Acid alpha-glucosidase: Difference between revisions

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{{Infobox_gene}}
{{Infobox_gene}}
'''Lysosomal alpha-glucosidase''', also called '''α-1,4-glucosidase'''<ref name="Voet">{{cite book
'''Acid alpha-glucosidase''', also called '''α-1,4-glucosidase'''<ref name="Voet">{{cite book | title = Principles of Biochemistry, Third edition | chapter = Additional Pathways in Carbohydrate Metabolism | author1 = Donald J. Voet | author2 = Judith G. Voet | author3 = Charlotte W. Pratt | publisher = Wiley | year = 2008 | isbn = 978-0470-23396-2 | page = 538 }}</ref> and '''acid maltase''',<ref name=entrez /> is an [[enzyme]] ({{EC number|3.2.1.20}}) that helps to break down [[glycogen]] in the [[lysosome]]. It is functionally similar to [[glycogen debranching enzyme]], but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol.<ref>{{cite web | title = Glycogen Metabolism in Humans | url = https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4802397/|}}</ref> In humans, it is encoded by the ''GAA'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2548| access-date = }}</ref> Errors in this gene cause [[glycogen storage disease type II]] (Pompe disease).
| title = Principles of Biochemistry, Third edition
| chapter = Additional Pathways in Carbohydrate Metabolism
| author1 = Donald J. Voet
| author2 = Judith G. Voet
| author3 = Charlotte W. Pratt
| publisher = Wiley
| year = 2008
| isbn = 978-0470-23396-2
| page = 538
}}</ref> and '''acid maltase''',<ref name=entrez /> is an [[enzyme]] ({{EC number|3.2.1.20}}) that in humans is encoded by the ''GAA'' [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=2548| accessdate = }}</ref> Errors in this gene cause [[glycogen storage disease type II]] (Pompe disease).


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== Function ==
{{PBB_Summary
| section_title =
| summary_text = This gene encodes '''acid alpha-glucosidase''', which is essential for the degradation of [[glycogen]] to [[glucose]] in [[lysosome]]s. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of [[glycogen storage disease type II|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.<ref name="entrez"/>
}}


==References==
This gene encodes '''lysosomal alpha-glucosidase''', which is essential for the degradation of [[glycogen]] to [[glucose]] in [[lysosome]]s. Different forms of acid alpha-glucosidase are obtained by proteolytic processing. Defects in this gene are the cause of [[glycogen storage disease type II|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.<ref name="entrez"/>
 
== References ==
{{reflist}}
{{reflist}}


==External links==
== Further reading ==
* [https://www.ncbi.nlm.nih.gov/books/NBK1261/ GeneReview/NIH/UW entry on Glycogen Storage Disease Type II (Pompe Disease)]
* {{UCSC gene info|GAA}}
 
==Further reading==
{{refbegin}}
{{refbegin}}
{{PBB_Further_reading
* {{cite journal | vauthors = Feizi T, Larkin M | title = AIDS and glycosylation | journal = Glycobiology | volume = 1 | issue = 1 | pages = 17–23 | date = September 1990 | pmid = 2136376 | doi = 10.1093/glycob/1.1.17 }}
| citations =
* {{cite journal | vauthors = Reuser AJ, Kroos MA, Hermans MM, Bijvoet AG, Verbeet MP, Van Diggelen OP, Kleijer WJ, Van der Ploeg AT | title = Glycogenosis type II (acid maltase deficiency) | journal = Muscle & Nerve. Supplement | volume = 3 | issue =  | pages = S61-9 | year = 1995 | pmid = 7603530 | doi = 10.1002/mus.880181414 }}
*{{cite journal |vauthors=Feizi T, Larkin M |title=AIDS and glycosylation. |journal=Glycobiology |volume=1 |issue= 1 |pages= 17–23 |year= 1992 |pmid= 2136376 |doi=10.1093/glycob/1.1.17 }}
* {{cite journal | vauthors = Land A, Braakman I | title = Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum | journal = Biochimie | volume = 83 | issue = 8 | pages = 783–90 | date = August 2001 | pmid = 11530211 | doi = 10.1016/S0300-9084(01)01314-1 }}
*{{cite journal |vauthors=Reuser AJ, Kroos MA, Hermans MM |title=Glycogenosis type II (acid maltase deficiency). |journal=Muscle Nerve |volume=3 |issue=  |pages= S61–9 |year= 1995 |pmid= 7603530 |doi=10.1002/mus.880181414 |display-authors=etal}}
* {{cite journal | vauthors = Zhong N, Martiniuk F, Tzall S, Hirschhorn R | title = 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 | journal = American Journal of Human Genetics | volume = 49 | issue = 3 | pages = 635–45 | date = September 1991 | pmid = 1652892 | pmc = 1683123 | doi =  }}
*{{cite journal |vauthors=Land A, Braakman I |title=Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum. |journal=Biochimie |volume=83 |issue= 8 |pages= 783–90 |year= 2001 |pmid= 11530211 |doi=10.1016/S0300-9084(01)01314-1 }}
* {{cite journal | vauthors = Fenouillet E, Gluckman JC | title = Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein | journal = The Journal of General Virology | volume = 72 ( Pt 8) | issue = 8 | pages = 1919–26 | date = August 1991 | pmid = 1678778 | doi = 10.1099/0022-1317-72-8-1919 }}
*{{cite journal |vauthors=Zhong N, Martiniuk F, Tzall S, Hirschhorn R |title=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. |journal=Am. J. Hum. Genet. |volume=49 |issue= 3 |pages= 635–45 |year= 1991 |pmid= 1652892 |doi= | pmc=1683123 }}
* {{cite journal | vauthors = Martiniuk F, Mehler M, Bodkin M, Tzall S, Hirschhorn K, Zhong N, Hirschhorn R | title = Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele | journal = DNA and Cell Biology | volume = 10 | issue = 9 | pages = 681–7 | date = November 1991 | pmid = 1684505 | doi = 10.1089/dna.1991.10.681 }}
*{{cite journal |vauthors=Fenouillet E, Gluckman JC |title=Effect of a glucosidase inhibitor on the bioactivity and immunoreactivity of human immunodeficiency virus type 1 envelope glycoprotein. |journal=J. Gen. Virol. |volume=72 |issue= 8|pages= 1919–26 |year= 1991 |pmid= 1678778 |doi=10.1099/0022-1317-72-8-1919 }}
* {{cite journal | vauthors = Ratner L, vander Heyden N, Dedera D | title = Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity | journal = Virology | volume = 181 | issue = 1 | pages = 180–92 | date = March 1991 | pmid = 1704656 | doi = 10.1016/0042-6822(91)90483-R }}
*{{cite journal |vauthors=Martiniuk F, Mehler M, Bodkin M |title=Identification of a missense mutation in an adult-onset patient with glycogenosis type II expressing only one allele |journal=DNA Cell Biol. |volume=10 |issue= 9 |pages= 681–7 |year= 1992 |pmid= 1684505 |doi=10.1089/dna.1991.10.681 |display-authors=etal}}
* {{cite journal | vauthors = Dedera DA, Gu RL, Ratner L | title = Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function | journal = Virology | volume = 187 | issue = 1 | pages = 377–82 | date = March 1992 | pmid = 1736542 | doi = 10.1016/0042-6822(92)90331-I }}
*{{cite journal |vauthors=Ratner L, vander Heyden N, Dedera D |title=Inhibition of HIV and SIV infectivity by blockade of alpha-glucosidase activity |journal=Virology |volume=181 |issue= 1 |pages= 180–92 |year= 1991 |pmid= 1704656 |doi=10.1016/0042-6822(91)90483-R }}
* {{cite journal | vauthors = Hermans MM, Kroos MA, van Beeumen J, Oostra BA, Reuser AJ | title = Human lysosomal alpha-glucosidase. Characterization of the catalytic site | journal = The Journal of Biological Chemistry | volume = 266 | issue = 21 | pages = 13507–12 | date = July 1991 | pmid = 1856189 | doi =  }}
*{{cite journal |vauthors=Dedera DA, Gu RL, Ratner L |title=Role of asparagine-linked glycosylation in human immunodeficiency virus type 1 transmembrane envelope function |journal=Virology |volume=187 |issue= 1 |pages= 377–82 |year= 1992 |pmid= 1736542 |doi=10.1016/0042-6822(92)90331-I }}
* {{cite journal | vauthors = Hermans MM, de Graaff E, Kroos MA, Wisselaar HA, Oostra BA, Reuser AJ | title = Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II | journal = Biochemical and Biophysical Research Communications | volume = 179 | issue = 2 | pages = 919–26 | date = September 1991 | pmid = 1898413 | doi = 10.1016/0006-291X(91)91906-S }}
*{{cite journal |vauthors=Hermans MM, Kroos MA, van Beeumen J |title=Human lysosomal alpha-glucosidase. Characterization of the catalytic site |journal=J. Biol. Chem. |volume=266 |issue= 21 |pages= 13507–12 |year= 1991 |pmid= 1856189 |doi=  |display-authors=etal}}
* {{cite journal | vauthors = Murphy CI, Lennick M, Lehar SM, Beltz GA, Young E | title = Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding | journal = Genetic Analysis, Techniques and Applications | volume = 7 | issue = 6 | pages = 160–71 | date = October 1990 | pmid = 2076345 | doi = 10.1016/0735-0651(90)90030-J }}
*{{cite journal |vauthors=Hermans MM, de Graaff E, Kroos MA |title=Identification of a point mutation in the human lysosomal alpha-glucosidase gene causing infantile glycogenosis type II |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 2 |pages= 919–26 |year= 1991 |pmid= 1898413 |doi=10.1016/0006-291X(91)91906-S |display-authors=etal}}
* {{cite journal | vauthors = Martiniuk F, Mehler M, Tzall S, Meredith G, Hirschhorn R | title = 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 | journal = DNA and Cell Biology | volume = 9 | issue = 2 | pages = 85–94 | date = March 1990 | pmid = 2111708 | doi = 10.1089/dna.1990.9.85 }}
*{{cite journal |vauthors=Murphy CI, Lennick M, Lehar SM |title=Temporal expression of HIV-1 envelope proteins in baculovirus-infected insect cells: implications for glycosylation and CD4 binding |journal=Genet. Anal. Tech. Appl. |volume=7 |issue= 6 |pages= 160–71 |year= 1991 |pmid= 2076345 |doi=10.1016/0735-0651(90)90030-J |display-authors=etal}}
* {{cite journal | vauthors = Kalyanaraman VS, Rodriguez V, Veronese F, Rahman R, Lusso P, DeVico AL, Copeland T, Oroszlan S, Gallo RC, Sarngadharan MG | title = Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 | journal = AIDS Research and Human Retroviruses | volume = 6 | issue = 3 | pages = 371–80 | date = March 1990 | pmid = 2187500 | doi = 10.1089/aid.1990.6.371 }}
*{{cite journal |vauthors=Martiniuk F, Mehler M, Tzall S |title=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 |journal=DNA Cell Biol. |volume=9 |issue= 2 |pages= 85–94 |year= 1990 |pmid= 2111708 |doi=10.1089/dna.1990.9.85 |display-authors=etal}}
* {{cite journal | vauthors = Martiniuk F, Bodkin M, Tzall S, Hirschhorn R | title = 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 | journal = American Journal of Human Genetics | volume = 47 | issue = 3 | pages = 440–5 | date = September 1990 | pmid = 2203258 | pmc = 1683879 | doi =  }}
*{{cite journal |vauthors=Kalyanaraman VS, Rodriguez V, Veronese F |title=Characterization of the secreted, native gp120 and gp160 of the human immunodeficiency virus type 1 |journal=AIDS Res. Hum. Retroviruses |volume=6 |issue= 3 |pages= 371–80 |year= 1990 |pmid= 2187500 |doi=10.1089/aid.1990.6.371 |display-authors=etal}}
* {{cite journal | vauthors = Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA | title = Characterization of the human lysosomal alpha-glucosidase gene | journal = The Biochemical Journal | volume = 272 | issue = 2 | pages = 493–7 | date = December 1990 | pmid = 2268276 | pmc = 1149727 | doi = 10.1042/bj2720493 }}
*{{cite journal |vauthors=Martiniuk F, Bodkin M, Tzall S, Hirschhorn R |title=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 |journal=Am. J. Hum. Genet. |volume=47 |issue= 3 |pages= 440–5 |year= 1990 |pmid= 2203258 |doi= | pmc=1683879 }}
* {{cite journal | vauthors = Shimizu H, Tsuchie H, Honma H, Yoshida K, Tsuruoka T, Ushijima H, Kitamura T | title = Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins | journal = Japanese Journal of Medical Science & Biology | volume = 43 | issue = 3 | pages = 75–87 | date = June 1990 | pmid = 2283726 | doi = 10.7883/yoken1952.43.75 }}
*{{cite journal |vauthors=Hoefsloot LH, Hoogeveen-Westerveld M, Reuser AJ, Oostra BA |title=Characterization of the human lysosomal alpha-glucosidase gene |journal=Biochem. J. |volume=272 |issue= 2 |pages= 493–7 |year= 1991 |pmid= 2268276 |doi= 10.1042/bj2720493| pmc=1149727  }}
* {{cite journal | vauthors = Leonard CK, Spellman MW, Riddle L, Harris RJ, Thomas JN, Gregory TJ | title = 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 | journal = The Journal of Biological Chemistry | volume = 265 | issue = 18 | pages = 10373–82 | date = June 1990 | pmid = 2355006 | doi =  }}
*{{cite journal |vauthors=Shimizu H, Tsuchie H, Honma H |title=Effect of N-(3-phenyl-2-propenyl)-1-deoxynojirimycin on the lectin binding to HIV-1 glycoproteins |journal=Jpn. J. Med. Sci. Biol. |volume=43 |issue= 3 |pages= 75–87 |year= 1991 |pmid= 2283726 |doi= 10.7883/yoken1952.43.75|display-authors=etal}}
* {{cite journal | vauthors = Pal R, Hoke GM, Sarngadharan MG | title = Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 86 | issue = 9 | pages = 3384–8 | date = May 1989 | pmid = 2541446 | pmc = 287137 | doi = 10.1073/pnas.86.9.3384 }}
*{{cite journal |vauthors=Leonard CK, Spellman MW, Riddle L |title=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 |journal=J. Biol. Chem. |volume=265 |issue= 18 |pages= 10373–82 |year= 1990 |pmid= 2355006 |doi=  |display-authors=etal}}
* {{cite journal | vauthors = Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP | title = Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport | journal = Journal of Virology | volume = 63 | issue = 6 | pages = 2452–6 | date = June 1989 | pmid = 2542563 | pmc = 250699 | doi =  }}
*{{cite journal |vauthors=Pal R, Hoke GM, Sarngadharan MG |title=Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1 |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 9 |pages= 3384–8 |year= 1989 |pmid= 2541446 |doi=10.1073/pnas.86.9.3384 | pmc=287137  }}
*{{cite journal |vauthors=Dewar RL, Vasudevachari MB, Natarajan V, Salzman NP |title=Biosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transport |journal=J. Virol. |volume=63 |issue= 6 |pages= 2452–6 |year= 1989 |pmid= 2542563 |doi= | pmc=250699 }}
}}
{{refend}}
{{refend}}


== External links ==
* [https://www.ncbi.nlm.nih.gov/books/NBK1261/ GeneReview/NIH/UW entry on Glycogen Storage Disease Type II (Pompe Disease)]
* {{UCSC gene info|GAA}}
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<!-- The EC number of the described enzyme should be 3.2.1.20, not 3.2.1.3 This is also apparent when checking the references. I do not know how to fix it, but maybe somebody can-->
<!-- The EC number of the described enzyme should be 3.2.1.20, not 3.2.1.3 This is also apparent when checking the references. I do not know how to fix it, but maybe somebody can-->


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Latest revision as of 21:24, 13 October 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Acid alpha-glucosidase, also called α-1,4-glucosidase[1] and acid maltase,[2] is an enzyme (EC 3.2.1.20) that helps to break down glycogen in the lysosome. It is functionally similar to glycogen debranching enzyme, but is on a different chromosome, processed differently by the cell and is located in the lysosome rather than the cytosol.[3] In humans, it is encoded by the GAA gene.[2] Errors in this gene cause glycogen storage disease type II (Pompe disease).

Function

This gene encodes lysosomal 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. ↑ 2.0 2.1 2.2 "Entrez Gene: GAA glucosidase, alpha; acid (Pompe disease, glycogen storage disease type II)".
  3. ↑ "Glycogen Metabolism in Humans".

Further reading

External links


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