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Results 1 - 10 of 28 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20D122A D122A mutation results in a marked reduction in the overall, lipoate adenylation, and lipoate transfer reaction activities (0.14, 4, and 4% of those of wild type, respectively) 725416
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20E116A/E312K/L328F mutations allow a LipB knockout strain to grow on a glucose minimal medium 704311
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20F15S/T101A/S114I mutations allow a LipB knockout strain to grow on a glucose minimal medium 704311
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20F35L/V113I mutations allow a LipB knockout strain to grow on a glucose minimal medium 704311
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20G76S substitution in LplA ligase gene, is identical to slr1 selenolipoate restistance mutation 665358
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20H149A mutations does not cause a significant reduction in three reaction activities (overall, lipoate adenylation, and lipoate transfer reaction activities), Km value for ATP and lipoic acid increases to 15 and 5.8fold, respectively, relative to those of wild-type 725416
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20K133A K133A mutation almost completely abolishes the overall reaction activity (0.01% of that of wild type) and causes marked reduction in lipoate adenylation and lipoate transfer activities (0.2 and 2.5% of that of wild type, respectively) 725416
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20more construction of truncated mutants of enzyme PfLipL1, PfLipL1DELTA259-269, PfLipL1DELTA254-274, and PfLipL1D249-279 746406
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20more enzyme null mutant, normal transport of lipoic acid, but severe defect in incorporation and utilization of exogenously supplied lipoic acid and lipoic acid analogues. Strain is highly resistant to selenolipoate 665466
Show all pathways known for 6.3.1.20Display the word mapDisplay the reaction diagram Show all sequences 6.3.1.20more establishment of an enzyme-mediated two-step labeling protocol suitable for live-cell labeling: construction of a fusion protein LAP-eDHFR-His6, in which eDHFR bears an N-terminal LAP extension and a C-terminal His-tag for purification. In the first step, substrate 6-[[(1S,2R,4S)-bicyclo[2.2.1]hept-5-ene-2-carbonyl]amino]hexanoic acid is coupled to purified recombinant LAP-eDHFR. After removal of excess norbornene substrate with centrifugal filter devices, the modified protein is successfully labeled with tetrazine-fluorescein 744699
Results 1 - 10 of 28 > >>