Aspartate carbamoyltransferase

Revision as of 13:04, 22 December 2014 by Michal Harel (talk | contribs)


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. 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).

Disease

Relevance

Structural highlights

Structure of E. coli aspartate carbamoyltransferase catalytic (grey and pink) and regulatory (green and yellow) subunits complex with CTP (stick figure) and Zn+2 (grey) (PDB code 1raa).

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3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase

Updated on 22-December-2014

ReferencesReferences

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Michal Harel, Alexander Berchansky, Joel L. Sussman