Literature summary for 3.2.1.176 extracted from

Wang, M.; Ma, Y.; Li, L.; Wang, B.; Wei, X.; Zhang, M.; Wang, J.; Cui, Q.; Li, Z.; Xu, H.
The diversity of glycosylation of cellobiohydrolase I from Trichoderma reesei determined with mass spectrometry (2019), Biochem. Biophys. Res. Commun., 508, 818-824 .

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Organism

Organism	UniProt	Comment	Textmining
Trichoderma reesei	-	-	-
Trichoderma reesei QM9414	-	-	-
Trichoderma reesei RUT C-30	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	there are four N-glycosylation sites at N270, N384, N45 and N64. N45 and N64 are N-glycosylated with high mannose type glycans. The catalytic domain of the enzyme is extensively O-glycosylated with hexoses and N-acetylhexosamines. There are several glycosylation sites (such as T383, S8, and S46) at the openings of the substrate-binding tunnel, and potentially involve in the binding of cellulose	Trichoderma reesei

Purification (Commentary)

Purification (Comment)	Organism
Sephacryl S-200 gel filtration	Trichoderma reesei

Synonyms

Synonyms	Comment	Organism
CBHI	-	Trichoderma reesei
cellobiohydrolase I	-	Trichoderma reesei

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Release 2023.1 (January 2023)