Enzyme

Download
EC Tree
     3. Hydrolases
        3.2 Glycosylases
            3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
ID:3.2.1.188
Description:Avenacosidase.

3D structure

Click one PDB to see exact 3D structure provided by NGL.

Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.2.1.188
BRENDA Enzyme Link: BRENDA 3.2.1.188
KEGG Enzyme Link: KEGG3.2.1.188
BioCyc Enzyme Link: BioCyc 3.2.1.188
ExPASy Enzyme Link: ExPASy3.2.1.188
EC2PDB Enzyme Link: EC2PDB 3.2.1.188
ExplorEnz Enzyme Link: ExplorEnz 3.2.1.188
PRIAM enzyme-specific profiles Link: PRIAM 3.2.1.188
IntEnz Enzyme Link: IntEnz 3.2.1.188
MEDLINE Enzyme Link: MEDLINE 3.2.1.188
MSA:

3.2.1.188;

Phylogenetic Tree:

3.2.1.188;

Uniprot:
M-CSA:
RHEA:38911 avenacoside B + H2O = 26-desgluco-avenacoside B + D-glucose
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:6].[*:5]-[OH;+0:4]
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
The amino acid sequence previously attributed to a protein kinase or a TCP1-related molecular chaperone and co-purified with phytochrome is a beta-glucosidase.Gus-Mayer S, Brunner H, Schneider-Poetsch HA, Lottspeich F, Eckerskorn C, Grimm R, Rüdiger W1994 Jun 208013661
Avenacosidase from oat: purification, sequence analysis and biochemical characterization of a new member of the BGA family of beta-glucosidases.Gus-Mayer S, Brunner H, Schneider-Poetsch HA, Rüdiger W1994 Nov8000004