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Journal articles on the topic 'Enzymatic glycosylation'

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Published: 9 March 2023
Last updated: 10 March 2023

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1

Kennedy, L., and T. J. Lyons. "Non-enzymatic glycosylation." British Medical Bulletin 45, no. 1 (1989): 174–90. http://dx.doi.org/10.1093/oxfordjournals.bmb.a072310.

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2

Chang, Cheng-Wei Tom. "Predictable Enzymatic Glycosylation." Chemistry & Biology 16, no. 6 (June 2009): 579–80. http://dx.doi.org/10.1016/j.chembiol.2009.06.001.

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3

Rivas, Francisco, Andres Parra, Antonio Martinez, and Andres Garcia-Granados. "Enzymatic glycosylation of terpenoids." Phytochemistry Reviews 12, no. 2 (April 26, 2013): 327–39. http://dx.doi.org/10.1007/s11101-013-9301-9.

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4

WEIGNEROVÁ, Lenka, Jaroslav SPÍZEK, Lucie NAJMANOVÁ, and Vladimír KREN. "Enzymatic Glycosylation of Lincomycin." Bioscience, Biotechnology, and Biochemistry 65, no. 8 (January 2001): 1897–99. http://dx.doi.org/10.1271/bbb.65.1897.

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5

Jeong, Hee Yong, Ji Youn Lee, and Tai Hyun Park. "Specificity of enzymatic in vitro glycosylation by PNGase F: a comparison of enzymatic and non-enzymatic glycosylation." Enzyme and Microbial Technology 35, no. 6-7 (December 2004): 587–91. http://dx.doi.org/10.1016/j.enzmictec.2004.08.010.

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6

Bojarová, Pavla, Ruben R. Rosencrantz, Lothar Elling, and Vladimír Křen. "Enzymatic glycosylation of multivalent scaffolds." Chemical Society Reviews 42, no. 11 (2013): 4774. http://dx.doi.org/10.1039/c2cs35395d.

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7

Council, Claire E., Kelly J. Kilpin, Jessica S. Gusthart, Sarah A. Allman, Bruno Linclau, and Seung Seo Lee. "Enzymatic glycosylation involving fluorinated carbohydrates." Organic & Biomolecular Chemistry 18, no. 18 (2020): 3423–51. http://dx.doi.org/10.1039/d0ob00436g.

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This contribution reviews the enzymatic synthesis, including optimisation efforts, of fluorinated carbohydrates involving fluorinated donors and/or acceptors, as well as the enzymatic activation of the fluorinated donors.
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8

Schultz, Michael, and Horst Kunz. "Enzymatic glycosylation of o-glycopeptides." Tetrahedron Letters 33, no. 37 (September 1992): 5319–22. http://dx.doi.org/10.1016/s0040-4039(00)79082-4.

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9

Zhou, Maoquan, and Jon S. Thorson. "Asymmetric Enzymatic Glycosylation of Mitoxantrone." Organic Letters 13, no. 10 (May 20, 2011): 2786–88. http://dx.doi.org/10.1021/ol200977u.

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10

Mestrom, Przypis, Kowalczykiewicz, Pollender, Kumpf, Marsden, Bento, et al. "Leloir Glycosyltransferases in Applied Biocatalysis: A Multidisciplinary Approach." International Journal of Molecular Sciences 20, no. 21 (October 23, 2019): 5263. http://dx.doi.org/10.3390/ijms20215263.

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Enzymes are nature’s catalyst of choice for the highly selective and efficient coupling of carbohydrates. Enzymatic sugar coupling is a competitive technology for industrial glycosylation reactions, since chemical synthetic routes require extensive use of laborious protection group manipulations and often lack regio- and stereoselectivity. The application of Leloir glycosyltransferases has received considerable attention in recent years and offers excellent control over the reactivity and selectivity of glycosylation reactions with unprotected carbohydrates, paving the way for previously inaccessible synthetic routes. The development of nucleotide recycling cascades has allowed for the efficient production and reuse of nucleotide sugar donors in robust one-pot multi-enzyme glycosylation cascades. In this way, large glycans and glycoconjugates with complex stereochemistry can be constructed. With recent advances, LeLoir glycosyltransferases are close to being applied industrially in multi-enzyme, programmable cascade glycosylations.
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11

Popova, E. A., R. S. Mironova, and M. K. Odjakova. "Non-Enzymatic Glycosylation and Deglycating Enzymes." Biotechnology & Biotechnological Equipment 24, no. 3 (January 2010): 1928–35. http://dx.doi.org/10.2478/v10133-010-0066-7.

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12

Chen, Kuan, Junbin He, Zhimin Hu, Wei Song, Liyan Yu, Kai Li, Xue Qiao, and Min Ye. "Enzymatic glycosylation of oleanane-type triterpenoids." Journal of Asian Natural Products Research 20, no. 7 (June 17, 2018): 615–23. http://dx.doi.org/10.1080/10286020.2018.1478818.

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13

Wu, Jiumn-Yih, Tzi-Yuan Wang, Hsiou-Yu Ding, Yun-Rong Zhang, Shu-Yuan Lin, and Te-Sheng Chang. "Enzymatic Synthesis of Novel Vitexin Glucosides." Molecules 26, no. 20 (October 16, 2021): 6274. http://dx.doi.org/10.3390/molecules26206274.

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Vitexin is a C-glucoside flavone that exhibits a wide range of pharmaceutical activities. However, the poor solubility of vitexin limits its applications. To resolve this limitation, two glycoside hydrolases (GHs) and four glycosyltransferases (GTs) were assayed for glycosylation activity toward vitexin. The results showed that BtGT_16345 from the Bacillus thuringiensis GA A07 strain possessed the highest glycosylation activity, catalyzing the conversion of vitexin into new compounds, vitexin-4′-O-β-glucoside (1) and vitexin-5-O-β-glucoside (2), which showed greater aqueous solubility than vitexin. To our knowledge, this is the first report of vitexin glycosylation. Based on the multiple bioactivities of vitexin, the two highly soluble vitexin derivatives might have high potential for pharmacological usage in the future.
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14

Abraham, E. C., and M. M. Elseweidy. "Non-enzymatic glycosylation influences Hb S polymerization." Hemoglobin 10, no. 2 (January 1986): 173–83. http://dx.doi.org/10.3109/03630268609046443.

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15

Parajuli, Prakash, Ramesh Prasad Pandey, Anaya Raj Pokhrel, Gopal Prasad Ghimire, and Jae Kyung Sohng. "Enzymatic glycosylation of the topical antibiotic mupirocin." Glycoconjugate Journal 31, no. 8 (July 30, 2014): 563–72. http://dx.doi.org/10.1007/s10719-014-9538-6.

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16

BLANCHARD, S., and J. THORSON. "Enzymatic tools for engineering natural product glycosylation." Current Opinion in Chemical Biology 10, no. 3 (June 2006): 263–71. http://dx.doi.org/10.1016/j.cbpa.2006.04.001.

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17

Zähner, Dagmar, Remedios Ramirez, and Willy J. Malaisse. "Non-enzymatic protein glycosylation: back-titration assay." Diabetes Research and Clinical Practice 8, no. 1 (January 1990): 61–68. http://dx.doi.org/10.1016/0168-8227(90)90097-d.

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18

Bojarova, Pavla, Ruben R. Rosencrantz, Lothar Elling, and Vladimir Kren. "ChemInform Abstract: Enzymatic Glycosylation of Multivalent Scaffolds." ChemInform 44, no. 34 (August 1, 2013): no. http://dx.doi.org/10.1002/chin.201334233.

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19

Muneeruddin, K., C. E. Bobst, R. Frenkel, D. Houde, I. Turyan, Z. Sosic, and I. A. Kaltashov. "Characterization of a PEGylated protein therapeutic by ion exchange chromatography with on-line detection by native ESI MS and MS/MS." Analyst 142, no. 2 (2017): 336–44. http://dx.doi.org/10.1039/c6an02041k.

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Detailed profiling of both enzymatic (e.g., glycosylation) and non-enzymatic (e.g., oxidation and deamidation) post-translational modifications (PTMs) is frequently required for the quality assessment of protein-based drugs.
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20

Nagy, A., K. Marciniak-Darmochwał, S. Krawczuk, D. Mierzejewska, H. Kostyra, and É. Gelencsér. "Influence of glycation and pepsin hydrolysis on immunoreactivity of albumin/globulin fraction of herbicide resistant wheat line." Czech Journal of Food Sciences 27, No. 5 (October 28, 2009): 320–29. http://dx.doi.org/10.17221/48/2008-cjfs.

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The aim of this study was to investigate the influence of non-enzymatic glycosylation on the immunogenic properties of soluble wheat proteins. Albumin/globulin fractions of herbicide resistant wheat line were non-enzymatically glycosylated using glucose for seven days at 37°C. The changes in their structures and immunoreactivity were then determined. The protein fractions were also hydrolysed with pepsin to determine the resistance to digestion. Albumin/globulin fractions before and after non-enzymatic glycosylation were analysed using <i>o</i>-phthaldialdehyde method and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The immunoreactivity of the protein fractions was determined using enzyme-linked immunosorbent assay methods, as well as affinity chromatography. The soluble wheat proteins showed smaller amounts of available α-amino groups after non-enzymatic glycosylation, and were stronger immunogens after glycation, but their antigenicity was not been affected significantly. However, pepsin hydrolysis of wheat proteins decreased their immunoreactivity.
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21

Dozio, Elena, Luca Massaccesi, and Massimiliano Marco Corsi Romanelli. "Glycation and Glycosylation in Cardiovascular Remodeling: Focus on Advanced Glycation End Products and O-Linked Glycosylations as Glucose-Related Pathogenetic Factors and Disease Markers." Journal of Clinical Medicine 10, no. 20 (October 19, 2021): 4792. http://dx.doi.org/10.3390/jcm10204792.

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Glycation and glycosylation are non-enzymatic and enzymatic reactions, respectively, of glucose, glucose metabolites, and other reducing sugars with different substrates, such as proteins, lipids, and nucleic acids. Increased availability of glucose is a recognized risk factor for the onset and progression of diabetes-mellitus-associated disorders, among which cardiovascular diseases have a great impact on patient mortality. Both advanced glycation end products, the result of non-enzymatic glycation of substrates, and O-linked-N-Acetylglucosaminylation, a glycosylation reaction that is controlled by O-N-AcetylGlucosamine (GlcNAc) transferase (OGT) and O-GlcNAcase (OGA), have been shown to play a role in cardiovascular remodeling. In this review, we aim (1) to summarize the most recent data regarding the role of glycation and O-linked-N-Acetylglucosaminylation as glucose-related pathogenetic factors and disease markers in cardiovascular remodeling, and (2) to discuss potential common mechanisms linking these pathways to the dysregulation and/or loss of function of different biomolecules involved in this field.
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22

Xu, Tingting, Ziyun Fan, Junqiao Lou, Qi Du, Yue Kong, Yujia Lu, and Xueming Wu. "Enzymatic synthesis of vitexin glycosides and their activity." RSC Advances 12, no. 37 (2022): 23839–44. http://dx.doi.org/10.1039/d2ra04408k.

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23

Pandey, Ramesh Prasad, Tai Feng Li, Eun-Hee Kim, Tokutaro Yamaguchi, Yong Il Park, Joong Su Kim, and Jae Kyung Sohng. "Enzymatic Synthesis of Novel Phloretin Glucosides." Applied and Environmental Microbiology 79, no. 11 (March 29, 2013): 3516–21. http://dx.doi.org/10.1128/aem.00409-13.

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ABSTRACTA UDP-glycosyltransferase fromBacillus licheniformiswas exploited for the glycosylation of phloretin. Thein vitroglycosylation reaction confirmed the production of five phloretin glucosides, including three novel glucosides. Consequently, we demonstrated the application of the same glycosyltransferase for the efficient whole-cell biocatalysis of phloretin in engineeredEscherichia coli.
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24

Li, Bohan, Meilin Zhu, Hui Ma, Tao Ma, Yiqun Dai, Hongmei Li, Yu Li, and Cheng-Zhu Wu. "Biosynthesis of Novel Shikonin Glucosides by Enzymatic Glycosylation." Chemical and Pharmaceutical Bulletin 67, no. 10 (October 1, 2019): 1072–75. http://dx.doi.org/10.1248/cpb.c19-00284.

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25

Mironova, Roumyana, Toshimitsu Niwa, Hideki Hayashi, Rositsa Dimitrova, and Ivan Ivanov. "Evidence for non-enzymatic glycosylation in Escherichia coli." Molecular Microbiology 39, no. 4 (December 21, 2001): 1061–68. http://dx.doi.org/10.1046/j.1365-2958.2001.02304.x.

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26

Mironova, Roumyana, Toshimitsu Niwa, Yordan Handzhiyski, Angelina Sredovska, and Ivan Ivanov. "Evidence for non-enzymatic glycosylation ofEscherichia colichromosomal DNA." Molecular Microbiology 55, no. 6 (January 21, 2005): 1801–11. http://dx.doi.org/10.1111/j.1365-2958.2005.04504.x.

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27

Sullivan, R. "Contributions to Senescence: Non-Enzymatic Glycosylation of Proteins." Archives of Physiology and Biochemistry 104, no. 7 (January 1996): 797–806. http://dx.doi.org/10.1076/apab.104.7.797.13107.

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28

Meynial-salles, Isabelle, and Didier Combes. "In vitro glycosylation of proteins: An enzymatic approach." Journal of Biotechnology 46, no. 1 (April 1996): 1–14. http://dx.doi.org/10.1016/0168-1656(95)00174-3.

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29

Kieburg, Christoffer, Thisbe K. Lindhorst, and Vladimír Křen. "Enzymatic Glycosylation of Branched Symmetrical Non-Carbohydrate Polyols." Journal of Carbohydrate Chemistry 17, no. 8 (November 1998): 1239–47. http://dx.doi.org/10.1080/07328309808001896.

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30

Syrovy, I., and Z. Hodny. "In vitro non-enzymatic glycosylation of myofibrillar proteins." International Journal of Biochemistry 25, no. 6 (June 1993): 941–46. http://dx.doi.org/10.1016/0020-711x(93)90251-9.

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31

Liang, J. N., L. L. Hershorin, and L. T. Chylack. "Non-enzymatic glycosylation in human diabetic lens crystallins." Diabetologia 29, no. 4 (April 1986): 225–28. http://dx.doi.org/10.1007/bf00454880.

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32

Kalia, Kiran, Seema Sharma, and Kinnari Mistry. "Non-enzymatic glycosylation of immunoglobulins in diabetic nephropathy." Clinica Chimica Acta 347, no. 1-2 (September 2004): 169–76. http://dx.doi.org/10.1016/j.cccn.2004.04.016.

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33

Laurent, Nicolas, Josef Voglmeir, Adam Wright, Jonathan Blackburn, Nhan T. Pham, Stephen C. C. Wong, Simon J. Gaskell, and Sabine L. Flitsch. "Enzymatic Glycosylation of Peptide Arrays on Gold Surfaces." ChemBioChem 9, no. 6 (April 14, 2008): 883–87. http://dx.doi.org/10.1002/cbic.200700692.

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34

Iga, Dumitru Petru, Dumitru Popescu, and Florentina Duica. "The Use of Exoglycosidases for the Assay of Two New Enzymatic Substrates, b-D-xylopyranosyl-4-nitrocatechol-1-yl and a-lactosyl-4-nitrocatechol-1-yl." Revista de Chimie 68, no. 8 (September 15, 2017): 1771–75. http://dx.doi.org/10.37358/rc.17.8.5762.

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Glycosylation acceptor, 4-nitrocatechol, has been prepared via 4-nitrocatechol sulfate (2-hydroxy-5-nitrophenyl sulfate). The two carbohydrates, D-xylose and lactose, were peracetylated and then served as glycosylation donors in a modified Helferich glycosylation method, by using BF3� OBu2 as a promotor. The new synthesized glycosides were crystallized from ethanol and then submitted to Z�mplen saponification and separated by preparative thin layer chromatography (TLC). We have isolated two xylosides. Reaction mixture of lactoside proved to be unitary, a single product could be isolated. Small portions of the synthetic glycosides were re-acetylated and their 1H and 13C NMR spectra registered. The two separated xylosides were b- and a-xylopyranoside-4-nitrocatechol-1-yl. Being submitted to the action of an enzymatic extract from digestive tract of snail (Helix pomatia) only the b-anomer was susceptible to enzymatic hydrolysis. The isolated lactoside proved to be the a-isomer. Under the action of an enzymatic extract from wheat (Triticum aestivum) germs, it was sequencially cleaved, as indicated by a kinetic TLC analysis.
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35

Xu, Tingting, and Xueming Wu. "Preparative separation of mangiferin glycosides by high speed counter current chromatography and comparison of their antioxidant and antitumor activities." RSC Advances 10, no. 43 (2020): 25780–85. http://dx.doi.org/10.1039/d0ra04307a.

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36

Witte, Krista, Pamela Sears, Richard Martin, and Chi-Huey Wong. "Enzymatic Glycoprotein Synthesis: Preparation of Ribonuclease Glycoforms via Enzymatic Glycopeptide Condensation and Glycosylation." Journal of the American Chemical Society 119, no. 9 (March 1997): 2114–18. http://dx.doi.org/10.1021/ja961846z.

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37

Kim, Chang Sup, Hye Ryoung Heo, Jeong Hyun Seo, and Hyung Joon Cha. "On-chip biosynthesis of GM1 pentasaccharide-related complex glycans." Chemical Communications 55, no. 1 (2019): 71–74. http://dx.doi.org/10.1039/c8cc06526h.

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38

Ioannou, Irina, Eduardo Barboza, Gaëlle Willig, Thomas Marié, Andreïa Texeira, Pierre Darme, Jean-Hugues Renault, and Florent Allais. "Implementation of an Enzyme Membrane Reactor to Intensify the α-O-Glycosylation of Resveratrol Using Cyclodextrins." Pharmaceuticals 14, no. 4 (April 1, 2021): 319. http://dx.doi.org/10.3390/ph14040319.

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The O-glycosylation of resveratrol increases both its solubility in water and its bioavailability while preventing its oxidation, allowing a more efficient use of this molecule as a bioactive ingredient in pharmaceutical and cosmetic applications. Resveratrol O-glycosides can be obtained by enzymatic reactions. Recent developments have made it possible to selectively obtain resveratrol α-glycosides from the β-cyclodextrin–resveratrol complex in water with a yield of 35%. However, this yield is limited by the partial hydrolysis of the resveratrol glycosides produced during the reaction. In this study, we propose to intensify this enzymatic reaction by coupling the enzymatic reactor to a membrane process. Firstly, membrane screening was carried out at the laboratory scale and led to the choice of a GE polymeric membrane with a cut-off of 1 kDa. This membrane allowed the retention of 65% of the β-cyclodextrin–resveratrol complex in the reaction medium and the transfer of 70% of the resveratrol α-O-glycosides in the permeate. In a second step, this membrane was used in an enzymatic membrane reactor and improved the yield of the enzymatic glycosylation up to 50%.
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39

Bonnet, Véronique, Christophe Boyer, Virginie Langlois, Raphaël Duval, and Claude Rabiller. "An efficient, regioselective and fast enzymatic glycosylation for cyclodextrins." Tetrahedron Letters 44, no. 50 (December 2003): 8987–89. http://dx.doi.org/10.1016/j.tetlet.2003.10.003.

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40

Lee, Ji Youn, and Tai Hyun Park. "Enzymatic in vitro glycosylation using peptide-N-glycosidase F." Enzyme and Microbial Technology 30, no. 6 (May 2002): 716–20. http://dx.doi.org/10.1016/s0141-0229(02)00045-5.

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41

Carson, Dennis A., and D. Bruce Wasson. "Synthesis of 2′,3′-dideoxynucleosides by enzymatic trans-glycosylation." Biochemical and Biophysical Research Communications 155, no. 2 (September 1988): 829–34. http://dx.doi.org/10.1016/s0006-291x(88)80570-9.

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42

Xu, Lijuan, Tingting Qi, Li Xu, Lili Lu, and Min Xiao. "Recent progress in the enzymatic glycosylation of phenolic compounds." Journal of Carbohydrate Chemistry 35, no. 1 (January 2, 2016): 1–23. http://dx.doi.org/10.1080/07328303.2015.1137580.

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43

Hofer, Bernd. "Recent developments in the enzymatic O-glycosylation of flavonoids." Applied Microbiology and Biotechnology 100, no. 10 (March 31, 2016): 4269–81. http://dx.doi.org/10.1007/s00253-016-7465-0.

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44

Wong, Chi-Huey, and Kathryn M. Koeller. "ChemInform Abstract: Recycling of Sugar Nucleotides in Enzymatic Glycosylation." ChemInform 32, no. 12 (March 20, 2001): no. http://dx.doi.org/10.1002/chin.200112260.

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45

Traini, Mathew, Raani Kumaran, Morten Thaysen-Andersen, Maaike Kockx, Wendy Jessup, and Leonard Kritharides. "N-glycosylation of human sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is essential for stability, secretion and activity." Biochemical Journal 474, no. 7 (March 8, 2017): 1071–92. http://dx.doi.org/10.1042/bcj20160735.

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Sphingomyelin phosphodiesterase acid-like 3A (SMPDL3A) is a recently identified phosphodiesterase, which is a secreted N-linked glycoprotein. SMPDL3A is highly homologous to acid sphingomyelinase (aSMase), but unlike aSMase cannot cleave sphingomyelin. Rather, SMPDL3A hydrolyzes nucleotide tri- and diphosphates and their derivatives. While recent structural studies have shed light on these unexpected substrate preferences, many other aspects of SMPDL3A biology, which may give insight into its function in vivo, remain obscure. Here, we investigate the roles of N-glycosylation in the expression, secretion and activity of human SMPDL3A, using inhibitors of N-glycosylation and site-directed mutagenesis, with either THP-1 macrophages or CHO cells expressing human SMPDL3A. Tunicamycin (TM) treatment resulted in expression of non-glycosylated SMPDL3A that was not secreted, and was largely degraded by the proteasome. Proteasomal inhibition restored levels of SMPDL3A in TM-treated cells, although this non-glycosylated protein lacked phosphodiesterase activity. Enzymatic deglycosylation of purified recombinant SMPDL3A also resulted in significant loss of phosphodiesterase activity. Site-directed mutagenesis of individual N-glycosylation sites in SMPDL3A identified glycosylation of Asn69 and Asn222 as affecting maturation of its N-glycans and secretion. Glycosylation of Asn356 in SMPDL3A, an N-linked site conserved throughout the aSMase-like family, was critical for protection against proteasomal degradation and preservation of enzymatic activity. We provide the first experimental evidence for a predicted 22 residue N-terminal signal peptide in SMPDL3A, which is essential for facilitating glycosylation and is removed from the mature protein secreted from CHO cells. In conclusion, site-specific N-glycosylation is essential for the intracellular stability, secretion and activity of human SMPDL3A.
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46

Valverde, Pablo, Jean-Baptiste Vendeville, Kristian Hollingsworth, Ashley P. Mattey, Tessa Keenan, Harriet Chidwick, Helene Ledru, et al. "Chemoenzymatic synthesis of 3-deoxy-3-fluoro-l-fucose and its enzymatic incorporation into glycoconjugates." Chemical Communications 56, no. 47 (2020): 6408–11. http://dx.doi.org/10.1039/d0cc02209h.

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47

Thomson, R. Brent, Claire L. Thomson, and Peter S. Aronson. "N-glycosylation critically regulates function of oxalate transporter SLC26A6." American Journal of Physiology-Cell Physiology 311, no. 6 (December 1, 2016): C866—C873. http://dx.doi.org/10.1152/ajpcell.00171.2016.

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The brush border Cl−-oxalate exchanger SLC26A6 plays an essential role in mediating intestinal secretion of oxalate and is crucial for the maintenance of oxalate homeostasis and the prevention of hyperoxaluria and calcium oxalate nephrolithiasis. Previous in vitro studies have suggested that SLC26A6 is heavily N-glycosylated. N-linked glycosylation is known to critically affect folding, trafficking, and function in a wide variety of integral membrane proteins and could therefore potentially have a critical impact on SLC26A6 function and subsequent oxalate homeostasis. Through a series of enzymatic deglycosylation studies we confirmed that endogenously expressed mouse and human SLC26A6 are indeed glycosylated, that the oligosaccharides are principally attached via N-glycosidic linkage, and that there are tissue-specific differences in glycosylation. In vitro cell culture experiments were then used to elucidate the functional significance of the addition of the carbohydrate moieties. Biotinylation studies of SLC26A6 glycosylation mutants indicated that glycosylation is not essential for cell surface delivery of SLC26A6 but suggested that it may affect the efficacy with which it is trafficked and maintained in the plasma membrane. Functional studies of transfected SLC26A6 demonstrated that glycosylation at two sites in the putative second extracellular loop of SLC26A6 is critically important for chloride-dependent oxalate transport and that enzymatic deglycosylation of SLC26A6 expressed on the plasma membrane of intact cells strongly reduced oxalate transport activity. Taken together, these studies indicated that oxalate transport function of SLC26A6 is critically dependent on glycosylation and that exoglycosidase-mediated deglycosylation of SLC26A6 has the capacity to profoundly modulate SLC26A6 function.
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48

Kadokawa, Jun-ichi. "α-Glucan Phosphorylase-Catalyzed Enzymatic Reactions Using Analog Substrates to Synthesize Non-Natural Oligo- and Polysaccharides." Catalysts 8, no. 10 (October 19, 2018): 473. http://dx.doi.org/10.3390/catal8100473.

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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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49

Tseng, Hsin-Kai, Yung-Yu Su, Ting-Wei Chang, Hsin-Chien Liu, Pei-Jhen Li, Pei-Yun Chiang, and Chun-Cheng Lin. "Acceptor-mediated regioselective enzyme catalyzed sialylation: chemoenzymatic synthesis of GAA-7 ganglioside glycan." Chemical Communications 57, no. 28 (2021): 3468–71. http://dx.doi.org/10.1039/d1cc00653c.

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50

Galibert, Mathieu, Véronique Piller, Friedrich Piller, Vincent Aucagne, and Agnès F. Delmas. "Combining triazole ligation and enzymatic glycosylation on solid phase simplifies the synthesis of very long glycoprotein analogues." Chemical Science 6, no. 6 (2015): 3617–23. http://dx.doi.org/10.1039/c5sc00773a.

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Abstract:
Solid phase chemical ligation followed by enzymatic glycosylation exploits the advantages of a solid support to minimize the purification steps, constituting a promising approach for the synthesis of complex glycoproteins.
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