaline pH, and are sensitive to phosphofluoridate or other serine esterase inhibitors (12, 27, 29). [Pg.152]

They are susceptible to DFP or PMSF, which is a serine esterase inhibitor. [Pg.320]

A potent irreversible inhibitor (abbreviated DFP) of many serine proteinases and serine esterases (especially acetylcholinesterase). This substance is EXTREMELY POISONOUS, but the vapor state can be minimized by using dry, water-miscible solvents such as 2-propanoL. Aqueous solutions become inactivated by hydrolysis, but solutions made with dry 2-propanol are stable at -20°C for many months. [Pg.203]

The greatly increased nucleophilicity of the catalytic serine distinguishes it from all other serine residues and makes it an ideal candidate for modification via activity-based probes [58]. Of the electrophilic probe types to profile serine hydrolases, the fluorophosphonate (FP)-based probes are the most extensively used and were first introduced by Cravatt and coworkers [38, 39]. FPs have been well-known inhibitors of serine hydrolases for over 80 years and were first applied as chemical weapons as potent acetylcholine esterase inhibitors. As FPs do not resemble a peptide or ester substrate, they are nonselective towards a particular serine hydrolase, thus allowing the entire family to be profiled. FPs also show minimal cross-reactivity with other classes of hydrolases such as cysteine-, metallo-, and aspartylhydrolases [59]. Furthermore, FP-based probes react only with the active serine hydrolase, and not the inactive zymogen, allowing these probes to interact only with functional species within the proteome [59]. Extensive use of this probe family has demonstrated their remarkable selectivity for serine hydrolases and resulted in the identification of over 100 distinct serine hydrolases... [Pg.12]

The inhibitory and postinhibitory steps in the interaction of an OP compound with a serine hydrolase (E-OH) sueh as NTE or AChE are illustrated in Figure 57.6. The mathe-matieal relationships deseribing the kineties of irreversible inhibition of serine esterases by OP eompounds and post-inhibitory reaetions of the enzyme-inhibitor adduet (eonjugate) summarized here were elegantly set forth in the elassie work by Aldridge and Reiner (1972), and synopses are available in other sourees (Clothier et al, 1981 Main, 1980 Riehardson, 1992). The equations featured below... [Pg.863]

Since MGL is a serine hydrolase, its sensitivity to many of the available serine hydrolase inhibitors has been explored (Table 3). The results support the hypothesis that MGL can be inhibited by compounds that interact with its reactive serine. On the other hand, the potencies of the inhibitors are quite variable in some cases, this likely reflects differences in assay methodology (i.e., substrate concentration, pH, form of the enzyme). However, in a few cases, the same assay conditions revealed very different inhibitory potencies (e.g., compare the platelet and macrophage membrane studies by Di Marzo et al. 1999). In any event, studies of these compounds are not likely to yield selective inhibitors of MGL. All of these compounds are inhibitors of FAAH (see above) and many are also inhibitors of PLA2, diacylglycerol lipase, and acetylcholine esterase, among other hydrolases. By analogy to the development of the URB series of FAAH inhibitors (Kathuria et al. 2003), it is likely that selective inhibitors of MGL will come from other synthetic avenues. [Pg.198]

Antithrombin III (AT-III), a single-chain glycoprotein of 58 kDa and 480 amino acids, is synthesized in the liver. It is a serine protease inhibitor, and acts as the most important inhibitor in the coagulation cascade to avoid blood clot formation. AT-III inhibits a wide spectram of serine proteases induding thrombin, factors IXa, Xa and XIa, kaUikrein, plasmin, urokinase, Cl-esterase, and trypsin. AT-III interacts with heparin by binding to specific sul-fated and non-sulfated monosaccharide units on heparin. The binding of AT-III to heparin enhances the inhibition of factors IXa, Xa, and thrombin. [Pg.855]

Enzyme inhibitors are often poisonous. For example, diisopropyl-fluorophosphate is a nerve poison because the enzyme acetylcholinesterase has a reactive site serine. Chymotrypsin and acetylcholinesterase are both members of the class of enzymes known as serine esterases, which are all inhibited by diisopropylfluorophosphate. [Pg.111]

Several protease inhibitors from plasma, tissue, and plant sources did not inhibit the esterase and C3 convertase activity (Cooper, 1975b). Recently, Medicus et al. (1976a) proposed that C2a is a serine esterase. [Pg.184]

The protease/esterase inhibitor diisopropyl phosphofluoridate (LFP) was shown to block the cleavage of poliovirus polyprotein (7) This implicates a protease with a serine-containing active site. [Pg.169]

Analytical procedures applied to diagnosis and retrospective verification of exposure to OP include (Worek et al., 2005) (i) biochemical determination of ChE activity (ii) identification of imbound OP (iii) identification of decomposition products (iv) fluoride-induced reactivation of inhibited ChE, followed by analysis of the inhibitor and (v) analysis of phosphyl-protein-adducts after tryptic digestion of the protein. The last procedure is regarded to be the most specific and sensitive, but it has the drawback of being strongly dependent on the analysis of butyrylcholinesterase (BChE), the most abim-dant plasma serine esterase with a half-life of about 16 days. [Pg.117]


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See also in sourсe #XX -- [ Pg.26 ]




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Esterase

Esterase inhibitor

Esterases

Esterases esterase

Inhibitors esterases)

Inhibitors of Serine Esterases

Inhibitors serine esterases

Inhibitors serine esterases

Serine esterase

Serine esterases

Serine inhibitor

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