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Advances in the Study of Glycosyltransferases in Plant Secondary Metabolite Biosynthesis

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DOI: 10.23977/medcm.2022.040102 | Downloads: 4 | Views: 236

Author(s)

Jiang Lingmin 1, Luo Yuefang 2

Affiliation(s)

1 Changde Vocational Technical College, Changde, 415000, Hunan, China
2 Xintian County Market Supervision Administration, Yongzhou, Hunan, 425700, China

Corresponding Author

Jiang Lingmin

ABSTRACT

Glycosyltransferases are enzymes that can catalyze the transfer of glycosyl groups from an activated donor to a specific receptor molecule, which is ubiquitous in organisms and forms a super gene family. Glycosyltransferases are involved in various biological processes of plant life activities, and play an important role in plant secondary metabolism. This paper summarizes the progress of glycosyltransferases in plant secondary metabolic pathway, describes the gene family and its relationship with the evolution of plant secondary metabolic pathway, and summarizes the current methods of cloning glycosyltransferases Strategy.

KEYWORDS

Glycosyltransferase, Plant secondary metabolic pathway

CITE THIS PAPER

Jiang Lingmin, Luo Yuefang, Advances in the Study of Glycosyltransferases in Plant Secondary Metabolite Biosynthesis. MEDS Chinese Medicine (2022) Vol. 4: 8-13. DOI: http://dx.doi.org/10.23977/medcm.2022.040102.

REFERENCES

[1] Zouhar J, Vevodova J, Marek J, Damborsky J, Su X D,Brzobohaty B. 2001.Insights into the functional architecture of the catalytic center of a maize  β-glucosidase Zm-p60.1. Plant Physiol., 127: 973–985 .
[2] Vogt T , Jones P . Glycosyltransferases in plant natural product syn-thesis: characterization of a supergene family. Trends in plant science, 2000,5(9):380~386.
[3] Hu Y, Walker S. Remarkable structural similarities between diverse  glycosyltransferases. Chemistry & biology, 2002, 9(12):1287 ~1296.
[4] Xu JF, Su ZG, Feng PS. Activity of tyrosol glucosyltransferase and improved salidroside production through biotransformation of tyrosol in Rhodiola sachalinensis cell cultures. J Biotechnol, 1998, 61(1): 69−73.
[5] Mao GX, Deng HB, Yuan LG, et al. Protective role of salidroside against aging                    in a mouse model induced by D-galactose. Biomed Environ Sci, 2010, 23(2): 161−166.
[6] Coutinho PM, Deleury E, Davies GJ, et al . An evolving hierarchicalfamily      classification for glycosyltransferases. Journal of molecular bi-ology, 2003 , 328 (2):307 ~317 .
[7] Achnine L, Blancaflor E B, Rasmussen S, Dixon R A. 2004.Colocalization of    L-phenylalanine ammonia-lyase and cinnamate4-hydroxylase for metabolic         channeling in phenylpropanoidbiosynthesis. Plant Cell, 16: 3,098–3,109
[8] Brugliera F , Holton TA, Stevenson TW, et al . Isolation and charac-terization of a c DNA clone corresponding to the Rt locus of Petuniahybrida. The Plant Journal , 1994, 5(1):81~92.
[9] Boss PK, Davies C, Robinson SP . Expression of anthocyanin biosyn-thesis   pathway genes in red and white grapes. Plant Molecular Biol-ogy, 1996,  32(3 ):565~569.
[10] Fukuchi -Mizutani M, Okuhara H, Fukui Y, et al . Biochemical andmolecular characterization of a novel UDP -glucose: anthocyanin 3' -O -glucosyltransferase, a key enzyme for blue anthocyanin biosynthe-sis, from gentian. Plant physiology, 2003 , 132(3 ):1652.
[11] Xu JF, Su ZG. Regulation of metabolism for improved salidroside production in cell suspension culture of Rhodiola sachalinensis A. Bor: the effect of precursors. Nat Prod Res Dev, 1997, 10(2): 8−14.
[12] Landtag J, Baumert A, Degenkolb T, et al. Accumulation of tyrosol glucoside in transgenic potato plants expressing a parsley tyrosine decarboxylase. Phytochemistry, 2002, 60(7): 683−689.
[13] Shi LL, Wang L, Zhang YX, Liu YJ (2007) Approaches tobiosynthesis of salidroside and its key metabolic enzymes. ForStud China 9(4):295–299.
[14] Yao K, De Luca V, Brisson N. Creation of a metabolic sink for tryptophan alters the phenylpropanoid pathway and the susceptibility of potato to Phytophthora infestans. Plant Cell, 1995, 7(11): 1787−1799.
[15] Facchini PJ, Huber-Allanach KL, Tari LW. Plant aromatic L-amino acid decarboxylases: evolution, biochemistry, regulation, and metabolic engineering applications. Phytochemistry, 2000, 54(2): 121−138
[16] Staswick PE, Tiryaki I. The oxylipin signal jasmonic acid is acti -vated by an enzyme that conjugates it to isoleucine in Arabidopsis.The Plant Cell , 2004, 16(8 ):2117 .
[17] Armah C, Mackie A, Roy C, et al . The membrane -permeabilizingeffect of avenacin A -1 involves the reorganization of bilayer cholesterol . Biophysical journal , 1999, 76(1): 281~290.
[18] Shirley AM, Mc Michael CM, Chapple C. The sng2 mutant of Ara -bidopsis is defective in the gene encoding the serine carboxypepti-dase like protein sinapoylglucose: choline sinapoyltransferase. ThePlant Journal , 2001, 28(1): 83~94.
[19] Lehfeldt C, Shirley AM, Meyer K, et al . Cloning of the SNG1 geneof Arabidopsis reveals a role for a serine carboxypeptidase -like pro-tein as an acyltransferase in secondary metabolism. The Plant CellOnline, 2000, 12(8): 1295~1306.
[20] Chemical Industry Press, 110–153 (in Chinese) Thorlby G, Fourrier N, Warren G. 2004. The sensitive to freezing gene, required for freezing tolerance in Arabidopsis thaliana, encodes a β-glucosidase. Plant Cell, 16: 2,192–2,203
[21] Tikunov Y, Lommen A, Bovy A G, Verhoeven H A, Bino R J, Hall R D, Bovy A G. 2005. A novel approach for nontargeted data analysis for metabolomics: large-scale profiling of tomato fruit volatiles. Plant Physiol., 139: 1,125–1,137
[22] Shao H, He X, Achnine L, et al . Crystal structures of a multifunc-tional triterpene/flavonoid glycosyltransferase from Medicago truncat-ula. The Plant Cell Online , 2005, 17(11): 3141~3154.
[23] Hou B, Lim EK, Higgins GS, et al . N -glucosylation of cytokininsby glycosyltransferases of Arabidopsis thaliana. Journal of BiologicalChemistry, 2004, 279(46): 47822.
[24] Nitnaware KM, Naik DG, Nikam TD (2011) Thidiazuron-induced shoot organogenesis and production of hepatoprotective lignan phyllanthin and hypophyllanthin in Phyllanthus amarus. Plant Cell Tissue Organ Cult 104:101–110.
[25] Gachon CMM, Langlois -Meurinne M, Henry Y, et al . Transcrip-tional co -regulation of secondary metabolism enzymes in Arabidop-sis: functional and evolutionary implications. Plant Molecular Biolo-gy, 2005, 58(2): 229~245.
[26] Jorgensen K, Rasmussen AV, Morant M, et al . Metabolon formationand metabolic channeling in the biosynthesis of plant natural prod-ucts. Current opinion in plant biology, 2005, 8(3): 280~291.
[27] Wink M. Evolution of secondary metabolites from an ecological andmolecular phylogenetic perspective. Phytochemistry, 2003, 64(1):3~19.
[28] Bufler G, Bangerth F (1982) UV-induced peroxidase and phenylalanine ammonia lyase activity and phaseollin accumulation in leaves of Phaseolus vulgaris L. in relation to ethylene. Plant Sci Lett 25(2):227–237
[29] Abidov, M., Grachev, S., Seifulla, R.D. & Ziegenfuss, T.N. (2004): Extract of Rhodiola rosea radix reduces the level of C-reactive protein and creatinine kinase in the blood. Bull. Exp. Biol. Medicine, 7, 63–64.
[30] Goossens A, Hakkinën S T, Laakso I, Seppänen-Laakso T, Biondi S, De Sutter V, Lammertyn F, Nuutila A M, Söderlund H, Zabeau M, Inzé D, Oksman-Caldentey K M. 2003. A functional genomics approach toward the understanding of secondary metabolism in plant cells. Proc. Nat. Acad. Sci. USA, 100: 8,595–8,600.
[31] Herrmann K M. 1995. The shikimate pathway as an entry to aromatic secondary metabolism. Plant Physiol., 107: 7–12
[32] Jiang C J, Yu Y B. 2001. The research progress of PAL. J. Anhui Agric. Univ., 28(4): 425–430 (in Chinese with an English abstract)
[33] Landtag, J., Baumert, A., Degenkolb, T., Schmidt, J., Wray, V., Scheel, D., Strack, D. & Rosahl, S. (2002): Accumulation of tyrosol glucoside in transgenic potato plants expressing a parsley tyrosine decarboxylase. Phytochemistry, 60, 683–689.
[34] Lacombe, E., Hawkins, S., Van Doorsselaere, J., Piquemal, J., Goffner, D., Poeydomenge, O., Boudet, A.-M. & Grima-Pettenati, J. (1997): Cinnamoyl CoA reductase, the first committed enzyme of the lignin branch biosynthetic pathway: cloning, expression and phylogenetic relationships. Pl. J., 11, 429–441.
[35] Lu, S., Zhou, Y., Li, L. & Chiang, V.L. (2006): Distinct roles of cinnamate 4-hydroxylase genes in Populus. Pl. Cell Physiol., 47, 905–914.
[36] Ma, L.Q., Liu, B.Y., Gao, D.Y., Pang, X.B., Lu, S.Y., Yu, H.S., Wang, H., Yan, F., Li, Z.Q., Li, Y.F. & Ye, H.C. (2007): Molecular cloning and overexpression of a novel UDP-glucosyltransferase elevating salidroside levels in Rhodiola sachalinensis. Pl. Cell Rep., 26, 989–999.
[37] D W, Iyanagi T, Lancet D, Louisot P, Magdalou J, Chowdhury J R, Ritter J K,  Schachter H, Tephly T R, Tipton K F, Nebert D W. 1997. The UDP glycosyltransferase gene superfamily: recommended nomenclature update based on evolutionary divergence. Pharmacogenetics, 7: 255–269.

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