フコシダーゼ、フコシド分解酵素
- 関
- alpha-L-fucosidase
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出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2016/03/07 22:57:39」(JST)
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Fucosidase, alpha-L- 1, tissue |
Identifiers |
Symbols |
FUCA1 ; FUCA |
External IDs |
OMIM: 612280 MGI: 95593 HomoloGene: 20078 ChEMBL: 4176 GeneCards: FUCA1 Gene |
EC number |
3.2.1.51 |
Gene ontology |
Molecular function |
• alpha-L-fucosidase activity
|
Cellular component |
• cytoplasm
• lysosome
• extracellular exosome
|
Biological process |
• fucose metabolic process
• glycosaminoglycan catabolic process
• glycoside catabolic process
|
Sources: Amigo / QuickGO |
|
RNA expression pattern |
|
More reference expression data |
Orthologs |
Species |
Human |
Mouse |
Entrez |
2517 |
71665 |
Ensembl |
ENSG00000179163 |
ENSMUSG00000028673 |
UniProt |
P04066 |
Q99LJ1 |
RefSeq (mRNA) |
NM_000147 |
NM_024243 |
RefSeq (protein) |
NP_000138 |
NP_077205 |
Location (UCSC) |
Chr 1:
23.85 – 23.87 Mb |
Chr 4:
135.92 – 135.94 Mb |
PubMed search |
[2] |
[3] |
|
Tissue alpha-L-fucosidase is an enzyme that in humans is encoded by the FUCA1 gene.[1][2]
Alpha-Fucosidase is an enzyme that breaks down fucose.[3]
Fucosidosis is an autosomal recessive lysosomal storage disease caused by defective alpha-L-fucosidase with accumulation of fucose in the tissues. Different phenotypes include clinical features such as neurologic deterioration, growth retardation, visceromegaly, and seizures in a severe early form; coarse facial features, angiokeratoma corporis diffusum, spasticity and delayed psychomotor development in a longer surviving form; and an unusual spondylometaphyseoepiphyseal dysplasia in yet another form.[supplied by OMIM][2]
Contents
- 1 See also
- 2 References
- 3 Further reading
- 4 External links
See also
References
- ^ Occhiodoro T, Beckmann KR, Morris CP, Hopwood JJ (Nov 1989). "Human alpha-L-fucosidase: complete coding sequence from cDNA clones". Biochem. Biophys. Res. Commun. 164 (1): 439–45. doi:10.1016/0006-291X(89)91739-7. PMID 2803312.
- ^ a b "Entrez Gene: FUCA1 fucosidase, alpha-L- 1, tissue".
- ^ HPRD entry [1]
Further reading
- Willems PJ, Gatti R, Darby JK, et al. (1991). "Fucosidosis revisited: a review of 77 patients". Am. J. Med. Genet. 38 (1): 111–31. doi:10.1002/ajmg.1320380125. PMID 2012122.
- Willems PJ, Seo HC, Coucke P, et al. (1999). "Spectrum of mutations in fucosidosis". Eur. J. Hum. Genet. 7 (1): 60–7. doi:10.1038/sj.ejhg.5200272. PMID 10094192.
- Yang M, Allen H, DiCioccio RA (1993). "A mutation generating a stop codon in the alpha-L-fucosidase gene of a fucosidosis patient". Biochem. Biophys. Res. Commun. 189 (2): 1063–8. doi:10.1016/0006-291X(92)92312-L. PMID 1281988.
- Fukushima H, Nishimoto J, Okada S (1991). "Sequencing and expression of a full-length cDNA for human alpha-L-fucosidase". J. Inherit. Metab. Dis. 13 (5): 761–5. doi:10.1007/BF01799583. PMID 2174090.
- Kretz KA, Darby JK, Willems PJ, O'Brien JS (1990). "Characterization of EcoRI mutation in fucosidosis patients: a stop codon in the open reading frame". J. Mol. Neurosci. 1 (3): 177–80. doi:10.1007/BF02918904. PMID 2642067.
- O'Brien JS, Willems PJ, Fukushima H, et al. (1988). "Molecular biology of the alpha-L-fucosidase gene and fucosidosis". Enzyme 38 (1–4): 45–53. PMID 2894306.
- Fukushima H, de Wet JR, O'Brien JS (1985). "Molecular cloning of a cDNA for human alpha-L-fucosidase". Proc. Natl. Acad. Sci. U.S.A. 82 (4): 1262–5. doi:10.1073/pnas.82.4.1262. PMC 397235. PMID 2983333.
- Fowler ML, Nakai H, Byers MG, et al. (1987). "Chromosome 1 localization of the human alpha-L-fucosidase structural gene with a homologous site on chromosome 2". Cytogenet. Cell Genet. 43 (1–2): 103–8. doi:10.1159/000132304. PMID 3780313.
- Kido A, Komatsu N, Ose Y, Oya M (1987). "alpha-L-fucosidase phenotyping in human tissues, dental pulps and hair roots". Forensic Sci. Int. 33 (1): 53–9. doi:10.1016/0379-0738(87)90139-3. PMID 3817676.
- Hopfer RL, Alhadeff JA (1985). "Solubilization and characterization of pellet-associated human brain alpha-L-fucosidase activity". Biochem. J. 229 (3): 679–85. PMC 1145111. PMID 4052017.
- Johnson K, Dawson G (1986). "Molecular defect in processing alpha-fucosidase in fucosidosis". Biochem. Biophys. Res. Commun. 133 (1): 90–7. doi:10.1016/0006-291X(85)91845-5. PMID 4074382.
- de Wet JR, Fukushima H, Dewji NN, et al. (1985). "Chromogenic immunodetection of human serum albumin and alpha-L-fucosidase clones in a human hepatoma cDNA expression library". DNA 3 (6): 437–47. doi:10.1089/dna.1.1984.3.437. PMID 6096099.
- Cragg H, Winchester B, Seo HC, et al. (1995). "Molecular basis of the common electrophoretic polymorphism (Fu1/Fu2) in human alpha-L-fucosidase". J. Med. Genet. 31 (8): 659–60. doi:10.1136/jmg.31.8.659-a. PMC 1050044. PMID 7815431.
- Beyer E, Ivleva T, Artykova G, Wiederschain G (1995). "Change of isoforms' spectra of alpha-L-fucosidase from human skin fibroblasts in intracellular storage of nonhydrolyzable substances". Biochim. Biophys. Acta 1270 (1): 7–11. doi:10.1016/0925-4439(94)00062-u. PMID 7827138.
- Seo HC, Yang M, Tonlorenzi R, et al. (1995). "A missense mutation (S63L) in alpha-L-fucosidase is responsible for fucosidosis in an Italian patient". Hum. Mol. Genet. 3 (11): 2065–6. PMID 7874128.
- Williamson M, Cragg H, Grant J, et al. (1993). "A 5' splice site mutation in fucosidosis". J. Med. Genet. 30 (3): 218–23. doi:10.1136/jmg.30.3.218. PMC 1016303. PMID 8097260.
- Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
- Yang M, Allen H, DiCioccio RA (1993). "Pedigree analysis of alpha-L-fucosidase gene mutations in a fucosidosis family". Biochim. Biophys. Acta 1182 (3): 245–9. doi:10.1016/0925-4439(93)90065-9. PMID 8399358.
External links
- Fucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)
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
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|
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3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
|
|
Metabolism: carbohydrate metabolism · glycoprotein enzymes
|
|
Anabolism |
- Dolichol kinase
- GCS1
- Oligosaccharyltransferase
|
|
Catabolism |
- Neuraminidase
- Beta-galactosidase
- Hexosaminidase
- mannosidase
- alpha-Mannosidase
- beta-mannosidase
- Aspartylglucosaminidase
- Fucosidase
- NAGA
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|
Transport |
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M6P tagging |
- N-acetylglucosamine-1-phosphate transferase
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UpToDate Contents
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English Journal
- Preparative scale purification of fucosyl-N-acetylglucosamine disaccharides and their evaluation as potential prebiotics and antiadhesins.
- Becerra JE1, Coll-Marqués JM, Rodríguez-Díaz J, Monedero V, Yebra MJ.
- Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2015 May 16. [Epub ahead of print]
- Fucosyl-N-acetylglucosamine disaccharides are important core structures that form part of human mucosal and milk glyco-complexes. We have previously shown that AlfB and AlfC α-L-fucosidases from Lactobacillus casei are able to synthesize fucosyl-α-1,3--N-acetylglucosamine (Fuc-α1,3-GlcNAc) and fu
- PMID 25977209
- Polymeric iminosugars improve the activity of carbohydrate-processing enzymes.
- Brissonnet Y1, Ladevèze S2, Tezé D1, Fabre E3, Deniaud D1, Daligault F4, Tellier C4, Šesták S5, Remaud-Simeon M2, Potocki-Veronese G2, Gouin SG1.
- Bioconjugate chemistry.Bioconjug Chem.2015 Apr 15;26(4):766-72. doi: 10.1021/acs.bioconjchem.5b00081. Epub 2015 Mar 13.
- Multivalent iminosugars have recently emerged as powerful tools to inhibit the activities of specific glycosidases. In this work, biocompatible dextrans were coated with iminosugars to form linear and ramified polymers with unprecedently high valencies (from 20 to 900) to probe the evolution of the
- PMID 25741759
- Characterization of an α-l-fucosidase from the periodontal pathogen Tannerella forsythia.
- Megson ZA1, Koerdt A, Schuster H, Ludwig R, Janesch B, Frey A, Naylor K, Wilson I, Stafford GP, Messner P, Schäffer C.
- Virulence.Virulence.2015 Apr 3;6(3):282-92. doi: 10.1080/21505594.2015.1010982.
- The periodontal pathogen Tannerella forsythia expresses several glycosidases which are linked to specific growth requirements and are involved in the invasion of host tissues. α-l-Fucosyl residues are exposed on various host glycoconjugates and, thus, the α-l-fucosidases predicted in the T. forsyt
- PMID 25831954
Japanese Journal
- Differences in the Substrate Specificities and Active-Site Structures of Two α-L-Fucosidases (Glycoside Hydrolase Family 29) from Bacteroides thetaiotaomicron
- SAKURAMA Haruko,TSUTSUMI Erika,ASHIDA Hisashi [他],KATAYAMA Takane,YAMAMOTO Kenji,KUMAGAI Hidehiko
- Bioscience, biotechnology, and biochemistry 76(5), 1022-1024, 2012-05-23
- Recent studies suggest that α-L-fucosidases of glycoside hydrolase family 29 can be divided into two subfamilies based on substrate specificity and phylogenetic clustering. To explore the validity of …
- NAID 10030753211
- Tissue-Specific Expression of Fucosylated Glycosphingolipid Species in Rat Prostate
- Miyanaka Hiroshi,Nakamura Takanori,Nishi Nozomu
- Bioscience, biotechnology, and biochemistry 74(6), 1261-1266, 2010-06-23
- … PFGs were also susceptible to α1,3/4-L-fucosidase but not to peptide-<I>N</I>-glycosidase F. …
- NAID 10027556503
- Analyses of Bifidobacterial Glycosidases Involved in the Metabolism of Oligosaccharides
- YAMAMOTO Kenji,KATAYAMA Takane,KITAOKA Motomitsu,FUSHINOBU Shinya
- Bioscience and microflora 29(1), 23-30, 2010-01-01
- … The gene encoding a specific 1,2-α -L-fucosidase was cloned from B.bifidum. … The genes encoding sialidase and α-1,3/4-L-fucosidase were also cloned from B.bifidum. …
- NAID 10026975142
Related Links
- 単独で糸状菌のプロトプラストが調製可能 Yatalase(糸状菌細胞壁溶解酵素) フコースの結合を識別 α-1,3/4-L-Fucosidase 陰イオン交換カラムで高速、高収量プラスミド精製(エンドトキシンフリー) NucleoBond ® Xtra Midi/Maxi EF illumina ...
- フコースの結合を識別 糖質分析 ... 注意事項 弊社の取扱い製品はすべて研究用として販売しております。ヒト、動物への医療、臨床診断用には使用しないようご注意ください。
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