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EC Number Protein Variants Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118D148G diazaborine-resistant mutant 748518
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118E219A diazaborine-resistant mutant 748518
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118E219G diazaborine-resistant mutant 748518
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I16T diazaborine-resistant mutant 748518
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I16T mutation in the glycine-rich loop. Although very flexible, in the wild-type enzyme/NADH complex, the NADH molecule keeps its extended conformation firmly bound to the binding site of the enzyme. In the mutant complex, the NADH pyrophosphate moiety undergoes considerable conformational changes, reducing its interactions with its binding site and probably indicating the initial phase of ligand expulsion from the cavity -, 747286
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I202T diazaborine-resistant mutant 748518
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I21V isoniazid-resistant mutant -, 748433
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I21V mutation in the glycine-rich loop. Although very flexible, in the wild-type enzyme/NADH complex, the NADH molecule keeps its extended conformation firmly bound to the binding site of the enzyme. In the mutant complex, the NADH pyrophosphate moiety undergoes considerable conformational changes, reducing its interactions with its binding site and probably indicating the initial phase of ligand expulsion from the cavity -, 747286
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I21V similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE -, 749238
Display the word mapDisplay the reaction diagram Show all sequences 1.3.1.118I47T similar to wild-type InhA, cross-linking of the isoniazid resistant mutant gives three bands on SDS-PAGE assigned to monomer, dimer, and tetrameric forms of the protein. The inhibition of the enzyme with the isoniazid-NAD adduct results in loss of the band assigned to tetramer. In contrast, cross-linking in the presence of saturating concentrations of NADH yields a lower amount of the tetramer upon SDS-PAGE -, 749238
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