LIGNIN PEROXIDASE FROM THE BASIDIOMYCETE PHANEROCHAETE-CHRYSOSPORIUM IS SYNTHESIZED AS A PREPROENZYME

被引：45

作者：

RITCH, TG

NIPPER, VJ

AKILESWARAN, L

SMITH, AJ

PRIBNOW, DG

GOLD, MH

机构：

[1] OREGON GRAD INST SCI & TECHNOL,DEPT CHEM & BIOL SCI,19600 NW VON NEUMANN DR,BEAVERTON,OR 97006

[2] STANFORD UNIV,MED CTR,BECKMAN CTR,STANFORD,CA 94305

来源：

GENE | 1991年 / 107卷 / 01期

基金：

美国国家科学基金会;

关键词：

PROPEPTIDE; SIGNAL PEPTIDE; CDNA SEQUENCE; FILAMENTOUS FUNGUS; LIGNIN DEGRADATION; RECOMBINANT DNA;

D O I：

10.1016/0378-1119(91)90304-T

中图分类号：

Q3 [遗传学];

学科分类号：

071007 ; 090102 ;

摘要：

The cDNA clone L18 encoding lignin peroxidase LiP2, the most highly expressed LiP isozyme from Phanerochaete chrysosporium strain OGC101, was isolated and sequenced. Comparison of the cDNA sequence with the N-terminal sequence of the mature LiP2 protein isolated from culture medium suggests that the mature protein contains 343 amino acids (aa) and is preceded by a 28-aa leader sequence. In vitro transcription followed by in vitro translation and processing by signal peptidase resulted in cleavage at a site following the Ala21 (counted from the N-terminal Met1 of the initial translation product). The resultant protein contains a 7-aa propeptide, indicating that LiP is synthesized as a preproenzyme.

引用

页码：119 / 126

页数：8