Enzyme

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EC Tree
     3. Hydrolases
        3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
            3.5.1 In linear amides
ID:3.5.1.62
Description:Acetylputrescine deacetylase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 3.5.1.62
BRENDA Enzyme Link: BRENDA 3.5.1.62
KEGG Enzyme Link: KEGG3.5.1.62
BioCyc Enzyme Link: BioCyc 3.5.1.62
ExPASy Enzyme Link: ExPASy3.5.1.62
EC2PDB Enzyme Link: EC2PDB 3.5.1.62
ExplorEnz Enzyme Link: ExplorEnz 3.5.1.62
PRIAM enzyme-specific profiles Link: PRIAM 3.5.1.62
IntEnz Enzyme Link: IntEnz 3.5.1.62
MEDLINE Enzyme Link: MEDLINE 3.5.1.62
MSA:

3.5.1.62;

Phylogenetic Tree:

3.5.1.62;

Uniprot:
M-CSA:
RHEA:23412 H2O + N-acetylputrescine = acetate + putrescine
RULE(radius=1) [*:1]=[C;H0;+0:2](-[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:5]-[NH2;+0:4].[*:1]=[C;H0;+0:2](-[*:3])-[OH;+0:6]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme.Sakurada K, Ohta T, Fujishiro K, Hasegawa M, Aisaka K1996 Oct8824626
Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata.Fujishiro K, Ando M, Uwajima T1988 Dec 303207420
Substrate specificity and function of acetylpolyamine amidohydrolases from Pseudomonas aeruginosa.Krämer A, Herzer J, Overhage J, Meyer-Almes FJ2016 Mar 926956223