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Get Aspartic Proteinases: Structure, Function, Biology, and PDF

By Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana Rao-Naik (auth.), Kenji Takahashi (eds.)

ISBN-10: 1461357616

ISBN-13: 9781461357612

ISBN-10: 1461518717

ISBN-13: 9781461518716

The fifth foreign convention on Aspartic Proteinases used to be hung on September 19 via 24, 1993, at Naito Museum of Pharmaceutical technological know-how and undefined, Kawashima­ cho, Gifu Prefecture, Japan, approximately 15 miles northwest of Nagoya urban. approximately a hundred scientists attended the convention, together with fifty two from 14 international locations outdoors Japan, and 32 papers have been awarded by way of invited audio system, and fifty eight papers as posters. the aim of this convention used to be to offer and speak about new details at the constitution, functionality, and biology, and comparable themes, together with biomedical implications, of aspartic proteinases, and this publication is a collec­ tion of approximately the entire papers provided on the assembly. Aspartic proteinases belong to at least one of the 4 significant periods of proteinases, the others being serine, cysteine, and metalloproteinases, and are so known as considering they've got catalytic aspartic acid residues in universal of their lively websites. such a lot of them are optimally lively at acidic pH, therefore the long-used identify "acid proteinases," which, certainly, was once the main name of the 1st convention of this sequence. even if, a few of them are lively at round impartial pH, indicating their physiological roles in a much broader variety of pH than hitherto considered.

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Additional resources for Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications

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2 A resolution of bovine chymosin, J. Mol. Bioi. 221:1295-1309 (1991). 16. K. R. A. Padlan, E. Subramanian, S. N. R. 8 A resolution of the aspartic proteinase from Rhizopus chinensis, J. Mol. Bioi. 196:877-900, (1987). 17. G. R. 8 A resolution, J. Mol. Bioi. 163:299-361 (1983). 18. M. J. A. E. G. James, Crystallographic analysis of transition-state mimics bound to penicillopepsin phosphorous-containing peptide analogue, Biochern. 31:5201-5214 (1992). 19. L. A. T. H. B. P. Wood, B. 1 A resolution of endothiapepsin, J.

8 Aresolution, J. Mol. BioI. 214: 143-170 (1990). 2. S. G. James, Why does pepsin have a negative charge at very low pH? M. , Plenum Press, New York, London, 39-45 (1991). 3. K. A. W. D. R. Davies, Binding ofa reduced peptide inhibitor to the aspartic proteinase from Rhizopus chinensis: Implications for a mechanism of action, Proc. Natl. Acad. of Sci. 84:7009-7013 (1987). 4. C. R. Sielecki, K. H. Gelb, Crystallographic analysis of transition state mimics bound to penicillopepsin: difluorostatine- and difluorostatone-containing peptides, Biochem.

Enhelhardt Institute of Molecular Biology Russian Academy of Sciences Moscow, Russia INTRODUCTION A detailed inspection of the highly refined three-dimensional structure of porcine pepsin (1) offers the explanation of important properties of this enzyme. One of the first results of these studies was the detection of charged groups responsible for unusual electrophoretic behavior of pepsin and its abnormal stability in extreme acidic conditions (1,2). However, very important steps of these investigations have to explain the structural grounds for catalytic properties of pepsin.

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Aspartic Proteinases: Structure, Function, Biology, and Biomedical Implications by Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana Rao-Naik (auth.), Kenji Takahashi (eds.)

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