Electron density map of chicken heart cytosol aspartate transaminase at 3.5 A resolution.
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.
D000818:Animals; D001219:Aspartate Aminotransferases; D001665:Binding Sites; D002645:Chickens; D003600:Cytosol / Q000201:enzymology; D006860:Hydrogen Bonding; D009206:Myocardium / Q000201:enzymology*; D011487:Protein Conformation; D013329:Structure-Activity Relationship; D014961:X-Ray Diffraction
D001219:Aspartate Aminotransferases