Synthesis of highly branched anionic α-glucans by thermostable phosphorylase-catalyzed α-glucuronylation

Takemoto, Yasutaka; Izawa, Hironori; Umegatani, Yuta; Yamamoto, Katsuhiro; Kubo, Akiko; Yanase, Michiyo; Takaha, Takeshi; Kadokawa, Jun‐ichi

doi:10.1016/j.carres.2012.11.007

Cited by 23 publications

(11 citation statements)

References 32 publications

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“…Kadokawa and co-workers have extensively investigated the flexibility of α-glucan phosphorylases towards the insertion of single or multiple non-cognate monosaccharides into maltooligosaccharides [37] , [38] , [39] , [40] , [41] , [42] . In particular, α-glucan phosphorylase from potato was able to effect single addition of GlcN onto maltotetraose [38] .…”

Section: Resultsmentioning

confidence: 99%

Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis

O’Neill

Pergolizzi

Stevenson

et al. 2017

Carbohydrate Research

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The GH94 glycoside hydrolase cellodextrin phosphorylase (CDP, EC 2.4.1.49) produces cellodextrin oligomers from short β-1→4-glucans and α-D-glucose 1-phosphate. Compared to cellobiose phosphorylase (CBP), which produces cellobiose from glucose and α-D-glucose 1-phosphate, CDP is biochemically less well characterised. Herein, we investigate the donor and acceptor substrate specificity of recombinant CDP from Ruminiclostridium thermocellum and we isolate and characterise a glucosamine addition product to the cellobiose acceptor with the non-natural donor α-D-glucosamine 1-phosphate. In addition, we report the first X-ray crystal structure of CDP, along with comparison to the available structures from CBPs and other closely related enzymes, which contributes to understanding of the key structural features necessary to discriminate between monosaccharide (CBP) and oligosaccharide (CDP) acceptor substrates.

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Section: Resultsmentioning

confidence: 99%

Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis

O’Neill

Pergolizzi

Stevenson

et al. 2017

Carbohydrate Research

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“…First, the glucuronylation of GD was carried out using the different equiv. for the number of non‐reducing ends (Table ) by thermostable phosphorylase catalysis according to the literature procedure previously reported by us to obtain the dendritic anionic α‐glucans . The products were isolated by dialysis of the reaction mixtures against water and lyophilization.…”

Section: Resultsmentioning

confidence: 99%

“…In addition to the recognizability of GlcN‐1‐P, we have also found that α‐ D ‐glucuronic acid 1‐phosphate (GlcA‐1‐P) could be used as a glycosyl donor in the enzymatic glucuronylation of maltotriose as a glycosyl acceptor by thermostable phosphorylase (from Aquifex aeolicus VF5) catalysis to produce an acidic tetrasaccharide having a GlcA unit as a carboxy group source at the non‐reducing end; maltotriose is a smallest acceptor for the thermostable phosphorylase catalysis . By means of the thermostable phosphorylase‐catalyzed glucuronylation, furthermore, dendritic anionic α‐glucans were synthesized by using highly branched cyclic dextrin (glucan dendrimer, GD) as a multifunctional glycosyl acceptor . GD is water‐soluble dextrin that is produced from amylopectin by the cyclization reaction of a branching enzyme (BE, EC 2.4.1.18) .…”

Section: Introductionmentioning

confidence: 99%

Enzymatic Synthesis of Dendritic Amphoteric α‐Glucans by Thermostable Phosphorylase Catalysis

Takata

Shimohigoshi

Yamamoto

et al. 2014

Macromolecular Bioscience

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This article reports the enzymatic synthesis of dendritic amphoteric α-glucans having both glucuronic acid and glucosamine residues at the non-reducing ends by thermostable phosphorylase-catalyzed successive glucuronylation and glucosaminylation of a glucan dendrimer having α-(1 → 4)-glucan non-reducing ends using α-D-glucuronic acid 1-phosphate and α-D-glucosamine 1-phosphate as glycosyl donors, respectively. The structure of the products is confirmed by the (1)H NMR analysis. The products exhibit inherent isoelectric points (pIs) determined by the ζ-potential measurement. These materials self-assemble in water at pH = pI to form large aggregates, but disassemble at pH shifted from pI.

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“…By means of the above-mentioned thermostable GP-catalyzed glucosaminylation and glucuronylation, amphoteric polysaccharides with highly branched structure, such as an amphoteric glycogen, having both the basic GlcN and acidic GlcA residues at the non-reducing ends, have been synthesized (Figure 4b) [52,53]. The thermostable GP-catalyzed glucuronylation using GlcA-1-P with highly branched polysaccharides has been conducted to produce acidic materials [54]. Then, the thermostable GP-catalyzed glucosaminylation using GlcN-1-P with the acidic products was performed to obtain amphoteric highly branched polysaccharides.…”

Section: Synthesis Of Non-natural Oligosaccharides By Phosphorylase-cmentioning

confidence: 99%

α-Glucan Phosphorylase-Catalyzed Enzymatic Reactions Using Analog Substrates to Synthesize Non-Natural Oligo- and Polysaccharides

Kadokawa

2018

Catalysts

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As natural oligo- and polysaccharides are important biomass resources and exhibit vital biological functions, non-natural oligo- and polysaccharides with a well-defined structure can be expected to act as new functional materials with specific natures and properties. α-Glucan phosphorylase (GP) is one of the enzymes that have been used as catalysts for practical synthesis of oligo- and polysaccharides. By means of weak specificity for the recognition of substrates by GP, non-natural oligo- and polysaccharides has precisely been synthesized. GP-catalyzed enzymatic glycosylations using several analog substrates as glycosyl donors have been carried out to produce oligosaccharides having different monosaccharide residues at the non-reducing end. Glycogen, a highly branched natural polysaccharide, has been used as the polymeric glycosyl acceptor and primer for the GP-catalyzed glycosylation and polymerization to obtain glycogen-based non-natural polysaccharide materials. Under the conditions of removal of inorganic phosphate, thermostable GP-catalyzed enzymatic polymerization of analog monomers occurred to give amylose analog polysaccharides.

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Synthesis of highly branched anionic α-glucans by thermostable phosphorylase-catalyzed α-glucuronylation

Cited by 23 publications

References 32 publications

Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis

Cellodextrin phosphorylase from Ruminiclostridium thermocellum: X-ray crystal structure and substrate specificity analysis

Enzymatic Synthesis of Dendritic Amphoteric α‐Glucans by Thermostable Phosphorylase Catalysis

α-Glucan Phosphorylase-Catalyzed Enzymatic Reactions Using Analog Substrates to Synthesize Non-Natural Oligo- and Polysaccharides

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