Computational approach towards the three-dimensional structure of E. coli tyrosine aminotransferase.
We present a new model for E. coli tyrosine aminotransferase based on the X-ray structures of the wild type and Val39Leu mutant of E. coli aspartate aminotransferase and computer simulation studies. Active site characteristics of the model are correlated with experimental observations on the specificity of these enzymes towards aromatic/dicarboxylic acid substrates.
Biozentrum Universität Basel, Switzerland.
J
J
Jäger
T
T
Solmajer
J N
JN
Jansonius
D000818:Animals; D001665:Binding Sites; D002645:Chickens; D003198:Computer Simulation; D004926:Escherichia coli / Q000201:enzymology*; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D014444:Tyrosine Transaminase / Q000737:chemistry* / Q000235:genetics; D014961:X-Ray Diffraction
D014444:Tyrosine Transaminase