Glycosyl fluorides in enzymatic reactions

Williams, Spencer J.; Withers, Stephen G.

doi:10.1016/s0008-6215(00)00041-0

Cited by 212 publications

(159 citation statements)

References 119 publications

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“…22 for a concise summary). These compounds are, in effect, slow substrates that allow the formation of the glycosyl-enzyme at reasonable rates but that dramatically reduce the rate of enzyme deglycosylation, thus favoring accumulation of the intermediate.…”

Section: Discussionmentioning

confidence: 99%

Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase

Piens

Fauré

Sundqvist

et al. 2008

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase

Piens

Fauré

Sundqvist

et al. 2008

Journal of Biological Chemistry

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“…It should be noted that b-maltosyl ‰uoride possesses the opposite anomeric conˆguration of the normal substrates that are hydrolyzed by the enzyme. Later, various inverting enzymes were found to hydrolyze the so called`w rong'' glycosyl ‰uorides as shown in Table 1 ( [14][15][16][17][18][19][20], suggesting that the reaction is common among inverting GHs (Fig. 2).…”

Section: B the Hehre Resynthesis-hydrolysis Reactionmentioning

confidence: 99%

“…The mechanism was conˆrmed by analyzing the reaction of trehalase, which hydrolyzes the a-1, a-1 linkage with anomeric inversion (20). This mechanism was later named the``Hehre resynthesishydrolysis mechanism'' (14,15).…”

Section: B the Hehre Resynthesis-hydrolysis Reactionmentioning

confidence: 99%

“…The Hehre resynthesis-hydrolysis mechanism is often di‹cult to detect because many enzymes recognize glycosyl ‰uoride not only as a donor but also as an acceptor (13)(14)(15)18,21,22), such as b-maltosyl ‰uoride for bamylase and b-glucosyl ‰uoride for glucoamylase. However, reliable experimental evidence for this mechanism was reported for trehalase using b-glucosyl ‰uoride as the donor and glucose or xylose as the acceptor (19,20).…”

Section: B the Hehre Resynthesis-hydrolysis Reactionmentioning

confidence: 99%

“…In 1998, Withers' group reported theˆrst glycosynthase in which a mutant retaining enzyme, GH1 b-glucosidase from Agrobacterium sp., with a mutation of its nucleophilic residue (E358), catalyzed the synthesis of various b-glucosides using a-glucosyl ‰uoride as a donor and various 4-nitrophenyl-b-glycosides as acceptors (23,24). Since then, by substituting their nucleophilic residues, various retaining GHs have been converted into glycosynthases as summarized in Table 2 (15,.…”

Section: Glycosynthasementioning

confidence: 99%

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Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy

Kitaoka

Honda

Fushinobu

et al. 2009

TIGG

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23Trends in Glycoscience and Glycotechnology Vol. 21 No. 117 (2009) AbstractReducing-end xylose-releasing exo-oligoxylanase (Rex, EC. 3.2.1.156) is an inverting xylanolytic enzyme, belonging to the glycoside hydrolase (GH) family 8, which hydrolyzes xylooligosaccharides to release xylose (X1) from its reducing end. Rex hydrolyzes a-xylobiosyl ‰uo-ride (a-X2F) to yield xylobiose (X2) only in the presence of X1, conˆrming the Hehre resynthesis-hydrolysis mechanism. A library of mutant Rex at the catalytic base (D263) was constructed by saturation mutagenesis, in which D263C accumulated the highest level of xylotriose (X 3 ) from a-X 2 F and X 1 . However, F -releasing activities of the mutants were much less than that of the wild type. Next, Y198 residue of Rex that forms a hydrogen bond with nucleophilic water was substituted with phenylalanine, causing a marked decrease in hydrolytic activity and a small increase in the F -releasing activity from a-X2F in the presence of X1. Y198F of Rex accumulated more product during the glycosynthase reaction than D263C. Recently, an inverting a-1,2-fucosidase belonging to GH95 was converted into glycosynthase by mutating a catalytic base residue. In both cases, the catalytic base should be intact.

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Carbohydrases

Brumer

2010

Encyclopedia of Catalysis

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The enzymes that catalyze the synthesis and degradation of oligo‐ and polysaccharides are among the most important in the biosphere, because of the key role they play in the global carbon cycle. Thanks to a long and rich history of scientific study, the catalytic mechanisms of the glycoside hydrolases and transglycosylases are generally well understood in terms of enzyme‐substrate interactions and transition state structure. Recent structure‐function studies of polysaccharide lyases have also begun to unravel the secrets of catalysis in these distinct classes of carbohydrate‐active enzymes. Built upon a firm understanding of enzyme structure and mechanism, an impressive number of technological applications highlight the prowess of these biological catalysts.

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Glycosyl fluorides in enzymatic reactions

Cited by 212 publications

References 119 publications

Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase

Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase

Conversion of inverting glycoside hydrolases into catalysts for synthesizing glycosides employing a glycosynthase strategy

Carbohydrases

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