GANC

Glucosidase, alpha; neutral C
Identifiers
Symbols	GANC ; MGC138256
External IDs	Template:OMIM5 HomoloGene: 25627
Gene ontology Molecular function Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Glucosidase, alpha; neutral C, also known as GANC, is a human gene.

Glycosyl hydrolase enzymes hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. This gene encodes a member of glycosyl hydrolases family 31. This enzyme hydrolyses terminal, non-reducing 1,4-linked alpha-D-glucose residues and releases alpha-D-glucose. This is a key enzyme in glycogen metabolism and its gene localizes to a chromosomal region (15q15) that is associated with susceptibility to diabetes.

Further reading

• Feizi T, Larkin M (1992). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. PMID 2136376.
• Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. PMID 11530211.
• Kamimura H, Ogata H, Takahara H (1992). "Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases". Drug Metab. Dispos. 20 (2): 309–15. PMID 1352226.CS1 maint: Multiple names: authors list (link)
• Fenouillet E, Gluckman JC (1991). "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". J. Gen. Virol. 72 ( Pt 8): 1919–26. PMID 1678778.
• Ratner L, vander Heyden N, Dedera D (1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology. 181 (1): 180–92. PMID 1704656.CS1 maint: Multiple names: authors list (link)
• Dedera DA, Gu RL, Ratner L (1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology. 187 (1): 377–82. PMID 1736542.CS1 maint: Multiple names: authors list (link)
• Murphy CI, Lennick M, Lehar SM; et al. (1991). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genet. Anal. Tech. Appl. 7 (6): 160–71. PMID 2076345.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Kalyanaraman VS, Rodriguez V, Veronese F; et al. (1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Res. Hum. Retroviruses. 6 (3): 371–80. PMID 2187500.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Shimizu H, Tsuchie H, Honma H; et al. (1991). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Jpn. J. Med. Sci. Biol. 43 (3): 75–87. PMID 2283726.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Leonard CK, Spellman MW, Riddle L; et al. (1990). "Assignment of intrachain disulfide bonds and characterization of potential glycosylation sites of the type 1 recombinant human immunodeficiency virus envelope glycoprotein (gp120) expressed in Chinese hamster ovary cells". J. Biol. Chem. 265 (18): 10373–82. PMID 2355006.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Pal R, Hoke GM, Sarngadharan MG (1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 86 (9): 3384–8. PMID 2541446.CS1 maint: Multiple names: authors list (link)
• Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". J. Virol. 63 (6): 2452–6. PMID 2542563.CS1 maint: Multiple names: authors list (link)
• Kozarsky K, Penman M, Basiripour L; et al. (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". J. Acquir. Immune Defic. Syndr. 2 (2): 163–9. PMID 2649653.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Walker BD, Kowalski M, Goh WC; et al. (1987). "Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine". Proc. Natl. Acad. Sci. U.S.A. 84 (22): 8120–4. PMID 2825177.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Robinson WE, Montefiori DC, Mitchell WM (1988). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. PMID 2829950.CS1 maint: Multiple names: authors list (link)
• Gruters RA, Neefjes JJ, Tersmette M; et al. (1987). "Interference with HIV-induced syncytium formation and viral infectivity by inhibitors of trimming glucosidase". Nature. 330 (6143): 74–7. doi:10.1038/330074a0. PMID 2959866.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Blough HA, Pauwels R, De Clercq E; et al. (1987). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. PMID 3099781.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Usuki F, Ishiura S, Nonaka I, Sugita H (1988). "alpha-Glucosidase isoenzymes in normal and acid maltase-deficient human skeletal muscles". Muscle Nerve. 11 (4): 365–71. doi:10.1002/mus.880110413. PMID 3135493.CS1 maint: Multiple names: authors list (link)
• Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. PMID 3264072.CS1 maint: Multiple names: authors list (link)