- 関
- Glc、glucose、grape sugar
WordNet
- a monosaccharide sugar that has several forms; an important source of physiological energy
PrepTutorEJDIC
- ブドウ糖
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/10/06 18:42:52」(JST)
[Wiki en表示]
| GBA |
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| Available structures |
| PDB |
Ortholog search: PDBe RCSB |
| List of PDB id codes |
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1OGS, 1Y7V, 2F61, 2J25, 2NSX, 2NT0, 2NT1, 2V3D, 2V3E, 2V3F, 2VT0, 2WCG, 2WKL, 2XWD, 2XWE, 3GXD, 3GXF, 3GXI, 3GXM, 3KE0, 3KEH, 3RIK, 3RIL
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| Identifiers |
| Aliases |
GBA, GBA1, GCB, GLUC, glucosylceramidase beta, Glucocerebrosidase |
| External IDs |
OMIM: 606463 MGI: 95665 HomoloGene: 68040 GeneCards: 2629 |
| Gene ontology |
| Molecular function |
• hydrolase activity, acting on glycosyl bonds
• protein binding
• hydrolase activity
• receptor binding
• glucosylceramidase activity
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| Cellular component |
• membrane
• lysosome
• extracellular exosome
• lysosomal lumen
• lysosomal membrane
• extracellular fluid
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| Biological process |
• termination of signal transduction
• skin morphogenesis
• glycosphingolipid metabolic process
• positive regulation of protein dephosphorylation
• carbohydrate metabolic process
• lipid metabolic process
• response to testosterone
• cellular response to starvation
• negative regulation of interleukin-6 production
• response to thyroid hormone
• ceramide biosynthetic process
• cellular response to tumor necrosis factor
• sphingosine biosynthetic process
• positive regulation of proteolysis involved in cellular protein catabolic process
• response to glucocorticoid
• regulation of water loss via skin
• response to estrogen
• glucosylceramide catabolic process
• positive regulation of macroautophagy
• negative regulation of MAP kinase activity
• response to pH
• regulation of proteasomal ubiquitin-dependent protein catabolic process
• metabolic process
• negative regulation of inflammatory response
• regulation of macroautophagy
• sphingolipid metabolic process
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| Sources:Amigo / QuickGO |
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| RNA expression pattern |
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| More reference expression data |
| Orthologs |
| Species |
Human |
Mouse |
| Entrez |
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| Ensembl |
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| UniProt |
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| RefSeq (mRNA) |
NM_000157
NM_001005741
NM_001005742
NM_001005749
NM_001005750
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NM_001171811
NM_001171812
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| RefSeq (protein) |
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NP_000148.2
NP_001005741.1
NP_001005742.1
NP_001165282.1
NP_001165283.1
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NP_001070879.1
NP_032120.1
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| Location (UCSC) |
Chr 1: 155.23 – 155.24 Mb |
Chr 3: 89.2 – 89.21 Mb |
| PubMed search |
[1] |
[2] |
| Wikidata |
| View/Edit Human |
View/Edit Mouse |
β-Glucocerebrosidase (also called acid β-glucosidase, D-glucosyl-N-acylsphingosine glucohydrolase, or GCase) is an enzyme with glucosylceramidase activity (EC 3.2.1.45) that is needed to cleave, by hydrolysis, the beta-glucosidic linkage of the chemical glucocerebroside, an intermediate in glycolipid metabolism. It is localized in the lysosome and has a molecular weight of 59700 Daltons.
Clinical significance
Mutations in the glucocerebrosidase gene cause Gaucher's disease, a lysosomal storage disease characterized by an accumulation of glucocerebrosides. A related pseudogene is approximately 12 kb downstream of this gene on chromosome 1. Alternative splicing results in multiple transcript variants encoding the same protein.[3]
Mutations in the glucocerebrosidase gene are also associated with Parkinson's disease.[4][5]
Drugs
Alglucerase (Ceredase) was a version of glucocerebrosidase that was harvested from human placental tissue and then modified with enzymes.[6] It was approved by the FDA in 1991[7] and has been withdrawn from the market[8][9] due to the approval of similar drugs made with recombinant DNA technology instead of being harvested from tissue; drugs made recombinantly, since there is no concern about diseases being transmitted from the tissue used in harvesting, and are less expensive to manufacture.[6]
Recombinant glucocerebrosidases used as drugs include:[10]
- Imiglucerase (Cerezyme) [6]
- Velaglucerase (Vpriv) [6]
- Taliglucerase alfa (Elelyso) [11]
See also
- Closely related enzymes
- GBA2: acid β-glucosidase (bile acid), also EC 3.2.1.45
- GBA3: acid β-glucosidase (cytosolic), EC 3.2.1.21
References
- ^ "Human PubMed Reference:".
- ^ "Mouse PubMed Reference:".
- ^ "Entrez Gene: GBA glucosidase, beta; acid (includes glucosylceramidase)".
- ^ "PDGene". Alzheimer Research Forum. 2008-11-12. Retrieved 2008-11-13.
- ^ Lwin A, Orvisky E, Goker-Alpan O, LaMarca ME, Sidransky E (January 2004). "Glucocerebrosidase mutations in subjects with parkinsonism". Molecular Genetics and Metabolism. 81 (1): 70–3. doi:10.1016/j.ymgme.2003.11.004. PMID 14728994.
- ^ a b c d Deegan PB, Cox TM (2012). "Imiglucerase in the treatment of Gaucher disease: a history and perspective". Drug Design, Development and Therapy. 6: 81–106. doi:10.2147/DDDT.S14395. PMC 3340106. PMID 22563238.
- ^ "Regulatory Matters" (PDF). WHO Drug Information. 5 (3): 123–4. 1991.
- ^ "Enzyme-replacement Therapy for Lysosomal Storage Disorders". Clinical Policy Bulletin Number: 0442. Aetna. 2014-08-08.
- ^ "FDA Prescription and Over-the-Counter Drug Product List" (PDF). Additions/Deletions for Prescription Drug Product List. U.S. Food and Drug Administration. March 2012.
- ^ Grabowski GA (2012). "Gaucher disease and other storage disorders". Hematology / the Education Program of the American Society of Hematology. American Society of Hematology. Education Program. 2012: 13–8. doi:10.1182/asheducation-2012.1.13. PMID 23233555.
- ^ Yukhananov, Anna (1 May 2012). "U.S. FDA approves Pfizer/Protalix drug for Gaucher". Chicago Tribune. Reuters. Retrieved 2 May 2012.
Further reading
- Horowitz M, Zimran A (1994). "Mutations causing Gaucher disease". Human Mutation. 3 (1): 1–11. doi:10.1002/humu.1380030102. PMID 8118460.
- Tayebi N, Stone DL, Sidransky E (October 1999). "Type 2 gaucher disease: an expanding phenotype". Molecular Genetics and Metabolism. 68 (2): 209–19. doi:10.1006/mgme.1999.2918. PMID 10527671.
- Stone DL, Tayebi N, Orvisky E, Stubblefield B, Madike V, Sidransky E (2000). "Glucocerebrosidase gene mutations in patients with type 2 Gaucher disease". Human Mutation. 15 (2): 181–8. doi:10.1002/(SICI)1098-1004(200002)15:2<181::AID-HUMU7>3.0.CO;2-S. PMID 10649495.
- Caillaud C, Poenaru L (2002). "[Gaucher's and Fabry's diseases: biochemical and genetic aspects]". Journal De La Société De Biologie. 196 (2): 135–40. PMID 12360742.
- Fabrega S, Durand P, Mornon JP, Lehn P (2002). "[The active site of human glucocerebrosidase: structural predictions and experimental validations]". Journal De La Société De Biologie. 196 (2): 151–60. PMID 12360744.
- Alfonso P, Aznarez S, Giralt M, Pocovi M, Giraldo P (2007). "Mutation analysis and genotype/phenotype relationships of Gaucher disease patients in Spain". Journal of Human Genetics. 52 (5): 391–6. doi:10.1007/s10038-007-0135-4. PMID 17427031.
External links
- GeneReviews/NCBI/UW/NIH entry on Gaucher disease
- Glucocerebrosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
- Proteopedia Acid-beta-glucosidase
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PDB gallery
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1ogs: HUMAN ACID-BETA-GLUCOSIDASE
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1y7v: X-ray structure of human acid-beta-glucosidase covalently bound to conduritol B epoxide
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2f61: Crystal structure of partially deglycosylated acid beta-glucosidase
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2j25: PARTIALLY DEGLYCOSYLATED GLUCOCERAMIDASE
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2nsx: Structure of acid-beta-glucosidase with pharmacological chaperone provides insight into Gaucher disease
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2nt0: Acid-beta-glucosidase low pH, glycerol bound
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2nt1: Structure of acid-beta-glucosidase at neutral pH
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Metabolism, lipid metabolism, glycolipid enzymes
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| Sphingolipid |
| To glycosphingolipid |
- Glycosyltransferase
- Sulfotransferase
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| To ceramide |
- From ganglioside
- Beta-galactosidase
- Hexosaminidase A
- Neuraminidase
- Glucocerebrosidase
- From globoside
- Hexosaminidase B
- Alpha-galactosidase
- Beta-galactosidase
- Glucocerebrosidase
- From sphingomyelin
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 1
- From sulfatide
- Arylsulfatase A
- Galactosylceramidase
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| To sphingosine |
- Ceramidase
- ACER1
- ACER2
- ACER3
- ASAH1
- ASAH2
- ASAH2B
- ASAH2C
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| Other |
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| NCL |
- Palmitoyl protein thioesterase
- Tripeptidyl peptidase I
- CLN3
- CLN5
- CLN6
- CLN8
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| Ceramide synthesis |
- Serine C-palmitoyltransferase (SPTLC1)
- Ceramide glucosyltransferase (UGCG)
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Hydrolase: sugar hydrolases (EC 3.2)
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| 3.2.1: Glycoside hydrolases |
| Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
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| Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
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| 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
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3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
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Enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
- Enzyme kinetics
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Types |
- EC1 Oxidoreductases(list)
- EC2 Transferases(list)
- EC3 Hydrolases(list)
- EC4 Lyases(list)
- EC5 Isomerases(list)
- EC6 Ligases(list)
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UpToDate Contents
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- 1. 胸部PET thoracic positron emission tomography
English Journal
- Multinuclear Complex Formation between Ca(II) and Gluconate Ions in Hyperalkaline Solutions.
- Pallagi A1, Bajnóczi EG, Canton SE, Bolin T, Peintler G, Kutus B, Kele Z, Pálinkó I, Sipos P.
- Environmental science & technology.Environ Sci Technol.2014 Jun 17;48(12):6604-11. doi: 10.1021/es501067w. Epub 2014 Jun 5.
- Alkaline solutions containing polyhydroxy carboxylates and Ca(II) are typical in cementitious radioactive waste repositories. Gluconate (Gluc(-)) is a structural and functional representative of these sugar carboxylates. In the current study, the structure and equilibria of complexes forming in such
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- Chandler KB1, Brnakova Z, Sanda M, Wang S, Stalnaker SH, Bridger R, Zhao P, Wells L, Edwards NJ, Goldman R.
- Journal of proteome research.J Proteome Res.2014 Jun 12. [Epub ahead of print]
- Inter-alpha-trypsin inhibitor heavy chain H4 (ITIH4) is a 120 kDa acute-phase glycoprotein produced primarily in the liver, secreted into the blood, and identified in serum. ITIH4 is involved in liver development and stabilization of the extracellular matrix (ECM), and its expression is altered in l
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- Optimization and validation of a high throughput method for detecting neutralizing antibodies against human papillomavirus (HPV) based on pseudovirons.
- Nie J1, Huang W, Wu X, Wang Y.
- Journal of medical virology.J Med Virol.2014 Jun 4. doi: 10.1002/jmv.23995. [Epub ahead of print]
- The pseudoviron-based neutralization assay is accepted as the gold standard to evaluate the functional humoral immune response against HPV. The goal of this study was to develop and optimize a human papillomavirus (HPV) neutralization assay using HPV pseudovirons with Gaussia luciferase (Gluc) as th
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Japanese Journal
- piggyBac transposon-mediated long-term gene expression in mice.
- Nakanishi Hideyuki,Higuchi Yuriko,Kawakami Shigeru,Yamashita Fumiyoshi,Hashida Mitsuru
- Molecular therapy 18(4), 707-714, 2010-01-26
- … We constructed PB-based plasmid DNA (pDNA) containing reporter [firefly and Gaussia luciferase (Gluc)] genes. …
- NAID 120002515182
- 4-Hydroxy-3-methoxymethamphetamine Glucuronide as a Phase II Metabolite of 3,4-Methylenedioxymethamphetamine: Enzyme-Assisted Synthesis and Involvement of Human Hepatic Uridine 5′-Diphosphate-Glucuronosyltransferase 2B15 in the Glucuronidation
- Shoda Takuji,Fukuhara Kiyoshi,Goda Yukihiro,Okuda Haruhiro
- CHEMICAL & PHARMACEUTICAL BULLETIN 57(5), 472-475, 2009
- … In the present study, enzyme kinetic studies with various microsomes showed that rat liver microsomes pretreated with Aroclor 1254 were most suitable for the enzyme-assisted synthesis of the glucuronide (HMMA-Gluc). … This method selectively produced the β-anomer of HMMA-Gluc in a very high, isolated yield (71%), and with a purity that was sufficient for use in an analysis of MDMA intake and for enzyme kinetic studies. …
- NAID 130000124558
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★リンクテーブル★
[★]
ブドウ糖、グルコース
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[★]
UDPグルコース・ヘキソース-1-リン酸ウリジルトランスフェラーゼ
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