2020
DOI: 10.1105/tpc.20.00002
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Crystal Structures of the C-Glycosyltransferase UGT708C1 from Buckwheat Provide Insights into the Mechanism of C-Glycosylation

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Cited by 32 publications
(21 citation statements)
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“…Currently, 24 crystal structures of plant UGTs family 1 are available these include AtUGT72B1, 53 AtUGT74F2, 54 and AtUGT89C1 55 from Arabidopsis thaliana , CtUGT78K6 from Clitoria ternatea , 56 FeUGT708C1 from Fagopyrum esculentum , 57 GgCGT from Glycyrrhiza glabra , 58 UGT73P12 from Glycyrrhiza uralensis (; 7c2x), LpCGTa and b from Landoltia punctate , 59 MtUGT71G1, 60 MtUGT85H2, 61 and MtUGT78G1 62 from Medicago truncatula , Os79 from Oryza sativa , 63 PtigS from Persicaria tinctoria , 64,65 PaGT2 66 and 3 67 from Phytolacca americana , SbCGTa and b from Scutellaria baicalensis , 59 mogrol glucosyltransferase SgUGT74AC1 and AC2 from Siraitia grosvenorii , 39,68 SrUGT76G1 from Stevia rebaudiana , 69–71 C -glycosyltransferase from Trollius chinensis , 72 VvGT1 from Vitis vinifera , 32 and ZmCGTa from Zea mays 59 (). The 3-dimensional structures show remarkable conservation in their secondary and tertiary structures.…”
Section: Strategies For Functional Analysis Of Ugtsmentioning
confidence: 99%
“…Currently, 24 crystal structures of plant UGTs family 1 are available these include AtUGT72B1, 53 AtUGT74F2, 54 and AtUGT89C1 55 from Arabidopsis thaliana , CtUGT78K6 from Clitoria ternatea , 56 FeUGT708C1 from Fagopyrum esculentum , 57 GgCGT from Glycyrrhiza glabra , 58 UGT73P12 from Glycyrrhiza uralensis (; 7c2x), LpCGTa and b from Landoltia punctate , 59 MtUGT71G1, 60 MtUGT85H2, 61 and MtUGT78G1 62 from Medicago truncatula , Os79 from Oryza sativa , 63 PtigS from Persicaria tinctoria , 64,65 PaGT2 66 and 3 67 from Phytolacca americana , SbCGTa and b from Scutellaria baicalensis , 59 mogrol glucosyltransferase SgUGT74AC1 and AC2 from Siraitia grosvenorii , 39,68 SrUGT76G1 from Stevia rebaudiana , 69–71 C -glycosyltransferase from Trollius chinensis , 72 VvGT1 from Vitis vinifera , 32 and ZmCGTa from Zea mays 59 (). The 3-dimensional structures show remarkable conservation in their secondary and tertiary structures.…”
Section: Strategies For Functional Analysis Of Ugtsmentioning
confidence: 99%
“…3). The histidine residue at the N‐terminal region and the aspartic acid residue at the 120–130 th amino acid residues are conserved in the UGT708 family enzymes and considered essential for recognizing open‐chain‐type substrates such as 2‐hydroxynaringenin, phloretin, and maclurin [21]. However, the corresponding residues in HpGTs were replaced with asparagine (the 18 th residue) and serine (the 114 th residue), respectively (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…In the case of UGT708 enzymes, histidine at the N‐terminal region and aspartic acid at the 120–130 th residues (Fig. 3) are essential for recognizing open‐chain‐type substrates [21]. Since the lack of these residues in N4CGT1 and N4CGT2 (Fig.…”
Section: Discussionmentioning
confidence: 99%
“…The mutation (E396A) in the PSPG motif of TcCGT1 abolished the catalytic activity 21 . Other cases also reported that mutations in this region lead to a complete loss of enzymatic activity 17 , 50 , but the single mutation of P361W in the PSPG motif of TcOGT4 switched the sugar donor preference from UDP-Gal to UDP-Glc 48 . Our studies revealed more key residues in this motif that formed hydrogen bonds with the specific hydroxyl groups of sugar moieties, i.e., M296 and Q318 interacted with O4 and O2 of the sugar, respectively.…”
Section: Discussionmentioning
confidence: 99%