Rosenthal Cindy, Mueller Uwe, Panjikar Santosh, Sun Lianli, Ruppert Martin, Zhao Yu, Stöckigt Joachim
Department of Pharmaceutical Biology, Institute of Pharmacy, Johannes Gutenberg-University Mainz, Staudinger Weg 5, D-55099 Mainz, Germany.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Dec 1;62(Pt 12):1286-9. doi: 10.1107/S174430910605041X. Epub 2006 Nov 30.
Perakine reductase (PR) is a novel member of the aldo-keto reductase enzyme superfamily from higher plants. PR from the plant Rauvolfia serpentina is involved in the biosynthesis of monoterpenoid indole alkaloids by performing NADPH-dependent reduction of perakine, yielding raucaffrinoline. However, PR can also reduce cinnamic aldehyde and some of its derivatives. After heterologous expression of a triple mutant of PR in Escherichia coli, crystals of the purified and methylated enzyme were obtained by the hanging-drop vapour-diffusion technique at 293 K with 100 mM sodium citrate pH 5.6 and 27% PEG 4000 as precipitant. Crystals belong to space group C222(1) and diffract to 2.0 A, with unit-cell parameters a = 58.9, b = 93.0, c = 143.4 A.
佩拉金还原酶(PR)是高等植物醛酮还原酶超家族的一个新成员。来自萝芙木的PR通过对佩拉金进行NADPH依赖的还原反应参与单萜吲哚生物碱的生物合成,生成劳卡弗林碱。然而,PR也能还原肉桂醛及其一些衍生物。在大肠杆菌中对PR的一个三重突变体进行异源表达后,通过悬滴气相扩散技术,在293 K下,以100 mM柠檬酸钠pH 5.6和27% PEG 4000作为沉淀剂,获得了纯化和甲基化酶的晶体。晶体属于空间群C222(1),衍射分辨率为2.0 Å,晶胞参数a = 58.9,b = 93.0,c = 143.4 Å。