کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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2050586 | 1074175 | 2006 | 7 صفحه PDF | دانلود رایگان |
(1 → 3)-α-Glucanases catalyze the hydrolysis of fungal cell wall (1 → 3)-α-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)-α-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum. We observed that MutAp releases predominantly β-glucose upon hydrolysis of crystalline (1 → 3)-α-glucan, indicating inversion of the anomeric configuration. After having identified (1 → 3)-α-glucan tetrasaccharide as the minimal substrate for MutAp, we showed that reduced (1 → 3)-α-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)-α-glucan, and then continues its hydrolysis towards the non-reducing end by releasing β-glucose residues in a processive manner.
Journal: FEBS Letters - Volume 580, Issue 16, 10 July 2006, Pages 3780–3786