Article
3-D structure of a mutant (Asp101-->Ser) of E.coli alkaline phosphatase with higher catalytic activity.
Protein engineering - 1 Oct 1992
Chen L, Neidhart D, Kohlbrenner W M, Mandecki W, Bell S, Sowadski J, Abad-Zapatero C
Abstract excerpt
Mutagenesis of the absolutely conserved residue Asp101 of the non-specific monoesterase alkaline phosphatase (E.C. 3.1.3.1) from E. coli has produced an enzyme with increased kcat. The carboxyl group of the Asp101 residue has been proposed to be involved in the positioning of Arg166 and the formation of the helix that contains the active site Ser102. The crystal structure of the Asp101-->Ser mutant has been...
Topics
- Alkaline Phosphatase
- Aspartic Acid
- Catalysis
- Enzyme Stability
- Escherichia coli
- Genetic Engineering
- Kinetics
- Mutation
- Protein Conformation
- Serine