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EC Number KM Value [mM] KM Value Maximum [mM] Substrate Commentary Reference
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more - 393008, 644620, 644621, 644625, 644639, 644640, 644645, 644647, 644655, 644658
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more detailed kinetics of wild-type in comparison to mutant enzymes, overview 689359
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more enzyme kinetics at all pH values studied is non-hyperbolic, and the use of the Michaelis-Menten equation is not adequate 676238
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more in vitro steady-state kinetic studies, kinetics with cofactor cytochrome C, overview 705243
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more kinetic analysis, Michaelis-Menten model, detailed overview. Binding of a 6-formylpterin at one of the two xanthine oxidase active sites slows down the turnover rate of xanthine at the adjacent active site and converts the V-[S] plot from substrate inhibition kinetic pattern to a classical Michaelis-Menten hyperbolic saturation pattern. In contrast, binding of xanthine at an active site accelerates the turnover rate of 6-formylpterin at the neighboring active site 714785
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more Michaelis-Menten and Lineweaver-Burk kinetics 745461
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more pH-dependent steady-state kinetics and reductive half-reaction, stopped flow kinetics, kinetic analysis of wild-type and mutant xanthine dehydrogenases, detailed overview. kred, the limiting rate constant for reduction at high [xanthine], is significantly compromised in the mutant variant E232Q, a result that is inconsistent with Glu232 being neutral in the active site of the wild-type enzyme. The ionized Glu232 of wild-type enzyme plays an important role in catalysis by discriminating against the monoanionic form of substrate, effectively increasing the pKa of the substrate by two pH units and ensuring that at physiological pH the neutral form of the substrate predominates in the Michaelis complex. The product release is principally rate-limiting in catalysis. The disparity in rate constants for the chemical step of the reaction and product release is not as great in the bacterial enzyme as compared with the vertebrate forms. The faster turnover observed with the bacterial enzyme is due to a faster rate constant for product release than is seen with the vertebrate enzyme 745314
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more steady-state and reductive half-reaction rapid kinetics at pH 7.0 and pH 8.5, overview 715538
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more steady-state kinetics analysis of wild-type and mutant enzymes with hypoxanthine of xanthine, and of mutant enzymes with benzaldehyde or 4-(dimethyamino)cinnamaldehyde as aldehyde oxidase substrates, overview 674374
Display the word mapDisplay the reaction diagram Show all sequences 1.17.3.2-999 - more steady-state kinetics of DTT-treated and untreated C-terminally truncated enzyme mutant 744875
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