The catalytic mechanism of protein tyrosine phosphatases revisited

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 l...

Full description

Saved in:
Bibliographic Details
Published inFEBS Letters Vol. 498; no. 2; pp. 208 - 213
Main Authors Kolmodin, Karin, Åqvist, Johan
Format Book Review Journal Article
LanguageEnglish
Published England Elsevier B.V 08.06.2001
Subjects
Animals
Catalysis
Catalytic mechanism
Hydrogen-Ion Concentration
Kinetics
Models, Molecular
Molecular Structure
pH rate profile
Protein Binding
Protein Conformation
Protein tyrosine phosphatase
Protein Tyrosine Phosphatases - chemistry
Protein Tyrosine Phosphatases - genetics
Protein Tyrosine Phosphatases - metabolism
Protein tyrosine phosphatase
Catalytic mechanism
pH rate profile
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(01)02479-6