| pubmed-article:12441672 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12441672 | lifeskim:mentions | umls-concept:C0995305 | lld:lifeskim |
| pubmed-article:12441672 | lifeskim:mentions | umls-concept:C0016787 | lld:lifeskim |
| pubmed-article:12441672 | lifeskim:mentions | umls-concept:C0332464 | lld:lifeskim |
| pubmed-article:12441672 | lifeskim:mentions | umls-concept:C0037791 | lld:lifeskim |
| pubmed-article:12441672 | pubmed:issue | 10 | lld:pubmed |
| pubmed-article:12441672 | pubmed:dateCreated | 2002-11-20 | lld:pubmed |
| pubmed-article:12441672 | pubmed:abstractText | An alpha-L-fucosidase (E.C. 3.2.1.51) exhibiting a wide aglycon specificity expressed in ability of cleaving alpha1 --> 6-, alpha1 -->3-, alpha1 --> 4-, and alpha1 --> 2-O-fucosyl bonds in fucosylated oligosaccharides, has been isolated from culture filtrate of Thermus sp. strain Y5. The alpha-L-fucosidase hydrolyzes p-nitrophenyl alpha-L-fucopyranoside with V(max) of 12.0 +/- 0.1 microM/min/mg and K(m) = 0.20 +/- 0.05 mM and is able to cleave off about 90% of total L-fucose from pronase-treated fractions of fucosyl-containing glycoproteins and about 30% from the native glycoproteins. The purified enzyme is a tetramer with a molecular mass of 240 +/- 10 kDa consisting of four identical subunits with a molecular mass of 61.0 +/- 0.5 kDa. The N-terminal sequence showed homology to some alpha-L-fucosidases from microbial and plant sources. Hydrolysis of p-nitrophenyl alpha-L-fucopyranoside occurs with retention of the anomeric configuration. Transglycosylating activity of the alpha-L-fucosidase was demonstrated in reactions with such acceptors as alcohols, N-acetylglucosamine and N-acetylgalactosamine while no transglycosylation products were observed in the reaction with p-nitrophenyl alpha-L-fucopyranoside. The enzyme can be classified in glycosyl hydrolase family 29. | lld:pubmed |
| pubmed-article:12441672 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12441672 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12441672 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:12441672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12441672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12441672 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12441672 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12441672 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:12441672 | pubmed:issn | 0282-0080 | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:SaenkoA IAI | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:KalkkinenNN | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:NeustroevK... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:ChepurnayaO... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:EneyskayaE... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:KulminskayaA... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:ShabalinK AKA | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:NifantievN... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:ArutyunyanA... | lld:pubmed |
| pubmed-article:12441672 | pubmed:author | pubmed-author:ArbatskiiN... | lld:pubmed |
| pubmed-article:12441672 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12441672 | pubmed:volume | 18 | lld:pubmed |
| pubmed-article:12441672 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12441672 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12441672 | pubmed:pagination | 827-34 | lld:pubmed |
| pubmed-article:12441672 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:meshHeading | pubmed-meshheading:12441672... | lld:pubmed |
| pubmed-article:12441672 | pubmed:year | 2001 | lld:pubmed |
| pubmed-article:12441672 | pubmed:articleTitle | An alpha-L-fucosidase from Thermus sp. with unusually broad specificity. | lld:pubmed |
| pubmed-article:12441672 | pubmed:affiliation | Molecular and Radiation Biophysics Division, Petersburg Nuclear Physics Institute, Russian Academy of Science, 188300 Gatchina, Orlova roscha, Russia. | lld:pubmed |
| pubmed-article:12441672 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12441672 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:12441672 | lld:pubmed |
