EC |
1.1.5.14 |
Accepted name: |
fructose 5-dehydrogenase |
Reaction: |
D-fructose + a ubiquinone = 5-dehydro-D-fructose + a ubiquinol |
Other name(s): |
fructose 5-dehydrogenase (acceptor); D-fructose dehydrogenase; D-fructose:(acceptor) 5-oxidoreductase |
Systematic name: |
D-fructose:ubiquinone 5-oxidoreductase |
Comments: |
The enzyme, characterized from the bacterium Gluconobacter japonicus, is a heterotrimer composed of an FAD-containing large subunit, a small subunit, and a heme c-containing subunit, which is responsible for anchoring the complex to the cytoplasmic membrane and for transferring the electrons to ubiquinone. |
Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 37250-85-4 |
References: |
1. |
Yamada, Y., Aida, K. and Uemura, T. Enzymatic studies on the oxidation of sugar and sugar alcohol. I. Purification and properties of particle-bound fructose dehydrogenase. J. Biochem. (Tokyo) 61 (1967) 636–646. [PMID: 6059959] |
2. |
Ameyama, M. and Adachi, O. D-Fructose dehydrogenase from Gluconobacter industrius, membrane-bound. Methods Enzymol. 89 (1982) 154–159. |
3. |
Nakashima, K., Takei, H., Adachi, O., Shinagawa, E. and Ameyama, M. Determination of seminal fructose using D-fructose dehydrogenase. Clin. Chim. Acta 151 (1985) 307–310. [DOI] [PMID: 4053391] |
4. |
Kawai, S., Goda-Tsutsumi, M., Yakushi, T., Kano, K. and Matsushita, K. Heterologous overexpression and characterization of a flavoprotein-cytochrome c complex fructose dehydrogenase of Gluconobacter japonicus NBRC3260. Appl. Environ. Microbiol. 79 (2013) 1654–1660. [DOI] [PMID: 23275508] |
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[EC 1.1.5.14 created 1972 as EC 1.1.99.11, transferred 2021 to EC 1.1.5.14] |
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