Biochemistry, Molecular Biology, and Physiology of by Moseley Waite (auth.), Anil B. Mukherjee (eds.)

By Moseley Waite (auth.), Anil B. Mukherjee (eds.)

During the previous decade there was a dramatic enlargement of our wisdom on phospholipases quite often, and phospholipase A2 (PLA2) particularly. development during this box has been glaring on many fronts, with novel info quickly amassing within the literature concerning the chemistry and molecular biology of this enzyme and its position in lots of vital physiological techniques. those contain mobile sign transduction through the G-protein cycle, and within the new release of many mobile mediators, comparable to the platelet activating issue (PAF) and the eicosanoids that perform the initiation and propagation of irritation, to say a number of. This symposium was once geared up to acquire an summary of present investigations in this enzyme from the viewpoint of its chemistry, molecular biology and body structure. one other very important concentration of this symposium issues the law of PLA2, together with endogenous and artificial inhibitors and activators of this enzyme. to study those vital components in PLA2 study we invited scientists who made major contributions during this box. The papers during this quantity are geared up to stress the hot advances in numerous parts of research, together with: (I) the constitution and mechanism of motion of PLA2, (2) mechanism of activation of PLA2, (3) molecular biology, body structure and endogenous inhibitors of this enzyme and eventually, (4) scientific investigations emphasizing the pathophysiological function of this enzyme in human ailments. the 1st article during this quantity is by means of Dr.

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Additional info for Biochemistry, Molecular Biology, and Physiology of Phospholipase A2 and Its Regulatory Factors

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These include the quaternary structure of the activated enzyme:Ca + + complex, the exact location of the two substrate molecules in that structure, the chemical mechanism of catalysis, and the specificity of the enzyme, to cite but a few. 45 ENVOI The mechanism of surface recognition by bifunctional enzymes, proposed in this paper, is consistent with all salient features of PLA2-catalyzed surface reactions and is validated experimentally for a few representative enzymes. For the time being, it is based only on a patchwork of experimental observations, select reports from the literature, and a lavish number of extrapolations.

Figure 8 shows a Group I phopholipase A2 (left, bovine pancrease) and a member of Group II (right,C. atrox), each in the "standard position" of figures 2 and 3, and both adorned with their solvent accessible coats of several colors. Differences in surface features become apparent in this display. Note the surface pockets leading to the site of activity . The tyrosine69 of the porcine molecule contrasted with the lysine-69 at the equivalent position dramatically alters the nature of access to this pocket.

Finally, our proposed bifunctional mechanism of surface recognition provides a new framework within which to address fundamental questions concerning PLA2 catalysis. These include the quaternary structure of the activated enzyme:Ca + + complex, the exact location of the two substrate molecules in that structure, the chemical mechanism of catalysis, and the specificity of the enzyme, to cite but a few. 45 ENVOI The mechanism of surface recognition by bifunctional enzymes, proposed in this paper, is consistent with all salient features of PLA2-catalyzed surface reactions and is validated experimentally for a few representative enzymes.

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