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Results 1 - 8 of 8
EC Number pH Minimum pH Maximum Commentary Reference
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.4-999 - Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0 744450
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.4-999 - comparison of the pH dependence of both kred and kred/Kd from reductive half-reaction experiments between wild-type enzyme and mutant E232Q, overview. 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 745314
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.44 11.5 activity range, bell-shaped pH-activity relationships for both the recombinant split variants 744255
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.44.5 9 the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above 743904
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.46 9.2 trends to increasing activities at higher values 644558
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.46.6 8 - 706259
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.47.2 8.7 - 706471
Show all pathways known for 1.17.1.4Display the word mapDisplay the reaction diagram Show all sequences 1.17.1.48 8.5 - 659314
Results 1 - 8 of 8