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蛋白酶ω的初步晶体学数据。

Preliminary crystallographic data for protease omega.

作者信息

Pickersgill R W, Sumner I G, Goodenough P W

机构信息

Department of Biotechnology and Enzymology, Reading Laboratory, Shinfield, England.

出版信息

Eur J Biochem. 1990 Jun 20;190(2):443-4. doi: 10.1111/j.1432-1033.1990.tb15594.x.

DOI:10.1111/j.1432-1033.1990.tb15594.x
PMID:2194805
Abstract

Protease omega from Carica papaya L. has been purified and crystallized. The crystals are trigonal, space group P3(1)12 (or P3(2)12), with a = 7.42 +/- 0.02 nm, c = 7.79 +/- 0.02 nm with one molecule in the asymmetric unit. The crystals diffract to 0.19-nm resolution using synchrotron radiation.

摘要

番木瓜蛋白酶ω已被纯化并结晶。晶体呈三角形状,空间群为P3(1)12(或P3(2)12),a = 7.42 +/- 0.02纳米,c = 7.79 +/- 0.02纳米,不对称单位中有一个分子。使用同步辐射,晶体的衍射分辨率达到0.19纳米。

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引用本文的文献

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Structure of chymopapain M the late-eluted chymopapain deduced by comparative modelling techniques and active-centre characteristics determined by pH-dependent kinetics of catalysis and reactions with time-dependent inhibitors: the Cys-25/His-159 ion-pair is insufficient for catalytic competence in both chymopapain M and papain.
糜蛋白酶M的结构:通过比较建模技术推导得出的晚期洗脱糜蛋白酶,以及通过pH依赖性催化动力学和与时间依赖性抑制剂反应确定的活性中心特征:半胱氨酸-25/组氨酸-159离子对对于糜蛋白酶M和木瓜蛋白酶的催化活性而言均不充分。
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):805-20. doi: 10.1042/bj3000805.
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