Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties

被引：45

作者：

Parenicová, L ^{[1
]}

Kester, HCM ^{[1
]}

Benen, JAE ^{[1
]}

Visser, J ^{[1
]}

机构：

[1] Agr Univ Wageningen, Sect Mol Genet Ind Microorganisms, NL-6703 HA Wageningen, Netherlands

来源：

FEBS LETTERS | 2000年 / 467卷 / 2-3期

关键词：

endopolygalacturonase; processivity; methylated oligogalacturonate; Aspergillus niger;

D O I：

10.1016/S0014-5793(00)01173-X

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：

We isolated and characterized a new type of endopolygalacturonase (PG)-encoding gene, pgaD, from Aspergillus niger. The primary structure of PGD differs from that of other A, niger PGs by a 136 amino acid residues long N-terminal extension. Biochemical analysis demonstrated extreme processive behavior of the enzyme on oligomers longer than five galacturonate units. Furthermore, PGD is the only A. niger PG capable of hydrolyzing di-galacturonate. It is tentatively concluded that the enzyme is composed of four subsites, The physiological role of PGD is discussed. (C) 2000 Federation of European Biochemical Societies.

引用

页码：333 / 336

页数：4

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