Aspartate carbamoyltransferase
From Proteopedia
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. 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 highlightsATC is composed of 2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R). Click to see two catalytic trimers and three regulatory dimers. 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. [1] 3D structures of aspartate carbamoyltransferaseAspartate carbamoyltransferase 3D structures
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References
- ↑ Jin L, Stec B, Lipscomb WN, Kantrowitz ER. Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 A. Proteins. 1999 Dec 1;37(4):729-42. PMID:10651286
