净化、描述和分析的初级和二级结构prolyl oligopeptidase从人类淋巴细胞。证据表明,这种酶属于α/β水解酶折叠的家庭。
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古森斯F·德·梅斯特我,Vanhoof G•D, Vriend G, Scharpe年代
净化、描述和分析的初级和二级结构prolyl oligopeptidase从人类淋巴细胞。证据表明,这种酶属于α/β水解酶折叠的家庭。
欧元。1995 10月15日,233 (2):432 - 41。
- PubMed ID
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7588785 (在PubMed]
- 文摘
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Prolyl oligopeptidase分离和纯化从人类淋巴细胞同质性,产生一个特定活动的7780亩/毫克。使用凝胶排阻层析法匹配的分子质量76 kDa通过SDS /页面。这提供了证据表明prolyl oligopeptidase单体。等电点为4.8根据等电点聚焦在自由的解决方案。Di-isopropyl fluorophosphate和氟化phenylmethylsulphonyl完全废除活动,分类作为一个丝氨酸蛋白酶的酶。p-chloromercuribenzoic酸表示的抑制活性部位附近的自由巯基的重要性。α1-Casein和鸟氨酸脱羧酶,两种蛋白质包含一个害虫序列,抑制prolyl oligopeptidase,但没有水解。这表明prolyl oligopeptidase不是根据PEST-dependent参与蛋白质的代谢途径。α1-Antitrypsin部分抑制酶,但相比之下,抑肽酶没有。无法打通促肾上腺皮质激素的释放因子、泛素蛋白和抑肽酶,连同之间缓激肽的水解Pro7-Arg8证实的亲和力prolyl oligopeptidase对小肽。 Multiple sequence alignment does not reveal any similarity with proteases of known tertiary structure. Secondary-structure prediction displays striking similarity with dipeptidyl peptidase IV and acylaminoacyl peptidase. Two characteristic features of the members of the prolyl oligopeptidase family of serine proteases are high-lighted: the linear arrangement of the catalytic triad is nucleophile-acid-base and the proteolytic cleavage releasing the catalytically active C-terminal region of around 500 amino acids from the N-terminal sequence. Secondary structure prediction and comparison of the active-site of serine proteinases with known three-dimensional coordinates prove that Asp641 is the third member of the catalytic triad. The secondary structural organization of the protease domain of prolyl oligopeptidase is in accordance with the alpha/beta hydrolase fold.