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Results 1 - 10 of 13 > >>
EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1C222F 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
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1F126Y 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
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1F131M mutant enzyme is more active than wild-type enzyme 695860
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1F178Y 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
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1H11F mutation of residue in FAD binding site, the enzymatic activity is unchanged 695860
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1H173Y mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding 695860
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1H177R mutation of residues implicated in zinc chelating (His173 or His177) has no effect on radioligand binding 695860
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1I128Y 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
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1more 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
Display the word mapDisplay the reaction diagram Show all sequences 1.10.5.1more mutation of residue Phe178 completely abolishes the function of NQO2 and augments the TRAIL sensitization 763861
Results 1 - 10 of 13 > >>