Cloned (Comment) | Organism |
---|---|
CHO-K1 cells transiently expressing the mutated form of hQR2 | Homo sapiens |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Homo sapiens |
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 | Comment | Organism |
---|---|---|
QR2 | - |
Homo sapiens |
quinone oxidoreductase 2 | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
25 | - |
assay at | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8.5 | - |
assay at | Homo sapiens |
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 |