Abstract
Phosphatases are enzymes that catalyze the hydrolysis of a phosphate monoester, or, in other words, the phosphoryl transfer from an ester substrate to water. Some phosphatases, utilizing a binuclear metal center, accomplish this reaction in a single step. Others, some of which also utilize two-metal ion catalysis and some of which do not, first form a phosphoenzyme intermediate, which is hydrolyzed by attack of water in a second step. Protein-tyrosine phosphatases utilize a conserved cysteine residue and form a phosphocysteine intermediate. Alkaline phosphatases utilize two zinc ions and form a phosphoserine intermediate. The protein serine/threonine phosphatases and the purple acid phosphatases have a dinuclear metal center and catalyze the direct transfer of the phosphoryl group to a metal-coordinated hydroxide. A number of phosphatases have been found capable of catalyzing other hydrolysis reactions, such as those of sulfate esters, or of phosphate and phosphonate diesters. Such so-called promiscuous activities arise from the ability of the enzymes to stabilize a trigonal bipyramidal transition state, which is common to the reaction of its native substrate as well as the alternate substrates.
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Further Reading
-
T. S. Widlanski and
W. Taylor, in
D. Barton and
D. Meth-Cohn, eds.
Comprehensive Natural Products Chemistry,
Vol. 5,
Elsevier,
1999, pp.
139–162.
10.1016/B978-0-08-091283-7.00112-0 Google Scholar
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- A. C. Hengge, Adv. Phys. Org. Chem. 40, 49–108 (2005).
