| Autor: |
Bagiya, Foma G., Eneyskaya, Elena V., Kulminskaya, Anna A., Savel'ev, Andrew N., Shabalin, Konstantin A., Neustroev, Kirill N. |
| Předmět: |
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| Zdroj: |
European Journal of Biochemistry; 10/1/97, Vol. 249 Issue 1, p286-292, 7p |
| Abstrakt: |
α-Marmosidase was isolated from the culture liquid of Oerskovia sp. The purified enzyme had a molecular mass of 480 kDa and comprises four identical subunits. The enzyme cleaves bonds in side chains of yeast mannan (Km = 0.08 mM, kcat = 1.02 μmol min-1 · mg-1) and reveals a low activity towards p-nitrophenyl α-D-mannopyranoside. The a-mannosidase is a Ca2+-dependent enzyme and is inhibited by EDTA. The enzyme possess no endo-mannosidase activity releasing only mannose in the reaction with the inversion of anomeric configuration and could be classified as exo-α-mannanase. The enzyme revealed a high deglycosylating activity towards the short mannose-rich O-linked carbohydrate chains of glycoproteins. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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