Aspartate carbamoyltransferase

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Function

Aspartate carbamoyltransferase (ATC) is part of the pyrimidine biosynthesis pathway. ATC catalyzes the condensation of aspartate and carbamoyl phosphate to N-carbamyl-L-aspartate and phosphate. The Zn atom is essential for the association of the subunits. Binding of the substrate to the catalytic subunits results in a high-affinity state while binding of CTP to the regulatory subunit results in a low-affinity state. Malate and phosphonoacetyl-L-aspartate (PALA) are inhibitors of ATC. For additional details see Aspartate Transcarbamoylase (ATCase).

Structural highlights

ATC is composed of . The catalytic subunit contains an aspartate-binding domain and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain.


Structure of E. coli aspartate carbamoyltransferase catalytic (grey and pink) and regulatory (green and yellow) subunits complex with inhibitor PALA and Zn+2 ions (grey) (PDB code 1d09).

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3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase

Updated on 10-November-2015

ReferencesReferences

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