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Mechanism of action of the endo-(1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum.
FEBS Lett. 2006 Jul 10; 580(16):3780-6.FL

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.

Authors+Show Affiliations

Grün CH
Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, Padualaan 8, 3584 CH Utrecht, The Netherlands.
Dekker N
No affiliation info available
Nieuwland AA
No affiliation info available
Klis FM
No affiliation info available
Kamerling JP
No affiliation info available
Vliegenthart JF
No affiliation info available
Hochstenbach F
No affiliation info available

MeSH

Carbohydrate ConformationCatalysisGlucansGlucoseGlycoside HydrolasesHydrolysisModels, BiologicalPolysaccharidesSubstrate SpecificityTrichoderma

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

16780840

Citation

Grün, Christian H., et al. "Mechanism of Action of the Endo-(1-->3)-alpha-glucanase MutAp From the Mycoparasitic Fungus Trichoderma Harzianum." FEBS Letters, vol. 580, no. 16, 2006, pp. 3780-6.
Grün CH, Dekker N, Nieuwland AA, et al. Mechanism of action of the endo-(1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum. FEBS Lett. 2006;580(16):3780-6.
Grün, C. H., Dekker, N., Nieuwland, A. A., Klis, F. M., Kamerling, J. P., Vliegenthart, J. F., & Hochstenbach, F. (2006). Mechanism of action of the endo-(1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum. FEBS Letters, 580(16), 3780-6.
Grün CH, et al. Mechanism of Action of the Endo-(1-->3)-alpha-glucanase MutAp From the Mycoparasitic Fungus Trichoderma Harzianum. FEBS Lett. 2006 Jul 10;580(16):3780-6. PubMed PMID: 16780840.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Mechanism of action of the endo-(1-->3)-alpha-glucanase MutAp from the mycoparasitic fungus Trichoderma harzianum. AU - Grün,Christian H, AU - Dekker,Nick, AU - Nieuwland,Alexander A, AU - Klis,Frans M, AU - Kamerling,Johannis P, AU - Vliegenthart,Johannes F G, AU - Hochstenbach,Frans, Y1 - 2006/06/09/ PY - 2006/04/21/received PY - 2006/05/25/revised PY - 2006/05/30/accepted PY - 2006/6/20/pubmed PY - 2006/8/15/medline PY - 2006/6/20/entrez SP - 3780 EP - 6 JF - FEBS letters JO - FEBS Lett VL - 580 IS - 16 N2 - (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. SN - 0014-5793 UR - https://www.unboundmedicine.com/medline/citation/16780840/Mechanism_of_action_of_the_endo__1__>3__alpha_glucanase_MutAp_from_the_mycoparasitic_fungus_Trichoderma_harzianum_ DB - PRIME DP - Unbound Medicine ER -