Structure, catalytic mechanism, posttranslational lysine carbamylation, and inhibition of dihydropyrimidinases.
Sign Up to like & getrecommendations! Published in 2020 at "Advances in protein chemistry and structural biology"
DOI: 10.1016/bs.apcsb.2020.05.002
Abstract: Dihydropyrimidinase catalyzes the reversible hydrolytic ring opening of dihydrouracil and dihydrothymine to N-carbamoyl-β-alanine and N-carbamyl-β-aminoisobutyrate, respectively. Dihydropyrimidinase from microorganisms is normally known as hydantoinase because of its role as a biocatalyst in the synthesis of… read more here.
Keywords: dihydropyrimidinase; mechanism; catalytic mechanism; inhibition ... See more keywords
Molecular Insights into How the Dimetal Center in Dihydropyrimidinase Can Bind the Thymine Antagonist 5-Aminouracil: A Different Binding Mode from the Anticancer Drug 5-Fluorouracil
Sign Up to like & getrecommendations! Published in 2022 at "Bioinorganic Chemistry and Applications"
DOI: 10.1155/2022/1817745
Abstract: Dihydropyrimidinase (DHPase) is a key enzyme for pyrimidine degradation. DHPase contains a binuclear metal center in which two Zn ions are bridged by a posttranslationally carbamylated lysine. DHPase catalyzes the hydrolysis of dihydrouracil to N-carbamoyl-β-alanine.… read more here.
Keywords: anticancer drug; dihydropyrimidinase; dhpase; molecular insights ... See more keywords