Autor: Olga V. Chepurnaya, Elena V. Eneyskaya, Alexander V. Arutyunyan, Nilkolay P. Arbatskii, Nisse Kalkkinen, Anna I. Saenko, Anna A. Kulminskaya, Kirill N. Neustroev, Konstantin A. Shabalin, Nikolay E. Nifantiev
Rok vydání: 2001
Předmět:
Zdroj: Glycoconjugate Journal. 18:827-834
ISSN: 0282-0080
DOI: 10.1023/a:1021163720282
Popis: An α-L-fucosidase (E.C. 3.2.1.51) exhibiting a wide aglycon specificity expressed in ability of cleaving α1 → 6-, α1 →3-, α1 → 4-, and α1 → 2-O-fucosyl bonds in fucosylated oligosaccharides, has been isolated from culture filtrate of Thermus sp. strain Y5. The α-L-fucosidase hydrolyzes p-nitrophenyl α-L-fucopyranoside with Vmax of 12.0 ± 0.1 μM/min/mg and Km = 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 α-L-fucosidases from microbial and plant sources. Hydrolysis of p-nitrophenyl α-L-fucopyranoside occurs with retention of the anomeric configuration. Transglycosylating activity of the α-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 α-L-fucopyranoside. The enzyme can be classified in glycosyl hydrolase family 29.
Databáze: OpenAIRE
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