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Phospholipase Bacillus cereus

Figure 16 Schematic drawing of the active site of Bacillus cereus phospholipase C complexed with a phosphonate substrate analog inhibitor (reproduced by permission of Springer from Hergenrother and... Figure 16 Schematic drawing of the active site of Bacillus cereus phospholipase C complexed with a phosphonate substrate analog inhibitor (reproduced by permission of Springer from Hergenrother and...
Massing U, Eibl H (1994) Substrates for phospholipase C and sphingomyelinase from Bacillus cereus. In Woolley P, Petersen SB (eds) Lipases. Their structure, biochemistry and application. Cambridge University Press, Cambridge, p 225... [Pg.165]

A consistent catalytic mechanism of phospholipase C from Bacillus cereus based on molecular mechanics calculations was reported by da Graja Thrige and coworkers . The... [Pg.20]

A considerable amount of data has been reported on the substrate preference of the phospholipase C present in the organism Bacillus cereus. Interestingly, three phospholipases C have been isolated and purified, the first of which has high specificity for phosphatidylcholine, the second for phospha-tidylinositol, and the third for sphingomyelin (often termed sphingomyelinase). Similar substrate requirements have been noted in the phospholipase C isolated from other bacteria. [Pg.88]

An additional structure proof assay involves the use of phospholipase C isolated from Bacillus cereus. This reaction, which is conducted in the exact same way as described earlier in this chapter, yields an alkylacyl glycerol and an 0-phosphocholine. These two products can be analyzed by the same procedures as outlined at that point. [Pg.108]

El-Sayed, M. Y., DeBose, C. D., Coury, L. A., and Roberts, M. F. (1985) Sensitivity of phospholipase C (Bacillus cereus) activity to phosphatidylcholine structural modifications, Biochim. Biophys. Acta 837, 325-335. [Pg.199]

Doi O., Nojima, S. 1971. Phospholipase C from Bacillus cereus. Biochim. Biophys. Acta 248, 234-244. [Pg.537]

Heinz, D.W., Ryan, M., Bullock, T.L., and Griffith, O.H., 1995, Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myoinositol EMBOJ. 14 3855-3863. [Pg.130]

Two zinc enzymes with dinuclear active sites have been characterized, promoting interest in dinuclear zinc model systems. Phospholipase C from Bacillus cereus 103) contains three zinc atoms per subunit. An X-ray crystal structure determination at good resolution (1.5 A) revealed that two of these constitute a dinuclear site with a Zn—Zn distance of 3.3 A. The metal atoms are symmetrically bridged by an aspartate residue and by OH or H2O. Each zinc atom has approximate trigonal bipyramidal geometry with the ligation shown in Fig. 22. The third zinc atom is quite close to the bridged pair. [Pg.351]

Martin SF, Follows BC, Hergenrother PJ, Franklin CL. A novel class of zinc-binding inhibitors for the phosphatidylcholine-preferring phospholipase C from Bacillus cereus. J. Org. Chem. 2000 65 4509-4514. [Pg.2046]

It is striking that at least two other enzymes, which carry out similar hydrolysis functions for phosphate esters, show related constellations of metal ions in the active site (60, 81). The high-resolution structure (1.5 A) of phospholipase C from Bacillus cereus (81) shows three five-coordinate... [Pg.238]

Bitty cream is caused by the hydrolysis of phospholipids of the fat globule membrane by phospholipases secreted by bacteria, especially Bacillus cereus, but also by psychrotrophs the partially denuded globules coalesce when closely packed, as in cream or in the cream layer of milk, forming aggregates rather than a solid mass of fat. [Pg.118]

A lipopeptide antibiotic complex from cultures of Bacillus cereus. As phospholipase A2, C, and D inhibitors the P. have antiallergic and bronchodilatory activities. They are yellow solids and have been characterized as the potassium salts, see formula and table. UL J. Antibiot. (Tokyo) 39, 737, 745, 755, 860 (1986). -[HS 294190]... [Pg.501]

Compound 126 has been prepared as an isosteric and isopolar inhibitor of a phosphatidylinositol-specific phospholipase C (PI-PLC) fKsm Bacillus cereus ... [Pg.245]

The available methods are suitable only for fractionation according to the basic moieties, whereas phosphatides differing in the lipid moieties are not separated from each other. Compounds which contain differing functional groups in the lipid moiety can be indirectly separated from each other using the following procedure [174] the enzyme phospholipase C from bacteria [Clostridium perfringens or Bacillus cereus) splits off phosphoryl ethanolamine and phosphoryl choline from the phosphatides. The lipophilic hydrolysis products can then be separated as acetyl derivatives (I, II, III) on adsorbent layers. [Pg.392]


See other pages where Phospholipase Bacillus cereus is mentioned: [Pg.604]    [Pg.300]    [Pg.604]    [Pg.300]    [Pg.247]    [Pg.134]    [Pg.248]    [Pg.598]    [Pg.135]    [Pg.90]    [Pg.90]    [Pg.139]    [Pg.494]    [Pg.195]    [Pg.247]    [Pg.123]    [Pg.598]    [Pg.136]    [Pg.185]    [Pg.136]    [Pg.79]    [Pg.1496]    [Pg.1496]    [Pg.248]    [Pg.6743]    [Pg.610]    [Pg.667]    [Pg.509]    [Pg.112]   
See also in sourсe #XX -- [ Pg.83 ]

See also in sourсe #XX -- [ Pg.83 ]




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