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 Lettjournal_title
FEBS lettersauthors
Grün CH,Dekker N,Nieuwland AA,Klis FM,Kamerling JP,Vliegenthart JF,Hochstenbach Fdoi
10.1016/j.febslet.2006.05.062subject
Has Abstractpub_date
2006-07-10 00:00:00pages
3780-6issue
16eissn
0014-5793issn
1873-3468pii
S0014-5793(06)00679-Xjournal_volume
580pub_type
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