Repository logo
 
Publication

Molecular characterisation of a versatile peroxidase from a bjerkandera strain

2005Journal article Open access
Simple item page
dc.contributor.authorMoreira, Patrícia R.
dc.contributor.authorDuez, C.
dc.contributor.authorDehareng, D.
dc.contributor.authorAntunes, A.
dc.contributor.authorAlmeida-Vara, E.
dc.contributor.authorFrère, J. M.
dc.contributor.authorMalcata, F. Xavier
dc.contributor.authorDuarte, J. C.
dc.date.accessioned2010-11-11T16:51:18Z
dc.date.available2010-11-11T16:51:18Z
dc.date.issued2005
dc.description.abstractThe 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 strainpor
dc.identifier.citationMOREIRA, Patrícia R...[et al.] - Molecular characterisation of a versatile peroxidase from a bjerkandera strain. Journal of Biotechnology. ISSN 0168-1656. Vol. 118, n.º 4 (2005), p. 339–352por
dc.identifier.doi10.1016/j.jbiotec.2005.05.014
dc.identifier.urihttp://hdl.handle.net/10400.14/3389
dc.language.isoengpor
dc.publisherElsevierpor
dc.subjectLigninolytic peroxidasespor
dc.subjectWhite-rot fungipor
dc.subjectCloning and sequencingpor
dc.subjectTertiary structurepor
dc.subjectIntronspor
dc.subjectrbpa genepor
dc.titleMolecular characterisation of a versatile peroxidase from a bjerkandera strainpor
dc.typejournal article
dspace.entity.typePublication
person.familyNameMoreira
person.familyNameMalcata
person.givenNamePatrícia
person.givenNameFrancisco
person.identifier.ciencia-id3A17-0D5A-2C03
person.identifier.ciencia-id1B13-38A5-35F5
person.identifier.orcid0000-0002-0004-851X
person.identifier.orcid0000-0003-3073-1659
person.identifier.scopus-author-id7006510563
person.identifier.scopus-author-id7102542478
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationcd69b8c0-d44f-46ae-91d2-24a36418f50a
relation.isAuthorOfPublicationa06c00da-0e2f-4434-8ede-4d7b22c0dfe9
relation.isAuthorOfPublication.latestForDiscoverycd69b8c0-d44f-46ae-91d2-24a36418f50a

Files

Original bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
Molecular characterisation of a versatile peroxidase.pdf
Size:
447.09 KB
Format:
Adobe Portable Document Format
Download
License bundle
Now showing 1 - 1 of 1
No Thumbnail Available
Name:
license.txt
Size:
3.44 KB
Format:
Item-specific license agreed upon to submission
Description:
Download

Collections

ESB - Contribuições em Revistas Científicas / Contribution to Journals