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

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 Biophys

authors

Hawwa R,Aikens J,Turner RJ,Santarsiero BD,Mesecar AD

doi

10.1016/j.abb.2009.06.005

subject

Has Abstract

pub_date

2009-08-15 00:00:00

pages

109-20

issue

2

eissn

0003-9861

issn

1096-0384

pii

S0003-9861(09)00182-9

journal_volume

488

pub_type

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