Mechanism of action of the endo-(1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum.

Abstract:

:(1-->3)-alpha-glucanases catalyze the hydrolysis of fungal cell wall (1-->3)-alpha-glucan, and function during cell division of yeasts containing this cell wall component or act in mycoparasitic processes. Here, we characterize the mechanism of action of the (1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum. We observed that MutAp releases predominantly beta-glucose upon hydrolysis of crystalline (1-->3)-alpha-glucan, indicating inversion of the anomeric configuration. After having identified (1-->3)-alpha-glucan tetrasaccharide as the minimal substrate for MutAp, we showed that reduced (1-->3)-alpha-glucan pentasaccharide is cleaved into a trisaccharide and a reduced disaccharide, demonstrating that MutAp displays endo-hydrolytic activity. We propose a model for the catalytic mechanism of MutAp, whereby the enzyme breaks an intrachain glycosidic linkage of (1-->3)-alpha-glucan, and then continues its hydrolysis towards the non-reducing end by releasing beta-glucose residues in a processive manner.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Grün CH,Dekker N,Nieuwland AA,Klis FM,Kamerling JP,Vliegenthart JF,Hochstenbach F

doi

10.1016/j.febslet.2006.05.062

subject

Has Abstract

pub_date

2006-07-10 00:00:00

pages

3780-6

issue

16

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(06)00679-X

journal_volume

580

pub_type

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