EC number:3.5.5.7

Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.5 In nitriles
ID:3.5.5.7
Description:Aliphatic nitrilase.
Prosite: PDOC00712;
PDB:
PDBScop

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.5.7
BRENDA Enzyme Link: BRENDA 3.5.5.7
KEGG Enzyme Link: KEGG3.5.5.7
BioCyc Enzyme Link: BioCyc 3.5.5.7
ExPASy Enzyme Link: ExPASy3.5.5.7
EC2PDB Enzyme Link: EC2PDB 3.5.5.7
ExplorEnz Enzyme Link: ExplorEnz 3.5.5.7
PRIAM enzyme-specific profiles Link: PRIAM 3.5.5.7
IntEnz Enzyme Link: IntEnz 3.5.5.7
MEDLINE Enzyme Link: MEDLINE 3.5.5.7

EC number:3.5.5.7

MSA:

3.5.5.7;
Phylogenetic Tree:

3.5.5.7;
Uniprot:
M-CSA:
RHEA:46188 an aliphatic nitrile + 2 H2O = a carboxylate + NH4(+)
RULE(radius=1) [*:1]-[C;H0;+0:2]#[N;H0;+0:3].[OH2;+0:4].[OH2;+0:5]>>[*:1]-[C;H0;+0:2](=[O;H0;+0:5])-[OH;+0:4].[NH3;+0:3]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
A new nitrilase from Bradyrhizobium japonicum USDA 110. Gene cloning, biochemical characterization and substrate specificity.Zhu D, Mukherjee C, Yang Y, Rios BE, Gallagher DT, Smith NN, Biehl ER, Hua L2008 Feb 118061298
Primary structure of an aliphatic nitrile-degrading enzyme, aliphatic nitrilase, from Rhodococcus rhodochrous K22 and expression of its gene and identification of its active site residue.Kobayashi M, Yanaka N, Nagasawa T, Yamada H1992 Sep 221390687
The nitrilase superfamily: classification, structure and function.Pace HC, Brenner C200111380987