Aspartate carbamoyltransferase: Difference between revisions

'''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.  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)]].