EC number:3.5.1.112
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.112 |
|---|---|
| Description: | 2'-N-acetylparomamine deacetylase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.112 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.112 |
| KEGG Enzyme Link: | KEGG3.5.1.112 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.112 |
| ExPASy Enzyme Link: | ExPASy3.5.1.112 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.112 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.112 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.112 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.112 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.112 |
EC number:3.5.1.112
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:34031 | 2'-N-acetylparomamine + H2O = acetate + paromamine |
| 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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Involvement of two distinct N-acetylglucosaminyltransferases and a dual-function deacetylase in neomycin biosynthesis. | Yokoyama K, Yamamoto Y, Kudo F, Eguchi T | 2008 Apr 14 | 18311744 |
| Characterization of the enzyme BtrD from Bacillus circulans and revision of its functional assignment in the biosynthesis of butirosin. | Truman AW, Huang F, Llewellyn NM, Spencer JB | 2007 | 17226887 |