|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 126.96.36.199
Enzymes and Genes:
|Zymomonas mobilis:||glucose-fructose oxidoreductase: gfo|
In Pathway: sorbitol biosynthesis II
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Mass balance status: Balanced.
Enzyme Commission Primary Name: glucose-fructose oxidoreductase
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): -5.630005 [Latendresse13]
Enzyme Commission Summary:
D-mannose, D-xylose, D-galactose, 2-deoxy-D-glucose and L-arabinose will function as aldose substrates, but with low affinities. The ketose substrate must be in the open-chain form. The apparent affinity for fructose is low, because little of the fructose substrate is in the open-chain form. Xylulose and glycerone (dihydroxyacetone) will replace fructose, but they are poor substrates. The enzyme from Zymomonas mobilis contains tightly bound NADP+.
Kanagasundaram92: Kanagasundaram V, Scopes RK (1992). "Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis." J Bacteriol 174(5);1439-47. PMID: 1537789
Zachariou86: Zachariou M, Scopes RK (1986). "Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production." J Bacteriol 167(3);863-9. PMID: 3745122
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493