Reactome | CAD hexamer transforms CAP to N-carb-L-Asp

CAD hexamer transforms CAP to N-carb-L-Asp

Stable Identifier

R-HSA-73573

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

carbamoyl phosphate + L-aspartate <=> N-carbamoyl L-aspartate + orthophosphate, carbamoyl phosphate and L-aspartate combine to form N-Carbamoyl-L-aspartate

ReviewStatus

5/5

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CAD hexamer transforms CAP to N-carb-L-Asp

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The synthesis of N-carbamoyl L-aspartate from carbamoyl phosphate and L-aspartate is catalyzed by the aspartate carbamoyltansferase activity of cytosolic trifunctional CAD (carbamoyl-phosphate synthetase 2, aspartate transcarbamylase, and dihydroorotase) protein (Ito and Uchino 1973; Iwahana et al. 1996). The purified human protein is active in several different oligomerization states as is its Syrian hamster homologue. The most abundant form of the latter is a hexamer, and the active human protein is annotated as a hexamer by inference (Ito and Uchino 1973; Lee et al. 1985).

Literature References

PubMed ID	Title	Journal	Year
4684686	Control of pyrimidine biosynthesis in human lymphocytes. Simultaneous increase in activities of glutamine-utilizing carbamyl phosphate synthetase and aspartate transcarbamylase in phytohemagglutinin-stimulated human peripheral lymphocytes and their enzyme co-purification Ito, K, Uchino, H	J Biol Chem	1973
2995985	Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells Lee, L, Kelly, RE, Pastra-Landis, SC, Evans, DR	Proc Natl Acad Sci USA	1985
8619816	Molecular cloning of a human cDNA encoding a trifunctional enzyme of carbamoyl-phosphate synthetase-aspartate transcarbamoylase-dihydroorotase in de Novo pyrimidine synthesis Iwahana, H, Fujimura, H, Ii, S, Kondo, M, Moritani, M, Takahashi, Y, Yamaoka, T, Yoshimoto, K, Itakura, M	Biochem Biophys Res Commun	1996