Literature summary for 3.2.1.182 extracted from

Czjzek, M.; Cicek, M.; Zamboni, V.; Bevan, D.R.; Henrissat, B.; Esen, A.
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes (2000), Proc. Natl. Acad. Sci. USA, 97, 13555-13560.

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Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Zea mays

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystal structure of inactive mutant E191D Glu1 in complex with DIMBO-glucoside, the free aglycone DIMBOA, and competitive inhibitor dhurrin is solved at 2.1, 2.1, 2.0 A resolution, respectively. The free enzyme is solved at 2.2 A resolution	Zea mays

Protein Variants

Protein Variants	Comment	Organism
E191D	catalytically inactive mutant is used for crystal structure determination	Zea mays

Inhibitors

Inhibitors	Comment	Organism	Structure
Dhurrin	-	Zea mays

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
120000	-	homodimer	Zea mays

Organism

Organism	UniProt	Comment	Textmining
Zea mays	P49235	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
DIMBOA-glucoside + H2O	-	Zea mays	DIMBOA + beta-D-glucose	-	?

Subunits

Subunits	Comment	Organism
homodimer	crystal structure	Zea mays

Synonyms

Synonyms	Comment	Organism
beta-glucosidase	-	Zea mays

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Release 2023.1 (January 2023)