Acid alpha-glucosidase

Glucosidase, alpha; acid
Identifiers
Symbols	GAA ; LYAG
External IDs	OMIM: 606800 MGI: 95609 HomoloGene: 37268 ChEMBL: 2608 GeneCards: GAA Gene
EC number	3.2.1.20
Gene ontology Molecular function • alpha-1,4-glucosidase activity • carbohydrate binding • maltose alpha-glucosidase activity Cellular component • lysosome • lysosomal membrane • membrane • lysosomal lumen • extracellular exosome Biological process • maltose metabolic process • regulation of the force of heart contraction • diaphragm contraction • heart morphogenesis • carbohydrate metabolic process • glycogen catabolic process • sucrose metabolic process • glucose metabolic process • lysosome organization • locomotory behavior • tissue development • vacuolar sequestering • small molecule metabolic process • muscle cell cellular homeostasis • neuromuscular process controlling posture • neuromuscular process controlling balance • cardiac muscle contraction Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	2548	14387
Ensembl	ENSG00000171298	ENSMUSG00000025579
UniProt	P10253	P70699
RefSeq (mRNA)	NM_000152	NM_001159324
RefSeq (protein)	NP_000143	NP_001152796
Location (UCSC)	Chr 17: 80.1 – 80.12 Mb	Chr 11: 119.27 – 119.29 Mb
PubMed search

Lysosomal alpha-glucosidase (also called α-1,4-glucosidase^[1] and acid maltase^[2]) is an enzyme that in humans is encoded by the GAA gene.^[2] Errors in this gene cause glycogen storage disease type II (Pompe disease).

This gene encodes acid alpha-glucosidase, which is essential for the degradation of glycogen to glucose in lysosomes. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of glycogen storage disease II, also known as Pompe disease, which is an autosomal recessive disorder with a broad clinical spectrum. Three transcript variants encoding the same protein have been found for this gene.^[2]

References

1. Donald J. Voet; Judith G. Voet; Charlotte W. Pratt (2008). "Additional Pathways in Carbohydrate Metabolism". Principles of Biochemistry, Third edition. Wiley. p. 538. ISBN 978-0470-23396-2.
2. "Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)".

External links

• GeneReview/NIH/UW entry on Glycogen Storage Disease Type II (Pompe Disease)

Further reading

• Feizi T, Larkin M (1992). "AIDS and glycosylation.". Glycobiology 1 (1): 17–23. doi:10.1093/glycob/1.1.17. PMID 2136376.
• Reuser AJ, Kroos MA, Hermans MM; et al. (1995). "Glycogenosis type II (acid maltase deficiency).". Muscle Nerve 3: S61–9. doi:10.1002/mus.880181414. PMID 7603530.
• Land A, Braakman I (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.
• Zhong N, Martiniuk F, Tzall S, Hirschhorn R (1991). "Identification of a missense mutation in one allele of a patient with Pompe disease, and use of endonuclease digestion of PCR-amplified RNA to demonstrate lack of mRNA expression from the second allele.". Am. J. Hum. Genet. 49 (3): 635–45. PMC 1683123. PMID 1652892.
• 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) (8): 1919–26. doi:10.1099/0022-1317-72-8-1919. PMID 1678778.
• Martiniuk F, Mehler M, Bodkin M; et al. (1992). "Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele". DNA Cell Biol. 10 (9): 681–7. doi:10.1089/dna.1991.10.681. PMID 1684505.
• 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. doi:10.1016/0042-6822(91)90483-R. 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. doi:10.1016/0042-6822(92)90331-I. PMID 1736542.
• Hermans MM, Kroos MA, van Beeumen J; et al. (1991). "Human lysosomal alpha-glucosidase. Characterization of the catalytic site". J. Biol. Chem. 266 (21): 13507–12. PMID 1856189.
• Hermans MM, de Graaff E, Kroos MA; et al. (1991). "Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II". Biochem. Biophys. Res. Commun. 179 (2): 919–26. doi:10.1016/0006-291X(91)91906-S. PMID 1898413.
• 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. doi:10.1016/0735-0651(90)90030-J. PMID 2076345.
• Martiniuk F, Mehler M, Tzall S; et al. (1990). "Sequence of the cDNA and 5'-flanking region for human acid alpha-glucosidase, detection of an intron in the 5' untranslated leader sequence, definition of 18-bp polymorphisms, and differences with previous cDNA and amino acid sequences". DNA Cell Biol. 9 (2): 85–94. doi:10.1089/dna.1990.9.85. PMID 2111708.
• 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. doi:10.1089/aid.1990.6.371. PMID 2187500.
• Martiniuk F, Bodkin M, Tzall S, Hirschhorn R (1990). "Identification of the base-pair substitution responsible for a human acid alpha glucosidase allele with lower "affinity" for glycogen (GAA 2) and transient gene expression in deficient cells". Am. J. Hum. Genet. 47 (3): 440–5. PMC 1683879. PMID 2203258.
• Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA (1991). "Characterization of the human lysosomal alpha-glucosidase gene". Biochem. J. 272 (2): 493–7. PMC 1149727. PMID 2268276.
• 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. doi:10.7883/yoken1952.43.75. 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. doi:10.1073/pnas.86.9.3384. PMC 287137. 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. PMC 250699. PMID 2542563.