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.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Hawwa R,Aikens J,Turner RJ,Santarsiero BD,Mesecar ADdoi
10.1016/j.abb.2009.06.005subject
Has Abstractpub_date
2009-08-15 00:00:00pages
109-20issue
2eissn
0003-9861issn
1096-0384pii
S0003-9861(09)00182-9journal_volume
488pub_type
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