Enzyme

Download
EC Tree
     3. Hydrolases
        3.2 Glycosylases
            3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
ID:3.2.1.204
Description:1,3-alpha-isomaltosidase.

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 3.2.1.204
BRENDA Enzyme Link: BRENDA 3.2.1.204
KEGG Enzyme Link: KEGG3.2.1.204
BioCyc Enzyme Link: BioCyc 3.2.1.204
ExPASy Enzyme Link: ExPASy3.2.1.204
EC2PDB Enzyme Link: EC2PDB 3.2.1.204
ExplorEnz Enzyme Link: ExplorEnz 3.2.1.204
PRIAM enzyme-specific profiles Link: PRIAM 3.2.1.204
IntEnz Enzyme Link: IntEnz 3.2.1.204
MEDLINE Enzyme Link: MEDLINE 3.2.1.204
MSA:

3.2.1.204;

Phylogenetic Tree:

3.2.1.204;

Uniprot:
M-CSA:
RHEA:24844 cyclobis-(1->3)-alpha-isomaltosyl + 2 H2O = 2 isomaltose
RULE(radius=1) ([*:1]-[CH;+0:2](-[*:3])-[O;H0;+0:4]-[*:5].[*:6]-[O;H0;+0:7]-[CH;+0:8](-[*:9])-[*:10]).[OH2;+0:11].[OH2;+0:12]>>([*:9]-[CH;+0:8](-[*:10])-[OH;+0:12].[*:1]-[CH;+0:2](-[*:3])-[OH;+0:11]).([*:6]-[OH;+0:7].[*:5]-[OH;+0:4])
Reaction
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Two Novel Glycoside Hydrolases Responsible for the Catabolism of Cyclobis-(1→6)-α-nigerosyl.Tagami T, Miyano E, Sadahiro J, Okuyama M, Iwasaki T, Kimura A2016 Aug 527302067
Purification and characterization of an intracellular cycloalternan-degrading enzyme from Bacillus sp. NRRL B-21195.Kim YK, Kitaoka M, Hayashi K, Kim CH, Côté GL2004 Apr 2815063208