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Dihydroorotase plays a key role in pyrimidine biosynthesis by catalyzing the reversible interconversion of carbamoyl aspartate to dihydroorotate. The enzyme belongs to the amidohydrolase superfamily of proteins, which includes phosphotriesterase and urease, among others. High-resolution x-ray crystallographic analyses have shown that each active site of the dimeric enzyme contains a binuclear zinc metal center bridged by a carboxylated lysine residue. The enzyme was crystallized in the presence of its substrate, carbamoyl aspartate. Strikingly, dihydroorotate is observed bound in the active site of one subunit while carbamoyl aspartate is positioned in the active site of the second subunit. From the three-dimensional structures of the enzymebound substrate and product, it has been possible to propose a unique catalytic mechanism for this enzyme.

Structural and functional analyses of dihydroorotase fromEscherichia coli