EC number:3.5.1.30

Enzyme

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     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.30
Description:5-aminopentanamidase.
Alternative Name: 5-aminovaleramidase.

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.30
BRENDA Enzyme Link: BRENDA 3.5.1.30
KEGG Enzyme Link: KEGG3.5.1.30
BioCyc Enzyme Link: BioCyc 3.5.1.30
ExPASy Enzyme Link: ExPASy3.5.1.30
EC2PDB Enzyme Link: EC2PDB 3.5.1.30
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.30
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.30
IntEnz Enzyme Link: IntEnz 3.5.1.30
MEDLINE Enzyme Link: MEDLINE 3.5.1.30

EC number:3.5.1.30

MSA:

3.5.1.30;
Phylogenetic Tree:

3.5.1.30;
Uniprot:
M-CSA:
RHEA:15677 5-aminopentanamide + H2O = 5-aminopentanoate + NH4(+)
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH2;+0:4].[OH2;+0:5]>>[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:5].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Delta-aminovaleramidase of Pseudomonas putida.Reitz MS, Rodwell VW1970 Jun5432799
Studies on monooxygenases. I. General properties of crystalline L-lysine monooxygenase.Takeda H, Yamamoto S, Kojima Y, Hayaishi O1969 Jun 105772467