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Literature summary extracted from

  • Lienemann, M.; Boer, H.; Paananen, A.; Cottaz, S.; Koivula, A.
    Toward understanding of carbohydrate binding and substrate specificity of a glycosyl hydrolase 18 family (GH-18) chitinase from Trichoderma harzianum (2009), Glycobiology, 19, 1116-1126.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.2.1.14 D170A/E172Q improved binding afinities toward substrates (GlcNAc)5, (GlcNAc)6, and GlcNbeta-4(GlcNAc)4 Trichoderma harzianum
3.2.1.14 E172Q mutant of isoform Chi42, catalytically inactive. The E172Q mutant binds chitinoligosaccharides, tetra-, penta- and hexamers, with an increasing affinity from 12 to 0.2 microM whereas no binding of chitinbiose, -triose or 3-sialyl-N-acetyllactosamine can be measured Trichoderma harzianum
3.2.1.14 E317A/E172Q affinity decrease down to 20-25% of the affinity of the E172Q reference protein for substrates (GlcNAc)5, (GlcNAc)6 Trichoderma harzianum
3.2.1.14 T133D mutation alters substrate binding specificity of Chit42 toward binding of GlcNbeta-4(GlcNAc)4 by providing a counter charge at subsite -3 Trichoderma harzianum
3.2.1.14 T133D/E172Q decrease in affinities for all ligands by about 65-80% Trichoderma harzianum
3.2.1.14 T133N/E172Q no significant loss of affinity for any of the compounds tested, increase in the selectivity for Galbeta-4(GlcNAc)4 Trichoderma harzianum
3.2.1.14 W246A/E172Q strong decrease in affinity for all ligands tested Trichoderma harzianum
3.2.1.14 W48A/E172Q strong decrease in affinity for all ligands tested Trichoderma harzianum

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.14 allosamidin binding is dependent on the E172 residue, the acid/base catalyst of isoform Chit42 Trichoderma harzianum

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.14 Trichoderma harzianum
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