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 couple of court cases of symposia at the constitution and serve as of proteolytic enzymes were pub­ lished. Their assurance of acid proteases has been restricted, regularly as a result of loss of major new details at the constitution of those enzymes. within the final 4 years, notwithstanding, the first and tertiary constructions of a couple of acid proteases were deter­ mined, prompting the necessity to talk about the meanings of the previous facts and the probabilities for brand new experimentations. It was once for this objective that the "Conference on Acid Proteases: constitution, functionality, and Biology" was once equipped. It came about on the collage of Oklahoma on November 21-24, 1976. This booklet is a suite 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 gains are patently shared by means of those proteases, so much significantly, their inhibition by means of pepstatin. using energetic center-directed inactivators akin 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 beneficial properties have triggered the advice by way of numerous investigators to call this workforce of enzymes "aspartyl proteases" or "carboxyl proteases".

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10). A survey of over 40 possible heavy atom reagents suggested that the crystals were comparatively unreactive. 3. The heavy atom salts listed in Table I gave reasonable heavy atom derivatives, although in most cases the reaction conditions needed to be carefully controlled to avoid loss of isomorphism. Estimates of FH, the magnitude of the contribution of the heavy atom to the structure factor, were calculated from isomorphous differences and anomalous differences to give combination coefficients (11-15) .

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Acknowledgment We wish to thank Professor H. Umegawa f9r a generous gift of pepstatin. 5 A native map. The thick black lines represent the pepstatin contours. oo" \:/ :r:;,. J>,. » -I z m :£ » :s: » z :0 OJ C CIl m o CRYSTAL STRUCTURE OF R. 5 A resolution. 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.

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