Ontology highlight
ABSTRACT:
SUBMITTER: Kang C
PROVIDER: S-EPMC3551575 | biostudies-literature | 2012 Jan
REPOSITORIES: biostudies-literature
Kang ChulHee C Hayes Robert R Sanchez Emiliano J EJ Webb Brian N BN Li Qunrui Q Hooper Travis T Nissen Mark S MS Xun Luying L
Molecular microbiology 20111120 1
FurX is a tetrameric Zn-dependent alcohol dehydrogenase (ADH) from Cupriavidus necator JMP134. The enzyme rapidly reduces furfural with NADH as the reducing power. For the first time among characterized ADHs, the high-resolution structures of all reaction steps were obtained in a time-resolved manner, thereby illustrating the complete catalytic events of NADH-dependent reduction of furfural and the dynamic Zn(2+) coordination among Glu66, water, substrate and product. In the fully closed confor ...[more]