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

ŞAHUTOĞLU A. S., Duman H., Frese S. A., KARAV S.

TURKISH JOURNAL OF CHEMISTRY, cilt.44, sa.6, ss.1703-1715, 2020 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 44 Sayı: 6
  • Basım Tarihi: 2020
  • Doi Numarası: 10.3906/kim-2006-19
  • Dergi Adı: TURKISH JOURNAL OF CHEMISTRY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, TR DİZİN (ULAKBİM)
  • Sayfa Sayıları: ss.1703-1715
  • Anahtar Kelimeler: N-glycan, endo-beta-N-acetylglucosaminidase, EndoBI-1, EndoBI-2
  • Çanakkale Onsekiz Mart Üniversitesi Adresli: Evet

Özet

EndoBI-1 and EndoBI-2 are two endo-beta-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.