Biochemical Characterization of a Glycosyltransferase Homolog from an Oral Pathogen Fusobacterium nucleatum as a Human Glycan-modifying Enzymeopen access
- Authors
- Kim, Seonghun; Oh, Doo-Byoung; Kwon, Ohsuk; Jung, Jae Kap; Lee, Yun Mi; Ko, Kisung; Ko, Jeong Heon; Kang, Hyun Ah
- Issue Date
- May-2008
- Publisher
- 한국미생물·생명공학회
- Keywords
- Glycosyltransferase; nucleotide-sugar; Fusobacterium nucleatum; human-type N-linked glycan
- Citation
- Journal of Microbiology and Biotechnology, v.18, no.5, pp 859 - 865
- Pages
- 7
- Journal Title
- Journal of Microbiology and Biotechnology
- Volume
- 18
- Number
- 5
- Start Page
- 859
- End Page
- 865
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57516
- ISSN
- 1017-7825
1738-8872
- Abstract
- Bacterial glycosyltransferases have drawn growing attention as economical enzymes for oligosaccharide synthesis, with their easy expression and relatively broad substrate specificity. Here, we characterized a glycosyltransferase homolog (Fnu_GT) from a human oral pathogen, Fusobacterium nucleatum. Bioinformatic analysis showed that Fnu_GT belongs to the glycosyltransferases family II. The recombinant Fnu_GT (rFnu_GT) expressed in Escherichia coli displayed the highest glycosylation activity when UDP-galactose (Gal) was used as a donor nucleotide-sugar with heptose or N-acetylglucosamine (GlcNAc) as an acceptor sugar. Interestingly, rFnu_GT transferred the galactose moiety of UDP-Gal to a nonreducing terminal GlcNAc attached to the trimannosyl core glycan, indicating its potential as an enzyme for human-type N-glycan synthesis.
- Files in This Item
-
- Appears in
Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.