Liao Yuanping, Chen Shuai, Wang Dingli, Zhang Wangluo, Wang Shuang, Ding Jianfeng, Wang Yingming, Cai Lijun, Ran Xiaoyuan, Wang Xinquan, Zhu Huaxing
R&D Department, Novoprotein Scientific Inc. (Shanghai), R202, Building 2, 720 Cailun Road, Shanghai 201203, People's Republic of China.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Sep;69(Pt 9):967-72. doi: 10.1107/S174430911302160X. Epub 2013 Aug 19.
Formaldehyde dehydrogenase (FDH) is a member of the zinc-containing medium-chain alcohol dehydrogenase family which oxidizes toxic formaldehyde to formate using NAD(+) as an electron carrier. Three-dimensional structures have been reported for FDHs from several different species. Most FDHs are dependent on glutathione for catalysis, but the enzyme from Pseudomonas putida is an exception. In this structural communication, the recombinant production, crystallization and X-ray structure determination at 2.7 Å resolution of FDH from P. aeruginosa are described. Both the tetrameric assembly and the NAD(+)-binding mode of P. aeruginosa FDH are similar to those of P. putida FDH, which is in good agreement with the high sequence identity (87.97%) between these two proteins. Preliminary enzymatic kinetics studies of P. aeruginosa FDH also revealed a conserved glutathione-independent `ping-pong' mechanism of formaldehyde oxidization.
甲醛脱氢酶（FDH）是含锌中链醇脱氢酶家族的一员，它以NAD⁺作为电子载体，将有毒的甲醛氧化为甲酸。已经报道了几种不同物种的FDH的三维结构。大多数FDH的催化作用依赖于谷胱甘肽，但恶臭假单胞菌的该酶是个例外。在本结构通讯中，描述了铜绿假单胞菌FDH的重组表达、结晶以及2.7 Å分辨率的X射线结构测定。铜绿假单胞菌FDH的四聚体组装和NAD⁺结合模式均与恶臭假单胞菌FDH相似，这与这两种蛋白质之间的高序列同一性（87.97%）高度一致。对铜绿假单胞菌FDH的初步酶动力学研究还揭示了一种保守的、不依赖谷胱甘肽的甲醛氧化“乒乓”机制。
