EC number:3.5.1.121
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.121 |
|---|---|
| Description: | Protein N-terminal asparagine amidohydrolase. |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.121 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.121 |
| KEGG Enzyme Link: | KEGG3.5.1.121 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.121 |
| ExPASy Enzyme Link: | ExPASy3.5.1.121 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.121 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.121 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.121 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.121 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.121 |
EC number:3.5.1.121
| MSA: | |
|---|---|
| Phylogenetic Tree: | |
| Uniprot: | |
| M-CSA: |
| RHEA:50676 | H(+) + H2O + N-terminal L-asparaginyl-[protein] = N-terminal L-aspartyl-[protein] + NH4(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[NH2;+0:4].[H+;H0:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[NH3;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| A mouse amidase specific for N-terminal asparagine. The gene, the enzyme, and their function in the N-end rule pathway. | Grigoryev S, Stewart AE, Kwon YT, Arfin SM, Bradshaw RA, Jenkins NA, Copeland NG, Varshavsky A | 1996 Nov 8 | 8910481 |
| Protein NH2-terminal asparagine deamidase. Isolation and characterization of a new enzyme. | Stewart AE, Arfin SM, Bradshaw RA | 1994 Sep 23 | 8089117 |
| Expression and biochemical characterization of the human enzyme N-terminal asparagine amidohydrolase. | Cantor JR, Stone EM, Georgiou G | 2011 Apr 12 | 21375249 |