Structure–Function Relationships of Proteolytic Enzymes. by P. Desnuelle, H. Neurath, M. Ottesen

By P. Desnuelle, H. Neurath, M. Ottesen

Structure–Function Relationships of Proteolytic Enzymes presents details pertinent to the elemental points of proteolytic enzymes. This ebook offers the old position of proteolytic enzyme as a gaggle in protein and enzyme chemistry.

Organized into 23 chapters, this e-book starts with an summary of the implications got from research at the chymotrypsinogens of porcine beginning. this article then examines the variations of amino acid series among chymotrypsin, trypsin, and elastase that impact the substrate binding website, which replicate the specificity transformations among those enzymes. different chapters think about the kinetic parameters relating to the trypsin-catalyzed hydrolysis of numerous version peptides. This e-book discusses to boot the acetylation of trypsin, which lead to useful effects various from entire inactivation to promoting of job. the ultimate bankruptcy offers with the actual homes of stem bromelain compared to the information for 3 different sulfhydryl proteases of plant origin.

This booklet is a precious source for enzymologists, microbiologists, and biochemists.

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Read Online or Download Structure–Function Relationships of Proteolytic Enzymes. Proceedings of the International Symposium, Copenhagen, June 16–18, 1969, No. 37 in the Series of the International Union of Biochemistry Sponsored Symposia PDF

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Additional info for Structure–Function Relationships of Proteolytic Enzymes. Proceedings of the International Symposium, Copenhagen, June 16–18, 1969, No. 37 in the Series of the International Union of Biochemistry Sponsored Symposia

Example text

2). 7. This binding does not seem to involve any structural reorganization and has no effect on the rate of formation of inert proteins, but it accelerates very clearly the rate of hydrolysis by trypsin of the LyslIe bond (Fig. 2). The analysis of the results in Table I shows that this binding Bite is on the four N-terminal aspartyl residues. With trypsinogen, when the concentration of Ca+ + increases from 4 mM only if the most specific site is saturated to 50 mM when both binding sites are saturated Kill decreases by a factor of 3 and kcat is not changed.

1, temperature 20 0 C. Glazer (1965), proflavin is a competitive inhibitor of chymotrypsin and trypsin. We studied the dissociation of the dye-chymotrypsin complex at acidic pH (Delaage et al. 1968) and found that it follows practically exactly the structural transition of chymotrypsin described in Fig. 3. This experiment strongly suggests that the acidic conformational change destroys, at least partly, the proper geometry of the specificity site in chymotrypsin. To strengthen this conclusion, Fig.

Thus, even group-specific reagents may serve as useful probes for resi­ dues of functional import. Experiments of this nature have been carried out with trypsin using N - a c e t y l i m i d a z o l e and tetranitrometha­ ne. Both of these reagents were introduced by ments of chymotrypsin (Sanders et al. 1969). Thus, available evidence supports the h y p o ­ Riordan, Vallee, and their colleagues who showed that their primary reactivity was with thetical model and allows both for its specific tyrosyl residues exposed on protein surfaces examination and for its use in probing func­ (Riordan et al.

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