Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods |
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Authors: | Arif Sercan AHUTOLU Hatice DUMAN Steven Alex FRESE Sercan KARAV |
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Institution: | 1. Department of Chemistry, Faculty of Arts and Sciences, Çanakkale Onsekiz Mart University, Çanakkale, Turkey ; 2. Department of Molecular Biology and Genetics, Faculty of Arts and Sciences, Çanakkale Onsekiz Mart University, Çanakkale, Turkey ; 3. Evolve Biosystems, Inc., Davis, CA, USA ; 4. Department of Food Science and Technology, University of Nebraska, Lincoln, NE, USA |
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Abstract: | 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. |
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Keywords: | N
-glycan endo-
β -
N
-acetylglucosaminidase EndoBI-1 EndoBI-2 |
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