EC number:3.5.1.119
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.119 |
|---|---|
| Description: | Pup amidohydrolase. |
| Alternative Name: |
DPUP. Depupylase/deamidase. Depupylase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.119 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.119 |
| KEGG Enzyme Link: | KEGG3.5.1.119 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.119 |
| ExPASy Enzyme Link: | ExPASy3.5.1.119 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.119 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.119 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.119 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.119 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.119 |
EC number:3.5.1.119
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:47952 | [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamine + H2O = [prokaryotic ubiquitin-like protein]-C-terminal-L-glutamate + 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
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Pupylation as a signal for proteasomal degradation in bacteria. | Striebel F, Imkamp F, Özcelik D, Weber-Ban E | 2014 Jan | 23557784 |
| "Depupylation" of prokaryotic ubiquitin-like protein from mycobacterial proteasome substrates. | Burns KE, Cerda-Maira FA, Wang T, Li H, Bishai WR, Darwin KH | 2010 Sep 10 | 20705495 |
| Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo. | Imkamp F, Rosenberger T, Striebel F, Keller PM, Amstutz B, Sander P, Weber-Ban E | 2010 Feb | 20025664 |
| Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. | Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A, Weber-Ban E | 2009 Jun | 19448618 |