来自南极嗜冷菌嗜盐浮游交替单胞菌A23的α-淀粉酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23.
作者信息
Aghajari N, Feller G, Gerday C, Haser R
机构信息
Laboratoire d'Architecture et Fonction des Macromolécules Biologiques, UPR9039, Institut de Biologie Structurale et Microbiologie, IFRI, CNRS, Marseille, France.
出版信息
Protein Sci. 1996 Oct;5(10):2128-9. doi: 10.1002/pro.5560051021.
Abstract
A cold-active alpha-amylase was purified from culture supernatants of the antarctic psychrophile Alteromonas haloplanctis A23 grown at 4 degrees C. In order to contribute to the understanding of the molecular basis of cold adaptations, crystallographic studies of this cold-adapted enzyme have been initiated because a three-dimensional structure of a mesophilic counterpart, pig pancreatic alpha-amylase, already exists. alpha-Amylase from A. haloplanctis, which shares 53% sequence identity with pig pancreatic alpha-amylase, has been crystallized and data to 1.85 A have been collected. The space group is found to be C222(1) with a = 71.40 A, b = 138.88 A, and c = 115.66 A. Until now, a three-dimensional structure of a psychrophilic enzyme is lacking.
摘要
从在4℃下培养的南极嗜冷菌嗜盐栖热袍菌A23的培养上清液中纯化出一种冷活性α-淀粉酶。为了有助于理解冷适应的分子基础，已经开始对这种冷适应酶进行晶体学研究，因为已经存在嗜温对应物猪胰α-淀粉酶的三维结构。与猪胰α-淀粉酶具有53%序列同一性的嗜盐栖热袍菌α-淀粉酶已经结晶，并收集到了分辨率为1.85 Å的数据。发现空间群为C222(1)，a = 71.40 Å，b = 138.88 Å，c = 115.66 Å。到目前为止，还缺乏嗜冷酶的三维结构。
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