N-carbamoylsarcosine amidase
| N-carbamoylsarcosine amidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.5.1.59 | ||||||||
| CAS number | 92767-52-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / EGO | ||||||||
| |||||||||
In enzymology, a N-carbamoylsarcosine amidase (EC 3.5.1.59) is an enzyme that catalyzes the chemical reaction
- N-carbamoylsarcosine + H2O sarcosine + CO2 + NH3
Thus, the two substrates of this enzyme are N-carbamoylsarcosine and H2O, whereas its 3 products are sarcosine, CO2, and NH3.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is N-carbamoylsarcosine amidohydrolase. This enzyme is also called carbamoylsarcosine amidase. This enzyme participates in arginine and proline metabolism.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1NBA.
References
- Deeg R, Roeder A, Siedel J, Gauhl H, Ziegenhorn J (1984). "Process and reagent for the determination of N-carbamoylsarcosine with the use of a new enzyme". Chem. Abstr. 101: 18751.
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