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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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]

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]

External links

Fucosidase at the US National Library of Medicine Medical Subject Headings (MeSH)

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by expanding it.

This hydrolase article is a stub. You can help Wikipedia by expanding it.

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1. 原発性肝細胞癌の臨床的特徴および診断 clinical features and diagnosis of primary hepatocellular carcinoma

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

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「フコシダーゼ」

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
	v; t; e;