Aspartate carbamoyltransferase: Difference between revisions
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ATC is composed of <scene name='59/592660/Cv/10'>2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R)</scene>. Click to see <scene name='59/592660/Cv/11'>two catalytic trimers</scene> and <scene name='59/592660/Cv/12'>three regulatory dimers</scene>. The <scene name='59/592660/Cv/13'>catalytic subunit</scene> contains an <scene name='59/592660/Cv/14'>aspartate-binding domain</scene> and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. <ref>PMID:10651286</ref> | ATC is composed of <scene name='59/592660/Cv/10'>2 trimers of catalytic subunits (C) and 3 dimers of regulatory subunits (R)</scene>. Click to see <scene name='59/592660/Cv/11'>two catalytic trimers</scene> and <scene name='59/592660/Cv/12'>three regulatory dimers</scene>. The <scene name='59/592660/Cv/13'>catalytic subunit</scene> contains an <scene name='59/592660/Cv/14'>aspartate-binding domain</scene> and a carbamoyl-phosphate-binding domain. The regulatory subunit contains a nucleotide effectors-binding domain and a zinc domain. <ref>PMID:10651286</ref> | ||
==3D structures of aspartate carbamoyltransferase== | |||
[[Aspartate carbamoyltransferase 3D structures]] | |||
</StructureSection> | </StructureSection> | ||
Revision as of 14:14, 21 March 2019
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 . 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. [1] 3D structures of aspartate carbamoyltransferaseAspartate carbamoyltransferase 3D structures
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3D structures of aspartate carbamoyltransferase3D structures of aspartate carbamoyltransferase
Updated on 21-March-2019
ReferencesReferences
- ↑ 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