CAD protein: Difference between revisions
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<StructureSection load='6hg3' size='340' side='right' caption='Human CAD protein dihydroorotatase subunit | <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>. | '''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 2 Zn+2 ions and a flexible loop containing conserved Thr and Phe in a loop-out conformation<ref>PMID:30315107</ref>. | ||
==3D structures of CAD protein== | ==3D structures of CAD protein== | ||
Revision as of 17:52, 14 July 2022
FunctionCAD protein is a trifunctional enzyme which contains dihydroorotase domain (DHO), aspartate transcarbamoylase domain (ATC) and carbamoylphosphate synthetase domain[1]. The CAD protein catalyzes the first 3 of 6 reactions required for pyrimidine biosynthesis. DiseaseDeficiency in carbamoylphosphate synthetase leads to lack of urea and hyperammonemia[2] RelevanceStructural highlightsThe 3D structure of CAD protein dihydroorotase subunit complex with dihydroorotate shows the containing 2 Zn+2 ions and a flexible loop containing conserved Thr and Phe in a loop-out conformation[3]. 3D structures of CAD protein |
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ReferencesReferences
- ↑ Moreno-Morcillo M, Grande-Garcia A, Ruiz-Ramos A, Del Cano-Ochoa F, Boskovic J, Ramon-Maiques S. Structural Insight into the Core of CAD, the Multifunctional Protein Leading De Novo Pyrimidine Biosynthesis. Structure. 2017 Jun 6;25(6):912-923.e5. doi: 10.1016/j.str.2017.04.012. Epub 2017, May 25. PMID:28552578 doi:http://dx.doi.org/10.1016/j.str.2017.04.012
- ↑ Ng BG, Wolfe LA, Ichikawa M, Markello T, He M, Tifft CJ, Gahl WA, Freeze HH. Biallelic mutations in CAD, impair de novo pyrimidine biosynthesis and decrease glycosylation precursors. Hum Mol Genet. 2015 Jun 1;24(11):3050-7. doi: 10.1093/hmg/ddv057. Epub 2015 Feb, 12. PMID:25678555 doi:http://dx.doi.org/10.1093/hmg/ddv057
- ↑ Del Cano-Ochoa F, Grande-Garcia A, Reverte-Lopez M, D'Abramo M, Ramon-Maiques S. Characterization of the catalytic flexible loop in the dihydroorotase domain of the human multi-enzymatic protein CAD. J Biol Chem. 2018 Oct 12. pii: RA118.005494. doi: 10.1074/jbc.RA118.005494. PMID:30315107 doi:http://dx.doi.org/10.1074/jbc.RA118.005494