Faculty Profiles - TAMURA Takashi

MISC - TAMURA Takashi

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2-IV-20 組換えL-メチオニン脱炭酸酵素の精製および性質検討(一般演題要旨,ビタミン・バイオファクター研究のさらなる魅力〜大和まほろぱからの発信〜,第67回大会講演要旨)

林将也, 岡田茜, 田村隆, 稲垣賢二

ビタミン 89 ( 4 ) 261 - 261 2015.4

放線菌Streptomyces incarnatus NRRL8089のドラフトゲノムシーケンス

清水瞳, 大島健志朗, 服部正平, 稲垣賢二, 田村隆

日本農芸化学会大会講演要旨集(Web) 2015 3A37P07 (WEB ONLY) 2015.3

Rhodococcus属放線菌由来低基質特異性L‐アミノ酸酸化酵素の遺伝子クローニングと発現系の構築

村上佳穂, 田港静, 橋本義輝, 小林達彦, 山田美和, 礒部公安, 田村隆, 稲垣賢二

日本農芸化学会大会講演要旨集(Web) 2015 2C22P14 (WEB ONLY) 2015.3

海洋細菌Marinomonas mediterranea由来L‐リシンε‐オキシダーゼの大腸菌発現系の構築

赤地周作, 松井大亮, 浅野泰久, 田村隆, 稲垣賢二

日本農芸化学会大会講演要旨集(Web) 2015 2C22P15 (WEB ONLY) 2015.3

Improvement of dye-mediated dehydrogenase activity of pyranose oxidase by site-directed mutagenesis

荒木俊雄, 中柄朋子, 田村隆, 稲垣賢二

岡山大学農学部学術報告 104 1 - 4 2015.2

Language：Japanese Publisher：岡山大学農学部

Pyranose oxidase (EC 1.1.3.10 ; PROD) catalyzes the oxidation of aldopyranoses at the position C‒2to yield the corresponding 2‒keto-aldoses and H2O2 , using oxygen as an electron acceptor. The enzyme shows broad substrate specificity as well as reactivity for 1,5‒anhydro‒d‒glucitol (1,5‒AG), which is known as a clinical glycemic marker. It is considered that the reactivity of PROD for 1,5‒AG is useful in the development of an amperometric-type biosensor, which is a convenient diagnostic device for selfmonitoringblood glucose (SMBG). However, the levels of dissolved oxygen in blood affect biosensorsystems that are equipped with an artificial electron mediator. In the present study, we attempted to develop an O2‒insensitive oxidase that would improve the dye-mediated dehydrogenase activity. We performed site-directed mutagenesis on PROD isolated from basidiomycetous fungus No. 52, which generated 11 mutants. The amino acid substitution Q421A exhibited a significant decrease (8.8% of wild type) in its oxidase activity, whereas it maintained its dehydrogenase activity (67% of wild type). In this study, we characterized PROD mutants from basidiomycetous fungus No. 52, which showed improved dye-mediated dehydrogenase activity.

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海洋細菌Marinomonas mediterranea由来L -リシンε-オキシダーゼの精製と性質

稲垣賢二, 赤地周作, 田村隆, 松井大亮, 岡崎誠司, 浅野泰久

2014年度ビタミンB研究委員会報告書 88 ( 9 ) 1 - 1 2015

抗腫瘍性L-リシンα-オキシダーゼの異種発現系構築と基質複合体のX線結晶構造解析

天野万里, 橋本義輝, 小林達彦, 近藤裕輝, 今田勝巳, 日下部均, 田村隆, 稲垣賢二

2014年度ビタミンB研究委員会報告書 89 ( 3 ) 19 - 19 2015

3P-026 In vitro SPS assay using Thermus thermophiles HB8 PPDK

Asano Kaori, Tobe Ryuta, Mihara Hisaaki, Nemoto Michiko, Inagaki Kenji, Tamura Takashi

67 277 - 277 2015

2P-184 Identification of [NiFeSe]-hydrogenases from sulfate reducing bacteria using ICP-MS

Mishima Ayaka, Imoto Satoshi, Morikawa Daichi, Nemoto Michiko, Inagaki Kenji, Tamura Takashi

67 220 - 220 2015

2-I-27 セレノリン酸合成酵素のPEPジキナーゼ共役法の確立(一般演題要旨,第66回大会講演要旨)

田村隆, 鎌田早帆, 稲垣賢二

ビタミン 88 ( 4 ) 240 - 240 2014.4

2-IV-21 L-メチオニンγ-リアーゼ基質複合体のX線結晶構造解析と基質認識に関わる残基の機能解析(一般演題要旨,第66回大会講演要旨)

安田江里, 古谷和大, 佐藤暖, 福本充樹, 工藤大蔵, 志波智生, 原田繁春, 田村隆, 稲垣賢二

ビタミン 88 ( 4 ) 261 - 261 2014.4

海洋細菌Marinomonas mediterranea由来L-リシンε-オキシダーゼの精製と性質検討、X線結晶構造解析

赤地周作, 岡崎誠司, 松井大亮, 田村隆, 稲垣賢二, 浅野泰久

ビタミン 88 ( 4 ) 240 - 240 2014.4

Characterization of L-Arginine Oxidase Made from L-Glutamate Oxidase

中井隆一郎, 藤野志保子, 内海友宏, 田村隆, 日下部均, 稲垣賢二

岡山大学農学部学術報告 103 5 - 9 2014.2

Language：Japanese Publisher：岡山大学農学部

L‒Glutamate oxidase (LGOX) from Streptomyces sp. X‒119‒6 has strict substrate specificity towardL‒glutamate. Recently, we solved the X‒ray crystal structure of LGOX and this revealed that Arg305 inthe active site is the key residue involved in substrate recognition. Therefore, we created 19 mutantenzymes of R305X‒LGOX by saturation mutagenesis. One of them R305D‒LGOX, Arg305 substitutedwith Asp exhibited oxidase activity for L‒Arg. Optimum pH of R305D‒LGOX mutant enzyme was pH8.5. Interestingly, the activity of R305D‒LGOX toward L‒Arg was inhibited by phosphate. And furthermore,the substrate specificity of R305D‒LGOX was affected by using buffer. The results of inhibitionanalysis suggest, that phosphate is a competitive inhibitor of R305D‒LGOX when L‒Arg is used assubstrate. Kinetic analysis of R305D‒LGOX showed that Km value and kcat value of R305D‒LGOX towardl-Arg were 0.68 mM and 6.7 s-1 respectively. In this study, we showed that R305D‒LGOX mutantenzyme is a novel l-arginine oxidase and useful for l-arginine biosensor.

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1P-053 Purification and properties of a new L-tyrosine oxidase made from L-glutamate oxidase.

Fujino Shihoko, Tamura Takashi, Kusakabe Hitoshi, Inagaki Kenji

66 30 - 30 2014