EC number:3.5.1.59
Enzyme
Download| EC Tree |
| 3. Hydrolases |
| 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds |
| 3.5.1 In linear amides |
| ID: | 3.5.1.59 |
|---|---|
| Description: | N-carbamoylsarcosine amidase. |
| Alternative Name: |
N-carbamoylsarcosine amidohydrolase. CSHase. |
| Cath: | 3.40.50.850; |
3D structure
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External Links
| UniProtKB Enzyme Link: | UniProtKB 3.5.1.59 |
| BRENDA Enzyme Link: | BRENDA 3.5.1.59 |
| KEGG Enzyme Link: | KEGG3.5.1.59 |
| BioCyc Enzyme Link: | BioCyc 3.5.1.59 |
| ExPASy Enzyme Link: | ExPASy3.5.1.59 |
| EC2PDB Enzyme Link: | EC2PDB 3.5.1.59 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.5.1.59 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.5.1.59 |
| IntEnz Enzyme Link: | IntEnz 3.5.1.59 |
| MEDLINE Enzyme Link: | MEDLINE 3.5.1.59 |
| RHEA:20057 | 2 H(+) + H2O + N-carbamoylsarcosine = CO2 + NH4(+) + sarcosine |
| RULE(radius=1) | [*:1]-[N;H0;+0:2](-[*:3])-[C;H0;+0:4](=[*:5])-[NH2;+0:6].[H+;H0:7].[H+;H0:8].[OH2;+0:9]>>[*:1]-[NH;+0:2]-[*:3].[*:5]=[C;H0;+0:4]=[O;H0;+0:9].[NH3;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Crystallographic and fluorescence studies of ligand binding to N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. | Zajc A, Romão MJ, Turk B, Huber R | 1996 Oct 25 | 8913306 |
| Crystal structure analysis, refinement and enzymatic reaction mechanism of N-carbamoylsarcosine amidohydrolase from Arthrobacter sp. at 2.0 A resolution. | Romão MJ, Turk D, Gomis-Rüth FX, Huber R, Schumacher G, Möllering H, Rüssmann L | 1992 Aug 20 | 1381445 |
| Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases. | Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T | 2000 Jul 15 | 10903946 |