Aspartate carbamoyltransferase
FunctionAspartate 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. ATC is composed of 2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R). 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. 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 are inhibitors of ATC. For additional details see Aspartate Transcarbamoylase (ATCase). DiseaseRelevanceStructural highlights |
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3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase
Updated on 22-December-2014