Literature summary for 1.3.1.2 extracted from

Forouzesh, D.C.; Beaupre, B.A.; Butrin, A.; Wawrzak, Z.; Liu, D.; Moran, G.R.
The interaction of porcine dihydropyrimidine dehydrogenase with the chemotherapy sensitizer 5-ethynyluracil (2021), Biochemistry, 60, 1120-1132 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Sus scrofa

Inhibitors

Inhibitors	Comment	Organism	Structure
5-Ethynyluracil	covalently inactivates DPD by cross-linking with the active-site general acid cysteine in the pyrimidine binding site. This reaction is dependent on the simultaneous binding of 5-ethynyluracil and NADPH. The ternary complex induces DPD to become activated by taking up two electrons from the NADPH. The covalent inactivation of DPD by 5-ethynyluracil occurs concomitantly with this reductive activation with a rate constant of about 0.2 per s. This kinact value is correlated with the rate of reduction of one of the two flavin cofactors and the localization of a mobile loop in the pyrimidine active site	Sus scrofa

Organism

Organism	UniProt	Comment	Textmining
Sus scrofa	Q28943	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
5-fluorouracil + NADPH + H+	-	Sus scrofa	5-fluoro-5,6-dihydrouracil + NADP+	-	?

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Release 2023.1 (January 2023)