Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods
| Autor: | Arif Sercan Şahutoğlu, Hatice Duman, Steven A. Frese, Sercan Karav |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
Bifidobacterium longum
Chemistry Multidisciplinary In silico 010402 general chemistry 01 natural sciences Isozyme Article endo- β - N -acetylglucosaminidase N -glycan Glycoside hydrolase Glucosaminidase N-glycan endo-β-N-acetylglucosaminidase EndoBI-1 EndoBI-2 Thermostability chemistry.chemical_classification biology 010405 organic chemistry EndoBI-2 EndoBI-1 General Chemistry biology.organism_classification 0104 chemical sciences Enzyme chemistry Biochemistry Docking (molecular) Kimya Ortak Disiplinler |
| Zdroj: | Turkish Journal of Chemistry Volume: 44, Issue: 6 1703-1712 |
| ISSN: | 1303-6130 1300-0527 |
| Popis: | EndoBI-1 and EndoBI-2 are two endo- β-N- acetylglucosaminidase isoenzymes that cleave N-N’- diacetylchitobiosyl moieties found in various types of native N -glycans. These N -glycans are indigestible by human infants and adults due to the lack of responsible glycosyl hydrolases and they act as selective prebiotics for a probiotic microorganism, Bifidobacterium longum subsp . infantis , in the large intestine. The selectivity and the thermostability of EndoBI-1 and EndoBI-2 suggest that these enzymes may be useful for many scientific and industrial applications. In this study, the growing numbers of homologous sequences in different databases were exploited in a comparative approach to investigate structural properties of EndoBI-1 and EndoBI-2 enzymes. Moreover, the complete and partial homology models of these two enzymes were generated and evaluated. Selected models were used for docking studies of the plus subsite ligand of these enzymes for further understanding on the substrate selectivity of EndoBI enzymes. |
| Databáze: | OpenAIRE |
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