Literature summary for 3.2.1.14 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.

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Protein Variants

Protein Variants	Comment	Organism
D170A/E172Q	improved binding afinities toward substrates (GlcNAc)5, (GlcNAc)6, and GlcNbeta-4(GlcNAc)4	Trichoderma harzianum
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
E317A/E172Q	affinity decrease down to 20-25% of the affinity of the E172Q reference protein for substrates (GlcNAc)5, (GlcNAc)6	Trichoderma harzianum
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
T133D/E172Q	decrease in affinities for all ligands by about 65-80%	Trichoderma harzianum
T133N/E172Q	no significant loss of affinity for any of the compounds tested, increase in the selectivity for Galbeta-4(GlcNAc)4	Trichoderma harzianum
W246A/E172Q	strong decrease in affinity for all ligands tested	Trichoderma harzianum
W48A/E172Q	strong decrease in affinity for all ligands tested	Trichoderma harzianum

Inhibitors

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

Organism

Organism	UniProt	Comment	Textmining
Trichoderma harzianum	-	-	-

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Release 2023.1 (January 2023)