EC Tree |
3. Hydrolases |
3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
3.5.3 In linear amidines |
ID: | 3.5.3.10 |
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Description: | D-arginase. |
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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 3.5.3.10 |
BRENDA Enzyme Link: | BRENDA 3.5.3.10 |
KEGG Enzyme Link: | KEGG3.5.3.10 |
BioCyc Enzyme Link: | BioCyc 3.5.3.10 |
ExPASy Enzyme Link: | ExPASy3.5.3.10 |
EC2PDB Enzyme Link: | EC2PDB 3.5.3.10 |
ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.10 |
PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.10 |
IntEnz Enzyme Link: | IntEnz 3.5.3.10 |
MEDLINE Enzyme Link: | MEDLINE 3.5.3.10 |
RHEA:12901 | D-arginine + H2O = D-ornithine + urea |
RULE(radius=1) | [*:1]-[C;H0;+0:2](=[NH;+0:3])-[NH;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](-[NH2;+0:3])=[O;H0;+0:6].[*:5]-[NH2;+0:4] |
Reaction | ![]() |
Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
Title | Authors | Date | PubMed ID |
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D-arginase of Arthrobacter sp. KUJ 8602: characterization and its identity with Zn(2+)-guanidinobutyrase. | Arakawa N, Igarashi M, Kazuoka T, Oikawa T, Soda K | 2003 Jan | 12761196 |