The enzyme carbamoyl-serine ammonia-lyase (EC 4.3.1.13)
catalyzes
Catalysis () is the process of increasing the rate of a chemical reaction by adding a substance known as a catalyst (). Catalysts are not consumed in the reaction and remain unchanged after it. If the reaction is rapid and the catalyst recyc ...
the
chemical reaction
:''O''-carbamoyl-
L-serine + H
2O = pyruvate + 2 NH
3 + CO
2 (overall reaction)
::(1a) ''O''-carbamoyl-
L-serine = CO
2 + NH
3 + 2-aminoprop-2-enoate
::(1b) 2-aminoprop-2-enoate = 2-iminopropanoate (spontaneous)
::(1c) 2-iminopropanoate + H
2O = pyruvate + NH
3 (spontaneous)
This enzyme belongs to the family of
lyase
In biochemistry, a lyase is an enzyme that catalyzes the breaking (an elimination reaction) of various chemical bonds by means other than hydrolysis (a substitution reaction) and oxidation, often forming a new double bond or a new ring structure. ...
s, 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.
References
*
EC 4.3.1
Pyridoxal phosphate enzymes
Enzymes of unknown structure
{{lyase-stub