Isolation and characterization of the orotidine 5‘-monophosphate decarboxylase domain of the multifunctional protein uridine 5‘-monophosphate synthase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference36 articles.
1. Isolation and initial characterization of the single polypeptide that ssynthesizes uridine 5'-monophosphate from orotate in Ehrlich ascites carcinoma. Purification by tandem affinity chromatography of uridine-5'-monophosphate synthase
2. Interconversion of different molecular weight forms of the orotate phosphoribosyltransferase.orotidine-5'-phosphate decarboxylase enzyme complex from mouse Ehrlich ascites cells.
3. Dependence of the aggregation and conformation states of uridine 5'-phosphate synthase on pyrimidine nucleotides. Evidence for a regulatory site
4. Multifunctional Proteins;Schmincke-Ott,1980
5. Multifunctional Proteins
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2. Co-expression of human malaria parasite Plasmodium falciparum orotate phosphoribosyltransferase and orotidine 5’-monophosphate decarboxylase as enzyme complex in Escherichia coli: a novel strategy for drug development;Asian Biomedicine;2010-04-01
3. Structure and Inhibition of Orotidine 5′-Monophosphate Decarboxylase from Plasmodium falciparum;Biochemistry;2008-02-28
4. A Novel Enzyme Complex of Orotate Phosphoribosyltransferase and Orotidine 5‘-Monophosphate Decarboxylase in Human Malaria Parasite Plasmodium falciparum: Physical Association, Kinetics, and Inhibition Characterization,;Biochemistry;2005-01-14
5. Orotate phosphoribosyltransferase and orotidine 5′-monophosphate decarboxylase exist as multienzyme complex in human malaria parasite Plasmodium falciparum;Biochemical and Biophysical Research Communications;2004-06
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