Literature summary for 3.2.1.149 extracted from

Zhou, Y.; Zeng, L.; Gui, J.; Liao, Y.; Li, J.; Tang, J.; Meng, Q.; Dong, F.; Yang, Z.
Functional characterizations of beta-glucosidases involved in aroma compound formation in tea (Camellia sinensis) (2017), Food Res. Int., 96, 206-214 .

Search for more literature for 3.2.1.149

Cloned(Commentary)

Cloned (Comment)	Organism
phylogenetic analysis and tree	Camellia sinensis

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
cell wall	-	Camellia sinensis	5618	-
additional information	the enzyme is part of the secretory pathway	Camellia sinensis	-	-

Organism

Organism	UniProt	Comment	Textmining
Camellia sinensis	Q7X9A9	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
flower	-	Camellia sinensis	-
leaf	tea leaves only contain one beta-primeverosidase gene	Camellia sinensis	-

General Information

General Information	Comment	Organism
evolution	phylogenetic analysis and tree, the enzyme belongs to the glycosyl hydrolase family 1, GH1. All GH1 family beta-Glus in Camellia sinensis contain the same PfamB domain (PB027112) in the N-terminus, followed by a PfamA domain (PF00232, glyco_hydro_1)	Camellia sinensis
physiological function	many tea aroma compounds are present as glycosidically conjugated forms in tea leaves, and can be hydrolyzed by beta-glucosidase (beta-Glu) and beta-primeverosidase. beta-Primeverosidase hydrolyzes beta-primeverosidically bound volatiles to free volatiles. In tea leaves, beta-primeverosidase and beta-Glus are the main enzymes involved in the transformation of glycosidically bound volatiles (GBVs) into free volatiles. Disruption of the tea leaf cells is essential for the interaction of substrates (GBVs occur in vacuoles) and enzymes (beta-primeverosidase localized in cell walls)	Camellia sinensis

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Release 2023.1 (January 2023)