| ENGASE | |||||||||||||||||||||||||||||||||||||||||||||||||||
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| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ENGASE, endo-beta-N-acetylglucosaminidase | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | OMIM: 611898 MGI: 2443788 HomoloGene: 13666 GeneCards: ENGASE | ||||||||||||||||||||||||||||||||||||||||||||||||||
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| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
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Endo-beta-N-acetylglucosaminidase is a protein that in humans is encoded by the ENGASE gene. [5]
Function
This gene encodes a cytosolic enzyme which catalyzes the hydrolysis of peptides and proteins with mannose modifications to produce free oligosaccharides. [provided by RefSeq, Feb 2012].
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000167280 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000033857 - Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Entrez Gene: Endo-beta-N-acetylglucosaminidase". Retrieved 2018-08-24.
Further reading
- Suzuki T, Yano K, Sugimoto S, Kitajima K, Lennarz WJ, Inoue S, Inoue Y, Emori Y (July 2002). "Endo-beta-N-acetylglucosaminidase, an enzyme involved in processing of free oligosaccharides in the cytosol". Proc. Natl. Acad. Sci. U.S.A. 99 (15): 9691–6. Bibcode:2002PNAS...99.9691S. doi:10.1073/pnas.152333599. PMC 124980. PMID 12114544.
- Ortutay Z, Polgár A, Gömör B, Géher P, Lakatos T, Glant TT, Gay RE, Gay S, Pállinger E, Farkas C, Farkas E, Tóthfalusi L, Kocsis K, Falus A, Buzás EI (August 2003). "Synovial fluid exoglycosidases are predictors of rheumatoid arthritis and are effective in cartilage glycosaminoglycan depletion". Arthritis Rheum. 48 (8): 2163–72. doi:10.1002/art.11093. PMID 12905469.
- Butkinaree C, Cheung WD, Park S, Park K, Barber M, Hart GW (August 2008). "Characterization of beta-N-acetylglucosaminidase cleavage by caspase-3 during apoptosis". J. Biol. Chem. 283 (35): 23557–66. doi:10.1074/jbc.M804116200. PMC 2527095. PMID 18586680.
- Dorfmueller HC, van Aalten DM (February 2010). "Screening-based discovery of drug-like O-GlcNAcase inhibitor scaffolds". FEBS Lett. 584 (4): 694–700. doi:10.1016/j.febslet.2009.12.020. PMC 2828546. PMID 20026047.
- Park K, Saudek CD, Hart GW (July 2010). "Increased expression of beta-N-acetylglucosaminidase in erythrocytes from individuals with pre-diabetes and diabetes". Diabetes. 59 (7): 1845–50. doi:10.2337/db09-1086. PMC 2889787. PMID 20413512.
- Chantret I, Fasseu M, Zaoui K, Le Bizec C, Sadou Yayé H, Dupré T, Moore SE (July 2010). "Identification of roles for peptide: N-glycanase and endo-beta-N-acetylglucosaminidase (Engase1p) during protein N-glycosylation in human HepG2 cells". PLOS ONE. 5 (7): e11734. Bibcode:2010PLoSO...511734C. doi:10.1371/journal.pone.0011734. PMC 2909182. PMID 20668520.
- Xiao F, Zheng X, Cui M, Shi G, Chen X, Li R, Song Z, Rudolph KL, Chen B, Ju Z (October 2011). "Telomere dysfunction-related serological markers are associated with type 2 diabetes". Diabetes Care. 34 (10): 2273–8. doi:10.2337/dc10-2431. PMC 3177723. PMID 21873561.
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