ArticleBMC biochemistry2008
Functional role of the additional domains in inulosucrase (IslA) from Leuconostoc citreum CW28.
Article in BMC biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 27 citations in OpenAlex.
- Cold induced expression of a novel levansucrase gene sacB1 enhances exopolysaccharide production and stress resilience in Leuconostoc mesenteroides.Scientific reports · 2025Article
- Multidomain chimeric enzymes as a promising alternative for biocatalysts improvement: a minireview.Molecular biology reports · 2024Review
- Structure-Function Relationship Studies of Multidomain Levansucrases from Leuconostocaceae Family.Microorganisms · 2022Article
- Characterization of a Novel Fructosyltransferase from Lactobacillus crispatus, InuCA, That Attaches to the Cell Surface by Electrostatic Interaction.Applied and environmental microbiology · 2022Article
- Functional and Molecular Characterization of theMicroorganisms · 2021Article
- Extracellular polysaccharides produced by bacteria of the Leuconostoc genus.World journal of microbiology & biotechnology · 2020Review
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- Synthesis of Fructooligosaccharides by IslA4, a truncated inulosucrase from Leuconostoc citreum.BMC biotechnology · 2015Article
- Design of chimeric levansucrases with improved transglycosylation activity.Applied and environmental microbiology · 2012Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundInulosucrase (IslA) from Leuconostoc citreum CW28 belongs to a new subfamily of multidomain fructosyltransferases (FTFs), containing additional domains from glucosyltransferases. It is not known what the function of the additional domains in this subfamily is.
resultsThrough construction of truncated versions we demonstrate that the acquired regions are involved in anchoring IslA to the cell wall; they also confer stability to the enzyme, generating a larger structure that affects its kinetic properties and reaction specificity, particularly the hydrolysis and transglycosylase ratio. The accessibility of larger molecules such as EDTA to the catalytic domain (where a Ca2+ binding site is located) is also affected as demonstrated by the requirement of 100 times higher EDTA concentrations to inactivate IslA with respect to the smallest truncated form.
conclusionThe C-terminal domain may have been acquired to anchor inulosucrase to the cell surface. Furthermore, the acquired domains in IslA interact with the catalytic core resulting in a new conformation that renders the enzyme more stable and switch the specificity from a hydrolytic to a transglycosylase mechanism. Based on these results, chimeric constructions may become a strategy to stabilize and modulate biocatalysts based on FTF activity.
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