LIMITED PROTEOLYSIS OF HANSENULA-POLYMORPHA YEAST AMINE OXIDASE - ISOLATION OF A C-TERMINAL FRAGMENT CONTAINING BOTH A COPPER AND QUINO-COFACTOR

被引：6

作者：

PLASTINO, J ^{[1
]}

KLINMAN, JP ^{[1
]}

机构：

[1] UNIV CALIF BERKELEY,DEPT CHEM,BERKELEY,CA 94720

来源：

FEBS LETTERS | 1995年 / 371卷 / 03期

关键词：

TOPA QUINONE; COPPER PROTEIN; AMINE OXIDASE; COFACTOR BIOGENESIS; LIMITED PROTEOLYSIS;

D O I：

10.1016/0014-5793(95)00907-Q

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：

Limited proteolysis of recombinant Hansenula polymorpha yeast amino oxidase produces a 48 kDa fragment which corresponds to the C-terminal two-thirds of the protein, The fragment contains both TOPA (2,4,5-trihydroxyphenylalanine) and copper, as well as the histidine ligands implicated in copper binding. The fragment is proposed to be the domain responsible for cofactor production in yeast amine oxidase.

引用

页码：276 / 278

页数：3

共 11 条

[1]

ADAM ET, 1991, ADV PROTEIN CHEM, V42, P144

[2]

CAI DY, 1994, J BIOL CHEM, V269, P32039

[3] COPPER AMINE OXIDASE - HETEROLOGOUS EXPRESSION, PURIFICATION, AND CHARACTERIZATION OF AN ACTIVE ENZYME IN SACCHAROMYCES-CEREVISIAE [J].