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The Allosteric Regulation of Β-Ureidopropionase Depends on Fine-Tuned Stability of Active-Site Loops and Subunit Interfaces.
Biomolecules
December 2023
Department of Chemistry-BMC, Uppsala University, 751 23 Uppsala, Sweden.
The activity of β-ureidopropionase, which catalyses the last step in the degradation of uracil, thymine, and analogous antimetabolites, is cooperatively regulated by the substrate and product of the reaction. This involves shifts in the equilibrium of the oligomeric states of the enzyme, but how these are achieved and result in changes in enzyme catalytic competence has yet to be determined. Here, the regulation of human β-ureidopropionase was further explored via site-directed mutagenesis, inhibition studies, and cryo-electron microscopy.
View Article and Find Full Text PDFCrystal structure and pH-dependent allosteric regulation of human β-ureidopropionase, an enzyme involved in anticancer drug metabolism.
Biochem J
July 2018
Department of Chemistry - BMC, Uppsala University, Box 576, SE-75123 Uppsala, Sweden
β-Ureidopropionase (βUP) catalyzes the third step of the reductive pyrimidine catabolic pathway responsible for breakdown of uracil-, thymine- and pyrimidine-based antimetabolites such as 5-fluorouracil. Nitrilase-like βUPs use a tetrad of conserved residues (Cys233, Lys196, Glu119 and Glu207) for catalysis and occur in a variety of oligomeric states. Positive co-operativity toward the substrate -carbamoyl-β-alanine and an oligomerization-dependent mechanism of substrate activation and product inhibition have been reported for the enzymes from some species but not others.
View Article and Find Full Text PDFA recruited protease is involved in catabolism of pyrimidines.
J Mol Biol
May 2008
Department of Cell and Organism Biology, Lund University, SE-22362 Lund, Sweden.
In nature, the same biochemical reaction can be catalyzed by enzymes having fundamentally different folds, reaction mechanisms and origins. For example, the third step of the reductive catabolism of pyrimidines, the conversion of N-carbamyl-beta-alanine to beta-alanine, is catalyzed by two beta-alanine synthase (beta ASase, EC 3.5.
View Article and Find Full Text PDFExpression and properties of human liver beta-ureidopropionase.
J Nutr Sci Vitaminol (Tokyo)
April 2001
Faculty of Nutrition and High Technology Research Center, Kobe Gakuin University, Japan.
A cDNA encoding beta-ureidopropionase (BUP) was isolated from a human liver cDNA library, expressed in E. coli, and purified from the culture extract. The 2,006 bp cDNA contained a 1,152 bp open reading frame encoding a protein of 384 amino acids with a molecular weight of 43,165 Da.
View Article and Find Full Text PDFCharacterization of plant beta-ureidopropionase and functional overexpression in Escherichia coli.
Plant Physiol
February 2001
Dow AgroSciences, Discovery Research, 9330 Zionsville Road, Indianapolis, Indiana 46268, USA.
Pyrimidine bases are rapidly catabolized in growing plant tissues. The final enzyme of the catabolic pathway, beta-ureidopropionase (beta-UP; EC 3.5.
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