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The catalytic mechanism of protein tyrosine phosphatases revisited
Author(s) -
Kolmodin Karin,
Åqvist Johan
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02479-6
Subject(s) - protein tyrosine phosphatase , phosphatase , mechanism (biology) , tyrosine , chemistry , dual specificity phosphatase , enzyme , interpretation (philosophy) , hydrolysis , dual (grammatical number) , biochemistry , catalysis , reaction mechanism , computer science , physics , programming language , quantum mechanics , art , literature
Experimental and theoretical studies of the catalytic mechanism in protein tyrosine phosphatases and dual specific phosphatases are reviewed. The structural properties of these enzymes contributing to the efficient rate enhancement of phosphate monoester hydrolysis have been established during the last decade. There are, however, uncertainties in the interpretation of available experimental data that make the commonly assumed reaction mechanism somewhat doubtful. Theoretical calculations as well as analysis of crystal structures point towards an alternative interpretation of the ionisation state in the reactive complex.