Facile Enzymatic Synthesis of Ketoses

Wen, Liuqing; Huang, Kenneth; Wei, Mohui; Meisner, Jeffrey; Liu, Yunpeng; Garner, Kristina; Zang, Lanlan; Wang, Xuan; Li, Xu; Fang, Junqiang; Zhang, Houcheng; Wang, Peng George

doi:10.1002/ange.201505714

Cited by 18 publications

(12 citation statements)

References 38 publications

(26 reference statements)

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“…Rare sugars can be used as starting materials for the synthesis of potential natural products with important biological activities for applications in the food, pharmaceutical, medicinal, and chemical industries 1 , 2 . Sugar 4-epimerization is a valuable reaction for the production of rare sugars and their derivatives.…”

Section: Introductionmentioning

confidence: 99%

Structure-based prediction and identification of 4-epimerization activity of phosphate sugars in class II aldolases

Lee

Hong

et al. 2017

Sci Rep

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Sugar 4-epimerization reactions are important for the production of rare sugars and their derivatives, which have various potential industrial applications. For example, the production of tagatose, a functional sweetener, from fructose by sugar 4-epimerization is currently constrained because a fructose 4-epimerase does not exist in nature. We found that class II d-fructose-1,6-bisphosphate aldolase (FbaA) catalyzed the 4-epimerization of d-fructose-6-phosphate (F6P) to d-tagatose-6-phosphate (T6P) based on the prediction via structural comparisons with epimerase and molecular docking and the identification of the condensed products of C3 sugars. In vivo, the 4-epimerization activity of FbaA is normally repressed. This can be explained by our results showing the catalytic efficiency of d-fructose-6-phosphate kinase for F6P phosphorylation was significantly higher than that of FbaA for F6P epimerization. Here, we identified the epimerization reactions and the responsible catalytic residues through observation of the reactions of FbaA and l-rhamnulose-1-phosphate aldolases (RhaD) variants with substituted catalytic residues using different substrates. Moreover, we obtained detailed potential epimerization reaction mechanism of FbaA and a general epimerization mechanism of the class II aldolases l-fuculose-1-phosphate aldolase, RhaD, and FbaA. Thus, class II aldolases can be used as 4-epimerases for the stereo-selective synthesis of valuable carbohydrates.

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Section: Introductionmentioning

confidence: 99%

Structure-based prediction and identification of 4-epimerization activity of phosphate sugars in class II aldolases

Lee

Hong

et al. 2017

Sci Rep

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“… 38 The products were purified using the method reported previously. 39 , 40 10 and 11 was synthesized from 2 and 3 by CuAAC ligation, respectively ( Scheme S3 ). The products were confirmed by NMR and MS analysis (see Supporting Information ).…”

Section: Resultsmentioning

confidence: 99%

A One-Step Chemoenzymatic Labeling Strategy for Probing Sialylated Thomsen–Friedenreich Antigen

et al. 2018

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Abnormal expression of sialylated Thomsen–Friedenreich antigen (Neu5Acα2-3Galβ1-3GalNAcα-O-Ser/Thr, sialyl-T) has a strong relationship with various types of human cancers and many other diseases. However, the size and structural complexity, and relatively lower abundance of sialyl-T have posed a significant challenge to its detection. Therefore, details about the role of sialyl-T in a variety of physiological and pathological processes are still poorly understood. Here, a one-step chemoenzymatic labeling strategy to probe sialyl-T is described. This approach enables the sensitive, selective, and rapid detection of sialyl-T, and global profiling and identification of unknown sialyl-T-attached glycoproteins, which are potential therapeutic targets or biomarkers. The use of one-step labeling strategy not only has a higher sensitivity than a typical two-step reporter strategy but also avoids undergoing an additional chemical reaction step to introduce a reporter group after the labeling reaction, making it particularly useful for detecting low-abundance glycan epitopes on living cells.

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“…These kinases were essential for an efficient phosphorylation-dephosphorylation route to several rare sugars. [74] Galactokinase from Leminorella grimontii, which was cloned and prepared in Escherichia coli, was demonstrated to have a broad substrate scope for the phosphorylation of some galactose analogues in the 1-position. [75] Wild-type anomeric sugar kinases have been shown to catalyze phosphorylations of some fluorinated monosaccharides.…”

Section: Selective Kinase-catalyzed Phosphorylation Reactionsmentioning

confidence: 99%

“…These kinases were essential for an efficient phosphorylation‐dephosphorylation route to several rare sugars. [ 74 ]…”

Section: Selective Kinase‐catalyzed Phosphorylation Reactionsmentioning

confidence: 99%

Key advances in biocatalytic phosphorylations in the last two decades: Biocatalytic syntheses in vitro and biotransformations in vivo (in humans)

Wohlgemuth

2020

Biotechnology Journal

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Biocatalytic phosphorylation reactions provide several benefits, such as more direct, milder, more selective, and shorter access routes to phosphorylated products. Favorable characteristics of biocatalytic methodologies represent advantages for in vitro as well as for in vivo phosphorylation reactions, leading to important advances in the science of synthesis towards bioactive phosphorylated compounds in various areas. The scope of this review covers key advances of biocatalytic phosphorylation reactions over the last two decades, for biocatalytic syntheses in vitro and for biotransformations in vivo (in humans). From the origins of probiotic life to in vitro synthetic applications and in vivo formation of bioactive pharmaceuticals, the common purpose is to outline the importance, relevance, and underlying connections of biocatalytic phosphorylations of small molecules. Asymmetric phosphorylations attracting increased attention are highlighted. Phosphohydrolases, phosphotransferases, phosphorylases, phosphomutases, and other enzymes involved in phosphorus chemistry provide powerful toolboxes for resource-efficient and selective in vitro biocatalytic syntheses of phosphorylated metabolites, chiral building blocks, pharmaceuticals as well as in vivo enzymatic formation of biologically active forms of pharmaceuticals. Nature's large diversity of phosphoryl-group-transferring enzymes, advanced enzyme and reaction engineering toolboxes make biocatalytic asymmetric phosphorylations using enzymes a powerful and privileged phosphorylation methodology. K E Y W O R D S chiral building blocks, enzymatic phosphorylation, kinases, metabolites, pharmaceuticals, phosphatases, phosphomutases, phosphoryl-donor, phosphorylases, phosphotransferases 1 INTRODUCTION Biocatalysis and biotransformations involving the element phosphorus are fundamental bioprocesses. The exciting history of the element Abbreviations: API, active pharmaceutical ingredient; FDA, U.S. Food and Drug Administration; P(III)-Donor, donor group containing phosphorus in its oxidation state +3; P(V)-Donor, donor group containing phosphorus in its highest oxidation state +5 phosphorus has been linked to life and death on our planet from its discovery from human urine in 1669 by alchemist Hennig Brand. Many phosphorus bonds to build phosphorus-containing molecules have been synthesized by biocatalytic phosphorylations, either by nature or anthropogenic. [1,2] As many phosphorus-bearing species are structurally stable and functionally reactive, they are also of interest as signals of life and have been detected recently in space. [3,4] The discovery of phosphorus-bearing species in space is of much interest

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Facile Enzymatic Synthesis of Ketoses

Cited by 18 publications

References 38 publications

Structure-based prediction and identification of 4-epimerization activity of phosphate sugars in class II aldolases

Structure-based prediction and identification of 4-epimerization activity of phosphate sugars in class II aldolases

A One-Step Chemoenzymatic Labeling Strategy for Probing Sialylated Thomsen–Friedenreich Antigen

Key advances in biocatalytic phosphorylations in the last two decades: Biocatalytic syntheses in vitro and biotransformations in vivo (in humans)

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