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Literature summary 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)

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

Protein Variants

EC Number Protein Variants Comment Organism
1.10.5.1 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
1.10.5.1 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
1.10.5.1 F131M mutant enzyme is more active than wild-type enzyme Homo sapiens
1.10.5.1 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
1.10.5.1 H11F mutation of residue in FAD binding site, the enzymatic activity is unchanged Homo sapiens
1.10.5.1 H173Y mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding Homo sapiens
1.10.5.1 H177R mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding Homo sapiens
1.10.5.1 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
1.10.5.1 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
1.10.5.1 N18Q mutation of residue in FAD binding site, the enzymatic activity is diminished Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.10.5.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.10.5.1
-
 Homo sapiens

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.10.5.1 QR2
-
 Homo sapiens
1.10.5.1 quinone oxidoreductase 2
-
 Homo sapiens

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.10.5.1 25
-
 assay at Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.10.5.1 8.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.10.5.1 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