Altering of the Metal Specificity of Escherichia coliAlkaline Phosphatase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference30 articles.
1. The kinetics of the reaction of nitrophenyl phosphates with alkaline phosphatase from Escherichia coli
2. Function of arginine-166 in the active site of Escherichia coli alkaline phosphatase
3. 3-D structure of the D153G mutant of Escherichia coli alkaline phosphatase: an enzyme with weaker magnesium binding and increased catalytic activity
4. The mechanism of the alkaline phosphatase reaction: insights from NMR, crystallography and site-specific mutagenesis
5. Magnesium in the active site of Escherichia coli alkaline phosphatase is important for both structural stabilization and catalysis
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