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SCIENTIA SINICA Vitae, Volume 49, Issue 9: 1133-1142(2019) https://doi.org/10.1360/SSV-2019-0164

Research progress in understanding the structure, mechanism, and engineering of plant glycosyltransferases

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  • ReceivedAug 13, 2019
  • AcceptedAug 27, 2019
  • PublishedSep 6, 2019

Abstract

Glycosyltransferases (GTs) are found in a wide variety of organisms, where they are involved in maintaining cell metabolism through glycosylation reactions. Glycosyltransferases transfer activated sugar from donor molecules to a variety of acceptors, this can alter the hydrophilic properties, stability, and chemical properties as well as subcellular location and biological activity of the acceptors. Many compounds that are modified by glycosylation are important sources of drug molecules. However, natural products contain only small amounts of glycosylated compounds, and it is very difficult to extract and purify these compounds. Furthermore, during the chemical synthesis of glycosylated compounds, the raw material reagents and generated by-products tend to cause environmental pollution, and it is not possible to achieve glycosylation at the particular acceptor sites. Recently, GTs have garnered interest among researchers. Therefore, here we review the current structural studies and biotechnological applications of plant GTs that would provide useful information for glycosylation engineering and bioactive glycoside production.


Funded by

国家重点研发计划(2017YFA0504801,2018YFA0901800)

天津市自然科学基金(15JCZDJC65500)

南开大学交叉融合科学基金(63191138)


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  • Figure 1

    Four different folding patterns of glycosyltransferases (GTs). A: GT-A: the structure of nucleotide-diphospho-sugar transferase spsA from Bacillus subtilis (PDB 1QGQ). B: GT-B: the structure of bovine β1,4-galactosyltransferase T1 (PDB 1FR8). C: GT-C: the structure of full-length oligosaccharyltransferase PglB from Campylobacter lari (PDB 3RCE). D: GT-D: the structure of domain of unknown function 1792 (DUF1792) from Streptococcus parasanguinis (PDB 4PFX)

  • Figure 2

    The catalytic mechanisms of glycosyltransferases (GTs). A: GTs catalyze the transfer of sugars by either “inversion” or “retention”of the conformation with respect to the sugar donor substrates. B: the catalytic mechanism of “inversion” GTs. C: the catalytic mechanisms of “retention” GTs

  • Table 1   Crystal structure information of plant glycosyltransferases

    UGT 名称

    分辨率 (Å)

    晶体复合物

    PDB编号

    发表年份

    MtUGT71G1

    2.0

    UDP

    2ACV

    2005

    2.6

    UDP-glucose

    2ACW

    VvGT1

    1.9

    UDP

    2C1X

    2006

    1.9

    UDP-2FGlc, kaempferol

    2C1Z

    2.1

    UDP and quercetin

    2C9Z

    MtUGT85H2

    2.1

    Apo

    2PQ6

    2007

    AtUGT72B1

    1.45

    UDP

    2VCH

    2007

    1.75

    UDP and Tris

    2VG8

    1.9

    UDP-2FGlc, 2,4,5-trichlorophenol

    2VCE

    MtUGT78G1

    2.1

    UDP

    3HBJ

    2009

    2.1

    UDP and myricetin

    3HBF

    CtUGT78K6

    1.85

    Apo

    3WC4

    2015

    1.85

    UDP

    4WHM

    2.55

    Delphinidin

    4REM

    2.7

    Petunidin

    4REN

    1.75

    Kaempferol

    4REL

    Os79

    1.8

    UDP-open

    5TME

    2016

    2.3

    UDP-closed

    5TMB

    2.4

    UDP-2FGlc, trichothecene

    5TMD

    Os79Q202A

    1.47

    UDP

    6BKO

    2017

    Os79H122A/L123A

    1.29

    UDP

    6BK1

    Os79T291V

    1.58

    UDP

    6BK2

    Os79

    2.17

    UDP, deoxynivalenol-3-glucose

    6BK3

    AtUGT74F2

    2.56

    UDP, salicylic acid (BA)

    5U6M

    2017

    2.0

    UDP, 2-bromobenzoic acid (2BA)

    5U6S

    AtUGT74F2T15S

    2.0

    UDP, salicylic acid

    5U6N

    AtUGT74F2T15A

    2.0

    UDP, 2-bromobenzoic acid

    5V2K

    AtUGT74F2T15S

    1.8

    UDP, 2-bromobenzoic acid

    5V2J

    PtUGT1

    2.14

    Indoxyl sulfate

    5NLM

    2018

    AtUGT89C1

    2.7

    Apo

    6IJ7

    2019

    3.0

    UDP

    6IJ9

    3.21

    UDP-β-L-rhamnose

    6IJA

    3.2

    Quercetin

    6IJD

    UGT76G1

    1.8

    (SeMet) UDP

    6O86

    2019

    1.75

    UDP

    6O87

    1.99

    UDP, rebaudioside A

    6O88

    UGT76G1

    1.69

    UDP

    6INF

    2019

    UGT76G1H25A

    1.7

    UDP, GOL

    6ING

    UGT76G1

    2.1

    AQ9, GOL, UDP

    6INH

    UGT76G1

    1.7

    AQ9, AUO, GOL, UDP

    6INI

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