Faculty Profiles - TAMURA Takashi

MISC - TAMURA Takashi

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2P-062 Disulfide Isomerase Activity of E.coli dsbA [CXXC] Mutants

Suto Shinya, Kiyoto Asako, Inagaki Kenji, Tamura Takashi

65 119 - 119 2013

マンガン酸化系を構成する2種の細菌の相互作用解析

田村隆, 周藤慎也, 稲垣賢二

特別経費(プロジェクト分)－大学の特性を生かした多様な学術研究機能の充実－成果報告書 89 2013

抗腫瘍性酵素 L-リシンα-オキシダーゼのX線結晶構造解析

稲垣賢二, 天野万里, 田村隆, 佐野宰久, 今田勝己, 日下部均

ビタミン 87 ( 8 ) 463 - 464 2013

L-グルタミン酸オキシダーゼより作成したL-ヒスチジンオキシダーゼの構造解析とL-アルギニンオキシダーゼの特性解析

稲垣賢二, 中井隆一郎, 田村隆, 今田勝巳, 日下部均

ビタミンB研究委員会報告書 87 ( 1 ) 51 - 52 2013

2-V-16 セレノリン酸合成酵素SPS1/SPS2の相互作用(一般演題要旨,日本ビタミン学会第64回大会講演要旨)

田村隆, 奥河内貴大, 鎌田早帆, 高畑宗明, 稲垣賢二

ビタミン 86 ( 4 ) 289 - 289 2012.4

Purification and Characterization of Thermostable Amidase from Thermus sp.O-3-1

小林史明, 青峰弘起, 水無渉, 湯不二夫, 田村隆, 稲垣賢二

岡山大学農学部学術報告 101 1 - 6 2012.2

Language：Japanese Publisher：岡山大学農学部

The gene encoding a thermostable amidase (EC 3.5.1.4) from thermophilic bacterium Thermus sp.O-3-1, was cloned and expressed in Escherichia coli JM109. The cloned amidase gene (ami) is 930 bp and encodes a protein composed of 310 amino acids. The protein is predicted to have a molecular mass of 33,089 Da. The amidase from Thermus sp.O-3-1 was purified by heat treatment and DEAE Toyopearl 650M column chromatography. The molecular mass of the native enzyme was estimated to be about 70 kDa by gel filtration chromatography, indicating that the enzyme has a homodimeric structure. The purified enzyme was stable up to 80°C and within a pH range from 7.0 to 10.0. The optimum temperature and pH for enzyme activity were 90°C, and 9.0, respectively. The enzyme was strongly inhibited by the metal-chelating compound EDTA. The activity of the EDTA-treated enzyme was reactivated by the addition of Co(2+), Ni(2+) and Mn(2+) ions. Therefore the enzyme was predicted to be metalloenzyme. Finally,as a result of investigation into substrate specificity, the purified enzyme was suggested to be D-amino acid specific amidase, as it showed higher activity toward D-Leu-pNA than L-Leu-pNA.好熱性細菌Thermus sp.O-3-1 由来の耐熱性アミダーゼ遺伝子を大腸菌中にクローニングし，その塩基配列を決定した．ami 遺伝子は930 bp からなり，310アミノ酸をコードしていた．本酵素の分子量は33，089 Daであると予想された．Thermus sp.O-3-1 由来アミダーゼを大腸菌で生産させ，熱処理とDEAE-トヨパール650M陰イオン交換カラム等により精製した．ゲル濾過クロマトグラフィーとSDS-PAGE の結果から本酵素は分子質量33 kDa のサブユニット2分子からなるダイマー構造を有していることが明らかとなった．精製酵素の熱安定性は80℃まで，pH 安定性は7.0～10.0であり，安定性の高い酵素であった．最適温度は90℃，最適 pH は9.0であった．EDTA により活性が著しく阻害され，Co(2+)やNi(2+)，Mn(2+)によって活性の回復，向上が見られたため，本酵素は金属酵素であることが示唆された．基質特異性の検討の結果，L-Leu-pNA よりもD-Leu-pNA に対して高い活性を示したため，本酵素がＤ-アミノ酸基質に特異性を持つアミダーゼであることが判明した．本酵素は耐熱性を有するユニークなＤ-アミノ酸アミダーゼであり，今後産業利用が期待される．

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2Dp10 Molecular Evolution of [NiFeSe]H2ase based on Phylogenetic Tree and Modeling

Tamura Takashi, Tsunekawa Naoki, Hirano Toshiyuki, Sato Fumitoshi, Inagaki Kenji

64 52 - 52 2012

3Cp04 Analysis of the substrate recognition mechanism in high substrate specificity L-glutamate oxidase and characterization of substrate specificity modified enzymes

Nakai Ryuichiro, Tamura Takashi, Kusakabe Hitoshi, Imada Katsumi, Inagaki Kenji

64 123 - 123 2012

L-メチオニンγ-リアーゼC116H変異酵素の構造と機能解析

福本充樹, 工藤大蔵, 原田繁春, 田村隆, 稲垣賢二

ビタミンB研究委員会報告書 85 ( 8 ) 446 - 447 2012

2-I-28 ヒト由来セレノシステインβリアーゼ遺伝子の発現系構築と機能解析(一般演題要旨,日本ビタミン学会第63回大会講演要旨)

田村隆, 佐藤久美, 稲垣賢二

ビタミン 85 ( 4 ) 249 - 249 2011.4

2-IV-9 好熱好酸性アーキアSulfolobus tokodaii由来シスタチオニンγ-シンターゼのPhe97残基の機能解析(一般演題要旨,日本ビタミン学会第63回大会講演要旨)

山田哲也, 福本充樹, 柳谷昌彦, 工藤大蔵, 田村隆, 倉光成紀, 稲垣賢二

ビタミン 85 ( 4 ) 247 - 247 2011.4

Purification and characterization of L-methionine decarboxylase from Streptomyces sp. 590

前村知美, 内富久美子, 日下知香, 稲垣純子, 田村隆, 左右田健次, 稲垣賢二

Scientific Reports of the Faculty of Agriculture, Okayama University 100 ( 100 ) 3 - 7 2011.2

Language：Japanese Publisher：岡山大学農学部

L-Methionine decarboxylase [EC 4.1.1.57] catalyzes the decarboxylation of L-methionine and is a pyridoxal 5'-phosohate(PLP)-dependent enzyme. L-Methionine decarboxylase has been purified 630-fold by DEAE-Toyopearl 650M, Phenyl-Toyopearl 650M and Sephacryl S-300 column chromatographies from Streptomyces sp.590. The enzyme has a dimeric structure with identical subunits of Mr 60,000. This enzyme shows optimum activity at pH7.0 and 45°C, and is stable between pH5.7 and pH9.0. L-Methionine decarboxylase has antitumor activity against RERF-LC-AI and HeLa cells. Ten N-terminal amino acid sequence of L-methionine decarboxylase was determined, and the sequence showed no homology with other reported proteins.

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Structural Characterization of L-Glutamate Oxidase from Streptomyces sp. X-119-6

Arima Jiro, Sasaki Chiduko, Sakaguchi Chika, Mizuno Hiroshi, Tamura Takashi, Kashima Akiko, Kusakabe Hitoshi, Sugio Shigetoshi, Inagaki Kenji

Vitamins 85 ( 1 ) 23 - 24 2011.1

食品分析用小型うま味センサーの開発

稲垣賢二, 田村隆, 中井隆一郎

うま味研究会助成金による成果報告書 2011

ヒト由来セレノシステインβ-リアーゼ様タンパク質の発現, 活性確認と機能解析

田村隆, 佐藤久美, 稲垣賢二

ビタミン 85 ( 3 ) 155 - 155 2011

2Dp21 Structure and metal analysis of thermostable amidase from Thermus sp. O-3-1

Kobayashi Fumiaki, Aomine Hiroki, Ohtaki Akashi, Odaka Masafumi, Yohda Masafumi, Mizunashi Wataru, Yu Fujio, Tamura Takashi, Inagaki Kenji

63 140 - 140 2011

3Ea13 Random Mutation of DsbA and redox potentials

Kiyoto Asako, Tamura Takashi, Yoshida Takamasa, Inagaki Kenji

63 229 - 229 2011

Introduction of MOPAC simulation for experimental biochemists

TAMURA Takashi

82 ( 9 ) 863 - 867 2010.9

Production improvement of antifungal, antitrypanosomal nucleoside sinefungin by rpoB mutation and optimization of resting cell system of Streptomyces incarnatus NRRL 8089.

Koji Fukuda, Takashi Tamura, Hideyuki Ito, Sayaka Yamamoto, Kozo Ochi, Kenji Inagaki

Journal of bioscience and bioengineering 109 ( 5 ) 459 - 65 2010.5

Language：English

Sinefungin, a nucleoside antibiotic with potent antifungal, antiviral, and anti-trypanosome activities, has been a target for production enhancement in the past decades through medium optimization and strain improvement. For the purpose of introducing a more rational approach, we induced rpoB mutation in the producer strain, Streptomyces incarnatus NRRL 8089, by optimized UV-irradiation, and a resulting rifampicin-resistant strain rif-400 increased the sinefungin production by 7-fold. The growth and melanin production were obviously accelerated in the rifampicin-resistant high-producer mutant, while the morphological differentiation such as aerial mycelia and spiked-spore formation was retained. Molecular cloning and DNA sequencing identified a single mutation A1340G in the rpoB gene, which encodes the beta-subunit of RNA polymerase, and the resulting amino acid substitution Asp447Gly corresponded to one of mutations that reportedly allowed the transcriptional up-regulation of actinorhodin production in S. coelicolor A3(2). Sinefungin production was further enhanced by resting cell system using the rpoB mutant strain in the presence of 10 mM L-Arg. D-Arg or L-ornithine did not enhance the sinefungin production, and >50 mM urea strongly suppressed the nucleoside antibiotic production, supporting the proposed biosynthetic mechanism by which urea is liberated from the guanidino-group-bearing intermediate that is produced by enzymatic condensation of L-Arg and ATP.

DOI： 10.1016/j.jbiosc.2009.10.017

PubMed

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1-III-6 Pseudomonas putida由来L-メチオニン γ-リアーゼの活性中心残基への変異導入による基質特異性の改変(一般演題,日本ビタミン学会第62回大会発表要旨)

福本充樹, 工藤大蔵, 田村隆, 稲垣賢二

ビタミン 84 ( 4 ) 165 - 165 2010.4

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