Comparative Kinetic Analysis and Substrate Specificity of the Tandem Catalytic Domains of the Receptor-like Protein-tyrosine Phosphatase α
Open Access
- 1 March 1997
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (11) , 6994-7002
- https://doi.org/10.1074/jbc.272.11.6994
Abstract
No abstract availableKeywords
This publication has 58 references indexed in Scilit:
- Reactivity of Alcohols Toward the Phosphoenzyme Intermediate in the Protein-Tyrosine Phosphatase-Catalyzed Reaction: Probing the Transition State of the Dephosphorylation StepBiochemistry, 1996
- Probing the Function of Asp128 in the Low Molecular Weight Protein-Tyrosine Phosphatase-Catalyzed Reaction. A Pre-Steady-State and Steady-State Kinetic InvestigationBiochemistry, 1996
- Catalytic function of the conserved hydroxyl group in the protein tyrosine phosphatase signature motifBiochemistry, 1995
- Point Mutation in the Second Phosphatase Domain of CD45 Abrogates Tyrosine Phosphatase ActivityBiochemical and Biophysical Research Communications, 1995
- Reaction Energetics of a Mutant 3-Oxo-.DELTA.5-steroid Isomerase with an Altered Active Site Base (D38E)Biochemistry, 1994
- Aqueous Chemistry of Labile Oxovanadates: Relevance to Biological StudiesComments on Inorganic Chemistry, 1994
- Cloning, expression, and catalytic mechanism of the low molecular weight phosphotyrosyl protein phosphatase from bovine heartBiochemistry, 1992
- Catalytic domains of the LAR and CD45 protein tyrosine phosphatases from Escherichia coli expression systems: purification and characterization for specificity and mechanismBiochemistry, 1992
- Differential usage of three exons generates at least five different mRNAs encoding human leukocyte common antigens.The Journal of Experimental Medicine, 1987
- Site-directed mutants of staphylococcal nuclease. Detection and localization by proton NMR spectroscopy of conformational changes accompanying substitutions for glutamic acid-43Biochemistry, 1987