Electron density map of chicken heart cytosol aspartate transaminase at 3.5 Å resolution
| Autor: | B. K. Vainshtein, Borisova Sn, N.I. Sosfenov, V.V. Borisov |
|---|---|
| Rok vydání: | 1980 |
| Předmět: |
chemistry.chemical_classification
Binding Sites Multidisciplinary biology Protein Conformation Transamination Myocardium Resolution (electron density) Aspartate transaminase Hydrogen Bonding Structure-Activity Relationship Cytosol Enzyme Protein structure X-Ray Diffraction chemistry Biochemistry biology.protein Animals Structure–activity relationship Aspartate Aminotransferases Binding site Chickens |
| Zdroj: | Nature. 284:189-190 |
| ISSN: | 1476-4687 0028-0836 |
| DOI: | 10.1038/284189a0 |
| Popis: | Aspartate transaminase (EC 2.6.1.1., Asp-transaminase) has been studied extensively, and much is now known about its physico-chemical, catalytic and other properties. X-ray studies that can provide a structural foundation for the events that occur during the transamination reaction are under way on three species of Asp-transaminase: the cytosolic enzyme from pig and chicken hearts, and the mitochondrial chicken heart enzyme. We describe here the interpretation of an electron density map of Asp-transaminase from chicken heart cytosol at 3.5 A. |
| Databáze: | OpenAIRE |
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