EC Number |
Protein Variants |
Reference |
---|
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 |
695860 |
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 |
695860 |
1.10.5.1 | F131M |
mutant enzyme is more active than wild-type enzyme |
695860 |
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 |
695860 |
1.10.5.1 | H11F |
mutation of residue in FAD binding site, the enzymatic activity is unchanged |
695860 |
1.10.5.1 | H173Y |
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding |
695860 |
1.10.5.1 | H177R |
mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding |
695860 |
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 |
695860 |
1.10.5.1 | more |
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 |
394377 |
1.10.5.1 | more |
mutation of residue Phe178 completely abolishes the function of NQO2 and augments the TRAIL sensitization |
763861 |