Abstract
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 properties1. 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 pig2 and chicken3 hearts, and the mitochondrial chicken heart enzyme4. We describe here the interpretation of an electron density map of Asp-transaminase from chicken heart cytosol at 3.5 Å.
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Borisov, V., Borisova, S., Sosfenov, N. et al. Electron density map of chicken heart cytosol aspartate transaminase at 3.5 Å resolution. Nature 284, 189–190 (1980). https://doi.org/10.1038/284189a0
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DOI: https://doi.org/10.1038/284189a0
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