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Cited by 13Carbohydrate Chemistry and SynthesisPolysaccharides Composition and ApplicationsPolysaccharides and Plant Cell Walls

The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.

Functional and structural analysis of a cyclization domain in a cyclic β-1,2-glucan synthase

Open access
Tanaka, Nobukiyo, Saito, Ryotaro, Kobayashi, Kaito, Nakai, Hiroyuki, Kamo, Shogo, Kuramochi, Kouji, Taguchi, Hayao, Nakajima, Masahiro, Masaike, Tomoko·2024·Applied Microbiology and Biotechnology
DOI 10.1007/s00253-024-13013-9

Published version of a preprint

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Abstract

Cyclic β-1,2-glucan synthase (CGS) is a key enzyme in production of cyclic β-1,2-glucans (CβGs) which are involved in bacterial infection or symbiosis to host organisms. Nevertheless, a mechanism of cyclization, the final step in the CGS reaction, has not been fully understood. Here we performed functional and structural analyses of the cyclization domain of CGS alone from Thermoanaerobacter italicus (TiCGS Cy ). We first found that β-glucosidase-resistant compounds are produced by TiCGS Cy with linear β-1,2-glucans as substrates. The 1 H-NMR analysis revealed that these products are CβGs. Next, action pattern analyses using β-1,2-glucooligosaccharides revealed a unique reaction pattern: exclusive transglycosylation without hydrolysis and a hexasaccharide being the minimum length of the substrate. These analyses also showed that longer substrate β-1,2-glucooligosaccharides are preferred, being consistent with the fact that CGSs generally produce CβGs with degrees of polymerization of around 20. Finally, the overall structure of the cyclization domain of TiCGS Cy was found to be similar to those of β-1,2-glucanases in phylogenetically different groups. Meanwhile, the identified catalytic residues indicated clear differences in the reaction pathways between these enzymes. Overall, we propose a novel reaction mechanism of TiCGS Cy . Thus, the present group of CGSs defines a new glycoside hydrolase family, GH189. Key points: • It was clearly evidenced that cyclization domain alone produces cyclic β-1,2-glucans . • The domain exclusively catalyzes transglycosylation without hydrolysis . • The present catalytic domain defines as a new glycoside hydrolase family 189 . Graphical Abstract:

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Research works printed but not linked: 1

  1. de Grotthuss CJT (1806) Sur la décomposition de l’eau et des corps qu’elle tient en dissolution à l’aide de l’électricité galvanique. Ann Chim 58:54–73

Metadata

Authors
Tanaka, N., Saito, R., Kobayashi, K., Nakai, H., Kamo, S., Kuramochi, K., Taguchi, H., Nakajima, M., & Masaike, T.
Affiliations
  • Tokyo University of Science (JP)
  • Artificial Intelligence Research Center (JP)
  • Niigata University (JP)
Corresponding author
  • Tanaka, Nobukiyo
  • Nakajima, Masahiro
  • Masaike, Tomoko
ORCID
Venue
Applied Microbiology and Biotechnology
Publisher
Springer Science and Business Media LLC
Published
2024-02-01
Volume
108
Issue
1
Pages
187-187
ISSN
  • 0175-7598 (ISSN-L)
  • 1432-0614
DOI
10.1007/s00253-024-13013-9
OpenAlex
W4391448277
Cited by
13
References
52
Citations by year
2026: 3 · 2025: 6 · 2024: 4
FWCI
1.88
Type
journal article
Language
en
Open access
Licence
Locations
  • Applied Microbiology and Biotechnology (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Funders
Tokyo University of Science
Topics
  • Physical Sciences › Chemistry › Organic Chemistry › Carbohydrate Chemistry and Synthesis
  • Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Polysaccharides and Plant Cell Walls
Keywords
transglycosylation, substrate specificity, catalytic residues, enzyme mechanism
MeSH terms
Catalysis, Cyclization, Glucans, Glycoside Hydrolases, beta-Glucans

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