Characterization of a laccase gene from the white-rot fungus Trametes versicolor and structural features of basidiomycete laccases.
A gene coding for the multi-copper phenol oxidase laccase has been isolated from the white-rot basidiomycete Trametes versicolor. 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.
Jönsson
L
L
University of Lund, Sweden.
Sjöström
K
K
Häggström
I
I
Nyman
P O
PO
D000595:Amino Acid Sequence; D001483:Base Sequence; D001487:Basidiomycota / Q000201:enzymology* / Q000235:genetics; D004220:Disulfides / Q000737:chemistry; D042845:Laccase; D008969:Molecular Sequence Data; D010088:Oxidoreductases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D016415:Sequence Alignment
D004220:Disulfides; D010088:Oxidoreductases; D042845:Laccase