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EC Number
pH Minimum
pH Maximum
Commentary
Reference
1.17.1.4
-999
-
Acinetobacter baumannii XDH extends the pH tolerance to pH 11.0
744450
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
1.17.1.4
4
11.5
activity range, bell-shaped pH-activity relationships for both the recombinant split variants
744255
1.17.1.4
4.5
9
the enzyme is highly active at pH 5.0-8.0, shows low activity at pH 9.0, and is inactive above
743904
1.17.1.4
6
9.2
trends to increasing activities at higher values
644558
1.17.1.4
6.6
8
-
706259
1.17.1.4
7.2
8.7
-
706471
1.17.1.4
8
8.5
-
659314
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