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

Takata, Yusei; Shimohigoshi, Riko; Yamamoto, Katsuhiro; Kadokawa, Jun‐ichi

doi:10.1002/mabi.201400204

Cited by 23 publications

(25 citation statements)

References 33 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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“…The monomer, GlcN‐1‐P, was synthesized according to the literature procedure . Thermostable phosphorylase from Aquifex aeolicus VF5 was kindly supplied by Ezaki Glico Co. Ltd., Osaka, Japan .…”

Section: Methodsmentioning

confidence: 99%

“…The monomer, GlcN-1-P, was synthesized according to the literature procedure. 34 Thermostable phosphorylase from Aquifex aeolicus VF5 was kindly supplied by Ezaki Glico Co. Ltd., Osaka, Japan. 23,35,36 Maltotriose (Glc 3 ) was purchased from Hayashibara Co. Ltd., Okayama, Japan.…”

Section: Methodsmentioning

confidence: 99%

Hierarchically controlled assemblies from amylose analog aminopolysaccharides by reductive amination: From nano‐ to macrostructures

Nakauchida

Yamamoto

Kadokawa

2017

J of Applied Polymer Sci

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In this study, we found that hierarchically controlled assemblies from amylose analog aminopolysaccharides occurred by reductive amination to obtain nanoparticles, microaggregates, and macrohydrogels depending on reaction conditions. The polysaccharide substrate composed of α(1→4)‐linked glucosamine residues was synthesized by thermostable phosphorylase (from Aquifex aeolicus VF5)–catalyzed enzymatic polymerization of α‐d‐glucosamine 1‐phosphate according to the reaction manner reported in our previous study. The reductive amination of the produced polysaccharide was carried out in the presence of NaBH3CN as reductant in 0.1 mol/L acetic acid aq. at 60 °C for 1 h. When lower feed ratios of reductant to the reducing end of the substrate were employed for the reaction, nanoparticles were obtained. With increasing feed ratios of reductant, more α(1→4)‐GlcNn molecules assembled to further form water‐insoluble microaggregates and macrohydrogels. © 2017 Wiley Periodicals, Inc. J. Appl. Polym. Sci. 2018, 135, 45890.

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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].…”

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

Cited by 23 publications

References 33 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

Hierarchically controlled assemblies from amylose analog aminopolysaccharides by reductive amination: From nano‐ to macrostructures

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

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