α-1,4-グルコシダーゼ
WordNet
- first in order of importance; "the alpha male in the group of chimpanzees"; "the alpha star in a constellation is the brightest or main star"
- the 1st letter of the Greek alphabet
- the beginning of a series or sequence; "the Alpha and Omega, the first and the last, the beginning and the end"--Revelations
- early testing stage of a software or hardware product; "alpha version"
- any high mountain
PrepTutorEJDIC
- アルファ(ギリシア語アルファベットの第1字A,α;英語のA,aに相当) / アルファ星(星座の主星)
- 高山,高峰
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2014/12/05 15:18:39」(JST)
[Wiki en表示]
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-glucosidase activity
• carbohydrate binding
• maltose alpha-glucosidase activity
|
Cellular component |
• lysosome
• lysosomal membrane
• membrane
• extracellular vesicular exosome
|
Biological process |
• maltose metabolic process
• regulation of the force of heart contraction
• diaphragm contraction
• heart morphogenesis
• glycogen catabolic process
• sucrose metabolic process
• glucose metabolic process
• lysosome organization
• locomotory behavior
• tissue development
• vacuolar sequestering
• muscle cell cellular homeostasis
• neuromuscular process controlling posture
• neuromuscular process controlling balance
• cardiac muscle contraction
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
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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:
78.08 – 78.09 Mb |
Chr 11:
119.27 – 119.29 Mb |
|
PubMed search |
[1] |
[2] |
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Lysosomal alpha-glucosidase (also called α-1,4-glucosidase[1]) 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
- ^ 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.
- ^ a b "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.
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
- Debranching enzyme
|
|
Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
|
|
|
3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
|
|
- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
|
|
|
|
Metabolism: carbohydrate metabolism, glycogenesis and glycogenolysis enzymes
|
|
Glycogenesis |
- Phosphoglucomutase
- UDP-glucose pyrophosphorylase
- Glycogen synthase
- Glycogen branching enzyme
- Glycogenin
|
|
Glycogenolysis |
extralysosomal: |
- Glycogen phosphorylase
- Debranching enzyme
- Phosphoglucomutase
|
|
lysosomal: |
|
|
|
Regulation |
- Phosphorylase kinase
- Phosphoprotein phosphatase
|
|
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
|
m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- A cold-adapted and glucose-stimulated type II α-glucosidase from a deep-sea bacterium Pseudoalteromonas sp. K8.
- Li W1,2, Xue Y1,2, Li J1,2, Yuan J1,2, Wang X3, Fang W1,2, Fang Z4,5, Xiao Y1,2.
- Biotechnology letters.Biotechnol Lett.2015 Nov 13. [Epub ahead of print]
- OBJECTIVES: To express and characterize a putative α-glucosidase, Pagl, from Pseudoalteromonas sp. K8 obtained via genome mining approach.RESULTS: Pagl was expressed and purified to homogeneity, with a molecular mass of 60 kDa. It was optimally active at pH 8.5 and 30 °C, and showed cold-adapted
- PMID 26564409
- Modeling of cooked starch digestion process using recombinant human pancreatic α-amylase and maltase-glucoamylase for in vitro evaluation of α-glucosidase inhibitors.
- Cao X1, Zhang C1, Dong Y1, Geng P2, Bai F3, Bai G1.
- Carbohydrate research.Carbohydr Res.2015 Sep 23;414:15-21. doi: 10.1016/j.carres.2015.06.007. Epub 2015 Jun 26.
- In human, digestion of cooked starch mainly involves breaking down of α-amylase to α-limit dextrins and small linear malto-oligosaccharides, which are in turn hydrolyzed to glucose by the gut mucosal maltase-glucoamylase (MGAM). Human pancreatic α-amylase (HPA), amino- and carboxyl-terminal porti
- PMID 26162745
- Enzymatic transglycosylation of ginsenoside Rg1 by rice seed α-glucosidase.
- Kim MJ1, Kim YH1, Song GS1, Suzuki Y2, Kim MK1.
- Bioscience, biotechnology, and biochemistry.Biosci Biotechnol Biochem.2015 Sep 15:1-11. [Epub ahead of print]
- Six α-monoglucosyl derivatives of ginsenoside Rg1 (G-Rg1) were synthesized by transglycosylation reaction of rice seed α-glucosidase in the reaction mixture containing maltose as a glucosyl donor and G-Rg1 as an acceptor. Their chemical structures were identified by spectroscopic analysis, and the
- PMID 26372017
Japanese Journal
- Novel Mutations in the Gene Encoding Acid .ALPHA.-1,4-glucosidase in a Patient with Late-onset Glycogen Storage Disease Type II (Pompe Disease) with Impaired Intelligence
- Clinical analysis of five infants with glycogen storage disease of the heart-Pompe's disease.
- The adult form of acid maltase (alpha-1. 4-glucosidase)deficiency
Related Links
- Alpha 1,4 glucosidase deficiency symptoms, causes, diagnosis, and treatment information for Alpha 1,4 glucosidase deficiency (Glycogen storage disease type 2) with alternative diagnoses, full-text book chapters, misdiagnosis ...
- pyramid web application ... GO ID GO:0004558 Aspect Molecular Function Description Catalysis of the hydrolysis of terminal, non-reducing alpha-(1->4)-linked alpha-D-glucose residues with release of alpha-D-glucose.
★リンクテーブル★
[★]
- 英
- α-1,4-glucosidase, alpha-1,4-glucosidase
- 関
- α-グルコシダーゼ α-glucosidase
- α-1,4-グルコシド結合の加水分解を触媒する酵素
[★]
α、アルファ
- 関
- alfa