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
-
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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Engineering
Engineering on EC 1.10.5.1 - ribosyldihydronicotinamide dehydrogenase (quinone)
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C222F
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mutation, which is distant from the determined binding site of the ligand, increases the affinity of [125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine for the enzyme
F126Y
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substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
F178Y
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substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
H11F
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mutation of residue in FAD binding site, the enzymatic activity is unchanged
H173Y
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mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
H177R
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mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
I128Y
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substitution of the hydrophobic residue by tyrosines at the active site significantly increases enzymatic activity and decreases the affinity of a structural analog of melatonin, 2-[125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine
N161A
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mutation, which is distant from the determined binding site of the ligand, increases the affinity of [125I]-iodo-5-methoxycarbonylamino-N-acetyltryptamine for the enzyme
N161H
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results in the total loss of the enzymatic activity towards activation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide, whereas the rates of reduction towards menadione are not altered
N18Q
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mutation of residue in FAD binding site, the enzymatic activity is diminished
additional information
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construction of a chimeric enzyme of the human NQO2 with 43 amino acids from the carboxyl terminus of human DT-diaphorase. HNQO2-hDT43 still uses dihydronicotinamide riboside as an electron donor. The chimeric enzyme is inhibited by quercetin but not dicoumarol
additional information
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mutation of residue Phe178 completely abolishes the function of NQO2 and augments the TRAIL sensitization