CAD protein: Difference between revisions

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<StructureSection load='6hg3' size='340' side='right' caption='Human CAD protein dihydroorotatase subunit containing modified Lys complex with dihydroorotate, formate and Zn+2 ions (PDB ID [[6hg3]])' scene=''>
<StructureSection load='6hg3' size='340' side='right' caption='Human CAD protein dihydroorotatase subunit containing modified Lys complex with dihydroorotate, formate and Zn+2 ions (PDB ID [[6hg3]])' scene='91/917453/Cv/1'>


== Function ==
== Function ==


'''CAD protein''' is a trifunctional enzyme which contains dihydroorotase domain (DHO), aspartate transcarbamoylase domain (ATC) and carbamoylphosphate synthetase domain<ref>PMID:28552578</ref>. The CAD protein catalyzes the first 3 of 6 reactions required for pyrimidine biosynthesis.
'''CAD protein''' is a trifunctional enzyme which contains dihydroorotase domain (DHO), aspartate transcarbamoylase domain (ATC) and carbamoylphosphate synthetase domain<ref>PMID:28552578</ref>. The CAD protein catalyzes the first 3 of 6 reactions required for pyrimidine biosynthesis.


== Disease ==
== Disease ==
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== Structural highlights ==
== Structural highlights ==


The 3D structure of CAD protein dihydroorotase subunit complex with dihydroorotate shows the active site containing 2 Zn+2 ions and a flexible loop containing conserved Thr and Phe in a loop-out conformation<ref>PMID:30315107</ref>.
The 3D structure of CAD protein dihydroorotase subunit complex with dihydroorotate shows the <scene name='91/917453/Cv/4'>active site</scene> containing <scene name='91/917453/Cv/5'>2 Zn+2 ions</scene> and a flexible loop containing conserved Thr and Phe in a loop-out conformation<ref>PMID:30315107</ref>. Water molecules are shown as red spheres.


==3D structures of CAD protein==
==3D structures of CAD protein==

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Michal Harel, Alexander Berchansky