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Literature summary 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.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.2.1.182 expressed in Escherichia coli Zea mays

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.2.1.182 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.182 Dhurrin
-
 Zea mays

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.182 120000
-
 homodimer Zea mays

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.182 Zea mays P49235
-
-

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
3.2.1.182 homodimer crystal structure Zea mays

Synonyms

EC Number Synonyms Comment Organism
3.2.1.182 beta-glucosidase
-
 Zea mays