Mengyang Xue

Shandong University, Chi-nan-shih, Shandong Sheng, China

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Publications (10)20.36 Total impact

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    ABSTRACT: Globotriose is involved in numerous pathogenic processes and drug development strategies. Recent studies have demonstrated that globotriosylceramide could be used in colon cancer therapy and as a crucial indicator for susceptibility to HIV-1 infection. Therefore, the cost-effective and facile approaches for large-scale production of globotiose as potential drugs are highly required. Here, a multi-enzyme one-pot system containing a galactokinase (SpGalK, E.C., a UDP-glucose pyrophosphorylase (SpGalU, E.C., a α-1,4-galactosyltransferase (LgtC, E.C. and a commercial inorganic pyrophosphatase (PPase, EC was designed to achieve globotriose on preparative scales. This method exploits a cheaper initial substrate, galactose, for donor UDP-galactose production. More importantly, the substrate specificity of SpGalK and SpGalU is highly promiscuous and various UDP-galactose derivatives obtained could be used as the donor substrates for LgtC. This pointcut of rapid preparation of globotriose derivatives is proposed for the first time. Finally, three globotriose analogs were achieved by this one-pot multi-enzyme system in our study.
    European Journal of Medicinal Chemistry 04/2014; 80C:423-427. · 3.43 Impact Factor
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    ABSTRACT: Enzymatic synthesis of globotriose and its derivatives.
    European Journal of Medicinal Chemistry. 01/2014; 80:423–427.
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    ABSTRACT: A novel N-acetylglucosamine-1-phosphate pyrophosphorylase was identified from Campylobacter jejuni NCTC 11168. An unprecedented degree of substrate promiscuity has been revealed by systematic studies on its substrate specificities towards sugar-1-P and NTP. The yields of the synthetic reaction of seven kinds of sugar nucleotides catalyzed by the enzyme were up to 60%. In addition, the yields of the other nine were around 20%. With this enzyme, three novel sugar nucleotide analogs were synthesized on a preparative scale and well characterized.
    Bioorganic & medicinal chemistry letters 06/2013; · 2.65 Impact Factor
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    ABSTRACT: Nucleotide sugars are activated forms of monosaccharides and key intermediates of carbohydrate metabolism in all organisms. The availability of structurally diverse nucleotide sugars is particularly important for the characterization of glycosyltransferases. Given that limited methods are available for preparation of nucleotide sugars, especially their useful non-natural derivatives, we introduced herein an efficient one-step three-enzyme catalytic system for the synthesis of nucleotide sugars from monosaccharides. In this study, a promiscuous UDP-sugar pyrophosphorylase (USP) from Arabidopsis thaliana (AtUSP) was used with a galactokinase from Streptococcus pneumoniae TIGR4 (SpGalK) and an inorganic pyrophosphatase (PPase) to effectively synthesize four UDP-sugars. AtUSP has better tolerance for C4-derivatives of Gal-1-P compared to UDP-glucose pyrophosphorylase from S. pneumoniae TIGR4 (SpGalU). Besides, the nucleotide substrate specificity and kinetic parameters of AtUSP were systematically studied. AtUSP exhibited considerable activity toward UTP, dUTP and dTTP, the yield of which was 87%, 85% and 84%, respectively. These results provide abundant information for better understanding of the relationship between substrate specificity and structural features of AtUSP.
    Bioorganic & medicinal chemistry letters 05/2013; · 2.65 Impact Factor
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    ABSTRACT: A UTP-glucose-1-phosphate uridylyltransferase (SpGalU) and a galactokinase (SpGalK) were cloned from Streptococcus pneumoniae TIGR4 and were successfully used to synthesize UDP-galactose (UDP-Gal), UDP-glucose (UDP-Glc), and their derivatives in an efficient one-pot reaction system. The reaction conditions for the one-pot multi-enzyme synthesis were optimized and nine UDP-Glc/Gal derivatives were synthesized. Using this system, six unnatural UDP-Gal derivatives, including UDP-2-deoxy-Galactose and UDP-GalN3 which were not accepted by other approach, can be synthesized efficiently in a one pot fashion. More interestingly, this is the first time it has been reported that UDP-Glc can be synthesized in a simpler one-pot three-enzyme synthesis reaction system.
    Carbohydrate research 03/2013; 373C:76-81. · 2.03 Impact Factor
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    ABSTRACT: Nucleotide sugars are essential glycosyl donors for Leloir-type glycosyltransferases. The UDP-N-acetylgalactosamine pyrophosphorylase (UDP-GalNAc PP; AGX1) from Homo sapiens catalyzes the synthesis of UDP-N-acetylgalactosamine from N-acetylgalactosamine 1-phosphate and UTP. In this Letter, we systematically studied nucleotide substrate specificity of AGX1 during its uridyltransfer reaction, and described the capability of AGX1 to catalyze dUTP and dTTP to their corresponding nucleotide sugars for the first time. Furthermore, using such a eukaryotic enzyme, we synthesized dUDP-GalNAc and dTDP-GalNAc in multiple mg scale in vitro efficiently and rapidly.
    Bioorganic & medicinal chemistry letters 04/2012; 22(12):3957-61. · 2.65 Impact Factor
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    ABSTRACT: Galactokinases (GalKs) have attracted significant research attention for their potential applications in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 presents a remarkably broad substrate range including 14 diverse natural and unnatural sugars. TLC and MS studies revealed that GalKSpe4 had relaxed activity towards galactose derivatives with modifications on the C-6, 4- or 2-positions. Additionally, GalKSpe4 can also tolerate glucose while glucose derivatives with modifications on the C-6, 4- or 2-positions were unacceptable. More interestingly, GalKSpe4 can phosphorylate L-mannose in moderate yield (43%), while other L-sugars such as L-Gal cannot be recognized by this enzyme. These results are very significant because there is rarely enzyme reported that can phosphorylate such uncommon substrates as l-mannose.
    Bioorganic & medicinal chemistry letters 04/2012; 22(10):3540-3. · 2.65 Impact Factor
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    ABSTRACT: Glycopeptides are very useful substrates for the synthesis of various complex glycoproteins and glycopeptides that are indispensable materials for the structural and functional investigation of glycoproteins. This report provides an efficient and time- and cost-saving strategy for the large-scale production of a sialylglycopeptide (SGP) that carries an intact N-linked disialyl-biantennary complex-type sialyloligosaccharide. Consequently, 680 mg of SGP was obtained from 100 egg yolks after phenol treatment, Sephadex G-50 gel filtration, and filtration through graphitized carbon cartridges. The chemical structure and the glycosylation site of the isolated SGP were identified by NMR and ESI-MS/MS, and the purity measured with HPLC was over 95%.
    Journal of Carbohydrate Chemistry - J CARBOHYD CHEM. 01/2012; 31:436-446.
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    ABSTRACT: Galactokinases (GALK) have attracted significant research attention for their potential application in the enzymatic synthesis of unique sugar phosphates. The galactokinase (GalKSpe4) cloned from Streptococcus pneumoniae TIGR4 had a temperature optimum of 45°C, and a pH optimum of 8.0. The substrate specificity and kinetics studies revealed that GalKSpe4 had moderate activity toward glucose, in contrast with very low or no activity observed in other previously reported GALKs. Most interestingly, GalKSpe4 exhibited activity for GalNAc, which had never been recorded in other GALKs found by now. This is the first time to report that bacterial GALK can recognize GalNAc.
    Carbohydrate research 08/2011; 346(15):2421-5. · 2.03 Impact Factor
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    ABSTRACT: UDP-hexose 4-epimerases are critical in galactose metabolism and often important in lipopolysaccharide biosynthesis as well. Three groups of these enzymes have been reported based on their substrate specificity towards non-acetylated substrates (group 1), dual specificity towards N-acetylated and non-acetylated substrates (group 2) and specificity towards N-acetylated substrates (group 3). We recently reported the structure of a novel UDP-GalNAc 4-epimerase called WbgU and based on the structure proposed a model of specific substrate recognition by UDP-GalNAc 4-epimerases. In this work, we present an analysis of the proposed model of substrate recognition using site-directed mutagenesis of WbgU and crystal structure of the His305Ala mutant. This investigation reveals that the wild-type activity of WbgU is retained in most single-point mutants targeting the active site. However, a graded loss in activity is observed in double-and triple-point mutants with the quadruple-point mutant being completely inactive corroborating the proposed rationale of substrate recognition. Furthermore, crystal structure of the His305Ala mutant shows that the structure is significantly similar to the wild-type WbgU, albeit a loss in the critical hydrogen bond network seated at His305 and ensuing minor conformational changes. It is inferred that the specific and non-specific interactions throughout the active site confer it sufficient elasticity to sustain wild-type activity for several of the single-point mutations.
    Biochemical and Biophysical Research Communications 07/2011; 412(2):232-7. · 2.28 Impact Factor

Publication Stats

12 Citations
20.36 Total Impact Points


  • 2011–2014
    • Shandong University
      • State Key Laboratory for Microbial Technology
      Chi-nan-shih, Shandong Sheng, China
    • The Ohio State University
      • Department of Chemistry and Biochemistry
      Columbus, OH, United States
  • 2013
    • Center for Life Sciences
      Chi-nan-shih, Shandong Sheng, China