The Allosteric Regulation of Β-Ureidopropionase Depends on Fine-Tuned Stability of Active-Site Loops and Subunit Interfaces

The Allosteric Regulation of Β-Ureidopropionase Depends on Fine-Tuned Stability of Active-Site Loops and Subunit Interfaces

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 the...

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Bibliographic Details
Main Authors: Daniela Cederfelt, Dilip Badgujar, Ayan Au Musse, Bernhard Lohkamp, U. Helena Danielson, Doreen Dobritzsch
Format: Article
Language:English
Published: MDPI AG 2023-12-01
Series:Biomolecules
Subjects:
pyrimidine degradation
5-fluorouracil metabolism
amidohydrolase
allosteric regulation
cryo-electron microscopy
Online Access:https://www.mdpi.com/2218-273X/13/12/1763

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