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Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases

Jönsson, Leif ; Sjöström, Kjell ; Häggström, Ingrid and Nyman, Per-Olof LU (1995) In BBA - Protein Structure and Molecular Enzymology 1251(2). p.210-215
Abstract
A gene coding for the multi-copper phenol oxidase laccase has been isolated from the white-rot basidiomycete Trametes oersicolor. The gene, which is preceded by a TATA box and a pyrimidine-rich region, is predicted to contain ten introns. The mature translation product, preceded by a 22-residue signal peptide, should consist of 498 residues. Comparisons with Edman degradation data of peptides from T. versicolor laccase strongly suggest that two disulfide bridges are formed by Cys-85/Cys-487 and Cys-117/Cys-205, respectively. The encoded protein contains five Cys, and the sequence surrounding the remaining Cys-452 is consistent with its involvement in the ligation of type-1 copper. Alignment of sequences indicates that T. versicolor laccase... (More)
A gene coding for the multi-copper phenol oxidase laccase has been isolated from the white-rot basidiomycete Trametes oersicolor. The gene, which is preceded by a TATA box and a pyrimidine-rich region, is predicted to contain ten introns. The mature translation product, preceded by a 22-residue signal peptide, should consist of 498 residues. Comparisons with Edman degradation data of peptides from T. versicolor laccase strongly suggest that two disulfide bridges are formed by Cys-85/Cys-487 and Cys-117/Cys-205, respectively. The encoded protein contains five Cys, and the sequence surrounding the remaining Cys-452 is consistent with its involvement in the ligation of type-1 copper. Alignment of sequences indicates that T. versicolor laccase displays a Phe at the position corresponding to a residue (Met in ascorbate oxidase and azurin) considered important for the reduction potential of type-1 copper proteins. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Laccase, Phenol oxidase, Multi-copper enzyme, White-rot fungus, Lignin degradation, (T. versicolor)
in
BBA - Protein Structure and Molecular Enzymology
volume
1251
issue
2
pages
210 - 215
publisher
Elsevier
external identifiers
  • scopus:0029086873
ISSN
0167-4838
DOI
10.1016/0167-4838(95)00104-3
language
English
LU publication?
yes
id
056c3027-6df8-4866-be18-e18189f306a5 (old id 126496)
date added to LUP
2016-04-01 17:11:40
date last changed
2021-01-03 07:21:10
@article{056c3027-6df8-4866-be18-e18189f306a5,
  abstract     = {{A gene coding for the multi-copper phenol oxidase laccase has been isolated from the white-rot basidiomycete Trametes oersicolor. The gene, which is preceded by a TATA box and a pyrimidine-rich region, is predicted to contain ten introns. The mature translation product, preceded by a 22-residue signal peptide, should consist of 498 residues. Comparisons with Edman degradation data of peptides from T. versicolor laccase strongly suggest that two disulfide bridges are formed by Cys-85/Cys-487 and Cys-117/Cys-205, respectively. The encoded protein contains five Cys, and the sequence surrounding the remaining Cys-452 is consistent with its involvement in the ligation of type-1 copper. Alignment of sequences indicates that T. versicolor laccase displays a Phe at the position corresponding to a residue (Met in ascorbate oxidase and azurin) considered important for the reduction potential of type-1 copper proteins.}},
  author       = {{Jönsson, Leif and Sjöström, Kjell and Häggström, Ingrid and Nyman, Per-Olof}},
  issn         = {{0167-4838}},
  keywords     = {{Laccase; Phenol oxidase; Multi-copper enzyme; White-rot fungus; Lignin degradation; (T. versicolor)}},
  language     = {{eng}},
  number       = {{2}},
  pages        = {{210--215}},
  publisher    = {{Elsevier}},
  series       = {{BBA - Protein Structure and Molecular Enzymology}},
  title        = {{Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases}},
  url          = {{http://dx.doi.org/10.1016/0167-4838(95)00104-3}},
  doi          = {{10.1016/0167-4838(95)00104-3}},
  volume       = {{1251}},
  year         = {{1995}},
}