Enzyme

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EC Tree
     3. Hydrolases
        3.2 Glycosylases
            3.2.2 Hydrolysing N-glycosyl compounds
ID:3.2.2.4
Description:AMP nucleosidase.
Cath: 3.30.1730.10; 3.40.50.1580;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.2.2.4
BRENDA Enzyme Link: BRENDA 3.2.2.4
KEGG Enzyme Link: KEGG3.2.2.4
BioCyc Enzyme Link: BioCyc 3.2.2.4
ExPASy Enzyme Link: ExPASy3.2.2.4
EC2PDB Enzyme Link: EC2PDB 3.2.2.4
ExplorEnz Enzyme Link: ExplorEnz 3.2.2.4
PRIAM enzyme-specific profiles Link: PRIAM 3.2.2.4
IntEnz Enzyme Link: IntEnz 3.2.2.4
MEDLINE Enzyme Link: MEDLINE 3.2.2.4
MSA:

3.2.2.4;

Phylogenetic Tree:

3.2.2.4;

Uniprot:
M-CSA:
RHEA:20129 AMP + H2O = adenine + D-ribose 5-phosphate
RULE(radius=1) [*:1]:[n;H0;+0:2](:[*:3])-[CH;+0:4](-[*:5])-[*:6].[OH2;+0:7]>>[*:5]-[CH;+0:4](-[*:6])-[OH;+0:7].[*:1]:[nH;+0:2]:[*:3]
Reaction
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References

TitleAuthorsDatePubMed ID
Adenylate degradation in Escherichia coli. The role of AMP nucleosidase and properties of the purified enzyme.Leung HB, Schramm VL1980 Nov 257000783
The enzymatic cleavage of adenylic acid to adenine and ribose 5-phosphate.HURWITZ J, HEPPEL LA, HORECKER BL1957 May13428783
Nontargeted in vitro metabolomics for high-throughput identification of novel enzymes in Escherichia coli.Sévin DC, Fuhrer T, Zamboni N, Sauer U2017 Feb27941785