Download Acid Proteases:Structure, Function, and Biology by Bent Foltmann, Vibeke Barkholt Pedersen (auth.), Jordan Tang PDF

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

In the previous ten years, a few lawsuits of symposia at the constitution and serve as of proteolytic enzymes were pub­ lished. Their assurance of acid proteases has been restricted, mostly a result of 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of a couple of acid proteases were deter­ mined, prompting the necessity to talk about the meanings of the outdated information and the probabilities for brand spanking new experimentations. It used to be for this function that the "Conference on Acid Proteases: constitution, functionality, and Biology" used to be geared up. It happened on the college of Oklahoma on November 21-24, 1976. This ebook is a suite of the most lectures brought on the convention. Acid Proteases, by way of definition refers to a bunch of proteases having an optimum pH in acidic options. The vintage examples are pepsin and chymosin. a few catalytic positive aspects are patently shared by means of those proteases, so much particularly, their inhibition via pepstatin. using energetic center-directed inactivators similar to diazoacetyl­ norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane has proven that catalytic aspartyl residues are found in every one of these enzymes. those obvious cornmon good points have caused the recommendation by way of a number of investigators to call this staff of enzymes "aspartyl proteases" or "carboxyl proteases".

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The molecule is bilobal with a large cleft between the lobes. Pepstatin binds in the cleft near the catalytically active Asp-35. The overall folding of the molecule consists primarily of antiparallel B-strands, there being only four small helices. REFERENCES 1. 2. 3. 4. 5. 6. 7. 8. 9. 10. 11. 12. 13. 14. , and Yamamoto, T. (1967) Agr. BioI. Chern. 31, 710-717 Gripon, J. , Rhee, S. , Private Commun. , Jackson, K. , and Tang, J. (1975) Biochem. Biophys. Res. Commun. 63, 1106-1112 Graham, J. E. , and Hofmann, T.

And Fo1tmann, B. (1976) J. Dairy Res. 43, 85-95 31. , and Jenness, R. (1976) J. Dairy Sci. 59, 1398-1400 32. Henschel, M. J. (1973) Brit. J. Nutr. 30, 285-296 33. , and Bose, J. (1962) Proc. XVI Int. Dairy Congr. B, 643-654 34. , and Ry1e, A. P. (1967) Biochem. J. 104, 735-741 35. Meitner, P. , and Kasse11, B. (1971) Biochem. J. 121, 249-256 36. Rajagopa1an, T. , and Stein, W. H. (1966) J. BioI. Chern. 241, 4940-4950 37. Fo1tmann, B. (1964) C. R. Trav. Lab. Carlsberg 34, 319-325 37a. , and Takahashi, K.

The two lobes have contacts over a large area giving 38 E. SUB RAMAN IAN ET AL. Figure 2: Stereo drawing of the a-carbon chain tracing for the Rhizopus enzyme, viewed along the crystallographic b-axis. The NH 2 -terminal end of the chain is located in the right hand lobe. CRYSTAL STRUCTURE OF R. chinensis PROTEASJ;: 39 rise to a broad waist. The COOH-terminal lobe consists of eleven extended S-strands, which together with one short helical region, are wrapped around what is probably a hydrophobic core.

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