Enzymatic Glycosylation by Glycohydrolases and Glycosynthases

Thimm, Julian; Thiem, Joachim

doi:10.1007/978-3-540-30429-6_33

Cited by 11 publications

(6 citation statements)

References 111 publications

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“…Enzymes involved in the synthesis of polysaccharides via enzymatic glycosylations are categorized into two main classes: glycosyltransferases (EC 2.4) 362 and hydrolases (glycosidases, vide infra, 6.1). 363 Glycosyltransferase catalyzes the transfer of a sugar moiety from an activated donor onto both saccharide and nonsaccharide acceptors. They are divided into the Leloir and non-Leloir types according to the types of glycosyl donors.…”

Section: Glycosyltransferasesmentioning

confidence: 99%

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

et al. 2016

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The present article comprehensively reviews the macromolecular synthesis using enzymes as catalysts. Among the six main classes of enzymes, the three classes, oxidoreductases, transferases, and hydrolases, have been employed as catalysts for the in vitro macromolecular synthesis and modification reactions. Appropriate design of reaction including monomer and enzyme catalyst produces macromolecules with precisely controlled structure, similarly as in vivo enzymatic reactions. The reaction controls the product structure with respect to substrate selectivity, chemo-selectivity, regio-selectivity, stereoselectivity, and choro-selectivity. Oxidoreductases catalyze various oxidation polymerizations of aromatic compounds as well as vinyl polymerizations. Transferases are effective catalysts for producing polysaccharide having a variety of structure and polyesters. Hydrolases catalyzing the bond-cleaving of macromolecules in vivo, catalyze the reverse reaction for bond forming in vitro to give various polysaccharides and functionalized polyesters. The enzymatic polymerizations allowed the first in vitro synthesis of natural polysaccharides having complicated structures like cellulose, amylose, xylan, chitin, hyaluronan, and chondroitin. These polymerizations are "green" with several respects; nontoxicity of enzyme, high catalyst efficiency, selective reactions under mild conditions using green solvents and renewable starting materials, and producing minimal byproducts. Thus, the enzymatic polymerization is desirable for the environment and contributes to "green polymer chemistry" for maintaining sustainable society.

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Section: Glycosyltransferasesmentioning

confidence: 99%

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

et al. 2016

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“…In this study, we describe the enzymatic glycosylation approach for the synthesis of the chitin/chitosan stereoisomers, as it is a powerful and efficient technique for the connection of two unprotected glycosyl substrates (one donor and one acceptor), by a stereo-and regio-controlled glycosidic linkage. 11,12 Furthermore, enzymatic glycosylations have been employed for enzymatic polymerization according to the successive reaction manner for the production of polysaccharides, [13][14][15][16][17] such as the first report of the synthesis of cellulose via cellulase-catalyzed enzymatic polymerization by Kobayashi et al 18 By means of such reverse reactions catalyzed by glycosyl hydrolases such as cellulase, the enzymatic polymerization of monomers composed of both the glycosyl donor and acceptor structures in a molecule, yielded not only cellulose and its derivatives, 19 but also aminopolysaccharides. These aminopolysaccharides include chitin, glycosaminoglycans, and other related non-natural analogs, [20][21][22][23] where the structures are composed mainly of β-glycosidic linkages.…”

Section: Introductionmentioning

confidence: 99%

Synthesis of chitin and chitosan stereoisomers by thermostable α-glucan phosphorylase-catalyzed enzymatic polymerization of α-d-glucosamine 1-phosphate

et al. 2015

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The relationship between two aminopolysaccharide stereoisomers, namely α-(1→4)- and β-(1→4)-linked (N-acetyl)-D-glucosamine polymers, is of significant interest within the field of polysaccharide science, as they correspond to amino analogs of the representative abundant natural polysaccharides, viz. amylose and cellulose. While the latter glucosamine polymer is the basis of well-known natural polysaccharides, chitin and chitosan (linear polysaccharides composed of β-(1→4)-linked N-acetyl-D-glucosamine and D-glucosamine), to the best of our knowledge, the former (α-(1→4)-linked) has not been observed in nature. For the purpose of these studies, the synthesis of such non-natural aminopolysaccharides was performed by the thermostable α-glucan phosphorylase (from Aquifex aeolicus VF5)-catalyzed enzymatic polymerization of α-D-glucosamine 1-phosphate (GlcN-1-P), via successive α-glucosaminylations, in ammonia buffer containing Mg(2+) ions, resulting in the production of the α-(1→4)-linked D-glucosamine polymers, corresponding to the structure of the chitosan stereoisomer. Subsequent N-acetylation of the products gave the aminopolysaccharides, corresponding to the chitin stereoisomer.

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“…Enzymatic reaction, furthermore, can be operated under mild conditions, eliminating undesired side reactions [6,7]. Of the six main classes of enzymes, transferase (glycosyl transferase, GT) and hydrolase (glycosyl hydrolase, GH) have been used successfully as catalysts in practical synthesis of well-defined saccharide chains via the formation of glycosidic linkages [8,9]. In the enzymatically formation of glycosidic linkages, so-called 'enzymatic glycosylation', two substrates, that is, a glycosyl donor and a glycosyl acceptor are used, generally, in their unprotected forms in aqueous media.…”

Section: Introductionmentioning

confidence: 99%

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

Kadokawa

2018

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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 Glycosylation by Glycohydrolases and Glycosynthases

Cited by 11 publications

References 111 publications

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

Enzymes as Green Catalysts for Precision Macromolecular Synthesis

Synthesis of chitin and chitosan stereoisomers by thermostable α-glucan phosphorylase-catalyzed enzymatic polymerization of α-d-glucosamine 1-phosphate

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

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