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.
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 |