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Hydrolysis of terminal, non-reducing β-D-mannose residues in β-D-mannosides
This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with β-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement.[5]
^Adams, M.; Richtmyer, N.K. & Hudson, C.S. (1943). "Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases". J. Am. Chem. Soc. 65 (7): 1369–1380. doi:10.1021/ja01247a029.
^Deuel, H.; Lewuenberger, R. & Huber, G. (1950). "Über den enzymatischen Abbau von Carubin, dem Galaktomannan aus Ceratonia siliqua L". Helv. Chim. Acta. 33 (4): 942–946. doi:10.1002/hlca.19500330424.
Gao J, Arbman G, He L, et al. (2008). "MANBA polymorphism was related to increased risk of colorectal cancer in Swedish but not in Chinese populations". Acta Oncol. 47 (3): 372–8. doi:10.1080/02841860701644052. PMID17899454. S2CID45674826.
Robinson WE, Montefiori DC, Mitchell WM (1987). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID2829950.
Blough HA, Pauwels R, De Clercq E, et al. (1986). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID3099781.
This page was last edited on 3 December 2023, at 17:12