Open AccessStructure of formaldehyde dehydrogenase from Pseudomonas aeruginosa : the binary complex with the cofactor NAD +
Author(s) -
Liao Yuanping,
Chen Shuai,
Wang Dingli,
Zhang Wangluo,
Wang Shuang,
Ding Jianfeng,
Wang Yingming,
Cai Lijun,
Ran Xiaoyuan,
Wang Xinquan,
Zhu Huaxing
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430911302160x
Subject(s) - formaldehyde dehydrogenase , pseudomonas putida , nad+ kinase , cofactor , formate dehydrogenase , alcohol dehydrogenase , oxidoreductase , chemistry , dehydrogenase , formate , biochemistry , stereochemistry , glutathione , formaldehyde , enzyme , catalysis
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.