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Lysozyme hydrolysis studies

Additional studies of the enzyme-substrate complementarity in other complexes along the reaction path are under way. Since the initial report of an alternative pathway for lysozyme hydrolysis (8,9.28) work on the solution hydrolysis of glucosides has demonstrated the existence of a ring opening mechanism (29,30). ... [Pg.387]

Aiba, S. 1992. Studies on chitosan 4. Lysozymic hydrolysis of partially A-acetylated chitosans. International Journal of Biological Macromolecules 14 225-228. [Pg.79]

S. Aiba, Studies on chitosan Lysozymic hydrolysis of partially N-acetylated chitosans, Int J. Biol Macromol, 14 (4), 225-228,1992. [Pg.57]

The mechanism of the lysozyme reaction is shown in Figures 16.36 and 16.37. Studies using O-enriched water showed that the Ci—O bond is cleaved on the substrate between the D and E sites. Hydrolysis under these conditions incorporates into the Ci position of the sugar at the D site, not into the oxygen at C4 at the E site (Figure 16.36). Model building studies place the cleaved bond approximately between protein residues Glu and Asp. Glu is in a nonpolar or hydrophobic region of the protein, whereas Asp is located in a much more polar environment. Glu is protonated, but Asp is ionized... [Pg.529]

Hen egg-white lysozyme catalyzes the hydrolysis of various oligosaccharides, especially those of bacterial cell walls. The elucidation of the X-ray structure of this enzyme by David Phillips and co-workers (Ref. 1) provided the first glimpse of the structure of an enzyme-active site. The determination of the structure of this enzyme with trisaccharide competitive inhibitors and biochemical studies led to a detailed model for lysozyme and its hexa N-acetyl glucoseamine (hexa-NAG) substrate (Fig. 6.1). These studies identified the C-O bond between the D and E residues of the substrate as the bond which is being specifically cleaved by the enzyme and located the residues Glu 37 and Asp 52 as the major catalytic residues. The initial structural studies led to various proposals of how catalysis might take place. Here we consider these proposals and show how to examine their validity by computer modeling approaches. [Pg.153]

Because 0-acyl chitins appear to be scarcely susceptible to lysozyme, the susceptibility of DBG to Upases has been studied to obtain insight into its biodegradability in vivo. The changes in infrared and X-ray diffraction spectra of the fibers support the slow degradation of DBG by Upases [125,126]. The chemical hydrolysis of DBG to chitin is the most recent way to produce regenerated chitin. [Pg.164]

The reduction of the rate of hydrolysis due to lowering the temperature 45 C in the solution containing 7 M NH4NO3 is Ah2o/ nh4N03,7m = 4.78, with an activation energy of 5 kcal mol . This solvent is not suitable for low-temperature studies of the lysozyme reaction. [Pg.261]

In one case, a small peptide with enzyme-like capability has been claimed. On the basis of model building and conformation studies, the peptide Glu-Phe-Ala-Ala-Glu-Glu-Phe-Ala-Ser-Phe was synthesized in the hope that the carboxyl groups in the center of the model would act like the carboxyl groups in lysozyme 17). The kinetic data in this article come from assays of cell wall lysis of M. lysodeikticus, chitin hydrolysis, and dextran hydrolysis. All of these assays are turbidimetric. Although details of the assay procedures were not given, the final equilibrium positions are apparently different for the reaction catalyzed by lysozyme and the reaction catalyzed by the decapeptide. Similar peptide models for proteases were made on the basis of empirical rules for predicting polypeptide conformations. These materials had no amidase activity and esterase activity only slightly better than that of histidine 59, 60). [Pg.209]

A pathway (Scheme I) (8.9) for the hydrolysis of oligoglycosides by lysozyme that differs from the previously accepted mechanism (Scheme II) (3,10-12) is described in this section. The alternative pathway, suggested by results of a 55-ps MD simulation of the lysozyme (GlcNAc)e complex (1), is consistent with the available experimental data and with stereoelectronic considerations. Experimental data have demonstrated that Glu 35 and Asp 52 are essential, as shown by recent site-directed mutagenesis results (13.) which corroborate chemical modification studies (3.14 and references cited therein), and that the reaction proceeds with retention of configuration at Ci Q and references cited therein). A fundamental feature of the alternative pathway is that an endocyclic bond is broken in the initial step, in contrast to the exocyclic bond cleavage in the accepted mechanism. [Pg.378]

Lysozyme catalyzes the hydrolysis of the polysaccharide component of plant cell walls and synthetic polymers of j8(l — 4)-linked units of A-acetylglucosamine (NAG) (Chapter 1). It is expected from studies on nonenzymatic reactions that one of the intermediates in the hydrolytic reaction is a oxocarbenium ion in which the conformation of the glucopyranose ring changes from a full-chair to a sofa (half-chair) conformation (Chapter 1). The transition state analogue I, in which the lactone ring mimics the carbonium ion-like transition state n, binds tightly to lysozyme = 8.3 X 10 8M.10... [Pg.190]

Hen egg white lysozyme is a small protein of Mr 14 500 and 129 amino acid residues. This enzyme was introduced in Chapter 1, where it was pointed out that examination of the crystal structure of the enzyme stimulated most of the solution studies. Hen egg white lysozyme has the distinction of being the first enzyme to have had its structure solved by x-ray crystallography.207 It is an atypical member of the hexosaminidase class of glycosyl transfer enzymes. It catalyzes the hydrolysis of substrates with retention of stereochemistry. T4 lysozyme was for many years thought to have the same fold and mechanism of lysozyme, despite there being no sequence homology. But it has now been found that the T4 enzyme has inversion of configuration and so operates by a different mechanism.208,209 A mechanism proposed for the enzymatic reaction was based on the structure of the... [Pg.587]

Lysozyme hydrolyses oligoglycosides. It is a P-glucosidase that cleaves a P-glucoside bond and releases P-glucose. Although lysozyme was the first enzyme to have its high resolution crystal structure determined (Blake et al. 1965) and the catalysis has been studied for many years, the mechanism is not fully understood and remains a source of discussion (Kirby 1987 Mooser 1992). Two features of the hydrolysis mechanism are unresolved (1) Whether the initial bond-breaking occurs via an... [Pg.164]


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