N-malonylurea hydrolase () is an enzyme characterised from the bacterium, Rhodococcus erythropolis that catalyzes the hydrolysis of 3-oxo-3-ureidopropanoic acid to malonic acid and urea:
The reaction is part of a pathway for catabolism of the pyrimidines uracil and thymine. Earlier steps involve the enzymes uracil/thymine dehydrogenase and barbiturase.
This enzyme is a hydrolase, one acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is 3-oxo-3-ureidopropanoate amidohydrolase (urea- and malonate-forming). This enzyme is also called ureidomalonase.
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