The gene, protein and glycan structures of laccase from Pleurotus ostreatus.
Eur J Biochem
; 235(3): 508-15, 1996 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-8654395
ABSTRACT
A member of the laccase multigene family in Pleurotus ostreatus has been cloned and sequenced. The gene structure has been determined by comparison with the corresponding cDNA, synthesized by reverse transcription/PCR amplification. The gene encode a laccase isoenzyme of 533 amino acids which has already been purified and characterized [Palmieri, G., Giardina, P., Marzullo, L., Desiderio, B., Nitti, G., Cannio, R. & Sannia, G.(1993) Appl. Microbiol. Biotechnol. 39, 632-636]. More than 92% of the protein sequence, including the N and C termini, has been verified by fast-atom-bombardment mass spectrometry, thus confirming the correspondence between the gene and its protein product. The protein was N-glycosylated Asn444. Glycan analysis showed the presence of only a high-mannose structure containing varying numbers of mannose residues. The presence of O-linked oligosaccharides as well as other post-translational modification could be ruled out by the mass analysis.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Oxirredutases
/
Polyporaceae
/
Polissacarídeos
Idioma:
En
Revista:
Eur J Biochem
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Itália