CATH Classification

Domain Context

CATH Clusters

Superfamily Aspartate/ornithine carbamoyltransferase
Functional Family Aspartate carbamoyltransferase catalytic subunit

Enzyme Information
Aspartate carbamoyltransferase.
based on mapping to UniProt P27708
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate.
based on mapping to UniProt P27708
(S)-dihydroorotate + H(2)O = N-carbamoyl-L-aspartate.
Carbamoyl-phosphate synthase (glutamine-hydrolyzing).
based on mapping to UniProt P27708
2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
-!- The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides. -!- The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length. -!- The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate. -!- The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate. -!- The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit. -!- The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate. -!- Cf. EC -!- Formerly EC

UniProtKB Entries (1)

Homo sapiens
CAD protein

PDB Structure

External Links
Primary Citation
Structure and Functional Characterization of Human Aspartate Transcarbamoylase, the Target of the Anti-Tumoral Drug Pala.
Ruiz-Ramos, A., Velazquez-Campoy, A., Grande-Garcia, A., Moreno-Morcillo, M., Ramon-Maiques, S.