| 词条 | Peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase |
| 释义 |
| Name = peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase | EC_number = 3.5.1.52 | CAS_number = 83534-39-8 | IUBMB_EC_number = 3/5/1/52 | GO_code = 0000224 | image = Protein_NGLY1_PDB_2ccq.png | width = | caption = Rendering based on {{PDB|2ccq}} }} In enzymology, a peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase ({{EC number|3.5.1.52}}) is an enzyme that catalyzes a chemical reaction that cleaves a N4-(acetyl-beta-D-glucosaminyl)asparagine residue in which the glucosamine residue may be further glycosylated, to yield a (substituted) N-acetyl-beta-D-glucosaminylamine and a peptide containing an aspartate residue. This enzyme belongs to the family of hydrolases, specifically those acting on carbon-nitrogen bonds other than peptide bonds in linear amides. The NGLY1 gene encodes the ortholog of this enzyme in humans. NomenclatureThe systematic name of this enzyme class is N-linked-glycopeptide-(N-acetyl-beta-D-glucosaminyl)-L-asparagine amidohydrolase. Other names in common use include:
Structural studiesThe enzyme uses a catalytic triad of cysteine-histidine-aspartate in its active site for hydrolysis by covalent catalysis.[2] A peptide with similar functionality was discovered in 2014 by group at Fudan University in Shanghai, China. This peptide also cleaves alpha 1,3 linkages, and has been named PNGase F-II.[3] References1. ^{{cite journal | vauthors = Altmann F, Paschinger K, Dalik T, Vorauer K | title = Characterisation of peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase A and its N-glycans | journal = European Journal of Biochemistry / FEBS | volume = 252 | issue = 1 | pages = 118–23 | date = Feb 1998 | pmid = 9523720 | doi = 10.1046/j.1432-1327.1998.2520118.x }} 2. ^{{cite journal | vauthors = Allen MD, Buchberger A, Bycroft M | title = The PUB domain functions as a p97 binding module in human peptide N-glycanase | journal = The Journal of Biological Chemistry | volume = 281 | issue = 35 | pages = 25502–8 | date = Sep 2006 | pmid = 16807242 | doi = 10.1074/jbc.M601173200 | url = http://www.jbc.org/content/281/35/25502}} 3. ^{{cite journal | vauthors = Sun G, Yu X, Bao C, Wang L, Li M, Gan J, Qu D, Ma J, Chen L | title = Identification and characterization of a novel prokaryotic peptide: N-glycosidase from Elizabethkingia meningoseptica | journal = The Journal of Biological Chemistry | volume = 290 | issue = 12 | pages = 7452–62 | date = Mar 2015 | pmid = 25614628 | doi = 10.1074/jbc.M114.605493 | url = http://www.jbc.org/content/290/12/7452 | pmc=4367255}} Further reading{{refbegin|33em}}
2 : EC 3.5.1|Enzymes of known structure |
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