Orginal Article |
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Enzymatic Glycosylation and Its Function in Metabolic Process of Cells |
Xiao-chen LIU,Hu LIU,Liang ZHANG,Chun LI() |
Institute for Biotransformation and Synthetic Biosystem, Department of Biological Engineering, Beijing Institute of Technology, Beijing 100081,China |
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Abstract The cell viability and functions are finely regulated through various biochemical modification occurred in the metabolism process. Enzymatic glycosylation is a common molecular modification in metabolic regulation and has an important impact on maintaining and regulating cells functions. Glycosyltransferases are enzymes that catalyze the transfer glycosyl moieties from activated donor to a wide and diverse range of acceptor molecules. The glycosylation of the acceptor molecules lead to changes of their intracellular properties such as stability, solubility and regional localization, and thus played important roles in many bioprocesses including cell cycles, signal transduction, protein expression, resistance responses, and clearance of pollutants. The classification, naming and catalytic mechanism of glycosyltransferase superfamily are briefly introduced. Then the glycosylation of protein and small molecule compounds and their functions in metabolic processes are reviewed, when the glycoside was transferred to intracellular biomolecule proteins and small molecule compounds. At last,the application prospects of glycosyltransferases and glycosylation reactions in the fields of human health pharmaceutical products, industrial catalysis, food and agriculture are looked forward.
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Received: 05 September 2017
Published: 31 January 2018
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[1] |
De B F, Maertens J, Beauprez J, et al.Biotechnological advances in UDP-sugar based glycosylation of small molecules. Biotechnology Advances, 2015, 33(2): 288-302.
doi: 10.1016/j.biotechadv.2015.02.005
pmid: 25698505
|
|
|
[2] |
Dennis J W, Granovsky M, Warren C E.Protein glycosylation in development and disease. Bioessays, 1999, 21(5): 412-421.
doi: 10.1002/(SICI)1521-1878(199905)21:53.0.CO;2-5
pmid: 10376012
|
|
|
[3] |
Tiwari P, Sangwan R S, Sangwan N S.Plant secondary metabolism linked glycosyltransferases: An update on expanding knowledge and scopes. Biotechnology Advances, 2016, 34(5): 714-739.
doi: 10.1016/j.biotechadv.2016.03.006
pmid: 27131396
|
|
|
[4] |
Ohtsubo K, Marth J D.Glycosylation in cellular mechanisms of health and disease. Cell, 2006, 126(5): 855-867.
doi: 10.1016/j.cell.2006.08.019
pmid: 16959566
|
|
|
[5] |
Campbell J A, Davies G J, Bulone V, et al.A classification of nucleotide-diphospho-sugar glycosyltransferases based on amino acid sequence similarities. Biochemical Journal, 1997, 326(3): 929-939.
doi: 10.1006/abbi.1997.0277
pmid: 9334165
|
|
|
[6] |
Coutinho P M, Deleury E, Davies G J, et al.An evolving hierarchical family classification for glycosyltransferases. Journal of Molecular Biology, 2003, 328(2): 307-317.
doi: 10.1002/ca.10202
pmid: 12691742
|
|
|
[7] |
Bock K W. The UDP-glycosyltransferase (UGT) superfamily expressed in humans, insects and plants: Animal-plant arms-race and co-evolution. Biochemical Pharmacology, 2016, 99: 11-17.
doi: 10.1016/j.bcp.2015.10.001
pmid: 26453144
|
|
|
[8] |
Liang D M, Liu J H, Wu H, et al.Glycosyltransferases: mechanisms and applications in natural product development. Chemical Society Reviews, 2015, 44(22): 8350-8374.
doi: 10.1039/c5cs00600g
|
|
|
[9] |
Nabokina S M, Subramanian V S, Said H M.The human colonic thiamine pyrophosphate transporter (hTPPT) is a glycoprotein and N-linked glycosylation is important for its function. Biochimica Et Biophysica Acta-Biomembranes, 2016, 1858(4): 866-871.
|
|
|
[10] |
Yu L Y, He H B, Hu Z F, et al.Comprehensive quantification of N-glycoproteome in Fusarium graminearum reveals intensive glycosylation changes against fungicide. Journal of Proteomics, 2016, 142: 82-90.
doi: 10.1016/j.jprot.2016.05.011
pmid: 27180282
|
|
|
[11] |
Cheng C M, Ru P, Geng F, et al.Glucose-mediated N-glycosylation of SCAP is essential for SREBP-1 activation and tumor growth. Cancer Cell, 2015, 28(5): 569-581.
doi: 10.1016/j.ccell.2015.09.021
pmid: 4643405
|
|
|
[12] |
Swamy M, Pathak S, Grzes K M, et al.Glucose and glutamine fuel protein O-GlcNAcylation to control T cell self-renewal and malignancy. Nature Immunology, 2016, 17(6): 712-720.
doi: 10.1038/ni.3439
pmid: 27111141
|
|
|
[13] |
Chen Y, Jin L, Xue B, et al.NRAGE induces beta-catenin/Arm O-GlcNAcylation and negatively regulates Wnt signaling. Biochemical and Biophysical Research Communications, 2017, 487(2): 433-437.
doi: 10.1016/j.bbrc.2017.04.080
|
|
|
[14] |
Krempl C, Sporer T, Reichelt M, et al.Potential detoxification of gossypol by UDP-glycosyltransferases in the two Heliothine moth species Helicoverpa armigera and Heliothis virescens. Insect Biochemistry and Molecular Biology, 2016, 71: 49-57.
doi: 10.1016/j.ibmb.2016.02.005
pmid: 26873292
|
|
|
[15] |
Konig S, Feussner K, Kaever A, et al.Soluble phenylpropanoids are involved in the defense response of Arabidopsis against Verticillium longisporum. New Phytologist, 2014, 202(3): 823-837.
doi: 10.1111/nph.12709
pmid: 24483326
|
|
|
[16] |
Liu Z, Yan J P, Li D K, et al.UDP-glucosyltransferase71C5, a major glucosyltransferase, mediates abscisic acid homeostasis in Arabidopsis. Plant Physiology, 2015, 167(4): 1659-U846.
doi: 10.1104/pp.15.00053
pmid: 25713337
|
|
|
[17] |
Wiederschain G Y.Glycobiology: Progress, problems, and perspectives. Biochemistry-Moscow, 2013, 78(7): 679-696.
doi: 10.1134/S0006297913070018
pmid: 24010832
|
|
|
[18] |
Bond M R, Hanover J A.A little sugar goes a long way: The cell biology of O-GlcNAc. Journal of Cell Biology, 2015, 208(7): 869-880.
doi: 10.1083/jcb.201501101
pmid: 25825515
|
|
|
[19] |
Van D S, Rudd P M, Dwek R A, et al.Concepts and principles of O-linked glycosylation. Critical Reviews in Biochemistry and Molecular Biology, 1998, 33(3): 151-208.
doi: 10.1080/10409239891204198
pmid: 9673446
|
|
|
[20] |
Zhang X Y, Wang Y Z.Glycosylation quality control by the golgi structure. Journal of Molecular Biology, 2016, 428(16): 3183-3193.
doi: 10.1016/j.jmb.2016.02.030
pmid: 26956395
|
|
|
[21] |
Zhang X L.Roles of glycans and glycopeptides in immune system and immune-related diseases. Current Medicinal Chemistry, 2006, 13(10): 1141-1147.
doi: 10.2174/092986706776360897
pmid: 16719775
|
|
|
[22] |
Takeuchi H, Haltiwanger R S.Role of glycosylation of Notch in development. Seminars in Cell & Developmental Biology, 2010, 21(6): 638-645.
doi: 10.1016/j.semcdb.2010.03.003
pmid: 2898917
|
|
|
[23] |
Bowles D, Isayenkova J, Lim E K, et al.Glycosyltransferases: managers of small molecules. Current Opinion in Plant Biology, 2005, 8(3): 254-263.
doi: 10.1016/j.pbi.2005.03.007
pmid: 15860422
|
|
|
[24] |
Rai A, Umashankar S, Rai M, et al.Coordinate regulation of metabolite glycosylation and stress hormone biosynthesis by TT8 in Arabidopsis. Plant Physiology, 2016, 171(4): 2499-2515.
doi: 10.1104/pp.16.00421
pmid: 27432888
|
|
|
[25] |
Dima O, Morreel K, Vanholme B, et al.Small glycosylated lignin oligomers are stored in Arabidopsis leaf vacuoles. Plant Cell, 2015, 27(3): 695-710.
doi: 10.1105/tpc.114.134643
pmid: 25700483
|
|
|
[26] |
Maag D, Dalvit C, Thevenet D, et al.3-beta-D-glucopyranosyl-6-methoxy-2-benzoxazolinone (MBOA-N-Glc) is an insect detoxification product of maize 1,4-benzoxazin-3-ones. Phytochemistry, 2014, 102(8): 97-105.
doi: 10.1016/j.phytochem.2014.03.018
pmid: 24713572
|
|
|
[27] |
Gwak H, Kim S, Dhanasekaran D N, et al.Resveratrol triggers ER stress-mediated apoptosis by disrupting N-linked glycosylation of proteins in ovarian cancer cells. Cancer Letters, 2016, 371(2): 347-353.
doi: 10.1016/j.canlet.2015.11.032
|
|
|
[28] |
Lauf P K, Adragna N C.K-CI cotransport: Properties and molecular mechanism. Cellular Physiology and Biochemistry, 2000, 10(5-6): 341-354.
doi: 10.1159/000016357
pmid: 11125215
|
|
|
[29] |
Weng T Y, Chiu W T, Liu H S, et al.Glycosylation regulates the function and membrane localization of KCC4. Biochimica Et Biophysica Acta-Molecular Cell Research, 2013, 1833(5): 1133-1146.
|
|
|
[30] |
Chen P H, Smith T J, Wu J, et al. Glycosylation of KEAP1 links nutrient sensing to redox stress signaling. The EMBO Journal, 2017,36(15):2233-2250.
|
|
|
[31] |
WellS L, Vosseller K, Hart G W. Glycosylation of nucleocytoplasmic proteins: Signal transduction and O-GlcNAc. Science, 2001, 291(5512): 2376-2378.
doi: 10.1126/science.1058714
pmid: 11269319
|
|
|
[32] |
Barron C C, Bilan P J, Tsakiridis T, et al.Facilitative glucose transporters: Implications for cancer detection, prognosis and treatment. Metabolism-Clinical and Experimental, 2016, 65(2): 124-139.
doi: 10.1016/j.metabol.2015.10.007
pmid: 26773935
|
|
|
[33] |
Preston G C, Sinclair L V, Kaskar A, et al.Single cell tuning of Myc expression by antigen receptor signal strength and interleukin-2 in T lymphocytes. Embo Journal, 2015, 34(15): 2008-2024.
doi: 10.15252/embj.201490252
pmid: 4551349
|
|
|
[34] |
Tan L, Showalter A M, Egelund J, et al. Arabinogalactan-proteins and the research challenges for these enigmatic plant cell surface proteoglycans. Frontiers in Plant Science, 2012, 3(140):1-10.
|
|
|
[35] |
Basu D, Tian L, Debrosse T, et al.Glycosylation of a fasciclin-like arabinogalactan-protein (SOS5) mediates root growth and seed mucilage adherence via a cell wall receptor-like kinase (FEI1/FEI2) pathway in Arabidopsis. PLoS One, 2016, 11(1): e0145092.
|
|
|
[36] |
Tan F Y Y, Tang C M, Exley R M. Sugar coating: bacterial protein glycosylation and host-microbe interactions. Trends in Biochemical Sciences, 2015, 40(7): 342-350.
doi: 10.1016/j.tibs.2015.03.016
pmid: 25936979
|
|
|
[37] |
Yuan J S, Tranel P J, Stewart C N.Non-target-site herbicide resistance: a family business. Trends in Plant Science, 2007, 12(1): 6-13.
doi: 10.1016/j.tplants.2006.11.001
|
|
|
[38] |
Poppenberger B, Berthiller F, Lucyshyn D, et al.Detoxification of the Fusarium mycotoxin deoxynivalenol by a UDP-glucosyltransferase from Arabidopsis thaliana. Journal of Biological Chemistry, 2003, 278(48): 47905-47914.
doi: 10.1074/jbc.M307552200
pmid: 12970342
|
|
|
[39] |
Lin J S, Huang X X, Li Q, et al.UDP-glycosyltransferase 72B1 catalyzes the glucose conjugation of monolignols and is essential for the normal cell wall lignification in Arabidopsis thaliana. Plant Journal, 2016, 88(1): 26-42.
doi: 10.1111/tpj.13229
pmid: 27273756
|
|
|
[40] |
Barros J, Serk H, Granlund I, et al.The cell biology of lignification in higher plants. Annals of Botany, 2015, 115(7): 1053-1074.
doi: 10.1093/aob/mcv046
pmid: 4648457
|
|
|
[41] |
Saema S, Rahman L U, Singh R, et al.Ectopic overexpression of WsSGTL1, a sterol glucosyltransferase gene in Withania somnifera, promotes growth, enhances glycowithanolide and provides tolerance to abiotic and biotic stresses. Plant Cell Reports, 2016, 35(1): 195-211.
doi: 10.1007/s00299-015-1879-5
|
|
|
[42] |
Mishra M K, Chaturvedi P, Singh R, et al.Overexpression of WsSGTL1 gene of withania somnifera enhances salt tolerance, heat tolerance and cold acclimation ability in transgenic Arabidopsis plants. PLoS One, 2013, 8(4): e63064.
doi: 10.1371/journal.pone.0063064
pmid: 23646175
|
|
|
[43] |
Li P, Li Y J, Zhang F J, et al.The Arabidopsis UDP-glycosyltransferases UGT79B2 and UGT79B3, contribute to cold, salt and drought stress tolerance via modulating anthocyanin accumulation. Plant Journal, 2017, 89(1): 85-103.
doi: 10.1111/tpj.13324
pmid: 27599367
|
|
|
[44] |
Morant A V, Jorgensen K, Jorgensen C, et al.beta-glucosidases as detonators of plant chemical defense. Phytochemistry, 2008, 69(9): 1795-1813.
doi: 10.1016/j.phytochem.2008.03.006
pmid: 18472115
|
|
|
[45] |
Ostrowski M, Jakubowska A.Udp-glycosyltransferases of plant hormones. Postepy Biologii Komorki, 2013, 40(1): 141-160.
doi: 10.2478/acb-2014-0003
|
|
|
[46] |
Jin S H, Ma X M, Han P, et al.UGT74D1 Is a novel auxin glycosyltransferase from Arabidopsis thaliana. PLoS One, 2013, 8(4): e61705.
doi: 10.1371/journal.pone.0061705
pmid: 23613909
|
|
|
[47] |
Song C K, Hong X T, Zhao S, et al.Glucosylation of 4-hydroxy-2,5-dimethyl-3(2H)-furanone, the key strawberry flavor compound in strawberry fruit. Plant Physiology, 2016, 171(1): 139-151.
doi: 10.1104/pp.16.00226
pmid: 26993618
|
|
|
[48] |
Jaakola L.New insights into the regulation of anthocyanin biosynthesis in fruits. Trends in Plant Science, 2013, 18(9): 477-483.
doi: 10.1016/j.tplants.2013.06.003
pmid: 23870661
|
|
|
[49] |
Miyoshi E, Kamada Y.Application of glycoscience to the early detection of pancreatic cancer. Cancer Science, 2016, 107(10): 1357-1362.
doi: 10.1111/cas.13011
pmid: 27418030
|
|
|
[50] |
Zuegg J, Muldoon C, Adamson G, et al.Carbohydrate scaffolds as glycosyltransferase inhibitors with in vivo antibacterial activity. Nature Communications, 2015, 6: 1-11.
doi: 10.1038/ncomms8719
pmid: 4530474
|
|
|
[51] |
Mullard A.Can next-generation antibodies offset biosimilar competition. Nature Reviews Drug Discovery, 2012, 11(6): 426-428.
doi: 10.1038/nrd3749
pmid: 22653202
|
|
|
[52] |
贺真蛟, 佟晨瑶, 耿放, 等. 糖基化修饰对IgG/IgY结构和功能特性的影响. 中国食品学报, 2017, 17(4): 174-181.
|
|
|
[52] |
He Z J, Tong C Y, Geng F, et al.The effects of glycosylation on the structure and functional properties of IgG/IgY. Journal of Chinese Institute of Food Science and Technology, 2017, 17(4): 174-181.
|
|
|
[53] |
张芳, 许之珏, 徐颖姣, 等. IgG糖基化与疾病相关性研究进展. 生命科学, 2017, 29(4): 319-330.
|
|
|
[53] |
Zhang F, Xu Z J, Xu Y J, et al.The glycosylation of immunoglobulin G and its alterations in diseases. Chinese Bulletin of Life Sciences, 2017, 29(4): 319-330.
|
|
|
[54] |
Huang G, Lv M, Hu J, et al.Glycosylation and activities of natural products. Mini-Reviews in Medicinal Chemistry, 2016, 16(12): 1013-1016.
|
|
|
[55] |
冯旭东,吕波,李春. 酶分子稳定性改造研究进展. 化工学报, 2016,67(1): 277-284.
doi: 10.11949/j.issn.0438-1157.20151025
|
|
|
[55] |
Feng X D, Lu B, Li C.Advances in enzyme stability modification. CIESC Journal, 2016, 67(1): 277-284.
doi: 10.11949/j.issn.0438-1157.20151025
|
|
|
[56] |
汪胡芳, 莫丽英, 王杏利, 等. 糖基化改性甜菊苷、橙皮苷及芦丁苷作为新型药物载体的研究与应用. 中国实验方剂学杂志, 2017, 23(23): 220-227.
|
|
|
[56] |
Wang H F, Mo L Y, Wang X L, et al. Research advances in application of transglycosylated stevioside, hesperidin and rutin as new drug carrier materials. Chinese Journal of Experimental Traditional Medical Formulae, 2017, 23(23): 220-227.
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