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

Jönsson, Leif (författare)

Sjöström, Kjell (författare)

Häggström, Ingrid (författare)

Nyman, Per-Olof (författare): Lund University,Lunds universitet,Biokemi och Strukturbiologi,Centrum för Molekylär Proteinvetenskap,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biochemistry and Structural Biology,Center for Molecular Protein Science,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH

(creator_code:org_t)

Elsevier BV, 1995
1995
Engelska.
Ingår i: BBA - Protein Structure and Molecular Enzymology. - : Elsevier BV. - 0167-4838. ; 1251:2, s. 210-215

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Abstract Ämnesord

Stäng

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.

Av författaren/redakt...: Jönsson, Leif; Sjöström, Kjell; Häggström, Ingri ...; Nyman, Per-Olof

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