Article
Three-dimensional structure of a mutant E. coli aspartate aminotransferase with increased enzymic activity.
Protein engineering - 1 May 1994
Jäger J, Pauptit R A, Sauder U, Jansonius J N
Abstract excerpt
The aspartate and tyrosine aminotransferases from Escherichia coli have 43% sequence identity and nearly identical active sites. Both are equally good enzymes for dicarboxylate substrates, but the latter transaminates aromatic amino acids 1000 times faster. In an attempt to discover the critical...
Topics
- Aspartate Aminotransferases
- Computer Simulation
- Crystallization
- Crystallography, X-Ray
- Escherichia coli
- Fourier Analysis
- Models, Molecular
- Molecular Structure
- Mutagenesis
- Mutation
- Protein Conformation
- Structure-Activity Relationship