Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.

doi:10.1006/jmbi.1996.0195

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Article

Kinetic and structural consequences of replacing the aspartate bridge by asparagine in the catalytic metal triad of Escherichia coli alkaline phosphatase.

Journal of molecular biology - 5 Apr 1996

Tibbitts T T, Murphy J E, Kantrowitz E R

Abstract excerpt

In each subunit of the homodimeric enzyme Escherichia coli alkaline phosphatase, two of the three metal cofactors Zn2+ and Mg2+, are bound by an aspartate side-chain at position 51. Using site-specific mutagenesis, Asp51 was mutated both to alanine and to asparagine to produce the D51A and D51N e...

Topics

Alkaline Phosphatase
Asparagine
Aspartic Acid
Crystallography, X-Ray
Enzyme Activation
Escherichia coli
Hydrogen-Ion Concentration
Kinetics
Mutation

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