Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis

Crout, David H. G.; Vic, Gabin

doi:10.1016/s1367-5931(98)80041-0

Cited by 239 publications

(114 citation statements)

References 58 publications

Supporting

Mentioning

111

Contrasting

Unclassified

Order By: Relevance

“…Synthesis of various glycosides has mainly been achieved using mesophilic glycosidases such as -glucosidase (EC 3.2.1.21) from almonds via reversed hydrolysis reaction or transglycosylation reaction. 1,2) On the other hand, thermostable glycosidases have been recently isolated from hyperthermophilic microorganisms [3][4][5][6][7][8][9] and utilized for synthesis of alkyl glucosides and oligosaccharides. 2,[10][11][12][13][14][15] Glycosylation using thermostable glycosidases was performed at an elevated temperature to compensate for the low solubility of glycosyl acceptor and/or donor.…”

mentioning

confidence: 99%

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

Nagatomo

Matsushita

Sugamoto

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

Hyperthermostable -glucosidase from Pyrococcus furiosus was enclosed in gelatin gel by cross-linking with transglutaminase. Gelatin-immobilized -glucosidase was considerably more thermostable than the native enzyme. Lyophilized immobilisate was stored at 90 C for 1 month without loss of activity. The immobilized -glucosidase catalyzed transglucosylation of 5-phenylpentanol with 10.0 equivalent of cellobiose at pH 5.0 and 70 C for 12 h to afford 5-phenylpentyl -Dglucopyranoside in 41% yield. The immobilized enzyme was more effective than the native one in transglucosylation. The gelatin-immobilized Pfu--glucosidase recovered from the first run of the reaction was reusable on successive runs.

show abstract

mentioning

confidence: 99%

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

Nagatomo

Matsushita

Sugamoto

et al. 2005

Bioscience, Biotechnology, and Biochemistry

View full text Add to dashboard Cite

show abstract

“…Having been developed significantly in recent years, biocatalytic approaches to oligosaccharide synthesis offer many advantages over traditional methods (15,34). Glycosyltransferases, as well as glycosidases (29, 42), or whole cells of metabolically engineered bacteria have been applied in the synthesis of oligosaccharides and analogues (5,8,35). To date, catalysis with Leloir's glycosyltransferases (19, 47) as well innovations in the regeneration of glycosylation donors have greatly advanced the field (3,16,46,48,49).…”

mentioning

confidence: 99%

P1 Trisaccharide (Galα1,4Galβ1,4GlcNAc) Synthesis by Enzyme Glycosylation Reactions Using Recombinant Escherichia coli

Liu

Zhang

et al. 2003

Appl Environ Microbiol

View full text Add to dashboard Cite

The frequency of Escherichia coli infection has lead to concerns over pathogenic bacteria in our food supply and a demand for therapeutics. Glycolipids on gut cells serve as receptors for the Shiga-like toxin produced by E. coli. Oligosaccharide moiety analogues of these glycolipids can compete with receptors for the toxin, thus acting as antibacterials. An enzymatic synthesis of the P1 trisaccharide (Gal␣1,4Gal␤1,4GlcNAc), one of the oligosaccharide analogues, was assessed in this study. In the proposed synthetic pathway, UDP-glucose was generated from sucrose with an Anabaena sp. sucrose synthase and then converted with an E. coli UDP-glucose 4-epimerase to UDP-galactose. Two molecules of galactose were linked to N-acetylglucosamine subsequently with a Helicobacter pylori ␤-l,4-galactosyltransferase and a Neisseria meningitidis ␣-1,4-galactosyltransferase to produce one molecule of P1 trisaccharide. The four enzymes were coexpressed in a single genetically engineered E. coli strain that was then permeabilized and used to catalyze the enzymatic reaction. P1 trisaccharide was accumulated up to 50 mM (5.4 g in a 200-ml reaction volume), with a 67% yield based on the consumption of N-acetylglucosamine. This study provides an efficient approach for the preparative-scale synthesis of P1 trisaccharide with recombinant bacteria.Recently, vaccines have been introduced to prevent illness from pathogenic Escherichia coli, yet there remains a need for therapeutics to treat acute infection (27). Unlike endogenous E. coli from our intestine, the pathogenic strain (O157:H7) has acquired a gene from Shigella which produces a toxic protein. This Shiga-like toxin binds to glycolipid receptors on cells of the gut wall and can ultimately lead to dysentery, hemorrhagic colitis, and sometimes life-threatening complications (32). The attachment of the microbial protein onto mammalian cells through surface carbohydrates initiates a successful infection (18). The Shiga-like toxin will also bind other carbohydrate derivatives, including globotriosylceramide (Gal␣1,4Gal␤1, 4Glc-ceramide) found on the cell surface (4,(24)(25)(26)44) and trisaccharide analogues, such as globotriose (Gal␣1,4Gal␤1, 4Glc) and the trisaccharide moiety of P1 antigen (Gal␣1, 4Gal␤1,4GlcNAc) (1). The mechanism of action for the proposed therapy involves preventing the toxin from binding to cell receptors by introducing these molecules to the site of infection. Instead of binding to cell receptors, the toxic peptides bind to the carbohydrate analogues and are removed from the body without causing harm. Of the three carbohydrate moieties mentioned above, P1 trisaccharide is the most effective therapeutic. Although synthesis remains a limiting factor, if available in large quantities these trisaccharides have considerable potential as antiadhesive agents in the treatment of pathogenic E. coli infections (17,36,37).Chemical syntheses of oligosaccharides have always been complicated by their structural complexity and have traditionally involved laborious protection p...

show abstract

“…Glycoside hydrolases have two types, one is an endo-type and the other an exo-type enzyme. 25) For the enzymatic polymerization, endo-type enzymes have been found efficient, whose shape at the catalytic domain Cellulose synthesis: Finding a new method of enzymatic polymerization. Cellulose is the most abundant organic molecule in the plant world and of course on the Earth; some hundreds billion tons of cellulose are annually photo-synthesized.…”

Section: Enzymatic Polymerization To Synthesize Natural Polysaccharidesmentioning

confidence: 99%

New developments of polysaccharide synthesis via enzymatic polymerization

Kobayashi

2007

Proceedings of the Japan Academy. Ser. B: Physical and Biologic

View full text Add to dashboard Cite

This review focuses on the in vitro synthesis of polysaccharides, the method of which is ''enzymatic polymerization'' mainly developed by our group. Polysaccharides are formed by repeated glycosylation reactions between a glycosyl donor and a glycosyl acceptor. A hydrolysis enzyme was found very efficient as catalyst, where the monomer is designed based on the new concept of a ''transition-state analogue substrate'' (TSAS); sugar fluoride monomers for polycondensation and sugar oxazoline monomers for ring-opening polyaddition. Enzymatic polymerization enabled the first in vitro synthesis of natural polysaccharides such as cellulose, xylan, chitin, hyaluronan and chondroitin, and also of unnatural polysaccharides such as a cellulose-chitin hybrid, a hyaluronan-chondroitin hybrid, and others. Supercatalysis of hyaluronidase was disclosed as unusual enzymatic multi-catalyst functions. Mutant enzymes were very useful for synthetic and mechanistic studies. In situ observations of enzymatic polymerization by SEM, TEM, and combined SAS methods revealed mechanisms of the polymerization and of the self-assembling of high-order molecular structure formed by elongating polysaccharide molecules.

show abstract

Glycosidases and glycosyl transferases in glycoside and oligosaccharide synthesis

Cited by 239 publications

References 58 publications

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

Preparation and Properties of Gelatin-Immobilized β-Glucosidase fromPyrococcus furiosus

P1 Trisaccharide (Galα1,4Galβ1,4GlcNAc) Synthesis by Enzyme Glycosylation Reactions Using Recombinant Escherichia coli

New developments of polysaccharide synthesis via enzymatic polymerization

Contact Info

Product

Resources

About