Refine your search:     
Report No.
 - 
Search Results: Records 1-5 displayed on this page of 5
  • 1

Presentation/Publication Type

Initialising ...

Refine

Journal/Book Title

Initialising ...

Meeting title

Initialising ...

First Author

Initialising ...

Keyword

Initialising ...

Language

Initialising ...

Publication Year

Initialising ...

Held year of conference

Initialising ...

Save select records

Journal Articles

A Storm-induced flood and associated nearshore dispersal of the river-derived suspended $$^{137}$$Cs

Uchiyama, Yusuke*; Tokunaga, Natsuki*; Azuma, Kohei*; Kamidaira, Yuki; Tsumune, Daisuke*; Iwasaki, Toshiki*; Yamada, Masatoshi*; Tateda, Yutaka*; Ishimaru, Takashi*; Ito, Yukari*; et al.

Science of the Total Environment, 816, p.151573_1 - 151573_13, 2022/04

no abstracts in English

Journal Articles

Inventory analysis of suspended radiocesium derived from Niida River during a typhoon-induced flood event

Uchiyama, Yusuke*; Azuma, Kohei*; Odani, Sachika*; Iwasaki, Toshiki*; Tsumune, Daisuke*; Kamidaira, Yuki; Shimizu, Yasuyuki*; Onda, Yuichi*

Doboku Gakkai Rombunshu, B2 (Kaigan Kogaku) (Internet), 73(2), p.I_685 - I_690, 2017/10

no abstracts in English

Journal Articles

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

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

Protein Science, 24(3), p.395 - 407, 2015/03

 Times Cited Count:38 Percentile:85.24(Biochemistry & Molecular Biology)

UDP-glucose: anthocyanidin 3-${it O}$-glucosyltransferase (UGT78K6) from ${it Clitoria ternatea}$ catalyzes the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin. To understand the acceptor-recognition scheme of UGT78K6, the crystal structure of UGT78K6 and its complex forms with anthocyanidin delphinidin and petunidin, and flavonol kaempferol were determined to resolutions of 1.85 ${AA}$, 2.55 ${AA}$, 2.70 ${AA}$ and 1.75 ${AA}$ respectively. The anthocyanidin- and flavonol-acceptor binding details are almost identical in each complex structure, although the glucosylation activities against each acceptor were significantly different. The acceptor substrates in UGT78K6 are reversely bound to its binding site by a 180$$^{circ}$$ rotation about the O1-O3 axis of the flavonoid backbones observed in ${it Vv}$GT1 and UGT78G1. These substrate recognition schemes suggest the potential for controlled synthesis of natural pigments.

Journal Articles

Crystal structure of UDP-glucose:anthocyanidin 3-${it O}$-glucosyltransferase from ${it Clitoria ternatea}$

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

Journal of Synchrotron Radiation, 20(6), p.894 - 898, 2013/11

 Times Cited Count:34 Percentile:87.84(Instruments & Instrumentation)

Flowers of the butterfly pea (${it Clitoria ternatea}$) accumulate a group of polyacylated anthocyanins, named ternatins, in their petals. The first step in ternatin biosynthesis is the transfer of glucose from UDP-glucose to anthocyanidins such as delphinidin, a reaction catalyzed in ${it C. ternatea}$ by UDP-glucose:anthocyanidin 3-${it O}$-glucosyltransferase (${it Ct}$3GT-A; AB185904). To elucidate the structure-function relationship of ${it Ct}$3GT-A, recombinant ${it Ct}$3GT-A was expressed in ${it Escherichia coli}$ and its tertiary structure was determined to 1.85 ${AA}$, resolution by using X-ray crystallography. The structure of ${it Ct}$3GT-A shows a common folding topology, the GT-B fold, comprised of two Rossmann-like $$beta$$/$$alpha$$/$$beta$$ domains and a cleft located between the N- and C-domains containing two cavities that are used as binding sites for the donor (UDP-Glc) and acceptor substrates. By comparing the structure of ${it Ct}$3GT-A with that of the flavonoid glycosyltransferase ${it Vv}$GT1 from red grape (${it Vitis vinifera}$) in complex with UDP-2-deoxy-2-fluoro glucose and kaempferol, locations of the catalytic His-Asp dyad and the residues involved in recognizing UDP-2-deoxy-2-fluoro glucose were essentially identical in ${it Ct}$3GT-A, but certain residues of ${it Vv}$GT1 involved in binding kaempferol were found to be substituted in ${it Ct}$3GT-A. These findings are important for understanding the differentiation of acceptor-substrate recognition in these two enzymes.

Oral presentation

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*

no journal, , 

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.

5 (Records 1-5 displayed on this page)
  • 1