Molecular characterisation of a versatile peroxidase from a Bjerkandera strain

• Type: Article in International Scientific Journal
• Date: 2005

Authors

Moreira, PR (Author) Other; Duez, C (Author) Other; Dehareng, D (Author) Other; Antunes, A (Author) Other; Almeida Vara, E (Author) Other; Frere, JM (Author) Other; F. Xavier Malcata (Author) Other; Duarte, JC (Author) Other

Journal

Title: Journal of Biotechnology

Vol. 118

Pages: 339-352

ISSN: 0168-1656

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 47 Citations

Scopus - 50 Citations

Other information

Authenticus ID: P-000-1CW

DOI: 10.1016/j.jbiotec.2005.05.014

Abstract (EN): 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, RIBP 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 UP and MnP. In addition, the RBP enzyme appears to be closely related with the ligninolytic peroxidases from the Trametes versicolor strain. (C) 2005 Published by Elsevier B.V.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 14