Carbamoyl-serine ammonia-lyase
From Wikipedia, the free encyclopedia
In enzymology, a carbamoyl-serine ammonia-lyase (EC 4.3.1.13) is an enzyme that catalyzes the chemical reaction
- O-carbamoyl-L-serine + H2O
pyruvate + 2 NH3 + CO2
Thus, the two substrates of this enzyme are O-carbamoyl-L-serine and H2O, whereas its 3 products are pyruvate, NH3, and CO2.
This enzyme belongs to the family of lyases, specifically ammonia lyases, which cleave carbon-nitrogen bonds. The systematic name of this enzyme class is O-carbamoyl-L-serine ammonia-lyase (decarboxylating pyruvate-forming). Other names in common use include O-carbamoyl-L-serine deaminase, carbamoylserine deaminase, and O-carbamoyl-L-serine ammonia-lyase (pyruvate-forming). It employs one cofactor, pyridoxal phosphate.
[edit] References
- IUBMB entry for 4.3.1.13
- BRENDA references for 4.3.1.13 (Recommended.)
- PubMed references for 4.3.1.13
- PubMed Central references for 4.3.1.13
- Google Scholar references for 4.3.1.13
- Copper AJ, Meister A (1973). "Enzymatic conversion of O-carbamyl-L-serine to pyruvate and ammonia". Biochem. Biophys. Res. Commun. 55: 780–7. doi:. PMID 4761084.
[edit] External links
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- The CAS registry number for this enzyme class is 52227-64-2.

