Hyperthermophilic phosphotriesterases/lactonases for the environment and human health. (Articolo in rivista)

Type

• Articolo in rivista (Classe)
• Prodotto della ricerca (Classe)

Label

• Hyperthermophilic phosphotriesterases/lactonases for the environment and human health. (Articolo in rivista) (literal)

Anno

• 2010-01-01T00:00:00+01:00 (literal)

Alternative label

• Mandrich L, Merone L, Manco G. (2010)
  Hyperthermophilic phosphotriesterases/lactonases for the environment and human health.
  in Environmental technology
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Mandrich L, Merone L, Manco G. (literal)

Pagina inizio

• 1115 (literal)

Pagina fine

• 1127 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

• 31 (literal)

Rivista

• Environmental technology (Rivista)

Note

• ISI Web of Science (WOS) (literal)

Titolo

• Hyperthermophilic phosphotriesterases/lactonases for the environment and human health. (literal)

Abstract

• In the last decades the idea to use enzymes for environmental bioremediation has been more and more proposed and, in the light of this, new solutions have been suggested and detailed studies on some classes of enzymes have been performed. In particular, our attention in the last few years has been focused on the enzymes belonging to the amidohydrolase superfamily. Several members of this superfamily are endowed with promiscuous activities. The term 'catalytic promiscuity' describes the capability of an enzyme to catalyse different chemical reactions, called secondary activities, at the active site responsible for the main activity. Recently, a new family of microbial lactonases with promiscuous phosphotriesterase activity, dubbed PTE-Like Lactonase (PLL), has been ascribed to the amidohydrolase superfamily. Among members of this family are enzymes found in the archaea Sulfolobus solfataricus and Sulfolobus acidocaldarius, which show high thermophilicity and thermal resistance. Enzymes showing phosphotriesterase activity are attractive from a biotechnological point of view because they are capable of hydrolysing the organophosphate phosphotriesters (OPs), a class of synthetic compounds employed worldwide both as insecticides and chemical warfare agents. Furthermore, from a basic point of view, studies of catalytic promiscuity offer clues to understand natural evolution of enzymes and to translate this into in vitro adaptation of enzymes to specific human needs. Thermostable enzymes able to hydrolyse OPs are considered good candidates for the set-up of efficient detoxification tools. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)
• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)

Autore CNR

• LUIGIA MERONE (Unità di personale esterno)
• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale interno)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGIA MERONE (Unità di personale esterno)
• LUIGI MANDRICH (Unità di personale interno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)
• DR. MANCO : Studi di idrolasi da fonti diverse e proteine vegetali. (SV.P14.010.001) (Modulo)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Environmental technology (Rivista)