Tetaud E, Hall D R, Gourley D G, Leonard G A, Arkison S, Barrett M P, Hunter W N
The Wellcome Trust Building, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland.
Acta Crystallogr D Biol Crystallogr. 1998 Nov 1;54(Pt 6 Pt 2):1422-4. doi: 10.1107/s0907444998004909.
6-Phosphogluconate dehydrogenase is one of the seven enzymes involved in the pentose phosphate pathway. Crystals of a mammalian and a protozoan enzyme have been obtained previously and structures determined. It is reported here that a bacterial 6-phosphogluconate dehydrogenase, from Lactococcus lactis, has been purified and used in crystallization trials. Large prisms suitable for a detailed structural analysis have been obtained and characterized as orthorhombic, space group F222, with a = 70.4, b = 105.7, c = 474.6 A. Diffraction has been observed to 2.2 A resolution using synchrotron radiation. Structural analysis, in combination with ongoing biochemical characterization, will assist the elucidation of the structure-activity relationships of this enzyme.
6-磷酸葡萄糖酸脱氢酶是戊糖磷酸途径中涉及的七种酶之一。此前已获得一种哺乳动物和一种原生动物酶的晶体并确定了其结构。本文报道,已从乳酸乳球菌中纯化出一种细菌6-磷酸葡萄糖酸脱氢酶,并用于结晶试验。已获得适合详细结构分析的大棱柱晶体,其特征为正交晶系,空间群F222,a = 70.4,b = 105.7,c = 474.6 Å。使用同步辐射已观察到分辨率为2.2 Å的衍射。结构分析与正在进行的生化特性鉴定相结合,将有助于阐明该酶的构效关系。