N-malonylurea hydrolase

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N-malonylurea hydrolase
Identifiers
EC no. 3.5.1.95
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In enzymology, a N-malonylurea hydrolase (EC 3.5.1.95) is an enzyme that catalyzes the chemical reaction

3-oxo-3-ureidopropanoate + H2O malonate + urea

Thus, the two substrates of this enzyme are 3-oxo-3-ureidopropanoate and H2O, whereas its two products are malonate and urea.

This enzyme belongs to the family of hydrolases, those 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.

Related Research Articles

Barbiturase is a zinc-containing amidohydrolase. Its systemic name is barbiturate amidohydrolase (3-oxo-3-ureidopropanoate-forming). Barbiturase acts as a catalyst in the second step of oxidative pyrimidine degradation, promoting the ring-opening hydrolysis of barbituric acid to ureidomalonic acid. Although grouped into the naturally existing amidohydrolases, it demonstrates more homology with cyanuric acid amidohydrolase. Therefore, it has been proposed that barbiturase, along with cyanuric acid, should be grouped into a new family. KEGG

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<span class="mw-page-title-main">Amidase</span>

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<span class="mw-page-title-main">Dihydropyrimidinase</span>

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<span class="mw-page-title-main">Imidazolonepropionase</span>

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References


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