User:Jaime Prilusky/Test/references: Difference between revisions
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== | ==test pdbe-citations for 3rec== | ||
< | <div class="pdbe-citations 3rec" style="background-color:#fffaf0;"></div> | ||
==test pdbe-citations for 8sbr== | |||
<div class="pdbe-citations 8sbr" style="background-color:#fffaf0;"></div> | |||
== | == '''Overview''' == | ||
'''Phosphotriesterase-Like Lactonase (PLL)''' family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon <ref name='Merone'>PMID: 15909078</ref> <ref name='Porzio'>PMID:17337320</ref>. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity <ref name='Afriat'>PMID:17105187</ref>. | |||
<ref> | |||
== '''SsoPox''' == | |||
Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon ''Sulfolobus solfataricus'' and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C <ref name="Merone"/><ref name='Porzio'/>. | |||
Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs; suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works by the hydrolysis of the lactone bond of these AHLs. <ref name='Afriat'/> | |||
== References == | |||
<references/> | <references/> | ||
Latest revision as of 11:01, 4 February 2025
test pdbe-citations for 3rectest pdbe-citations for 3rec
test pdbe-citations for 8sbrtest pdbe-citations for 8sbr
OverviewOverview
Phosphotriesterase-Like Lactonase (PLL) family includes a group of enzymes that have main lactonase activity on lactones and acyl-homoserin lactones (AHLs) and, in addition, low promiscuous phosphotriesterase activity towards organophosphates compound (OPs). At the beginning most of them has been identified as putative phosphotriesterases and were called "Paraoxonases" (Pox) because able to degrade pesticides such as paraoxon [1] [2]. However, further structural, phylogenetic, and biochemical studies have revealed that these enzymes have a proficient lactonase activity, beside the weak phosphotriesterase activity [3].
SsoPoxSsoPox
Sso Pox is a protein of 314 aa deriving from the hyperthermophilic archaeon Sulfolobus solfataricus and it is the first protein with phosphotriesterase activities to be identified in Archaea. It has an exceptional thermal stability with denaturation half-life of 4h and 90 min at 95 °C and 100 °C [1][2]. Its activity depends on the presence of metal ions, with cobalt significantly enhancing catalysis. SsoPox have been reported to catalyse the hydrolysis of different N-acyl homoserine lactones AHLs; suggesting a physiological role as a quorum quencher lactonase. Infact the AHLs are natural molecules involved in the cell–cell communication process known as quorum sensing (QS) and any bacterial species may produce different AHLs, which vary in the length and substitution of the acyl chain. The anti-QS mechanisms of the enzyme works by the hydrolysis of the lactone bond of these AHLs. [3]
ReferencesReferences
- ↑ 1.0 1.1 Merone L, Mandrich L, Rossi M, Manco G. A thermostable phosphotriesterase from the archaeon Sulfolobus solfataricus: cloning, overexpression and properties. Extremophiles. 2005 Aug;9(4):297-305. Epub 2005 May 21. PMID:15909078 doi:10.1007/s00792-005-0445-4
- ↑ 2.0 2.1 Porzio E, Merone L, Mandrich L, Rossi M, Manco G. A new phosphotriesterase from Sulfolobus acidocaldarius and its comparison with the homologue from Sulfolobus solfataricus. Biochimie. 2007 May;89(5):625-36. Epub 2007 Jan 27. PMID:17337320 doi:http://dx.doi.org/10.1016/j.biochi.2007.01.007
- ↑ 3.0 3.1 Afriat L, Roodveldt C, Manco G, Tawfik DS. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry. 2006 Nov 21;45(46):13677-86. PMID:17105187 doi:http://dx.doi.org/10.1021/bi061268r