Enzymes
| UniProtKB help_outline | 1,033 proteins |
| Enzyme class help_outline |
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| GO Molecular Function help_outline |
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- Name help_outline an α-L-fucoside Identifier CHEBI:28349 Charge 0 Formula C6H11O5R SMILEShelp_outline C[C@@H]1O[C@@H](O[*])[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline L-fucose Identifier CHEBI:2181 (CAS: 2438-80-4) help_outline Charge 0 Formula C6H12O5 InChIKeyhelp_outline SHZGCJCMOBCMKK-DHVFOXMCSA-N SMILEShelp_outline C[C@@H]1OC(O)[C@@H](O)[C@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 11 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline an alcohol Identifier CHEBI:30879 Charge 0 Formula HOR SMILEShelp_outline O[*] 2D coordinates Mol file for the small molecule Search links Involved in 1,548 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:12288 | RHEA:12289 | RHEA:12290 | RHEA:12291 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Mammalian fucosidases. 2. alpha-L-Fucosidase.
LEVVY G.A., MCALLAN A.
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Purification of alpha-L-fucosidase of abalone livers.
Tanaka K., Nakano T., Noguchi S., Pigman W.
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Glycosidases of molluscs. Purification and properties of alpha-L-fucosidase from Chamelea gallina L.
Reglero A., Cabezas J.A.
An alpha-L-fucosidase had been purified approximately 300-fold from the liver (hepatopancreas) of the marine mollusc Chamelea gallina L. (= Venus gallina L.). During the different steps of the purification procedure it was difficult to remove the contaminant N-acetylglucosaminidase activity; but, ... >> More
An alpha-L-fucosidase had been purified approximately 300-fold from the liver (hepatopancreas) of the marine mollusc Chamelea gallina L. (= Venus gallina L.). During the different steps of the purification procedure it was difficult to remove the contaminant N-acetylglucosaminidase activity; but, after electrofocusing, a final preparation free of this and other glycosidades present in the crude extract was obtained. The purified enzyme has a broad specificity; it hydrolyzes p-nitrophenyl alpha-L-fucoside and natural substrates such as oligosaccharides containing fucosidic residues with alpha 1--2, alpha 1--3 and alpha 1--4 linkages; also it hydrolyzes fucose-containing glycopeptides, such as thyroglobulin glycopeptide, and glycoproteins as procine submaxillary mucin (previously rendered free of sialic acid). The enzyme has a pH optimum of 5.2 +/-0.2, with a Km of 7 X 10(-5) M using p-nitrophenyl L-fucoside as substrate. It is inhibited by Hg2+ and some sugars, and activated by CN-, Zn2+, Ca2+ and EDTA. It shows two peaks by isoelectric focusing (at 6.3 and 6.6). The molecular weight of the alpha-L-fucosidase by gel filtration was over 2000000. << Less
Eur J Biochem 66:379-387(1976) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.