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Acid alpha-glucosidase

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Title: Acid alpha-glucosidase  
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Subject: Glycogen storage disease type II, Glycogen debranching enzyme, GAA, HEXB, Glycogen storage disease
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Acid alpha-glucosidase

Glucosidase, alpha; acid
Identifiers
Symbols  ; LYAG
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
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.  
  2. ^ a b c "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.  
  • Reuser AJ, Kroos MA, Hermans MM; et al. (1995). "Glycogenosis type II (acid maltase deficiency).". Muscle Nerve 3: S61–9.  
  • Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum.". Biochimie 83 (8): 783–90.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA (1991). "Characterization of the human lysosomal alpha-glucosidase gene". Biochem. J. 272 (2): 493–7.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  




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