The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Kingston, R.L., Scopes, R.K., Baker, E.N.(1996) Structure 4: 1413-1428
- PubMed: 8994968 
- DOI: https://doi.org/10.1016/s0969-2126(96)00149-9
- Primary Citation of Related Structures:  
1OFG - PubMed Abstract: 
The organism Zymomonas mobilis occurs naturally in sugar-rich environments. To protect the bacterium against osmotic shock, the periplasmic enzyme glucose-fructose oxidoreductase (GFOR) produces the compatible, solute sorbitol by reduction of fructose, coupled with the oxidation of glucose to gluconolactone. Hence, Z mobilis can tolerate high concentrations of sugars and this property may be useful in the development of an efficient microbial process for ethanol production. Each enzyme subunit contains tightly associated NADP which is not released during the catalytic cycle.
Organizational Affiliation: 
Department of Biochemistry, Massey University, Palmerston North, New Zealand.