EC |
1.1.99.28 |
Accepted name: |
glucose-fructose oxidoreductase |
Reaction: |
D-glucose + D-fructose = D-gluconolactone + D-glucitol |
Systematic name: |
D-glucose:D-fructose oxidoreductase |
Comments: |
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+. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 94949-35-6 |
References: |
1. |
Zachariou, M. and Scopes, R.K. Glucose-fructose oxidoreductase: a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production. J. Bacteriol. 167 (1986) 863–869. [DOI] [PMID: 3745122] |
2. |
Hardman, M.J. and Scopes, R.K. The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis. Eur. J. Biochem. 173 (1988) 203–209. [DOI] [PMID: 3356190] |
3. |
Kanagasundaram, V. and Scopes, R.K. Cloning, sequence analysis and expression of the structural gene encoding glucose-fructose oxidoreductase. J. Bacteriol. 174 (1992) 1439–1447. [DOI] [PMID: 1537789] |
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[EC 1.1.99.28 created 1999] |
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