Faculty Profiles - TAMURA Takashi

MISC - TAMURA Takashi

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セレンは猛毒性・発癌性の栄養素?

田村隆

バイオアクティブ 11,15-18 2001

Molecular cloning of thioredoxin reductase isozymes, TrxR1 and TrxR2, from human lung adenocarcinoma cell line, NCI-H441

Proceedings Symposium on Trace Nutrients Research 18 149 - 153 2001

Streptomyces sp X-119-6 由来L-グルタミン酸オキシダーゼのクローニング及び発現

有馬二朗, 崎川智代, 田村隆, 芦内誠, 八木年春, 日下部均, 田中英彦, 稲垣賢二

微量栄養素研究 2001

709 放線菌由来L-グルタミン酸オキシダーゼを利用したL一GluセンサーとGOT・GPTセンシングへの応用

有馬二朗, 田村隆, 崎川智代, 金原陽平, 篠原寛明, 日下部均, 田中英彦, 稲垣賢二

日本生物工学会大会講演要旨集 13 289 - 289 2001

116 19F-nmrを用いるモノフルオロ酢酸生産のCosynthesis実験

田村隆, 澤本有香子, 田中英彦, 稲垣賢二

日本生物工学会大会講演要旨集 13 106 - 106 2001

Purification and some characteristics of a monomeric alanine racemase from an extreme thermophile, Thermus thermophilus

TK Seow, K Inagaki, T Nakamura, R Maeda, T Tamura, H Tanaka

JOURNAL OF BIOSCIENCE AND BIOENGINEERING 90 ( 3 ) 344 - 346 2000.9

Language：English Publisher：SOC BIOSCIENCE BIOENGINEERING JAPAN

We purified to homogeneity an alanine racemase (EC 5.1.1.1) from Thermus thermophilus HB8, an extreme thermophile. Interestingly, the enzyme possessed a monomeric structure with a molecular weight of about 38,000. The enzyme was most active at pH 8 and 75 degreesC, and remained active after incubation at 80 degreesC for 30 min.

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A colorimetric screening method for microorganisms having methionine gamma-lyase activity

LL Choo, T Tamura, RA Rahim, AM Ali, HM Ghazali, K Inagaki, H Tanaka

ASIA-PACIFIC JOURNAL OF MOLECULAR BIOLOGY AND BIOTECHNOLOGY 8 ( 1 ) 95 - 97 2000.6

Language：English Publisher：UNIV MALAYA

This paper reports a convenient screening method for detecting methionine gamma -lyase activity in microorganisms which can grow on DL-methionine as the sole nitrogen source. L-Methionine gamma -lyase has been known to have the most versatile catalytic properties among other pyridoxal-5'-phosphate-dependent enzymes, but only known from a limited number of biological sources. For an efficient screening of the enzyme, we employed 5,5'-dithiobis-(2-nitrobenzoic acid) (DTNB) to detect the enzyme reaction product methanethiol, which spontaneously reduces DTNB and develops a yellow coloration on and around colonies. The yellow color has emerged and faded away within 72 h, suggesting that the reduced DTNB may be oxidized by spontaneous and/or enzymatic formation of disulfide. This method, despite reduction in specificity compared to the standard assay, allowed us to select candidate microorganisms out of hundreds of other similar colonies merely by observing the yellow coloration.

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1-II-9 L-メチオニンγ-リアーゼの立体構造

稲垣賢二, 田村隆, 田中英彦, 本島浩之, 熊坂崇, 古市真木雄, 山本雅貴, 田中信夫, 江崎信芳, 左右田健次

ビタミン 74 ( 4 ) 197 - 197 2000.4

Preparation of NAD:penicillamine ADP transferase high producing Bacillus sphaericus.

Izumi Takuya, Tamura Takashi, Inagaki Kenji, Soda Kenji, Tanaka Hidehiko

12 34 - 34 2000

Purification and characterization of NAD:penicillamine ADP transferase from Bacillus sphaericus: A novel NAD-dependent enzyme catalyzing phosphoramide bond formation

Jun Yanagidani, Takashi Tamura, Kenji Inagaki, Kenji Soda, Hidehiko Tanaka

Journal of Biological Chemistry 274 ( 2 ) 795 - 800 1999.1

Language：English

A strain of Bacillus sphaericus isolated from a local soil sample has been found to use β,β-dimethyl-DL-cysteine (DL-penicillamine) as the sole nitrogen source. Crude cell extract of the bacterium showed potent penicillamine-consuming activity only in the presence of NAD, which, however, was not used as an electron acceptor. Characterization of reaction products revealed that penicillamine was derivatized to a phosphoramide adduct with the ADP moiety of NAD, whereas the nicotinamide-ribose group was released and hydrolyzed spontaneously to ribose and nicotinamide. The phosphoramide product, ADP-penicillamine, caused potent product inhibition on the purified enzyme, and adenylate deaminase was found to be effective in converting the inhibitory product into inosine-diphosphate-penicillamine and thereby maintained the catalysis for several hours. The novel enzyme, termed as NAD:penicillamine ADP transferase, showed a single band on SDS-polyacrylamide gel electrophoresis with a mass of approximately 42 kDa. The native enzyme was monomeric. The enzyme showed high substrate specificity to NAD (K(m) = 13.0 mM) and L-penicillamine (K(m) = 6.5 mM)
other nucleotides such as NADP, NAD(P)H, AMP, ADP, and ADP-ribose did not substitute for NAD, and L-valine, L-cysteine, L-homocysteine, L-cystine, L-leucine, and L-isoleucine did not serve as the substrate. Kinetic studies suggested an Ordered Bi Bi mechanism, with NAD as the first substrate to bind and ADP-L-penicillamine as the last product released. The novel NAD-dependent enzyme may catalyze the first step in penicillamine degradation in the strain of B. sphaericus.

DOI： 10.1074/jbc.274.2.795

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1. Thiobacillus thiooxidansのイソクエン酸脱水素酵素の性質と遺伝子クローニング

稲垣賢二, 井上宏之, 田村隆, 田中英彦

ビタミン 72 ( 10 ) 571 - 571 1998.10

Gene Cloning and Characterization of an Acidic Xylanase from Acidobacteriu

Kenji Inagaki, Ken Nakahira, Kazuhisa Mukai, Takashi Tamura, Hidehiko Tanaka

Bioscience, Biotechnology and Biochemistry 62 ( 6 ) 1061 - 1067 1998.1

Language：English

The gene xynA encoding an acid endo-β-1,4-xylanase from an acidophilic bacterium, Acidobacterium capsulatum 161, was cloned and expressed in Escherichia coli. The nucleotide sequence of the 1.6-kb DNA fragment containing xynA was analyzed, revealing an open reading frame of 1,215 bp encoding a peptide of 405 amino acid residues. The deduced amino acid sequence of XynA was very similar to other xylanases that are from the glycosyl hydrolase family 10. XynA was purified to homogeneity by SDS-polyacrylamide gel electrophoresis from E. coli transformants. The molecular mass and isoelectric point of XynA were 41 kDa and 7.3, respectively. The xylanase activity of the cloned XynA is an endo-acting enzyme that shows optimal activity at pH 5.0 and 65°C, and is stable pH between 3.0 and 8.0. The Km and Vmax with oat spelt xylan as a substrate at pH 5.0 and 30°C are 3.5 mg/ml and 403 μmol/min/mg. © 1998 Taylor &amp
Francis Group, LLC.

DOI： 10.1271/bbb.62.1061

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染料脱色微生物の検索, 単離及び, 脱色機構の解析

稲垣賢二, 川口将和, 田口隆章, 田村隆, 田中英彦

岡山大学農学部学術報告 87 47 - 51 1998

Alanine racemase from an acidophile, acidiphilium organovorum: Purification and characterization

Teck Keong Seow, Kenji Inagaki, Takashi Tamura, Kenji Soda, Hidehiko Tanaka

Bioscience, Biotechnology and Biochemistry 62 ( 2 ) 242 - 247 1998

Language：English

An alanine racemase (EC 5.1.1.1) from an acidophilic heterotrophic bacterium, Acidiphilium organovorum 13H, was purified and characterized. The enzyme had a dimeric structure with identical subunits of M, 33,000 each. Although A. organovorum 13H is an acidophile, the enzyme had its maximum velocity at pH 9, corresponding to its location in the cytoplasm. Activity was maximum between 50 and 60°C. For an enzyme from a mesophile, it was stable to heat, showing no loss of activity after a 30-min incubation at 65°C. The enzyme needed pyridoxal 5′. phosphate (PLP) as a cofactor for its activity, as seen from the loss of activity upon dialysis against PLP-free buffer containing hydroxylamine and its absorption maximum at 420 nm. Activity was ihhibited by common inhibitors of PLP-dependent enzymes. PLP content studies found that 1 mole of enzyme contained 2 moles of PLP. The enzyme catalyzed the symmetric reversible racemization of alanine exclusively. © 1998, Taylor &amp
Francis Group, LLC. All rights reserved.

DOI： 10.1271/bbb.62.242

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Pseudomonas putidaのL-メチオニン分解系オペロンの解析

井上宏之, 田村隆, 稲垣賢二, 田中英彦

岡山大学農学部学術報告 87 53 - 58 1998

Determination of methylation specificity of sequence-specific DNA methyltransferases using matrix assisted laser desorption/ionization time-of-flight mass spectrometry

Takashi Tamura, Yoshinori Araki, Seiji Yamaoka, Kenji Inagaki, Hidehiko Tanaka

Nucleic Acids Research 25 ( 20 ) 4162 - 4164 1997.10

Language：English Publishing type：Book review, literature introduction, etc.

We describe here a sensitive and straightforward method for characterizing the methylation specificity of type II DNA methyltransferase (MTase) using matrix-assisted laser desorption/ionization time-of-flight (MALDI-TOF) mass spectrometry. DNA substrate, prepared by ligation of a commercially available oligonucleotide, was modified by the subject MTase, and was derivatized to a mixture of single-stranded oligonucleotides through endonuclease treatment, heat-denaturation and limited digestion by 3'-terminus-specific phosphodiesterase I. MALDI-TOF mass spectrometry was used to determine the mass differences between the digestion products, and the methylated nucleotide was explicitly identified by the mass increase of 14 Da due to the base modification. The method was applicable to the three representative MTases M.EcoRI, M.BamHI and M.HaeIII.

DOI： 10.1093/nar/25.20.4162

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ゴ-ルドラッシュ時代を迎えたセレンの生化学研究 (特集最近の生命科学)

田村隆, 田中英彦

化学工業 48 ( 9 ) 720 - 726 1997.9

5.ペニシラミンの微生物代謝の酵素化学 : NADの新しい生理機能 : ビタミンB研究委員会第357回会議研究発表要旨

左右田健次, 柳谷純, 田村隆, 稲垣賢二, 田中英彦

ビタミン 71 ( 7 ) 312 - 313 1997.7

2-III-4 ADP-penicillamine合成酵素の精製と反応生成物の同定 : 第49回大会一般研究発表要旨

柳谷純, 田村隆, 稲垣賢二, 田中英彦, 左右田健次

ビタミン 71 ( 4 ) 210 - 210 1997.4

1-II-7 Pseudomonas putidaのメチオニン誘導性の新規α-ケト酪酸脱水素酵素E1について : 第49回大会一般研究発表要旨

井上宏之, 西藤晃, 田村隆, 稲垣賢二, 田中英彦

ビタミン 71 ( 4 ) 179 - 179 1997.4

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