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3.2.1.186: protodioscin 26-O-beta-D-glucosidase

This is an abbreviated version!
For detailed information about protodioscin 26-O-beta-D-glucosidase, go to the full flat file.

Word Map on EC 3.2.1.186

Reaction

protodioscin
+
H2O
=
26-deglucoprotodioscin
+
D-glucose

Synonyms

aveconasidase, avenacosidase, CSF26G1, F26G, furostanol 26-O-beta-D-glucoside glucohydrolase, furostanol glycoside 26-O-beta-D-glucosidase, S. torvum beta-glucosidase, SBgl3, Solanum torvum GH3 beta-glucosidase, torvosidase

ECTree

     3 Hydrolases
         3.2 Glycosylases
             3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
                3.2.1.186 protodioscin 26-O-beta-D-glucosidase

Subunits

Subunits on EC 3.2.1.186 - protodioscin 26-O-beta-D-glucosidase

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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
1 * 54000 + 1 * 58000, SDS-PAGE
monomer
multimer
x * 60000, the enzyme is highly aggregated. It consists of 300-350 kDa aggregates and multimers thereof
additional information
-
the enzyme has a quaternary protein structure of a three-dimensionally radiated assembly of long fibrillae. It is assembled by linear stacking of hollow trimeric units and the resulting fibril has a long central tunnel connecting to the outer medium via regularly distributed side fenestrations. The enzyme active sites are located within the central tunnel. This unique multimer assembly increases enzyme affinity to avenacosides, in vivo substrates, and may function to discriminate avenacosides from many other kinds of beta-glucoside in oat. The fibrillar multimer of oat beta-glucosidase is a novel quaternary protein structure for enzyme supramolecular assembly that may have a functional role in the regulation of enzyme affinity