1.10.5.1: ribosyldihydronicotinamide dehydrogenase (quinone)
This is an abbreviated version!
For detailed information about ribosyldihydronicotinamide dehydrogenase (quinone), go to the full flat file.
Word Map on EC 1.10.5.1
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1.10.5.1
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nadph:quinone
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resveratrol
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two-electron
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isoalloxazine
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medicine
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bnah
- 1.10.5.1
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nadph:quinone
- resveratrol
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two-electron
- isoalloxazine
- medicine
- bnah
Reaction
Synonyms
bQR2, dihydronicotinamide riboside:quinone oxidoreductase, dihydronicotinamide riboside:quinone oxidoreductase 2, dihydronicotinamide riboside:quinone reductase 2, EC 1.10.99.2, melatonin-binding site MT3, MT3, MT3/NQO2, N-ribosyldihydronicotinamide dehydrogenase (quinone), N-ribosyldihydronicotinamide:quinone oxidoreductase 2, NQO2, NRH-oxidizing enzyme, NRH:QR2, NRH:quinone oxidoreductase, NRH:quinone oxidoreductase 2, NRH:quinone oxireductase 2, NRH:quinone reductase 2, QR2, quinone oxidoreductase 2, quinone reductase 2, quinone reductase type 2
ECTree
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Cofactor
Cofactor on EC 1.10.5.1 - ribosyldihydronicotinamide dehydrogenase (quinone)
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FMN
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the enzyme contains FAD as the sole bound flavin. The prosthetic group can be removed by treatment with acid in ammonium sulfate, and the resolved enzyme may be reactivated by FAD or by higher concentrations FMN
FAD
contains 1 FAD per monomer firmly bound to the enzyme through multiple interactions
FAD
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mediates hydride transfer, very tightly bound to the enzyme. Activity of the purified enzyme is not further increased by added FAD
FAD
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the enzyme contains FAD as the sole bound flavin. The prosthetic group can be removed by treatment with acid in ammonium sulfate, and the resolved enzyme may be reactivated by FAD or by higher concentrations FMN
FAD
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very tightly bound to the enzyme. Activity of the purified enzyme is not further increased by added FAD
FAD
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dstabilisation of the cofactor FAD by mutation N18E shows that 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine binding is closely linked to the conformational integrity of quinone oxidoreductase 2
FAD
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flavoenzyme, binding structure, overview. 2 molecules per enzyme dimer, quantification, overview
additional information
enzyme cannot use NADH or NADPH as reducing agent
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