EC number:1.1.99.28

Enzyme

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EC Tree
     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.99 With unknown physiological acceptors
ID:1.1.99.28
Description:Glucose-fructose oxidoreductase.
Cath: 3.30.360.10; 3.40.50.720;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.99.28
BRENDA Enzyme Link: BRENDA 1.1.99.28
KEGG Enzyme Link: KEGG1.1.99.28
BioCyc Enzyme Link: BioCyc 1.1.99.28
ExPASy Enzyme Link: ExPASy1.1.99.28
EC2PDB Enzyme Link: EC2PDB 1.1.99.28
ExplorEnz Enzyme Link: ExplorEnz 1.1.99.28
PRIAM enzyme-specific profiles Link: PRIAM 1.1.99.28
IntEnz Enzyme Link: IntEnz 1.1.99.28
MEDLINE Enzyme Link: MEDLINE 1.1.99.28

EC number:1.1.99.28

MSA:

1.1.99.28;
Phylogenetic Tree:

1.1.99.28;
Uniprot:
M-CSA:
RHEA:20637 D-fructose + D-glucose = D-glucono-1,5-lactone + D-sorbitol
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[OH;+0:4].[*:5]-[O;H0;+0:6]-[C;H0;+0:7](-[*:8])(-[*:9])-[*:10]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:4].([*:8]-[CH;+0:7](-[*:9])-[*:10].[*:5]-[OH;+0:6])
Reaction
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References

TitleAuthorsDatePubMed ID
The structure of glucose-fructose oxidoreductase from Zymomonas mobilis: an osmoprotective periplasmic enzyme containing non-dissociable NADP.Kingston RL, Scopes RK, Baker EN1996 Dec 158994968
Glucose-fructose oxidoreductase, a new enzyme isolated from Zymomonas mobilis that is responsible for sorbitol production.Zachariou M, Scopes RK1986 Sep3745122
The kinetics of glucose-fructose oxidoreductase from Zymomonas mobilis.Hardman MJ, Scopes RK1988 Apr 53356190
Cloning, sequence analysis, and expression of the structural gene encoding glucose-fructose oxidoreductase from Zymomonas mobilis.Kanagasundaram V, Scopes RK1992 Mar1537789