Maraite Andy, Schmidt Thomas, Ansörge-Schumacher Marion B, Brzozowski A Marek, Grogan Gideon
Department of Biotechnology, Faculty of Natural Sciences, RWTH Aachen University, Worringerweg 1, 52074 Aachen, Germany.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jul 1;63(Pt 7):546-8. doi: 10.1107/S1744309107028576. Epub 2007 Jun 15.
Benzaldehyde lyase (BAL; EC 4.1.2.38) is a thiamine diphosphate (ThDP) dependent enzyme that catalyses the enantioselective carboligation of two molecules of benzaldehyde to form (R)-benzoin. BAL has hence aroused interest for its potential in the industrial synthesis of optically active benzoins and derivatives. The structure of BAL was previously solved to a resolution of 2.6 A using MAD experiments on a selenomethionine derivative [Mosbacher et al. (2005), FEBS J. 272, 6067-6076]. In this communication of parallel studies, BAL was crystallized in an alternative space group (P2(1)2(1)2(1)) and its structure refined to a resolution of 1.65 A, allowing detailed observation of the water structure, active-site interactions with ThDP and also the electron density for the co-solvent 2-methyl-2,4-pentanediol (MPD) at hydrophobic patches of the enzyme surface.
苯甲醛裂解酶(BAL;EC 4.1.2.38)是一种依赖硫胺二磷酸(ThDP)的酶,它催化两分子苯甲醛的对映选择性碳连接反应,生成(R)-安息香。因此,BAL因其在光学活性安息香及其衍生物的工业合成中的潜力而引起了人们的关注。之前通过对硒代甲硫氨酸衍生物进行多波长反常散射(MAD)实验,解析出了BAL的结构,分辨率达到2.6 Å [莫斯巴赫等人(2005年),《欧洲生物化学学会联合会杂志》272卷,6067 - 6076页]。在这篇平行研究的通讯文章中,BAL在另一个空间群(P2(1)2(1)2(1))中结晶,其结构被精修至1.65 Å的分辨率,这使得能够详细观察水的结构、活性位点与ThDP的相互作用,以及酶表面疏水区域共溶剂2 - 甲基 - 2,4 - 戊二醇(MPD)的电子密度。