3.5.1.60: N-(long-chain-acyl)ethanolamine deacylase
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For detailed information about N-(long-chain-acyl)ethanolamine deacylase, go to the full flat file.
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Synonyms
acylethanolamine acid amidase, amidase, acylethanolamine, hNAAA, N-acylethanolamine acid amidase, N-acylethanolamine amidohydrolase, N-acylethanolamine-hydrolyzing acid amidase, N-acylethanolaminehydrolyzing acid amidase, NAAA, Nacylethanolamine acid amidase, NAE-hydrolyzing acid amidase
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Posttranslational Modification
Posttranslational Modification on EC 3.5.1.60 - N-(long-chain-acyl)ethanolamine deacylase
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glycoprotein
proteolytic modification
glycoprotein
4 glycosylation sites Asn37, Asn107, Asn309, and Asn333, N-linked oligosaccharides of approximately 1500 Da, all cleavable by peptide-N-glycosidase F
self-proteolysis exposes the NAAA active site
proteolytic modification
the glycoprotein undergoes removal of an N-terminal signal peptide after biosynthesis. Autocatalytic acid cleavage of the zymogen into alpha- and beta-subunits (14.6 and 33.3 kDa) activates the enzyme. Cys126 is essential for the proteolytic cleavage of the pro-enzyme
proteolytic modification
self-proteolysis exposes the NAAA active site