Contains zinc and is specific for barbiturate as substrate . Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved . May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.
Contains zinc and is specific for barbiturate as substrate [3]. Forms part of the oxidative pyrimidine-degrading pathway in some microorganisms, along with EC 1.17.99.4 (uracil/thymine dehydrogenase) and EC 3.5.1.95 (N-malonylurea hydrolase). It was previously thought that the end-products of the reaction were malonate and urea but this has since been disproved [2]. May be involved in the regulation of pyrimidine metabolism, along with EC 2.4.2.9, uracil phosphoribosyltransferase.
the enzyme belongs to a protein family that consists of only cyanuric acid hydrolase (CAH) and barbiturase. CAH and barbiturase enzymes act on structurally analogous 6-membered ring substrates, yet each enzyme is specific and does not react with the other's substrate. While most organisms utilize a reductive pyrimidine degradation pathway, some actinobacteria use barbiturase in an oxidative catabolic pathway. Unlike barbiturase, cyanuric acid hydrolases are more broadly distributed throughout bacteria and fungi. The CAH/barbiturase family includes 169 different sequences of Actinobacteria, phylogenetic analysis and tree, overview
barbiturase participating in pyrimidine catabolism by some actinobacterial species. Barbiturase catalyzes the second step in the oxidative pyrimidine degradation pathway
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Enzyme Nomenclature
3.5.2.1 barbiturase
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