Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and structural importance of two disulfide bridges. (Articolo in rivista)

Type

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

Label

• Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and structural importance of two disulfide bridges. (Articolo in rivista) (literal)

Anno

• 2000-01-01T00:00:00+01:00 (literal)

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

• 10.1046/j.1432-1327.2000.01510.x (literal)

Alternative label

• Camardella L, Carratore V, Ciardiello MA, Servillo L, Balestrieri C, Giovane A. (2000)
  Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and structural importance of two disulfide bridges.
  in European journal of biochemistry (Print)
  (literal)

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

• Camardella L, Carratore V, Ciardiello MA, Servillo L, Balestrieri C, Giovane A. (literal)

Pagina inizio

• 4561 (literal)

Pagina fine

• 4565 (literal)

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

• 267 (literal)

Rivista

• European journal of biochemistry (Rivista)

Note

• ISI Web of Science (WOS) (literal)

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

• CNR, Inst Prot Biochem & Enzymol, I-00185 Rome, Italy; Univ Naples 2, Dept Biochem & Biophys, I-80138 Naples, Italy (literal)

Titolo

• Kiwi protein inhibitor of pectin methylesterase. Amino-acid sequence and structural importance of two disulfide bridges. (literal)

Abstract

• A protein acting as a powerful inhibitor of plant pectin methylesterase was isolated from kiwi (Actinidia chinensis) fruit. The complete amino-acid sequence of the pectin methylesterase inhibitor (PMEI) was determined by direct protein analysis. The sequence comprises 152 amino-acid residues, accounting for a molecular mass of 16 277 Da. The far-UV CD spectrum indicated a predominant alpha-helix conformation in the secondary structure. The protein has five cysteine residues but neither tryptophan nor methionine. Analysis of fragments obtained after digestion of the protein alkylated without previous reduction identified two disulfide bridges connecting Cys9 with Cys18, and Cys74 with Cys114; Cys140 bears a free thiol group. A database search pointed out a similarity between PMEI and plant invertase inhibitors. In particular, the four Cys residues, which in PMEI are involved in the disulfide bridges, are conserved. This allows us to infer that also in the homologous proteins, whose primary structure was deduced only by cDNA sequencing, those cysteine residues are engaged in two disulfide bridges, and constitute a common structural motif. The comparison of the sequence of these inhibitors confirms the existence of a novel class of proteins with moderate but significant sequence conservation, comprising plant proteins acting as inhibitors of sugar metabolism enzymes, and probably involved in various steps of plant development. (literal)

Prodotto di

• Institute of protein biochemistry (IBP) (Istituto)

Autore CNR

• MARIA ANTONIETTA CIARDIELLO (Persona)
• VITALE CARRATORE (Persona)
• LAURA CAMARDELLA (Unità di personale interno)

Incoming links:

Autore CNR di

• LAURA CAMARDELLA (Unità di personale interno)
• VITALE CARRATORE (Persona)
• MARIA ANTONIETTA CIARDIELLO (Persona)

Prodotto

• Institute of protein biochemistry (IBP) (Istituto)

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

• European journal of biochemistry (Rivista)