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
收藏
页码:210 / 215
页数:6
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