EC number:3.5.2.20

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.2 In cyclic amides
ID:3.5.2.20
Description:Isatin hydrolase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.2.20
BRENDA Enzyme Link: BRENDA 3.5.2.20
KEGG Enzyme Link: KEGG3.5.2.20
BioCyc Enzyme Link: BioCyc 3.5.2.20
ExPASy Enzyme Link: ExPASy3.5.2.20
EC2PDB Enzyme Link: EC2PDB 3.5.2.20
ExplorEnz Enzyme Link: ExplorEnz 3.5.2.20
PRIAM enzyme-specific profiles Link: PRIAM 3.5.2.20
IntEnz Enzyme Link: IntEnz 3.5.2.20
MEDLINE Enzyme Link: MEDLINE 3.5.2.20

EC number:3.5.2.20

MSA:

3.5.2.20;
Phylogenetic Tree:

3.5.2.20;
Uniprot:
M-CSA:
RHEA:43232 H2O + isatin = H(+) + isatinate
RULE(radius=1) [*:3]=[C;H0;+0:4](-[*:5])-[NH;+0:2]-[*:1].[OH2;+0:6]>>([*:1]-[NH2;+0:2].[*:3]=[C;H0;+0:4](-[*:5])-[OH;+0:6]).[H+;H0:7]
Reaction
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References

TitleAuthorsDatePubMed ID
A proton wire and water channel revealed in the crystal structure of isatin hydrolase.Bjerregaard-Andersen K, Sommer T, Jensen JK, Jochimsen B, Etzerodt M, Morth JP2014 Aug 124917679