ArticleJournal of bacteriology2005
Role of the two catalytic domains of DSR-E dextransucrase and their involvement in the formation of highly alpha-1,2 branched dextran.
Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 76 citations in OpenAlex.
- Dual-Activity Mannosyltransferase Phosphorylases in Family 130 of Glycoside Hydrolases.ACS catalysis · 2026Article
- One-step enzymatic synthesis of medium molecular weight dextran using engineered dextransucrase DarM fromFrontiers in microbiology · 2026Article
- The Discovery, Molecular Cloning, and Characterization of DextransucraseMolecules (Basel, Switzerland) · 2024Article
- Architecture, Function, Regulation, and Evolution of α-Glucans Metabolic Enzymes in Prokaryotes.Chemical reviews · 2024Review
- In Silico Analysis of the Dextransucrase Obtained FromBioinformatics and biology insights · 2023Article
- Exopolysaccharides Produced by Lactic Acid Bacteria: From Biosynthesis to Health-Promoting Properties.Foods (Basel, Switzerland) · 2022Review
- Bacterial α-Glucan and Branching Sucrases from GH70 Family: Discovery, Structure-Function Relationship Studies and Engineering.Microorganisms · 2021Review
- Unravelling Regioselectivity ofInternational journal of molecular sciences · 2021Article
- Redirecting substrate regioselectivity using engineered ΔNScientific reports · 2021Article
- Harnessing glycoenzyme engineering for synthesis of bioactive oligosaccharides.Interface focus · 2019Review
- Synthesis of glucooligosaccharides with prebiotic potential by glucansucrase URE 13-300 acceptor reactions with maltose, raffinose and lactose.Engineering in life sciences · 2018Article
- Engineering a branching sucrase for flavonoid glucoside diversification.Scientific reports · 2018Article
- Molecular and Functional Study of a Branching Sucrase-Like Glucansucrase Reveals an Evolutionary Intermediate between Two Subfamilies of the GH70 Enzymes.Applied and environmental microbiology · 2018Article
- Combining multi-scale modelling methods to decipher molecular motions of a branching sucrase from glycoside-hydrolase family 70.PloS one · 2018Article
- 4,3-α-Glucanotransferase, a novel reaction specificity in glycoside hydrolase family 70 and clan GH-H.Scientific reports · 2017Article
- Gsy, a novel glucansucrase from Leuconostoc mesenteroides, mediates the formation of cell aggregates in response to oxidative stress.Scientific reports · 2016Article
- Immobilization of Glycoside Hydrolase Families GH1, GH13, and GH70: State of the Art and Perspectives.Molecules (Basel, Switzerland) · 2016Review
- Structure-function relationships of family GH70 glucansucrase and 4,6-α-glucanotransferase enzymes, and their evolutionary relationships with family GH13 enzymes.Cellular and molecular life sciences : CMLS · 2016Review
- GH13 amylosucrases and GH70 branching sucrases, atypical enzymes in their respective families.Cellular and molecular life sciences : CMLS · 2016Review
- Characterization of the First α-(1→3) Branching Sucrases of the GH70 Family.The Journal of biological chemistry · 2016Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The dsrE gene from Leuconostoc mesenteroides NRRL B-1299 was shown to encode a very large protein with two potentially active catalytic domains (CD1 and CD2) separated by a glucan binding domain (GBD). From sequence analysis, DSR-E was classified in glucoside hydrolase family 70, where it is the only enzyme to have two catalytic domains. The recombinant protein DSR-E synthesizes both alpha-1,6 and alpha-1,2 glucosidic linkages in transglucosylation reactions using sucrose as the donor and maltose as the acceptor. To investigate the specific roles of CD1 and CD2 in the catalytic mechanism, truncated forms of dsrE were cloned and expressed in Escherichia coli. Gene products were then small-scale purified to isolate the various corresponding enzymes. Dextran and oligosaccharide syntheses were performed. Structural characterization by (13)C nuclear magnetic resonance and/or high-performance liquid chromatography showed that enzymes devoid of CD2 synthesized products containing only alpha-1,6 linkages. On the other hand, enzymes devoid of CD1 modified alpha-1,6 linear oligosaccharides and dextran acceptors through the formation of alpha-1,2 linkages. Therefore, each domain is highly regiospecific, CD1 being specific for the synthesis of alpha-1,6 glucosidic bonds and CD2 only catalyzing the formation of alpha-1,2 linkages. This finding permitted us to elucidate the mechanism of alpha-1,2 branching formation and to engineer a novel transglucosidase specific for the formation of alpha-1,2 linkages. This enzyme will be very useful to control the rate of alpha-1,2 linkage synthesis in dextran or oligosaccharide production.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.