Article
A few amino acid substitutions are responsible for the higher thermostability of a novel NAD(+)-dependent bacillar alcohol dehydrogenase.
European journal of biochemistry - 1 Jun 1994
Cannio R, Rossi M, Bartolucci S
Abstract excerpt
The gene adh-hT encoding a thermostable and thermophilic NAD(+)-dependent alcohol dehydrogenase (ADH) from the novel and more thermophilic Bacillus stearothermophilus LLD-R strain was cloned and its nucleotide sequence determined. The deduced protein sequence shows remarkable amino acid substitut...
Topics
- Alcohol Dehydrogenase
- Amino Acid Sequence
- Base Sequence
- Cloning, Molecular
- Enzyme Stability
- Genes, Bacterial
- Genetic Variation
- Geobacillus stearothermophilus
- Kinetics
- Molecular Sequence Data
- Oligonucleotide Probes
- Plasmids
- Protein Structure, Secondary
- Recombinant Proteins
- Restriction Mapping
- Sequence Homology, Amino Acid
- Species Specificity
- Sulfolobus