Beta-ureidopropionase
Definition:
EC Tree > 3 Hydrolases > 3.5 Acting on carbon-nitrogen bonds, other than peptide bonds > 3.5.1 In linear amides > 3.5.1.6 beta-ureidopropionase
N-(long-chain-acyl)ethanolamine deacylase is a lysosomal acid hydrolase found in viruses and cellular organisms. It acts best on palmitoyl ethanolamide, poorly on other N-(long-chain-acyl)ethanolamines, and only at acidic pH; unlike fatty acid amide hydrolase (EC 3.5.1.99) it does not act on primary amides such as oleamide and has marginal activity on anandamide. It is translated as an inactive proenzyme that autocatalytically cleaves into two subunits reassembling into an active heterodimer. It hydrolyzes N-(long-chain-acyl)ethanolamine into a long-chain carboxylate and ethanolamine. In lysosomes it degrades N-acyl ethanolamines. It features a proenzyme-activated deacylase fold.
N-(long-chain-acyl)ethanolamine deacylase is a lysosomal acid hydrolase found in viruses and cellular organisms. It acts best on palmitoyl ethanolamide, poorly on other N-(long-chain-acyl)ethanolamines, and only at acidic pH; unlike fatty acid amide hydrolase (EC 3.5.1.99) it does not act on primary amides such as oleamide and has marginal activity on anandamide. It is translated as an inactive proenzyme that autocatalytically cleaves into two subunits reassembling into an active heterodimer. It hydrolyzes N-(long-chain-acyl)ethanolamine into a long-chain carboxylate and ethanolamine. In lysosomes it degrades N-acyl ethanolamines. It features a proenzyme-activated deacylase fold.
References:
Biomedical Dictionary
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