Mn2+ modulates the kinetic properties of an archaeal member of the PLL family (Articolo in rivista)

Type

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

Label

• Mn2+ modulates the kinetic properties of an archaeal member of the PLL family (Articolo in rivista) (literal)

Anno

• 2013-01-01T00:00:00+01:00 (literal)

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

• 10.1016/J.CBI.2012.11.003 (literal)

Alternative label

• PORZIO E., DI GENNARO S., PALMA A., MANCO G. (2013)
  Mn2+ modulates the kinetic properties of an archaeal member of the PLL family
  in Chemico-biological interactions (Print)
  (literal)

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

• PORZIO E., DI GENNARO S., PALMA A., MANCO G. (literal)

Pagina inizio

• 251 (literal)

Pagina fine

• 256 (literal)

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

• 203 (literal)

Rivista

• Chemico-biological interactions (Rivista)

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

• 1 (literal)

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

• Istituto di Biochimica delle Proteine-CNR; AGROBIOS (literal)

Titolo

• Mn2+ modulates the kinetic properties of an archaeal member of the PLL family (literal)

Abstract

• Recently we reported on the characterization of an archaeal member of the amidohydrolase superfamily, namely Sulfolobus acidocaldarius lactonase, showing low but significant and extremely thermostable paraoxonase activity. This enzyme, that we have named SacPox, is a member of the new described family of phosphotriesterase-like lactonases (PLLs). In this family the binuclear metal centre, which is involved in the catalytic machinery, has been poorly studied up to now. In this work we describe the expression of the protein in presence of different metals showing Mn2+ to support the higher activity. The enzyme has been over-expressed, purified and characterized as a Mn2+-containing enzyme by inductive plasma coupled mass spectrometry (ICP-MS), showing also surprising kinetic differences in comparison with the cadmium-containing enzyme. The Mn2+ containing enzyme was about 30-fold more efficient with paraoxon as substrate and more stable than the Cd2+ counterpart, even though the Mn2+ affinity for the binuclear metal centre is apparently lower. These results increase our knowledge of the biochemical characteristics of SacPox mainly with regard to the metal-ions modulation of function. (C) 2012 Elsevier Ireland Ltd. All rights reserved. (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

• GIUSEPPE MANCO (Unità di personale interno)
• ELENA PORZIO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale interno)

Insieme di parole chiave

• Keywords of "Mn2+ modulates the kinetic properties of an archaeal member of the PLL family" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• LUIGI MANDRICH (Unità di personale interno)
• ELENA PORZIO (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

• Chemico-biological interactions (Rivista)

Insieme di parole chiave di

• Keywords of "Mn2+ modulates the kinetic properties of an archaeal member of the PLL family" (Insieme di parole chiave)