A preliminary neutron diffraction analysis of Achromobacter protease I

A preliminary neutron diffraction analysis of Achromobacter protease I
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无色杆菌蛋白酶 I 的初步中子衍射分析

DOI：
10.1088/1742-6596/251/1/012032
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发表时间：
2010
期刊：
Journal of Physics: Conference Series
影响因子：
--
通讯作者：
N. Niimura
N. Niimura
中科院分区：
--
文献类型：
--
作者：
Y. Ohnishi;T. Masaki;Taro Yamada;K. Kurihara;I. Tanaka;N. Niimura

文献摘要

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Achromobacter protease I (API, E.C. 3.4.21.50) is one of the serine proteases produced by Achromobacter lyticus M497-1. API is distinct from the other tripsin type protease in its lysine specificity. The neutron structure analysis of catalytic triad with Trp169 and His210 was presented. His57 was double protonated and formed hydrogen bonds to Ser194Oγ and Asp113Oδ1, Oδ2.