GANC

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Identifiers
Aliases|
External IDs| GeneCards: [1]
Orthologs
Species| Human| Mouse
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Wikidata
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Neutral alpha-glucosidase C is an enzyme that in humans is encoded by the GANC gene.[1][2][3]

## Function[edit | edit source]

Glycoside 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.[3]

## References[edit | edit source]

1. ↑ Martiniuk F, Hirschhorn R, Smith M (Oct 1980). "Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15". Cytogenetics and Cell Genetics. 27 (2–3): 168–75. doi:10.1159/000131478. PMID 6995030.
2. ↑ Hirschhorn R, Huie ML, Kasper JS (Oct 2002). "Computer assisted cloning of human neutral alpha-glucosidase C (GANC): a new paralog in the glycosyl hydrolase gene family 31". Proceedings of the National Academy of Sciences of the United States of America. 99 (21): 13642–6. doi:10.1073/pnas.202383599. PMC 129728. PMID 12370436.
3. ↑ 3.0 3.1 "Entrez Gene: GANC glucosidase, alpha; neutral C".

## Further reading[edit | edit source]

* Feizi T, Larkin M (Sep 1990). "AIDS and glycosylation". Glycobiology. 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID 2136376.
* Land A, Braakman I (Aug 2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. PMID 11530211.
* Kamimura H, Ogata H, Takahara H (1992). "Alpha-glucoside formation of xenobiotics by rat liver alpha-glucosidases". Drug Metabolism and Disposition. 20 (2): 309–15. PMID 1352226.
* Fenouillet E, Gluckman JC (Aug 1991). "Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein". The Journal of General Virology. 72 (8): 1919–26. doi:10.1099/0022-1317-72-8-1919. PMID 1678778.
* Ratner L, vander Heyden N, Dedera D (Mar 1991). "Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity". Virology. 181 (1): 180–92. doi:10.1016/0042-6822(91)90483-R. PMID 1704656.
* Dedera DA, Gu RL, Ratner L (Mar 1992). "Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function". Virology. 187 (1): 377–82. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.
* Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E (Oct 1990). "Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding". Genetic Analysis, Techniques and Applications. 7 (6): 160–71. doi:10.1016/0735-0651(90)90030-J. PMID 2076345.
* Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG (Mar 1990). "Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1". AIDS Research and Human Retroviruses. 6 (3): 371–80. doi:10.1089/aid.1990.6.371. PMID 2187500.
* Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T (Jun 1990). "Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins". Japanese Journal of Medical Science & Biology. 43 (3): 75–87. doi:10.7883/yoken1952.43.75. PMID 2283726.
* Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ (Jun 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". The Journal of Biological Chemistry. 265 (18): 10373–82. PMID 2355006.
* Pal R, Hoke GM, Sarngadharan MG (May 1989). "Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 86 (9): 3384–8. doi:10.1073/pnas.86.9.3384. PMC 287137. PMID 2541446.
* Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP (Jun 1989). "Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport". Journal of Virology. 63 (6): 2452–6. PMC 250699. PMID 2542563.
* Kozarsky K, Penman M, Basiripour L, Haseltine W, Sodroski J, Krieger M (1989). "Glycosylation and processing of the human immunodeficiency virus type 1 envelope protein". Journal of Acquired Immune Deficiency Syndromes. 2 (2): 163–9. PMID 2649653.
* Walker BD, Kowalski M, Goh WC, Kozarsky K, Krieger M, Rosen C, Rohrschneider L, Haseltine WA, Sodroski J (Nov 1987). "Inhibition of human immunodeficiency virus syncytium formation and virus replication by castanospermine". Proceedings of the National Academy of Sciences of the United States of America. 84 (22): 8120–4. doi:10.1073/pnas.84.22.8120. PMC 299490. 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 Research and Human Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
* Gruters RA, Neefjes JJ, Tersmette M, de Goede RE, Tulp A, Huisman HG, Miedema F, Ploegh HL (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, Cogniaux J, Sprecher-Goldberger S, Thiry L (Nov 1986). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochemical and Biophysical Research Communications. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
* Usuki F, Ishiura S, Nonaka I, Sugita H (Apr 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 (Dec 1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proceedings of the National Academy of Sciences of the United States of America. 85 (23): 9248–52. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.

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Hydrolase: sugar hydrolases (EC 3.2)

3.2.1: Glycoside hydrolases|

| Disaccharidase|

* Sucrase/Sucrase-isomaltase/Invertase
* Maltase
* Trehalase
* Lactase

|

Glucosidases|

* Cellulase
* Alpha-glucosidase
* Acid
* Neutral AB
* Neutral C
* Beta-glucosidase
* cytosolic
* Debranching enzyme

Other|

* Amylase
* Alpha-amylase
* Chitinase
* Lysozyme
* Neuraminidase
* NEU1
* NEU2
* NEU3
* NEU4
* Bacterial neuraminidase
* Viral neuraminidase
* Galactosidases
* Alpha
* Beta
* alpha-Mannosidase
* Glucuronidase
* Klotho
* Hyaluronidase
* Pullulanase
* Glucosylceramidase
* lysosomal
* non-lysosomal
* Galactosylceramidase
* Alpha-N-acetylgalactosaminidase
* NAGA
* Alpha-N-acetylglucosaminidase
* Fucosidase
* Hexosaminidase
* HEXA
* HEXB
* Iduronidase
* Maltase-glucoamylase
* Heparanase
* HPSE2

3.2.2: Hydrolysing
N-Glycosyl compounds|

* DNA glycosylases: Oxoguanine glycosylase

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