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 |
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Description: | Fructose 5-dehydrogenase. |
Alternative Name: |
D-fructose dehydrogenase. |
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Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.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: | |
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Phylogenetic Tree: | |
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 |
Title | Authors | Date | PubMed ID |
---|---|---|---|
Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase. | Marcinkeviciene J, Johansson G | 1993 Feb 22 | 8436220 |
D-fructose dehydrogenase of Gluconobacter industrius: purification, characterization, and application to enzymatic microdetermination of D-fructose. | Ameyama M, Shinagawa E, Matsushita K, Adachi O | 1981 Feb | 7462161 |
Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase. | Yamada Y, Aida K, Uemura T | 1967 May | 6059959 |
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 K | 2013 Mar | 23275508 |