CHARACTERIZATION OF A LACCASE GENE FROM THE WHITE-ROT FUNGUS TRAMETES-VERSICOLOR AND STRUCTURAL FEATURES OF BASIDIOMYCETE LACCASES

被引：76

作者：

JONSSON, L ^{[1
]}

SJOSTROM, K ^{[1
]}

HAGGSTROM, I ^{[1
]}

NYMAN, PO ^{[1
]}

机构：

[1] LUND UNIV,S-22100 LUND,SWEDEN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1995年 / 1251卷 / 02期

关键词：

LACCASE; PHENOL OXIDASE; MULTI-COPPER ENZYME; WHITE-ROT FUNGUS; LIGNIN DEGRADATION; (T-VERSICOLOR);

D O I：

10.1016/0167-4838(95)00104-3

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：210 / 215

页数：6

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