Inactivation of yeast enolase with tetranitromethane
| Autor: | John M. Brewer, S.G. Spencer |
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| Rok vydání: | 1982 |
| Předmět: |
Cations
Divalent Macromolecular Substances Enolase Saccharomyces cerevisiae Biophysics Biochemistry chemistry.chemical_compound Binding site Tyrosine Terbium Molecular Biology Edetic Acid chemistry.chemical_classification biology Nitrotyrosine Cell Biology Tetranitromethane biology.organism_classification Yeast Kinetics Enzyme chemistry Phosphopyruvate Hydratase Methane Protein Binding |
| Zdroj: | Biochemical and biophysical research communications. 105(4) |
| ISSN: | 0006-291X |
| Popis: | Yeast enolase is inactivated by tetranitromethane with production of 1.2 moles of nitrotyrosine per subunit. Protection is afforded by “conformational” metal ion alone. Enzyme thus inactivated no longer appears to bind “conformational” metal ion. There is evidence against direct coordination of the tyrosine to “conformational” metal ion, suggesting modification of the tyrosyl may obstruct the binding site. |
| Databáze: | OpenAIRE |
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