Redesigning the monovalent cation specificity of an enzyme
| Autor: | Angelene M. Cantwell, Leslie A. Bush, Enrico Di Cera, Kelly J. Wright, Swati Prasad, Dolly Banerjee Roy |
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| Jazyk: | angličtina |
| Rok vydání: | 2003 |
| Předmět: |
Models
Molecular Stereochemistry Sodium Kinetics chemistry.chemical_element In Vitro Techniques Protein Engineering Substrate Specificity Thrombin medicine Humans Binding site chemistry.chemical_classification Multidisciplinary Binding Sites biology Mutagenesis Protein engineering Biological Sciences Cations Monovalent Enzyme Allosteric enzyme chemistry Biochemistry biology.protein Mutagenesis Site-Directed Potassium Thermodynamics medicine.drug |
| Popis: | Monovalent-cation-activated enzymes are abundantly represented in plants and in the animal world. Most of these enzymes are specifically activated by K + , whereas a few of them show preferential activation by Na + . The monovalent cation specificity of these enzymes remains elusive in molecular terms and has not been reengineered by site-directed mutagenesis. Here we demonstrate that thrombin, a Na + -activated allosteric enzyme involved in vertebrate blood clotting, can be converted into a K + -specific enzyme by redesigning a loop that shapes the entrance to the cation-binding site. The conversion, however, does not result into a K + -activated enzyme. |
| Databáze: | OpenAIRE |
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