来自根瘤菌属菌株MTP - 10005的马来酰乙酸还原酶的结晶及初步X射线衍射研究。
Crystallization and preliminary X-ray diffraction studies of maleylacetate reductase from Rhizobium sp. strain MTP-10005.
作者信息
Fujii Tomomi, Goda Yuko, Yoshida Masahiro, Oikawa Tadao, Hata Yasuo
机构信息
Institute for Chemical Research, Kyoto University, Uji, Kyoto 611-0011, Japan.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Aug 1;64(Pt 8):737-9. doi: 10.1107/S1744309108022537. Epub 2008 Jul 31.
Abstract
Maleylacetate reductase (EC 1.3.1.32), which catalyzes the reduction of maleylacetate to 3-oxoadipate, plays an important role in the aerobic microbial catabolism of resorcinol. The enzyme has been crystallized at 293 K by the sitting-drop vapour-diffusion method supplemented with a microseeding technique, using ammonium sulfate as the precipitating agent. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 56.85, b = 121.13, c = 94.09 A, beta = 101.48 degrees , and contained one dimeric molecule in the asymmetric unit. It diffracted to 1.79 A resolution.
摘要
马来酰乙酸还原酶（EC 1.3.1.32）催化马来酰乙酸还原为3-氧代己二酸，在间苯二酚的需氧微生物分解代谢中起重要作用。该酶通过坐滴气相扩散法并辅以微种子技术，以硫酸铵作为沉淀剂，在293 K下结晶。晶体属于单斜空间群C2，晶胞参数a = 56.85，b = 121.13，c = 94.09 Å，β = 101.48°，不对称单元中包含一个二聚体分子。其衍射分辨率达到1.79 Å。
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