IPR006274
Carbamoyl-phosphate synthase, small subunit
InterPro entry
Short name | CarbamoylP_synth_ssu |
Overlapping homologous superfamilies |
Description
Carbamoyl phosphate synthase (CPSase) is a heterodimeric enzyme composed of a small and a large subunit (with the exception of CPSase III, see below). CPSase catalyses the synthesis of carbamoyl phosphate from biocarbonate, ATP and glutamine or ammonia, and represents the first committed step in pyrimidine and arginine biosynthesis in prokaryotes and eukaryotes, and in the urea cycle in most terrestrial vertebrates
[2, 1]. This entry represents the small subunit of the glutamine-dependent form (
6.3.5.5) of carbamoyl phosphate synthase. The small subunit catalyses the hydrolysis of glutamine to ammonia, which in turn used by the large chain to synthesize carbamoyl phosphate. The C-terminal domain of the small subunit of CPSase has glutamine amidotransferase activity.
References
1.Carbamoyl phosphate synthetase: an amazing biochemical odyssey from substrate to product. Holden HM, Thoden JB, Raushel FM. Cell. Mol. Life Sci. 56, 507-22, (1999). View articlePMID: 11212301
2.The amidotransferase family of enzymes: molecular machines for the production and delivery of ammonia. Raushel FM, Thoden JB, Holden HM. Biochemistry 38, 7891-9, (1999). View articlePMID: 10387030
Further reading
3. Structure, functional characterization, and evolution of the dihydroorotase domain of human CAD. Grande-Garcia A, Lallous N, Diaz-Tejada C, Ramon-Maiques S. Structure 22, 185-98, (2014). View articlePMID: 24332717
GO terms
biological process
cellular component
- None
Cross References
Representative structure
1a9x: CARBAMOYL PHOSPHATE SYNTHETASE: CAUGHT IN THE ACT OF GLUTAMINE HYDROLYSIS