Molecular characterisation of a versatile peroxidase from a bjerkandera strain

• Author(s): Moreira, Patrícia R. ; Duez, C. ; Dehareng, D. ; Antunes, A. ; Almeida-Vara, E. ; Frère, J. M. ; Malcata, F. Xavier ; Duarte, J. C.
• Date: 2005
• Persistent ID: http://hdl.handle.net/10400.14/3389
• Origin: Veritati - Repositório Institucional da Universidade Católica Portuguesa
• Subject(s): Ligninolytic peroxidases; White-rot fungi; Cloning and sequencing; Tertiary structure; Introns; rbpa gene
• Document Type: Article
• Language: English

Description

The cloning and sequencing of the rbpa gene coding for a versatile peroxidase from a novel Bjerkandera strain is hereby reported. The 1777 bp isolated fragment contained a 1698 bp peroxidase-encoding gene, interrupted by 11 introns. The 367 amino acid-deduced sequence includes a 27 amino acid-signal peptide. The molecular model, built via homology modelling with crystal structures of four fungal peroxidases, highlighted the amino acid residues putatively involved in manganese binding and aromatic substrate oxidation. The potential heme pocket residues (R44, F47, H48, E79, N85, H177, F194 and D239) include both distal and proximal histidines (H48 and H177). RBP possesses potential calcium-binding residues (D49, G67, D69, S71, S178, D195, T197, I200 and D202) and eight cysteine residues (C3, C15, C16, C35, C121, C250, C286, C316). In addition, RBP includes residues involved in substrate oxidation: three acidic residues (E37, E41 and D183)—putatively involved in manganese binding and H83 and W172—potentially involved in oxidation of aromatic substrates. Characterisation of nucleotide and amino acid sequences include RBP in versatile peroxidase group sharing catalytic properties of both LiP and MnP. In addition, the RBP enzyme appears to be closely related with the ligninolytic peroxidases from the Trametes versicolor strain