Article
Structure and function of L-lactate dehydrogenases from thermophilic and mesophilic bacteria, XI. Engineering thermostability and activity of lactate dehydrogenases from bacilli.
Biological chemistry Hoppe-Seyler - 1 May 1991
Zülli F, Schneiter R, Urfer R, Zuber H
Abstract excerpt
An extensive comparative structural analysis of lactate dehydrogenase (LDH) sequences from thermophilic, mesophilic and psychrophilic bacilli revealed characteristic primary structural differences. These specific amino-acid substitutions were found in the entire LDH molecule. However, in certain...
Topics
- Amino Acid Sequence
- Bacillus
- Enzyme Activation
- Enzyme Stability
- Fructosediphosphates
- Hot Temperature
- Kinetics
- L-Lactate Dehydrogenase
- Molecular Sequence Data
- Mutagenesis, Site-Directed
- Mutation
- Plasmids
- Protein Conformation
- Protein Engineering
- Sequence Homology, Nucleic Acid
- Structure-Activity Relationship