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J. Biol. Chem., Vol. 269, Issue 42, 26234-26238, 10, 1994
S Zhuo, JC Clemens, RL Stone and JE Dixon
The Ser/Thr phosphoprotein phosphatases (PPases) display similarities in
amino acid sequence and biochemical properties. Most members of this family
require transition metal ions for activity. The smallest family member, the
bacteriophage lambda PPase (lambda-PPase), has been successfully
overexpressed in Escherichia coli, purified, and characterized (Zhuo, S.,
Clemens, J.C., Hakes, D.J., Barford, D., and Dixon, J. E. (1993) J. Biol.
Chem. 268, 17754-17761). Site-directed mutagenesis has now been employed to
define amino acid residues in lambda-PPase required for metal ion binding
and catalysis. Conservative amino acid substitutions at residues Asp20,
His22, Asp49, His76, and Glu77 affected lambda-PPase catalysis and metal
ion binding, whereas substitutions at residues Arg53 and Arg73 affected
catalysis and substrate binding. Each of these residues is invariant in all
phosphoprotein phosphatases, suggesting that these residues may play
important roles in binding and catalysis in all of the PPases. Computer-
assisted sequence alignment further revealed that lambda-PPase residues
Asp20, His22, Asp49, His76, Arg53, and Arg73 lie within three larger
regions of PPase sequence identity with the consensus sequence (DXH-
(approximately 25)-GDXXD-(approximately 25)-GNHD/E). This motif can be
found in a wide variety of phosphoesterases unrelated to the PPases and
defines structural and catalytic features utilized by a diverse group of
enzymes for the hydrolysis of phosphate esters.
Mutational analysis of a Ser/Thr phosphatase. Identification of residues important in phosphoesterase substrate binding and catalysis
Department of Biological Chemistry, University of Michigan, Ann Arbor 48109.
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