Lysozyme as a transferase
| Autor: | Kravchenko Na |
|---|---|
| Rok vydání: | 1967 |
| Předmět: |
chemistry.chemical_classification
Stereochemistry Induction period General Engineering Substrate (chemistry) Oligosaccharide Chitobiose chemistry.chemical_compound Enzyme chemistry Transferases General Earth and Planetary Sciences Tetrasaccharide Muramidase Trisaccharide Lysozyme General Environmental Science |
| Zdroj: | Proceedings of the Royal Society of London. Series B. Biological Sciences. 167:429-430 |
| ISSN: | 2053-9193 0080-4649 |
| DOI: | 10.1098/rspb.1967.0039 |
| Popis: | Our first investigations of the action of lysozyme on tetrasaccharides isolated from chitin showed that lysozyme, like many other known glycosides, is a transferase. Under certain conditions (oligosaccharide concentration 1 to 2%, the enzyme concentration 0.5%) the synthetic process may yield an insoluble chitin-like product. Judging by the increase of the Morgan-Elson reaction, lysozyme digests the tetrasaccharide intensively (figure 44). The trisaccharide reacts after a short induction period. Chitobiose reacts with more difficulty, and the induction period is several hours. Addition of the tetrasaccharide increases the reaction rate considerably, just as in the case of certain glycosidases, e. g. chitobiose is a much worse acceptor of transglycosidic residues than the tetrasaccharide (figure 45). For the present we have no data about the correlation between the rates of formation of low-and high molecular products, nor about the rate of direct hydrolysis. The transglucosilation by lysozyme implies at least three binding sites for the substrate. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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