GANC

From Wikipedia, the free encyclopedia

Glucosidase, alpha; neutral C

Identifiers

GANC; MGC138256

External IDs

Gene ontology
Molecular Function:	• hydrolase activity, hydrolyzing O-glycosyl compounds • alpha-glucosidase activity
Biological Process:	• carbohydrate metabolic process • metabolic process

Orthologs

Human

Mouse

Entrez

2595

n/a

Refseq

NM_198141 (mRNA)
NP_937784 (protein)

n/a (mRNA)
n/a (protein)

Pubmed search

[1]

n/a

Glucosidase, alpha; neutral C, also known as GANC, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: GANC glucosidase, alpha; neutral C.

[edit] 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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.
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.