Read e-book online Acid Proteases:Structure, Function, and Biology PDF

By Bent Foltmann, Vibeke Barkholt Pedersen (auth.), Jordan Tang (eds.)

In the prior ten years, a few court cases of symposia at the constitution and serve as of proteolytic enzymes were pub­ lished. Their assurance of acid proteases has been restricted, often end result of the loss of major new info at the constitution of those enzymes. within the final 4 years, besides the fact that, the first and tertiary constructions of a few acid proteases were deter­ mined, prompting the necessity to talk about the meanings of the previous facts and the chances for brand spanking new experimentations. It was once for this goal that the "Conference on Acid Proteases: constitution, functionality, and Biology" used to be geared up. It happened on the collage of Oklahoma on November 21-24, 1976. This booklet is a set of the most lectures introduced on the convention. Acid Proteases, by way of definition refers to a gaggle of proteases having an optimum pH in acidic recommendations. The vintage examples are pepsin and chymosin. a few catalytic positive aspects are patently shared via those proteases, such a lot significantly, their inhibition via pepstatin. using energetic center-directed inactivators equivalent to diazoacetyl­ norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has proven that catalytic aspartyl residues are found in almost all these enzymes. those obvious cornmon good points have triggered the recommendation through numerous investigators to call this staff of enzymes "aspartyl proteases" or "carboxyl proteases".

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Shutzkever, N. , and Andreeva, N. S. (1968) Kristallogr. 13, 44-48 Andreeva, N. , Borisov, V. , Melik-Adamjan, V. , Raiz, V. , Trofimova, L. , and Shutzkever, N. E. (1971) Mol. Biophys. , and Perutz, M. F. (1967) J. Mol. BioI. 28, 117-156 Blow, D. , and Crick, F. H. C. (1959) Acta Crystallogr. , Chen, K. C. , and Lanier, J. P. (1973) Proc. Natl. Acad. Sci. A. 70, 3437-3439 Stepanov, V. , and Vaganova, T. I. (1968) Biochem. Biophys. iRes. Commun. , and Tang, J. (1972) J. BioI. Chern. 247, 2704-2710 Kitson, T.

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