{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Serre V"],"funding":["NIGMS NIH HHS"],"pagination":["6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC434488"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5"],"pubmed_abstract":["<h4>Background</h4>The S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein catalyses the first two reactions of the pyrimidine pathway. In this organism, these two reactions are feedback inhibited by the end product UTP. In the present work, the mechanisms of these integrated inhibitions were studied.<h4>Results</h4>The results obtained show that the inhibition is competitive in the case of carbamylphosphate synthetase and non-competitive in the case of aspartate transcarbamylase. They also identify the substrate whose binding is altered by this nucleotide and the step of the carbamylphosphate synthetase reaction which is inhibited. Furthermore, the structure of the domains catalyzing these two reactions were modelled in order to localize the mut"],"journal":["BMC biochemistry"],"pubmed_title":["Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein."],"pmcid":["PMC434488"],"funding_grant_id":["R01 GM060371"],"pubmed_authors":["Serre V","Penverne B","Souciet JL","Guy H","Vicart P","Herve G","Evans D","Potier S"],"additional_accession":[]},"is_claimable":false,"name":"Integrated allosteric regulation in the S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein.","description":"<h4>Background</h4>The S. cerevisiae carbamylphosphate synthetase - aspartate transcarbamylase multifunctional protein catalyses the first two reactions of the pyrimidine pathway. In this organism, these two reactions are feedback inhibited by the end product UTP. In the present work, the mechanisms of these integrated inhibitions were studied.<h4>Results</h4>The results obtained show that the inhibition is competitive in the case of carbamylphosphate synthetase and non-competitive in the case of aspartate transcarbamylase. They also identify the substrate whose binding is altered by this nucleotide and the step of the carbamylphosphate synthetase reaction which is inhibited. Furthermore, the structure of the domains catalyzing these two reactions were modelled in order to localize the mut","dates":{"release":"2004-01-01T00:00:00Z","publication":"2004 May","modification":"2025-04-04T21:18:32.144Z","creation":"2019-03-27T00:50:33Z"},"accession":"S-EPMC434488","cross_references":{"pubmed":["15128434"],"doi":["10.1186/1471-2091-5-6"]}}