ArticleThe Journal of biological chemistry2012
Structural elucidation of dextran degradation mechanism by streptococcus mutans dextranase belonging to glycoside hydrolase family 66.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 55 citations in OpenAlex.
- Structural and functional characterisation of the dextran utilisome fromJournal of structural biology: X · 2026Article
- Unique ecology of co-occurring functionally and phylogenetically undescribed species in the infant oral microbiome.PLoS computational biology · 2026Article
- Revisiting the endo and exo mode of action of dextran hydrolyzing enzymes, and their significance for Streptococcus mutans biofilm eradication.World journal of microbiology & biotechnology · 2025Article
- The impact of a-tomatine on shear bonding strength in different dentin types and on cariogenic microorganisms: an in vitro and in silico study.BMC oral health · 2024Article
- Biochemical properties of a Flavobacterium johnsoniae dextranase and its biotechnological potential for Streptococcus mutans biofilm degradation.World journal of microbiology & biotechnology · 2024Article
- Leuconostoc mesenteroides and Liquorilactobacillus mali strains, isolated from Algerian food products, are producers of the postbiotic compounds dextran, oligosaccharides and mannitol.World journal of microbiology & biotechnology · 2024Article
- Identification and Characterization of Dextran α-1,2-Debranching Enzyme fromJournal of applied glycoscience · 2023Article
- Regulatory mechanisms of exopolysaccharide synthesis and biofilm formation in Streptococcus mutans.Journal of oral microbiology · 2023Review
- Study of key amino acid residues of GH66 dextranase for producing high-degree polymerized isomaltooligosaccharides and improving of thermostability.Frontiers in bioengineering and biotechnology · 2022Article
- DexA70, the Truncated Form of a Self-Produced Dextranase, Effectively DisruptsFrontiers in microbiology · 2021Article
- Purification, Characterization, and Hydrolysate Analysis of Dextranase FromFrontiers in bioengineering and biotechnology · 2021Article
- Isomaltooligosaccharide-binding structure ofBioscience reports · 2017Article
- Structural advantage of sugar beet α-glucosidase to stabilize the Michaelis complex with long-chain substrate.The Journal of biological chemistry · 2015Article
- Structural elucidation of the cyclization mechanism of α-1,6-glucan by Bacillus circulans T-3040 cycloisomaltooligosaccharide glucanotransferase.The Journal of biological chemistry · 2014Article
- Crystallization and preliminary X-ray crystallographic analysis of cycloisomaltooligosaccharide glucanotransferase from Bacillus circulans T-3040.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
- Structural basis for biofilm formation via the Vibrio cholerae matrix protein RbmA.Journal of bacteriology · 2013Article
- Novel dextranase catalyzing cycloisomaltooligosaccharide formation and identification of catalytic amino acids and their functions using chemical rescue approach.The Journal of biological chemistry · 2012Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dextranase is an enzyme that hydrolyzes dextran α-1,6 linkages. Streptococcus mutans dextranase belongs to glycoside hydrolase family 66, producing isomaltooligosaccharides of various sizes and consisting of at least five amino acid sequence regions. The crystal structure of the conserved fragment from Gln(100) to Ile(732) of S. mutans dextranase, devoid of its N- and C-terminal variable regions, was determined at 1.6 Å resolution and found to contain three structural domains. Domain N possessed an immunoglobulin-like β-sandwich fold; domain A contained the enzyme's catalytic module, comprising a (β/α)(8)-barrel; and domain C formed a β-sandwich structure containing two Greek key motifs. Two ligand complex structures were also determined, and, in the enzyme-isomaltotriose complex structure, the bound isomaltooligosaccharide with four glucose moieties was observed in the catalytic glycone cleft and considered to be the transglycosylation product of the enzyme, indicating the presence of four subsites, -4 to -1, in the catalytic cleft. The complexed structure with 4',5'-epoxypentyl-α-d-glucopyranoside, a suicide substrate of the enzyme, revealed that the epoxide ring reacted to form a covalent bond with the Asp(385) side chain. These structures collectively indicated that Asp(385) was the catalytic nucleophile and that Glu(453) was the acid/base of the double displacement mechanism, in which the enzyme showed a retaining catalytic character. This is the first structural report for the enzyme belonging to glycoside hydrolase family 66, elucidating the enzyme's catalytic machinery.
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