Journals / Turkish Journal of Chemistry / 2020 / Cilt: 44 - Sayı: 6

Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods

Pages
1703–1712
Publication Date
2020-12-16
DOI
—
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AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

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.

📌 3 Key Takeaways

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Objective & Hypothesis: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.
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Key Findings & Data:The selectivity and the thermostability of EndoBI-1 and EndoBI-2 suggest that these enzymes may be useful for many scientific and industrial applications.
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Conclusion & Impact: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.
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:N-glycan · endo-β-N-acetylglucosaminidase · EndoBI-1

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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Cite This Article

SAHUTOGLU, A. S., DUMAN, H., FRESE, S. A., KARAV, S. (2020). Structural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods. Turkish Journal of Chemistry, Cilt: 44 - Sayı: 6, 1703–1712. https://ajindex.com/articles/208810

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