Function
Glucose-fructose oxidoreductase (GFOR) from the bacteria Zymomonas mobilis catalyzes the conversion of D-glucose and D-fructose to D-gluconolactone and D-glucitol (sorbitol)[1]. GFOR contains a tightly bound cofactor NADP+.
Structural highlights
GFOR active site contains the cofactor NADP+ and in this 3D structure the glycerol molecule seen in the active site occupies the position of the glucose ligand[2].
3D structures of glucose-fructose oxidoreductase
Updated on 07-March-2016
1ofg – GFOR + NADPH
1h6a, 1h6d - GFOR precursor + NADPH
1evj – GFOR (mutant) + NAD
1h6b, 1rye - GFOR + glycerol + NADPH
1h6c - GFOR + succinate + NADPH
1ryd - GFOR + glucose + NADPH
References
- ↑ Hardman MJ, Scopes RK. The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis. Eur J Biochem. 1988 Apr 5;173(1):203-9. PMID:3356190
- ↑ Nurizzo D, Halbig D, Sprenger GA, Baker EN. Crystal structures of the precursor form of glucose-fructose oxidoreductase from Zymomonas mobilis and its complexes with bound ligands. Biochemistry. 2001 Nov 20;40(46):13857-67. PMID:11705375
