Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. [electronic resource]
Producer: 20090910Description: 109-20 p. digitalISSN:- 1096-0384
- Amino Acid Sequence
- Binding Sites
- Carboxylic Ester Hydrolases -- metabolism
- Cloning, Molecular
- Crystallization
- Dimerization
- Enzyme Stability
- Escherichia coli -- genetics
- Genome, Bacterial
- Geobacillus stearothermophilus -- enzymology
- Hydrogen Bonding
- Hydrolysis
- Hydrophobic and Hydrophilic Interactions
- Kinetics
- Models, Chemical
- Models, Molecular
- Molecular Sequence Data
- Phosphoric Triester Hydrolases -- chemistry
- Plasmids -- genetics
- Promoter Regions, Genetic
- Protein Binding
- Protein Structure, Secondary
- Sequence Homology, Amino Acid
- Solubility
- Substrate Specificity
- Temperature
- Time Factors
- Transformation, Bacterial
- X-Rays
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Publication Type: Journal Article; Research Support, N.I.H., Extramural
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