Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.

Hawwa, Renda

Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus. [electronic resource] - Archives of biochemistry and biophysics Aug 2009 - 109-20 p. digital

Publication Type: Journal Article; Research Support, N.I.H., Extramural

1096-0384

10.1016/j.abb.2009.06.005 doi


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