Hawwa Renda, Aikens John, Turner Robert J, Santarsiero Bernard D, Mesecar Andrew D
Department of Medicinal Chemistry and Pharmacognosy and the Center for Pharmaceutical Biotechnology, University of Illinois at Chicago, Chicago, IL 60607, USA.
Arch Biochem Biophys. 2009 Aug 15;488(2):109-20. doi: 10.1016/j.abb.2009.06.005. Epub 2009 Jul 16.
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.
从嗜热栖热放线菌中鉴定出一种与磷酸三酯酶同源的新酶(GsP)。这种酶属于酰胺水解酶家族,具有水解内酯和有机磷酸酯(OP)化合物的能力,使其成为一种类磷酸三酯酶内酯酶(PLL)。GsP比最近鉴定的PLL具有更高的OP降解活性,并且具有极高的热稳定性。GsP在高达100摄氏度时仍具有活性,对乙基对氧磷的活化能为8.0千卡/摩尔,并且能够承受60摄氏度的孵育温度达两天。为了了解PLL的热稳定性,测定了GsP的X射线结构并与现有PLL的结构进行了比较。基于比较分析,开发了一种新的热优势评分和图表,结果表明多种不同因素有助于PLL的热稳定性。