Upregulation of CAD, the multifunctional protein that initiates and controls the de novo
biosynthesis of pyrimidines in animals, is essential for cell proliferation. Deciphering the …

Dihydroorotase (DHOase) is the third enzyme in the pathway used for the biosynthesis of
pyrimidine nucleotides. In mammals, DHOase is active in a trifunctional enzyme, CAD, which …

Cyclic amidohydrolases belong to a superfamily of enzymes that catalyze the hydrolysis of
cyclic C N bonds. They are commonly found in nucleotide metabolism of purine and …

The de novo pyrimidine biosynthesis pathway is essential for the proliferation of many
pathogens. One of the pathway enzymes, dihydroorotase (DHO), catalyzes the reversible …

Bacterial allantoinase (ALLase) and dihydroorotase (DHOase) are members of the cyclic
amidohydrolase family. ALLase and DHOase possess similar binuclear metal centers in the …

Dihydroorotase (DHOase) catalyzes the reversible cyclization of N-carbamyl-l-aspartate (CA-
asp) to l-dihydroorotate (DHO) in the de novo biosynthesis of pyrimidine nucleotides …

Dihydroorotase (DHOase), a dimetalloenzyme containing a carbamylated lysine within the
active site, is a member of the cyclic amidohydrolase family, which also includes …

In prokaryotes, the first three enzymes in pyrimidine biosynthesis, carbamoyl phosphate
synthetase (CPS), aspartate transcarbamoylase (ATC), and dihydroorotase (DHO), are …

The recombinant dihydropyrimidinase from Sinorhizobium meliloti CECT4114 (SmelDhp)
has been characterised and its crystal structure elucidated at 1.85 Å. The global architecture …

Abstract Bacterial allantoinase (ALLase; EC 3.5. 2.5), which catalyzes the conversion of
allantoin into allantoate, possesses a binuclear metal center in which two metal ions are …