EC number:3.5.3.3
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.3 In linear amidines |
| ID: | 3.5.3.3 |
|---|---|
| Description: | Creatinase. |
| Alternative Name: |
Creatine amidinohydrolase. |
| Cath: | 3.90.230.10; 3.40.350.10; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.3.3 |
| BRENDA Enzyme Link: | BRENDA 3.5.3.3 |
| KEGG Enzyme Link: | KEGG3.5.3.3 |
| BioCyc Enzyme Link: | BioCyc 3.5.3.3 |
| ExPASy Enzyme Link: | ExPASy3.5.3.3 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.3.3 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.3.3 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.3.3 |
| IntEnz Enzyme Link: | IntEnz 3.5.3.3 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.3.3 |
| RHEA:22456 | creatine + H2O = sarcosine + urea |
| RULE(radius=1) | [*:1]-[N;H0;+0:2](-[*:3])-[C;H0;+0:4](-[*:5])=[NH;+0:6].[OH2;+0:7]>>[*:5]-[C;H0;+0:4](-[NH2;+0:6])=[O;H0;+0:7].[*:1]-[NH;+0:2]-[*:3] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Enzymatic mechanism of creatine amidinohydrolase as deduced from crystal structures. | Coll M, Knof SH, Ohga Y, Messerschmidt A, Huber R, Moellering H, Rüssmann L, Schumacher G | 1990 Jul 20 | 1696320 |