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Structural basis for acceptor-substrate recognition of UDP-glucose: anthocyanidin 3-${it O}$-glucosyltransferase from ${it Clitoria ternatea}$

Hiromoto, Takeshi; Honjo, Eijiro*; Tamada, Taro; Kuroki, Ryota; Noda, Hisanobu*; Kazuma, Kohei*; Suzuki, Masahiko*

UDP-glucose: anthocyanidin 3-${it O}$-glucosyltransferase from ${it Clitoria ternatea}$ (${it Ct}$3GT-A) catalyzes the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin. The glucosylation of delphinidin at the 3-hydroxyl group has been proposed as an initial glucosylation step toward the biosynthesis of ternatins, which are blue anthocyanins found in the petals of ${it C. ternatea}$. Although the crystal structures of several flavonoid glycosyltransferases (UGTs) were determined, the acceptor-substrate complexes were limited to the flavonol-bound forms. Here, in order to understand the acceptor-recognition scheme of ${it Ct}$3GT-A, the crystal structures in complex with anthocyanidin delphinidin and petunidin, and flavonol kaempferol were determined to resolutions of 2.6 ${AA}$, 2.7 ${AA}$, and 1.8 ${AA}$ respectively. The enzyme recognition of unstable anthocyanidins was firstly observed in this structural determination; nevertheless, the molecular orientations of these three acceptors in the binding site are different from those of the known flavonoid UGTs, ${it Vv}$GT1 and UGT78G1. The crystal structures of ${it Ct}$3GT-A provide insight not only into anthocyanidin configurations in enzyme, but also into a different binding scheme for acceptor-substrate recognition compared with the known UGTs.

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