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Structural basis for thermostability revealed through the identification and characterization of a highly thermostable phosphotriesterase-like lactonase from Geobacillus stearothermophilus.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 2009 Aug 15; Vol. 488 (2), pp. 109-20. Date of Electronic Publication: 2009 Jul 16. - Publication Year :
- 2009
-
Abstract
- A new enzyme homologous to phosphotriesterase was identified from the bacterium Geobacillus stearothermophilus (GsP). This enzyme belongs to the amidohydrolase family and possesses the ability to hydrolyze both lactone and organophosphate (OP) compounds, making it a phosphotriesterase-like lactonase (PLL). GsP possesses higher OP-degrading activity than recently characterized PLLs, and it is extremely thermostable. GsP is active up to 100 degrees C with an energy of activation of 8.0 kcal/mol towards ethyl paraoxon, and it can withstand an incubation temperature of 60 degrees C for two days. In an attempt to understand the thermostability of PLLs, the X-ray structure of GsP was determined and compared to those of existing PLLs. Based upon a comparative analysis, a new thermal advantage score and plot was developed and reveals that a number of different factors contribute to the thermostability of PLLs.
- Subjects :
- Amino Acid Sequence
Binding Sites
Cloning, Molecular
Crystallization
Dimerization
Enzyme Stability
Escherichia coli genetics
Genome, Bacterial
Geobacillus stearothermophilus genetics
Hydrogen Bonding
Hydrolysis
Hydrophobic and Hydrophilic Interactions
Kinetics
Models, Chemical
Models, Molecular
Molecular Sequence Data
Phosphoric Triester Hydrolases genetics
Phosphoric Triester Hydrolases isolation & purification
Plasmids genetics
Promoter Regions, Genetic
Protein Binding
Protein Structure, Secondary
Sequence Homology, Amino Acid
Solubility
Substrate Specificity
Time Factors
Transformation, Bacterial
X-Rays
Carboxylic Ester Hydrolases metabolism
Geobacillus stearothermophilus enzymology
Phosphoric Triester Hydrolases chemistry
Phosphoric Triester Hydrolases metabolism
Temperature
Subjects
Details
- Language :
- English
- ISSN :
- 1096-0384
- Volume :
- 488
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 19615330
- Full Text :
- https://doi.org/10.1016/j.abb.2009.06.005