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

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dc.authoridDuman, Hatice/0000-0002-4526-6609
dc.authoridKARAV, SERCAN/0000-0003-4056-1673
dc.authoridSAHUTOGLU, Arif Sercan/0000-0003-1183-3553
dc.authoridFrese, Steven/0000-0003-2053-5830
dc.contributor.authorSahutoglu, Arif Sercan
dc.contributor.authorDuman, Hatice
dc.contributor.authorFrese, Steven Alex
dc.contributor.authorKarav, Sercan
dc.date.accessioned2025-01-27T20:53:52Z
dc.date.available2025-01-27T20:53:52Z
dc.date.issued2020
dc.departmentÇanakkale Onsekiz Mart Üniversitesi
dc.description.abstractEndoBI-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.
dc.description.sponsorshipEvolve Biosystems Inc.
dc.description.sponsorshipThis study is funded by Evolve Biosystems Inc. Molecular dynamic calculations reported in this study were fully performed at TUBITAK ULAKBIM, High Performance and Grid Computing Center (TRUBA resources).
dc.identifier.doi10.3906/kim-2006-19
dc.identifier.endpage+
dc.identifier.issn1300-0527
dc.identifier.issue6
dc.identifier.pmid33488263
dc.identifier.scopus2-s2.0-85098482779
dc.identifier.scopusqualityQ3
dc.identifier.startpage1703
dc.identifier.trdizinid525393
dc.identifier.urihttps://doi.org/10.3906/kim-2006-19
dc.identifier.urihttps://search.trdizin.gov.tr/tr/yayin/detay/525393
dc.identifier.urihttps://hdl.handle.net/20.500.12428/25878
dc.identifier.volume44
dc.identifier.wosWOS:000599807000022
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakTR-Dizin
dc.indekslendigikaynakPubMed
dc.language.isoen
dc.publisherTubitak Scientific & Technological Research Council Turkey
dc.relation.ispartofTurkish Journal of Chemistry
dc.relation.publicationcategoryinfo:eu-repo/semantics/openAccess
dc.rightsinfo:eu-repo/semantics/openAccess
dc.snmzKA_WoS_20250125
dc.subjectN-glycan
dc.subjectendo-beta-N-acetylglucosaminidase
dc.subjectEndoBI-1
dc.subjectEndoBI-2
dc.titleStructural insights of two novel N-acetyl-glucosaminidase enzymes through in silico methods
dc.typeArticle

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