EC number:3.5.1.48
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.48 |
|---|---|
| Description: | Acetylspermidine deacetylase. |
| Alternative Name: |
N-acetylspermidine deacetylase. N(8)-monoacetylspermidine deacetylase. N(8)-acetylspermidine deacetylase. N(8)-acetylspermidine amidohydrolase. N(1)-acetylspermidine amidohydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.48 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.48 |
| KEGG Enzyme Link: | KEGG3.5.1.48 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.48 |
| ExPASy Enzyme Link: | ExPASy3.5.1.48 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.48 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.48 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.48 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.48 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.48 |
| RHEA:23928 | H2O + N(8)-acetylspermidine = acetate + spermidine |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[NH2;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Acetylpolyamine amidohydrolase from Mycoplana ramosa: gene cloning and characterization of the metal-substituted enzyme. | Sakurada K, Ohta T, Fujishiro K, Hasegawa M, Aisaka K | 1996 Oct | 8824626 |
| Crystallization and some properties of acetylpolyamine amidohydrolase from Mycoplana bullata. | Fujishiro K, Ando M, Uwajima T | 1988 Dec 30 | 3207420 |
| Polyamine Deacetylase Structure and Catalysis: Prokaryotic Acetylpolyamine Amidohydrolase and Eukaryotic HDAC10. | Shinsky SA, Christianson DW | 2018 Jun 5 | 29533602 |
| Histone deacetylase 10 structure and molecular function as a polyamine deacetylase. | Hai Y, Shinsky SA, Porter NJ, Christianson DW | 2017 May 18 | 28516954 |