Britton K L, Rogers H F, Asano Y, Dairi T, Kato Y, Stillman T J
Krebs Institute for Biomolecular Research, Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, England.
Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):124-6.
The novel NAD+-linked opine dehydrogenase from a soil isolate Arthrobacter sp. strain 1C belongs to an enzyme superfamily whose members exhibit quite diverse substrate specificities. Crystals of this opine dehydrogenase, obtained in the presence or absence of co-factor and substrates, have been shown to diffract to beyond 1.8 A resolution. X-ray precession photographs have established that the crystals belong to space group P21212, with cell parameters a = 104.9, b = 80.0, c = 45.5 A and a single subunit in the asymmetric unit. The elucidation of the three-dimensional structure of this enzyme will provide a structural framework for this novel class of dehydrogenases to enable a comparison to be made with other enzyme families and also as the basis for mutagenesis experiments directed towards the production of natural and synthetic opine-type compounds containing two chiral centres.
从土壤分离物节杆菌属菌株1C中获得的新型烟酰胺腺嘌呤二核苷酸（NAD⁺）连接的章鱼碱脱氢酶属于一个酶超家族，其成员表现出相当多样的底物特异性。在存在或不存在辅因子和底物的情况下获得的这种章鱼碱脱氢酶晶体已显示出能衍射至1.8埃以上的分辨率。X射线进动照片已确定这些晶体属于空间群P21212，晶胞参数a = 104.9、b = 80.0、c = 45.5埃，不对称单元中有一个亚基。阐明这种酶的三维结构将为这类新型脱氢酶提供一个结构框架，以便能够与其他酶家族进行比较，同时也作为针对生产含有两个手性中心的天然和合成章鱼碱型化合物的诱变实验的基础。
