Aspartic Proteinases: Structure, Function, Biology, and by Ben M. Dunn, Paula E. Scarborough, W. Todd Lowther, Chetana

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

The fifth overseas 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 nations outdoors Japan, and 32 papers have been offered by means of invited audio system, and fifty eight papers as posters. the aim of this convention used to be to provide and talk about new info at the constitution, functionality, and biology, and similar subject matters, together with biomedical implications, of aspartic proteinases, and this publication is a collec­ tion of approximately the entire papers offered 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 that they've got catalytic aspartic acid residues in universal of their energetic websites. so much of them are optimally lively at acidic pH, as a result the long-used identify "acid proteinases," which, certainly, was once the key identify of the 1st convention of this sequence. in spite of the fact that, a few of them are lively at round impartial pH, indicating their physiological roles in a much wider diversity of pH than hitherto considered.

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Andreeva et al. it is hard to suppose that atomic displacements in the S3 binding pocket are main determinants of this feature. Detailed comparisons of the structure of pepsin to its liganded forms and to the structures of other aspartic proteinases offer the needed structural grounds which can explain their common properties, as well as some unique features of this enzyme. The whole work on the comparison of pepsin molecules to the other enzymes of this class is too large to be presented in one paper.

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Neidhart, J. w. M. , Plenum Press, New York, London, 9-21 (1991). II. G. R. 8 A resolution, Nature (London) 319:33-35 (1986). 12. R. Sielecki, M. J. G. 8 A resolution, J. Mol. Bioi. 219:671-692 (1991). 13. A. Hartsuck, G. J. Remington, The high-resolution crystal structure of porcine pepsinogen, Proteins: Structure, Function and Genetics 13: 1-25 (1992). 14. L. L. Winborn, J. Nachman, A. 3 A resolution, Proteins: Structure. Function and Genetics 8:82-101 (1990). 15. M. Newman, M. Safro, C. Frazao, G.

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