Expression, purification, and characterization of a cobalt-activated chitin deacetylase (Cda2p) from Saccharomyces cerevisiae

被引：55

作者：

Martinou, A

Koutsioulis, D

Bouriotis, V

机构：

[1] Univ Crete, Dept Biol, Div Appl Biol & Biotechnol, Iraklion 71409, Crete, Greece

[2] Inst Mol Biol & Biotechnol, Enzyme Biotechnol Div, Iraklion 71110, Crete, Greece

来源：

PROTEIN EXPRESSION AND PURIFICATION | 2002年 / 24卷 / 01期

关键词：

D O I：

10.1006/prep.2001.1547

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Chitin deacetylase (Cda2p) (EC 3.5.1.41) from Saccharomyces cerevisiae has been purified from vegetative cells grown in galactose and further characterized. The enzyme is a glycoprotein with an apparent molecular mass of similar to43 kDa and a carbohydrate content of approximately 18% by weight. With glycol chitin as substrate, the optimum temperature for enzyme activity is 50degreesC and the pH optimum is 8.0. The enzyme requires at least two N-acetyl-D-glucosamine residues (chitobiose) for catalysis and is partially inhibited by acetate. Deglycosylation of the enzyme causes total loss of enzyme activity, which can be restored by the addition Of CoCl2. (C) 2002 Elsevier Science (USA).

引用

页码：111 / 116

页数：6

共 22 条

[1] PURIFICATION OF A HEAT-STABLE CHITIN DEACETYLASE FROM ASPERGILLUS-NIDULANS AND ITS ROLE IN CELL-WALL DEGRADATION [J].