| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
| ID: | 3.5.3.14 |
|---|---|
| Description: | Amidinoaspartase. |
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.| UniProtKB Enzyme Link: | UniProtKB 3.5.3.14 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.14 |
| KEGG Enzyme Link: | KEGG3.5.3.14 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.14 |
| ExPASy Enzyme Link: | ExPASy3.5.3.14 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.14 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.14 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.14 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.14 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.14 |
| RHEA:14849 | H2O + N-amidino-L-aspartate = L-aspartate + urea |
| RULE(radius=1) | [*:1]-[NH;+0:2]-[C;H0;+0:3](-[*:4])=[NH;+0:5].[OH2;+0:6]>>[*:4]-[C;H0;+0:3](-[NH2;+0:5])=[O;H0;+0:6].[*:1]-[NH2;+0:2] |
| Reaction | ![]() |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Metabolism of guanidinosuccinic acid. I. Characterization of a specific amidino hydrolase from Pseudomonas chlororaphis. | Milstien S, Goldman P | 1972 Oct 10 | 4651648 |