2022
DOI: 10.1016/j.synbio.2022.01.003
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Exploring the catalytic function and active sites of a novel C-glycosyltransferase from Anemarrhena asphodeloides

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Cited by 13 publications
(7 citation statements)
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“…Sun, Chen, et al, 2020; Z. L. Wang et al, 2020), but as recent works have shown, a single dual‐specific di‐CGT can also be sufficient to form the fully di‐glycosylated product. Within a rapidly growing number (≥67) of plant CGTs isolated and characterized (Bao et al, 2022; Y. Q. Zhang et al, 2022), only a few enzymes manage the difficult task of iterative glycosylation to release the di‐ C ‐glucoside product: Fc CGT, Fortunella crassifolia and Cu CGT, Citrus unshiu (Ito et al, 2017); Mi CGTb, Mangifera indica (Chen, Fan, et al, 2018); Gg CGT, Glycyrrhiza glabra (M. Zhang et al., 2020); Dca CGT, Dendrobium catenatum (Ren et al, 2020); Ab CGT, Aloe barbadensis (Xie et al, 2020); Aa CGT, Anemarrhena asphodeloides (Huang et al., 2022), and Ad CGT, Angelica decursiva (Z. Wang et al., 2022). Compared to CGTs performing only a single C ‐glycosylation, a relatively open and spacious acceptor substrate‐binding pocket appears to be requirement of the protein structure for di‐CGT activity (Chen, Fan, et al, 2018; M. Zhang et al., 2020).…”
Section: Introductionmentioning
confidence: 99%
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“…Sun, Chen, et al, 2020; Z. L. Wang et al, 2020), but as recent works have shown, a single dual‐specific di‐CGT can also be sufficient to form the fully di‐glycosylated product. Within a rapidly growing number (≥67) of plant CGTs isolated and characterized (Bao et al, 2022; Y. Q. Zhang et al, 2022), only a few enzymes manage the difficult task of iterative glycosylation to release the di‐ C ‐glucoside product: Fc CGT, Fortunella crassifolia and Cu CGT, Citrus unshiu (Ito et al, 2017); Mi CGTb, Mangifera indica (Chen, Fan, et al, 2018); Gg CGT, Glycyrrhiza glabra (M. Zhang et al., 2020); Dca CGT, Dendrobium catenatum (Ren et al, 2020); Ab CGT, Aloe barbadensis (Xie et al, 2020); Aa CGT, Anemarrhena asphodeloides (Huang et al., 2022), and Ad CGT, Angelica decursiva (Z. Wang et al., 2022). Compared to CGTs performing only a single C ‐glycosylation, a relatively open and spacious acceptor substrate‐binding pocket appears to be requirement of the protein structure for di‐CGT activity (Chen, Fan, et al, 2018; M. Zhang et al., 2020).…”
Section: Introductionmentioning
confidence: 99%
“…Within a rapidly growing number (≥67) of plant CGTs isolated and characterized (Bao et al, 2022;Y. Q. Zhang et al, 2022), only a few enzymes manage the difficult task of iterative glycosylation to release the di-C-glucoside product: FcCGT, Fortunella crassifolia and CuCGT, Citrus unshiu (Ito et al, 2017); MiCGTb, Mangifera indica (Chen, Fan, et al, 2018); GgCGT, Glycyrrhiza glabra (M. Zhang et al, 2020); DcaCGT, Dendrobium catenatum (Ren et al, 2020); AbCGT, Aloe barbadensis (Xie et al, 2020); AaCGT, Anemarrhena asphodeloides (Huang et al, 2022), and AdCGT, Angelica decursiva (Z. Wang et al, 2022).…”
Section: Introductionmentioning
confidence: 99%
“…To determine the kinetic parameters of CtUGT3 for naringenin, assays containing 50 mM Na 2 HPO 4 −NaH 2 PO 4 (pH 8.0), 1 μM CtUGT3, saturating UDP-glucose, and varying concentrations (5,10,20,40,80,100,200, 400, 800, 1000, and 1500 μM) of naringenin were performed at 37 °C for 5 min with a final volume of 100 μL. To determine the kinetic parameters of CtUGT3 for apigenin, assays containing 50 mM Na 2 HPO 4 −NaH 2 PO 4 (pH 8.0), 1 μM CtUGT3, saturating UDP-glucose, and varying concentrations (5,10,20,40,80,100,200, 400, 800, 1000, and 1500 μM) of apigenin were performed at 37 °C for 5 min with a final volume of 100 μL. To determine the kinetic parameters of CtUGT3 for kaempferol, assays containing 50 mM Na 2 HPO 4 −NaH 2 PO 4 (pH 8.0), 1 μM CtUGT3, saturating UDP-glucose, and varying concentrations (100, 200, 400, 800, 1000, 1200, 1600, 1800, 2000, and 2400 μM) of kaempferol, were performed at 37 °C for 5 min with a final volume of 100 μL.…”
Section: ■ Introductionmentioning
confidence: 99%
“…To determine the kinetic parameters of CtUGT3 for naringenin, assays containing 50 mM Na 2 HPO 4 −NaH 2 PO 4 (pH 8.0), 1 μM CtUGT3, saturating UDP-glucose, and varying concentrations (5,10,20,40,80,100,200, 400, 800, 1000, and 1500 μM) of naringenin were performed at 37 °C for 5 min with a final volume of 100 μL. To determine the kinetic parameters of CtUGT3 for apigenin, assays containing 50 mM Na 2 HPO 4 −NaH 2 PO 4 (pH 8.0), 1 μM CtUGT3, saturating UDP-glucose, and varying concentrations (5,10,20,40,80,100,200, 400, 800, 1000, and 1500 μM) of apigenin were performed at 37 °C for 5 min with a final volume of 100 μL.…”
Section: ■ Introductionmentioning
confidence: 99%
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