Reactome | CAIR + Aspartate + ATP => SAICAR + ADP + Pi

CAIR + Aspartate + ATP => SAICAR + ADP + Pi

Stable Identifier

R-HSA-73805

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR) + L-aspartate + ATP => 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR) + ADP + orthophosphate

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

CAIR + Aspartate + ATP => SAICAR + ADP + Pi

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

The conversion of 5'-phosphoribosyl-5-aminoimidazole-4-carboxylate (CAIR) and aspartate to 5'-phosphoribosyl-5-aminoimidazole-4-N-succinocarboxamide (SAICAR), accompanied by the conversion of ATP to ADP and orthophosphate, is catalyzed by the phosphoribosylaminoimidazole succinocarboxamide synthetase domain of the bifunctional protein "phosphoribosylaminoimidazole carboxylase, phosphoribosylaminoimidazole succinocarboxamide synthetase" (PAICS) (Schild et al. 1990). The enzyme is an octamer (Li et al. 2007); it may associate in the cytosol with other enzymes of de novo IMP biosynthesis under some metabolic conditions (An et al. 2008).

Literature References

PubMed ID	Title	Journal	Year
18388293	Reversible compartmentalization of de novo purine biosynthetic complexes in living cells Benkovic, SJ, Sheets, ED, Kumar, R, An, S	Science	2008
2183217	Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations Brake, AJ, Kiefer, MC, Schild, D, Young, D, Barr, PJ	Proc Natl Acad Sci USA	1990
17224163	Octameric structure of the human bifunctional enzyme PAICS in purine biosynthesis Xie, XC, Wang, QH, Tong, YP, Li, SX, Li, SG, Zhang, ZY, Bi, RC, Zhou, HN, Zhang, XC, Gao, W, Han, Y	J Mol Biol	2007