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Carbamoyl phosphate synthase II
Enzyme From Wikipedia, the free encyclopedia
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Carbamoyl phosphate synthetase (glutamine-hydrolysing) (EC 6.3.5.5) is an enzyme that catalyzes the reactions that produce carbamoyl phosphate in the cytosol (as opposed to type I, which functions in the mitochondria). Its systemic name is hydrogen-carbonate:L-glutamine amido-ligase (ADP-forming, carbamate-phosphorylating).[1][2][3][4][5][6][7][8]
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In pyrimidine biosynthesis, it serves as the rate-limiting enzyme and catalyzes the following reaction:
- 2 ATP + L-glutamine + HCO3− + H2O 2 ADP + phosphate + L-glutamate + carbamoyl phosphate (overall reaction)
- (1a) L-glutamine + H2O L-glutamate + NH3
- (1b) 2 ATP + HCO3− + NH3 2 ADP + phosphate + carbamoyl phosphate
It is activated by ATP and PRPP[9] and it is inhibited by UTP (Uridine triphosphate)[10] Neither CPSI nor CPSII require biotin as a coenzyme, as seen with most carboxylation reactions.
It is one of the four functional enzymatic domains coded by the CAD gene.[11] The CAD gene is a large gene. It uses a single strand to code for these enzyme jobs. It is classified under EC 6.3.5.5.
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