Transglycosylation specificity of Acremonium sp. α-rhamnosyl-β-glucosidase and its application to the synthesis of the new fluorogenic substrate 4-methylumbelliferyl-rutinoside

Mazzaferro, Laura S.; Piñuel, Lucrecia; Erra‐Balsells, Rosa; Giudicessi, Silvana L.; Breccia, Javier D.

doi:10.1016/j.carres.2011.11.008

Cited by 27 publications

(37 citation statements)

References 30 publications

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“…Substrates catalyzed by glycoside hydrolase, such as sucrose and starch as glycosyl donors, are relatively inexpensive [18,47]. Many glycoside hydrolases have been employed in enzymatic transglycosylation reactions [28,42]. β-Glucosidases from bacterial or fungal origin possess significant transglycosylation activity in addition to hydrolytic properties.…”

Section: Introductionmentioning

confidence: 99%

“…A fungal α-rhamnosyl-βglucosidase from Acremonium sp. showed transglycosylation activity with broad acceptor specificity toward aliphatic and aromatic alcohols and the ability to synthesize the diglycoconjugated fluorogenic substrate 4-methylumbelliferylrutinoside [28]. Some hydrolytic enzymes in glycoside hydrolase (GH) family 13, including cyclodextrin glucanotransferase (CGTase), maltogenic amylase, maltodextrin glucosidase, and amylosucrase (ASase), were shown to have significant transglycosylation activity by forming an α-glycosidic linkage [42].…”

Section: Introductionmentioning

confidence: 99%

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Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

Kim¹,

Jung²,

Seo³

et al. 2016

Journal of Microbiology and Biotechnology

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The transglycosylation activity of amylosucrase (ASase) has received significant attention owing to its use of an inexpensive donor, sucrose, and broad acceptor specificity, including glycone and aglycone compounds. The transglycosylation reaction of recombinant ASase from (DRpAS) was investigated using various phenolic compounds, and quercetin-3--rutinoside (rutin) was found to be the most suitable acceptor molecule used by DRpAS. Two amino acid residues in DRpAS variants (DRpAS Q299K and DRpAS Q299R), assumed to be involved in acceptor binding, were constructed by site-directed mutagenesis. Intriguingly, DRpAS Q299K and DRpAS Q299R produced 10-fold and 4-fold higher levels of rutin transglycosylation product than did the wild-type (WT) DRpAS, respectively. According to in silico molecular docking analysis, the lysine residue at position 299 in the mutants enables rutin to more easily position inside the active pocket of the mutant enzyme than in that of the WT, due to conformational changes in loop 4.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

Kim¹,

Jung²,

Seo³

et al. 2016

Journal of Microbiology and Biotechnology

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show abstract

“…This approach was extended to more complex 4-methylumbelliferyl fluorogenic glycosides, such as di-, triand oligosaccharides [62][63][64][65][66][67], and challenging monosaccharides such as sialic acids [68][69][70]. 4-Methylumbelliferyl aglycone analogues were also explored to better suit the properties of glycosidases [71][72][73][74].…”

Section: Fluorogenic Glycosidase Substratesmentioning

confidence: 99%

Fluorescently labelled glycans and their applications

Yan

Yalagala

Yan³

2015

Glycoconj J

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This review summarises the literature on the synthesis and applications of fluorescently labelled carbohydrates. Due to the sensitivity of fluorescent detection, this approach provides a useful tool to study processes involving glycans. A few general categories of labelling are presented, in situ labelling of carbohydrates with fluorophores, fluorescently labelled glycolipids, fluorogenic glycans, pre-formed fluorescent glycans for intracellular applications, glycan-decorated fluorescent polymers, fluorescent glyconanoparticles, and other functional fluorescent glycans.

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“…This enzyme allowed the synthesis of the diglycoconjugated fluorogenic substrate 4-methylumbelliferyl-rutinoside. The synthesis was performed in one step from the corresponding aglycone, 4-methylumbelliferone, and hesperidin as rutinose donor with a 16% yield regarding the sugar acceptor [38]. Despite the low yield, the fluorogenic substrate formed, 4-methylumbelliferyl rutinoside (Figure 4), which is not commercially available, is important for the study of diglycosidases since it allows the detection of enzymes specific for rutinose mobilization.…”

Section: Natural Enzymes For the Synthesis Of Glycosidic Linkagesmentioning

confidence: 99%

Angling for Uniqueness in Enzymatic Preparation of Glycosides

Trincone

2013

Biomolecules

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In the early days of biocatalysis, limitations of an enzyme modeled the enzymatic applications; nowadays the enzyme can be engineered to be suitable for the process requirements. This is a general bird’s-eye view and as such cannot be specific for articulated situations found in different classes of enzymes or for selected enzymatic processes. As far as the enzymatic preparation of glycosides is concerned, recent scientific literature is awash with examples of uniqueness related to the features of the biocatalyst (yield, substrate specificity, regioselectivity, and resistance to a particular reaction condition). The invention of glycosynthases is just one of the aspects that has thrust forward the research in this field. Protein engineering, metagenomics and reaction engineering have led to the discovery of an expanding number of novel enzymes and to the setting up of new bio-based processes for the preparation of glycosides. In this review, new examples from the last decade are compiled with attention both to cases in which naturally present, as well as genetically inserted, characteristics of the catalysts make them attractive for biocatalysis.

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Transglycosylation specificity of Acremonium sp. α-rhamnosyl-β-glucosidase and its application to the synthesis of the new fluorogenic substrate 4-methylumbelliferyl-rutinoside

Cited by 27 publications

References 30 publications

Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

Acceptor Specificity of Amylosucrase from Deinococcus radiopugnans and Its Application for Synthesis of Rutin Derivatives

Fluorescently labelled glycans and their applications

Angling for Uniqueness in Enzymatic Preparation of Glycosides

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