Aspartate carbamoyltransferase

Revision as of 11:57, 18 November 2014 by Michal Harel (talk | contribs)

<StructureSection load='1raa' size='340' side='right' caption='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).' scene=>

FunctionFunction

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.

DiseaseDisease

RelevanceRelevance

Structural highlightsStructural highlights

3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase

Updated on 18-November-2014

ReferencesReferences

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman