EC number:3.2.2.2

Enzyme

Download
EC Tree
     3. Hydrolases
        3.2 Glycosylases
            3.2.2 Hydrolysing N-glycosyl compounds
ID:3.2.2.2
Description:Inosine nucleosidase.
Alternative Name: Inosinase.

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.
PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.2.2.2
BRENDA Enzyme Link: BRENDA 3.2.2.2
KEGG Enzyme Link: KEGG3.2.2.2
BioCyc Enzyme Link: BioCyc 3.2.2.2
ExPASy Enzyme Link: ExPASy3.2.2.2
EC2PDB Enzyme Link: EC2PDB 3.2.2.2
ExplorEnz Enzyme Link: ExplorEnz 3.2.2.2
PRIAM enzyme-specific profiles Link: PRIAM 3.2.2.2
IntEnz Enzyme Link: IntEnz 3.2.2.2
MEDLINE Enzyme Link: MEDLINE 3.2.2.2

EC number:3.2.2.2

MSA:

3.2.2.2;
Phylogenetic Tree:

3.2.2.2;
Uniprot:
M-CSA:
RHEA:16657 H2O + inosine = D-ribose + hypoxanthine
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[n;H0;+0:4]1:[*:5]:[*:6](:[c;H0;+0:7](-[OH;+0:8]):[n;H0;+0:9]:[*:10]):[n;H0;+0:11]:[*:12]:1.[OH2;+0:13]>>[*:1]-[CH;+0:2](-[*:3])-[OH;+0:13].[*:10]:[nH;+0:9]:[c;H0;+0:7](=[O;H0;+0:8]):[*:6]1:[*:5]:[n;H0;+0:4]:[*:12]:[nH;+0:11]:1
Reaction
Core-to-Core More
Core-to-Core More

References

TitleAuthorsDatePubMed ID
Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism.Parkin DW, Horenstein BA, Abdulah DR, Estupiñán B, Schramm VL1991 Nov 51939115
Fish muscle riboside hydrolases.TARR HL1955 Mar14363106
Nucleoside hydrolase from Leishmania major. Cloning, expression, catalytic properties, transition state inhibitors, and the 2.5-å crystal structure.Shi W, Schramm VL, Almo SC1999 Jul 2310409664