Aspartate carbamoyltransferase

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 . Click to see and . The contains an and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. 3D structures of aspartate carbamoyltransferase Aspartate carbamoyltransferase 3D structures

spinqualitylabelsall models Structure of E. coli aspartate carbamoyltransferase catalytic (cyan and pink) and regulatory (green and yellow) subunits complex with inhibitor PALA and Zn+2 ions (grey) (PDB code 1d09). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image