Analysis of thermal adaptation in the HSL enzyme family (Articolo in rivista)

Type

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

Label

• Analysis of thermal adaptation in the HSL enzyme family (Articolo in rivista) (literal)

Anno

• 2004-01-01T00:00:00+01:00 (literal)

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

• 10.1016/j.jmb.2003.10.038 (literal)

Alternative label

• Mandrich L.; Pezzullo M.; Del Vecchio P.; Barone G.; Rossi M.; Manco G. (2004)
  Analysis of thermal adaptation in the HSL enzyme family
  in Journal of Molecular Biology
  (literal)

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

• Mandrich L.; Pezzullo M.; Del Vecchio P.; Barone G.; Rossi M.; Manco G. (literal)

Pagina inizio

• 357 (literal)

Pagina fine

• 369 (literal)

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

• 335 (literal)

Rivista

• Journal of Molecular Biology (Rivista)

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

• 1 (literal)

Note

• ISI Web of Science (WOS) (literal)

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

• Ist Biochim Prot, Consiglio Nazl Ric, I-80131 Naples, Italy Univ Naples Federico II, Dipartimento Chim, I-80126 Naples, Italy (literal)

Titolo

• Analysis of thermal adaptation in the HSL enzyme family (literal)

Abstract

• The recently solved three-dimensional (3D) structures of two thermostable members of the carboxylesterase/lipase HSL family, namely the Alicyclobacillus (formerly Bacillus) acidocaldarius and Archaeoglobus fulgidus carboxylesterases (EST2 and AFEST, respectively) were compared with that of the mesophilic homologous counterpart Brefeldine A esterase from Bacillus subtilis. Since the 3D homology models of other members of the HSL family were also available, we performed a structural alignment with all these sequences. The resulting alignment was used to assess the amino acid \"traffic rule\" in the HSL family. Quite surprisingly, the data were in very good agreement with those recently reported from two independent groups and based on the comparison of a huge number of homologous sequences from the genus Bacillus, Methanococcus and einococcus/Thermus. Taken as a whole, the data point to the statistical meaning of defined amino acid conversions going from psychrophilic to hyperthermophilic sequences. We identified and mapped several such changes onto the EST2 structure and observed that such mutations were localized mostly in loops regions or alpha-helices and were mostly excluded from the active site. A site-directed mutagenesis of two of the identified residues confirmed they were involved in thermal stability. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• LUIGI MANDRICH (Unità di personale esterno)
• Mosè Rossi (Unità di personale esterno)
• GIUSEPPE MANCO (Unità di personale interno)
• MARGHERITA PEZZULLO (Unità di personale esterno)

Insieme di parole chiave

• Parole chiave di "Analysis of thermal adaptation in the HSL enzyme family" (Insieme di parole chiave)

Incoming links:

Autore CNR di

• GIUSEPPE MANCO (Unità di personale interno)
• Mosè Rossi (Unità di personale esterno)
• MARGHERITA PEZZULLO (Unità di personale esterno)
• LUIGI MANDRICH (Unità di personale esterno)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)

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

• Journal of Molecular Biology (Rivista)

Insieme di parole chiave di

• Parole chiave di "Analysis of thermal adaptation in the HSL enzyme family" (Insieme di parole chiave)