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

Reaction

1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide
+
a quinone
=
1-(beta-D-ribofuranosyl)nicotinamide
+
a quinol

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

     1 Oxidoreductases
         1.10 Acting on diphenols and related substances as donors
             1.10.5 With a quinone or related compound as acceptor
                1.10.5.1 ribosyldihydronicotinamide dehydrogenase (quinone)

Engineering

Engineering on EC 1.10.5.1 - ribosyldihydronicotinamide dehydrogenase (quinone)

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C222F
-
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
-
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
F131M
-
mutant enzyme is more active than wild-type enzyme
F178Y
-
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
-
mutation of residue in FAD binding site, the enzymatic activity is unchanged
H173Y
-
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
H177R
-
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding
I128Y
-
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
-
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
-
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
-
mutation of residue in FAD binding site, the enzymatic activity is diminished
additional information
-
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