Article
Crystal structures of L201A mutant of D-amino acid aminotransferase at 2.0 A resolution: implication of the structural role of Leu201 in transamination.
Protein engineering - 1 Aug 1998
Sugio S, Kashima A, Kishimoto K, Peisach D, Petsko G A, Ringe D, Yoshimura T, Esaki N
Abstract excerpt
The leucine-to-alanine mutation at residue 201 of D-amino acid aminotransferase provides a unique enzyme which gradually loses its activity while catalyzing the normal transamination; the co-enzyme form is converted from pyridoxal 5'-phosphate to pyridoxamine 5'-phosphate upon the inactivation [K...
Topics
- Alanine
- Alanine Transaminase
- Binding Sites
- Crystallography, X-Ray
- D-Alanine Transaminase
- Enzyme Activation
- Ketoglutaric Acids
- Leucine
- Models, Molecular
- Mutation
- Protein Conformation