Glucose-fructose oxidoreductase
<StructureSection load= size='350' side='right' caption='Glucose-fructose oxidoreductase complex with NADPH and glycerol (PDB entry 1evj)' scene='49/490077/Cv/1'>
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
The biological assembly of GFOR from Zymomonas mobilis is homotetramer. GFOR active site contains the cofactor NADPH and in this 3D structure the glycerol molecule seen in the active site occupies the position of the glucose ligand[2]. Water molecules shown as red spheres.
3D structures of glucose-fructose oxidoreductase
Updated on 08-August-2021
1ofg – GFOR + NADPH
1h6a, 1h6d - GFOR precursor + NADPH
1evj – GFOR (mutant) + NAD
1h6b, 1rye - GFOR + glycerol + NADPH
1h6c - GFOR precursor + 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
