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:1.1.99.11
Description:Fructose 5-dehydrogenase.
Alternative Name: D-fructose dehydrogenase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.99.11
BRENDA Enzyme Link: BRENDA 1.1.99.11
KEGG Enzyme Link: KEGG1.1.99.11
BioCyc Enzyme Link: BioCyc 1.1.99.11
ExPASy Enzyme Link: ExPASy1.1.99.11
EC2PDB Enzyme Link: EC2PDB 1.1.99.11
ExplorEnz Enzyme Link: ExplorEnz 1.1.99.11
PRIAM enzyme-specific profiles Link: PRIAM 1.1.99.11
IntEnz Enzyme Link: IntEnz 1.1.99.11
MEDLINE Enzyme Link: MEDLINE 1.1.99.11
MSA:

1.1.99.11;

Phylogenetic Tree:

1.1.99.11;

Uniprot:
M-CSA:
RHEA:22304 A + D-fructose = 5-dehydro-D-fructose + AH2
RULE(radius=1) [*:1]-[CH;+0:2]1-[*:3]-[*:4]-[C;H0;+0:5](-[*:6])(-[OH;+0:7])-[O;H0;+0:8]-1>>[*:1]-[C;H0;+0:2](=[O;H0;+0:8])-[*:3]-[*:4]-[C;H0;+0:5](-[*:6])=[O;H0;+0:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase.Marcinkeviciene J, Johansson G1993 Feb 228436220
D-fructose dehydrogenase of Gluconobacter industrius: purification, characterization, and application to enzymatic microdetermination of D-fructose.Ameyama M, Shinagawa E, Matsushita K, Adachi O1981 Feb7462161
Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase.Yamada Y, Aida K, Uemura T1967 May6059959
Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260.Kawai S, Goda-Tsutsumi M, Yakushi T, Kano K, Matsushita K2013 Mar23275508