Identification and characterisation of a novel acylpeptide hydrolase from sulfolobus solfataricus: structural and functional insights (Articolo in rivista)

Type

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

Label

• Identification and characterisation of a novel acylpeptide hydrolase from sulfolobus solfataricus: structural and functional insights (Articolo in rivista) (literal)

Anno

• 2012-01-01T00:00:00+01:00 (literal)

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

• 10.1371/journal.pone.0037921 (literal)

Alternative label

• Marta Gogliettino#1, Marco Balestrieri#1, Ennio Cocca 1, Sabrina Mucerino 1, Mose Rossi 1, Mauro Petrillo 2, Emanuela Mazzella 1, and Gianna Palmieri 1 (2012)
  Identification and characterisation of a novel acylpeptide hydrolase from sulfolobus solfataricus: structural and functional insights
  in PloS one
  (literal)

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

• Marta Gogliettino#1, Marco Balestrieri#1, Ennio Cocca 1, Sabrina Mucerino 1, Mose Rossi 1, Mauro Petrillo 2, Emanuela Mazzella 1, and Gianna Palmieri 1 (literal)

Pagina inizio

• 37921 (literal)

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

• http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3360023/ (literal)

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

• 7 (literal)

Rivista

• PloS one (Rivista)

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

• 5 (literal)

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

• 1. Institute of Protein Biochemistry, National Research Council (CNR-IBP), Naples, Italy 2. CEINGE - Biotecnologie Avanzate, Via Gaetano Salvatore, Naples, Italy (literal)

Titolo

• Identification and characterisation of a novel acylpeptide hydrolase from sulfolobus solfataricus: structural and functional insights (literal)

Abstract

• A novel acylpeptide hydrolase, named APEH-3Ss, was isolated from the hypertermophilic archaeon Sulfolobus solfataricus. APEH is a member of the prolyl oligopeptidase family which catalyzes the removal of acetylated amino acid residues from the N terminus of oligopeptides. The purified enzyme shows a homotrimeric structure, unique among the associate partners of the APEH cluster and, in contrast to the archaeal APEHs which show both exo/endo peptidase activities, it appears to be a \"true\" aminopeptidase as exemplified by its mammalian counterparts, with which it shares a similar substrate specificity. Furthermore, a comparative study on the regulation of apeh gene expression, revealed a significant but divergent alteration in the expression pattern of apeh-3Ss and apehSs (the gene encoding the previously identified APEHSs from S. solfataricus), which is induced in response to various stressful growth conditions. Hence, both APEH enzymes can be defined as stress-regulated proteins which play a complementary role in enabling the survival of S. solfataricus cells under different conditions. These results provide new structural and functional insights into S. solfataricus APEH, offering a possible explanation for the multiplicity of this enzyme in Archaea. (literal)

Prodotto di

• PROF. M. ROSSI: Applicazioni innovative di enzimi e biotrasformazioni (SV.P14.002.001) (Modulo)
• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• Sabrina Mucerino (Persona)
• MARTA GOGLIETTINO (Persona)
• GIANNA PALMIERI (Persona)
• MARCO BALESTRIERI (Unità di personale interno)
• ENNIO COCCA (Persona)
• Mosè Rossi (Unità di personale esterno)

Incoming links:

Autore CNR di

• MARCO BALESTRIERI (Unità di personale interno)
• GIANNA PALMIERI (Persona)
• Mosè Rossi (Unità di personale esterno)
• ENNIO COCCA (Persona)
• Sabrina Mucerino (Persona)
• MARTA GOGLIETTINO (Persona)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)
• PROF. M. ROSSI: Applicazioni innovative di enzimi e biotrasformazioni (SV.P14.002.001) (Modulo)

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

• PloS one (Rivista)