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Literature summary for 1.10.5.1 extracted from

  • Boutin, J.A.; Saunier, C.; Guenin, S.P.; Berger, S.; Moulharat, N.; Gohier, A.; Delagrange, P.; Coge, F.; Ferry, G.
    Studies of the melatonin binding site location onto quinone reductase 2 by directed mutagenesis (2008), Arch. Biochem. Biophys., 477, 12-19.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
CHO-K1 cells transiently expressing the mutated form of hQR2 Homo sapiens

Protein Variants

Protein Variants Comment Organism
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 Homo sapiens
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 Homo sapiens
F131M mutant enzyme is more active than wild-type enzyme Homo sapiens
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 Homo sapiens
H11F mutation of residue in FAD binding site, the enzymatic activity is unchanged Homo sapiens
H173Y mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding Homo sapiens
H177R mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding Homo sapiens
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 Homo sapiens
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 Homo sapiens
N18Q mutation of residue in FAD binding site, the enzymatic activity is diminished Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N-benzyldihydronicotinamide + coenzyme Q0
-
Homo sapiens N-benzylnicotinamide + ?
-
?
N-benzyldihydronicotinamide + coenzyme Q1
-
Homo sapiens N-benzylnicotinamide + ?
-
?
N-benzyldihydronicotinamide + menadione
-
Homo sapiens N-benzylnicotinamide + menadiol
-
?

Synonyms

Synonyms Comment Organism
QR2
-
Homo sapiens
quinone oxidoreductase 2
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Homo sapiens

Cofactor

Cofactor Comment Organism Structure
FAD 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 Homo sapiens