SwePub
Sök i LIBRIS databas

  Extended search

WFRF:(Hansen Anders Lønstrup)
 

Search: WFRF:(Hansen Anders Lønstrup) > Engineering Bifidob...

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist
  • Hansen, Dennis K.University of Copenhagen (author)

Engineering Bifidobacterium longum Endo-α-N-acetylgalactosaminidase for Neu5Acα2-3Galβ1-3GalNAc reactivity on Fetuin

  • Article/chapterEnglish2022

Publisher, publication year, extent ...

  • Elsevier BV,2022

Numbers

  • LIBRIS-ID:oai:lup.lub.lu.se:0f4e3ce3-c73d-4f1e-bb79-98f72d7494bf
  • https://lup.lub.lu.se/record/0f4e3ce3-c73d-4f1e-bb79-98f72d7494bfURI
  • https://doi.org/10.1016/j.abb.2022.109280DOI

Supplementary language notes

  • Language:English
  • Summary in:English

Part of subdatabase

Classification

  • Subject category:art swepub-publicationtype
  • Subject category:ref swepub-contenttype

Notes

  • Endo-α-N-acetylgalactosaminidase from Bifidobacterium longum (EngBF) belongs to the glycoside hydrolase family GH101 and has a strict preference towards the mucin type glycan, Galβ1-3GalNAc, which is O-linked to serine or threonine residues on glycopeptides and -proteins. While other enzymes of the GH101 family exhibit a wider substrate spectrum, no GH101 member has until recently been reported to process the α2-3 sialidated mucin glycan, Neu5Acα2-3Galβ1-3GalNAc. However, work published by others (ACS Chem Biol 2021, 16, 2004–2015) during the preparation of the present manuscript demonstrated that the enzymes from several bacteria are able to hydrolyze this glycan from the fluorophore, methylumbelliferyl. Based on molecular docking using the EngBF homolog, EngSP from Streptococcus pneumoniae, substitution of active site amino acid residues with the potential to allow for accommodation of Neu5Acα2-3Galβ1-3GalNAc were identified. Based on this analysis, the mutant EngBF variants W750A, Q894A, K1199A, E1294A and D1295A were prepared and tested, for activity towards the Neu5Acα2-3Galβ1-3GalNAc O-linked glycan present on bovine fetuin. Among the mutant EngBF variants listed above, only E1294A was shown to release Neu5Acα2-3Galβ1-3GalNAc from fetuin, which subsequently was also demonstrated for the substitutions: E1294 M, E1294H and E1294K. In addition, the kcat/KM of the EngBF variants for cleavage of the Neu5Acα2-3Galβ1-3GalNAc glycan increased between 5 and 70 times from pH 4.5 to pH 6.0.

Subject headings and genre

Added entries (persons, corporate bodies, meetings, titles ...)

  • Hansen, Anders LønstrupUniversity of Copenhagen (author)
  • Koivisto, Johanna M.University of Copenhagen (author)
  • Shuoker, BasharTechnical University of Denmark (author)
  • Abou Hachem, MaherLund University,Lunds universitet,Bioteknik,Centrum för tillämpade biovetenskaper,Kemiska institutionen,Institutioner vid LTH,Lunds Tekniska Högskola,Biotechnology,Center for Applied Life Sciences,Department of Chemistry,Departments at LTH,Faculty of Engineering, LTH,Technical University of Denmark(Swepub:lu)biot-mah (author)
  • Winther, Jakob R.University of Copenhagen (author)
  • Willemoës, MartinUniversity of Copenhagen (author)
  • University of CopenhagenTechnical University of Denmark (creator_code:org_t)

Related titles

  • In:Archives of Biochemistry and Biophysics: Elsevier BV7250003-9861

Internet link

Find in a library

To the university's database

  • 1 of 1
  • Previous record
  • Next record
  •    To hitlist

Kungliga biblioteket hanterar dina personuppgifter i enlighet med EU:s dataskyddsförordning (2018), GDPR. Läs mer om hur det funkar här.
Så här hanterar KB dina uppgifter vid användning av denna tjänst.

 
pil uppåt Close

Copy and save the link in order to return to this view