1OFG

GLUCOSE-FRUCTOSE OXIDOREDUCTASE

Summary for 1OFG

• Entry DOI: 10.2210/pdb1ofg/pdb
• Descriptor: GLUCOSE-FRUCTOSE OXIDOREDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE (3 entities in total)
• Functional Keywords: nadp binding, osmotic protection, oxidoreductase, periplasm
• Biological source: Zymomonas mobilis
• Cellular location: Periplasm: Q07982
• Total number of polymer chains: 6
• Total formula weight: 257756.27

Authors

Kingston, R.L.,Scopes, R.K.,Baker, E.N. (deposition date: 1996-10-17, release date: 1997-04-21, Last modification date: 2024-02-14)

Primary citation

Kingston, R.L.,Scopes, R.K.,Baker, E.N.
The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.
Structure, 4:1413-1428, 1996

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.

PubMed: 8994968
DOI: 10.1016/S0969-2126(96)00149-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)