Updated on 2021/04/27

写真a

 
KATO Dai-ichiro
 
Organization
Research Field in Science, Science and Engineering Area Graduate School of Science and Engineering (Science) Department of Science Chemistry Program Assistant Professor
Title
Assistant Professor

Degree

  • 博士(理学) ( 2005.3   慶應義塾大学 )

Research Interests

  • ポリアミド分解酵素

  • ファージディスプレイ

  • 抗体

  • チオエステル化

  • 生物発光

  • ホタルルシフェラーゼ

Research Areas

  • Nanotechnology/Materials / Structural organic chemistry and physical organic chemistry

  • Life Science / Bioorganic chemistry

  • Nanotechnology/Materials / Bio chemistry

  • Life Science / Bioorganic chemistry  / 酵素有機化学

Education

  • Keio University

    - 2005.3

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    Country: Japan

Research History

  • Kagoshima University   Research Field in Science, Science and Engineering Area Graduate School of Science and Engineering (Science) Department of Science Chemistry Program   Assistant Professor

    2020.4

  • Kagoshima University   Research Field in Science, Science and Engineering Area Graduate School of Science and Engineering (Science) Chemistry and Bioscience Course   Assistant Professor

    2014.10 - 2020.3

Professional Memberships

  • 日本生物工学会

    2005.4

  • 生体触媒化学研究会

    2000.4

  • 生物発光化学発光研究会

    2012.4

  • 日本農芸化学会

    2005.4

  • 日本化学会

    2000.4

Committee Memberships

  • 生体触媒化学研究会   幹事  

    2020.4   

  • 日本ペプチド学会若手ペプチド夏の勉強会   幹事  

    2017.4   

  • 日本生物工学会   和文誌編集委員  

    2012.1 - 2019.5   

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    Committee type:Other

 

Papers

  • Structural and functional characterization of nylon hydrolases .  Methods in Enzymology648   357 - 389   2021.1Reviewed International journal

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Methods in Enzymology  

    DOI: 10.1016/bs.mie.2020.11.004

    Scopus

    PubMed

  • Resurrecting the ancient glow of the fireflies .  Science Advances6 ( 49 )   2020.12Reviewed International journal

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Science Advances  

    DOI: 10.1126/sciadv.abc5705

    Scopus

  • Evaluation of the population structure and phylogeography of the Japanese Genji firefly, Luciola cruciata, at the nuclear DNA level using RAD-Seq analysis .  Scientific Reports10 ( 1 ) 1533   2020.12Reviewed International journal

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    Authorship:Lead author, Corresponding author   Language:English   Publishing type:Research paper (scientific journal)   Publisher:Scientific Reports  

    DOI: 10.1038/s41598-020-58324-9

    Scopus

    PubMed

  • Efficient Screening and Design of Variable Domain of Heavy Chain Antibody Ligands Through High Throughput Sequencing for Affinity Chromatography to Purify Fab Fragments .  Monoclonal Antibodies in Immunodiagnosis and Immunotherapy38 ( 5 ) 190 - 200   2019.10Reviewed International journal

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Monoclonal Antibodies in Immunodiagnosis and Immunotherapy  

    DOI: 10.1089/mab.2019.0027

    Scopus

    PubMed

  • Masahiro Takeo, Kenta Yamamoto, Masashi Sonoyama, Kana Miyanaga, Nana Kanbara, Koichi Honda, Dai-ichiro Kato, Seiji Negoro .  Characterization of the 3-methyl-4-nitrophenol degradation pathway and genes of Pseudomonas sp. strain TSN1 .  J. Biosci. Bioeng.126 ( 3 ) 355 - 362   2018.9Characterization of the 3-methyl-4-nitrophenol degradation pathway and genes of Pseudomonas sp. strain TSN1Reviewed

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  • Seiji Negoro, Naoki Shibata, Young-Ho Lee, Ikki Takehara, Ryo Kinugasa, Keisuke Nagai, Yusuke Tanaka, Dai-ichiro Kato, Masahiro Takeo, Yuji Goto, Yoshiki Higuchi .  Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolase .  Sci. Rep.8   9725   2018.6Structural basis of the correct subunit assembly, aggregation, and intracellular degradation of nylon hydrolaseReviewed

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  • 斎藤 達也, 石黒 直哉, 加藤 太一郎 .  mtDNA CO II遺伝子領域の解析によるゲンジボタルの養殖個体と野生個体の地域個体群の判定 .  DNA多型26 ( 1 ) 64 - 68   2018.6mtDNA CO II遺伝子領域の解析によるゲンジボタルの養殖個体と野生個体の地域個体群の判定Reviewed

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    Language:Japanese   Publishing type:Research paper (scientific journal)  

  • M.Takeo, K.Kimura, S.Mayilraj, T.Inoue, S.Tada, K.Miyamoto, M.Kashiwa, K.Ikemoto, P.Baranwal, D.Kato, S.Negoro .  Biosynthetic Pathway and Genes of Chitin/Chitosan-Like Bioflocculant in the Genus Citrobacter .  Polymers10 ( 3 ) 237   2018.2Biosynthetic Pathway and Genes of Chitin/Chitosan-Like Bioflocculant in the Genus CitrobacterReviewed

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  • I.Takehara, T.Fujii, Y.Tanimoto, D.Kato, M.Takeo, S.Negoro .  Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipate .  Appl. Microbiol. Biotechnol.102 ( 2 ) 801 - 814   2017.12Metabolic pathway of 6-aminohexanoate in the nylon oligomer-degrading bacterium Arthrobacter sp. KI72: identification of the enzymes responsible for the conversion of 6-aminohexanoate to adipateReviewed

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  • Juri Maeda, Dai-ichiro Kato, Kazunari Arima, Yuji Ito, Atsushi Toyoda, Hideki Noguchi .  The complete mitogenome and phylogenetic analysis of Japanese firefly ‘Genji Botaru’ Luciola cruciata (Coleoptera: Lampyridae) .  Mitochondrial DNA Part B2 ( 2 ) 522 - 523   2017.8The complete mitogenome and phylogenetic analysis of Japanese firefly ‘Genji Botaru’ Luciola cruciata (Coleoptera: Lampyridae)Reviewed

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    DOI: 10.1080/23802359.2017.1365641

  • Juri Maeda, Dai-ichiro Kato, Kazunari Arima, Yuji Ito, Atsushi Toyoda, Hideki Noguchi .  The complete mitochondrial genome sequence and phylogenetic analysis of Luciola lateralis, one of the most famous firefly in Japan (Coleoptera: Lampyridae) .  Mitochondrial DNA Part B2 ( 2 ) 546 - 547   2017.8The complete mitochondrial genome sequence and phylogenetic analysis of Luciola lateralis, one of the most famous firefly in Japan (Coleoptera: Lampyridae)Reviewed

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    DOI: 10.1080/23802359.2017.1365640

  • Kamrul Hasan Khan, Arisa Himeno, Shouhei Kosugi, Yosuke Nakashima, Abdur Rafique, Ayana Imamura, Takaaki Hatanaka, Dai-Ichiro Kato, Yuji Ito .  IgY-binding peptide screened from a random peptide library as a ligand for IgY purification .  J. Pep. Sci.23 ( 10 ) 790 - 797   2017.7IgY-binding peptide screened from a random peptide library as a ligand for IgY purificationReviewed

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  • I.Takehara, D.Kato, M.Takeo, S.Negoro .  Draft Genome Sequence of the Nylon Oligomer-Degrading Bacterium Arthrobacter sp. Strain KI72 .  Genome Announc.5 ( 17 ) e00217-17   2017.4Draft Genome Sequence of the Nylon Oligomer-Degrading Bacterium Arthrobacter sp. Strain KI72Reviewed

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    DOI: doi: 10.1128/genomeA.00217-17

  • J.Maeda; D.Kato, M.Okuda, M.Takeo, S.Negoro, K.Arima, Y.Ito, K.Niwa .  Biosynthesis-inspired deracemizative production of D-luciferin by combining luciferase and thioesterase .  Biochimi. Biophys. Acta (BBA) - General Subjects1861 ( 8 ) 2112 - 2118   2017.4Biosynthesis-inspired deracemizative production of D-luciferin by combining luciferase and thioesteraseReviewed

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  • S.Negoro, Y.Kawashima, N.Shibata, T.Kobayashi, T.Baba, Y.H.Lee, K.Kamiya, Y.Shigeta, K.Nagai, I.Takehara, D.Kato, M.Takeo, Y.Higuchi .  Mutations affecting the internal equilibrium of the reaction catalysed by 6-aminohexanoate-dimer hydrolase .  FEBS Lett.590 ( 18 ) 3133 - 3143   2016.8Mutations affecting the internal equilibrium of the reaction catalysed by 6-aminohexanoate-dimer hydrolaseReviewed

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  • A.Sotokawauchi, M.Kato-Murayama, K.Murayama, T.Hosaka, I.Maeda, M.Onjo, N.Ohsawa, D.Kato, K.Arima, M.Shirouzu .  Structural Basis of Cucumisin Protease Activity Regulation by Its Propeptide .  J. Biochem.161 ( 1 ) 45 - 53   2016.7Structural Basis of Cucumisin Protease Activity Regulation by Its PropeptideReviewed

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  • R.A.Prado, C.R.Santos, D.Kato, M.T.Murakami, V.Viviani .  The dark and bright sides of an enzyme: threedimensional structure of the N-terminal domain of Zophobas morio luciferase-like enzyme, inferences on the biological function and origin of oxygenase/luciferase activity .  Photochem. Photobiol. Sci.15   654 - 665   2016.3The dark and bright sides of an enzyme: threedimensional structure of the N-terminal domain of Zophobas morio luciferase-like enzyme, inferences on the biological function and origin of oxygenase/luciferase activityReviewed

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  • D.Kato, D.Shirakawa, R.Polz, M.Maenaka, M.Takeo, S.Negoro, K.Niwa .  Firefly inspired one-pot chemiluminescence system using n-propylphosphonic anhydride (T3P) .  Photochem. Photobiol. Sci.13 ( 12 ) 1640 - 1645   2014.12Firefly inspired one-pot chemiluminescence system using n-propylphosphonic anhydride (T3P)Reviewed

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  • R.Prado, D.Kato, M.Murakami, V.Viviani .  Thioesterification activity and the biological function of the enigmatic luciferase-like enzyme of Zophobas morio (Coleoptera; Tenebrionidae) Malpighian Tubules .  Luminescence29 ( S1 ) 89 - 89   2014.6Thioesterification activity and the biological function of the enigmatic luciferase-like enzyme of Zophobas morio (Coleoptera; Tenebrionidae) Malpighian TubulesReviewed

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  • K.Niwa, D.Kato, M.Maenaka, Y.Ohmiya .  Quantum yield and spectrum of D-aminoluciferin bioluminescence reaction .  Luminescence29 ( S1 ) 85 - 86   2014.6Quantum yield and spectrum of D-aminoluciferin bioluminescence reactionReviewed

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  • K.Nagai, K.Iida, K.Shimizu, R.Kinugasa, M.Izumi, D.Kato, M.Takeo, K.Mochiji, S.Negoro .  Enzymatic hydrolysis of nylons: quantification of the reaction rate of nylon hydrolase for thin-layered nylons .  Appl. Microbiol. Biotechnol.98 ( 20 ) 8751 - 8761   2014.5Enzymatic hydrolysis of nylons: quantification of the reaction rate of nylon hydrolase for thin-layered nylonsReviewed

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  • K.Kimura, T.Inoue, N.Nagayama, K.Miyamoto, M.Kashiwa, S.Mayilraj, D.Kato, S.Negoro, M.Takeo .  Effects of Organic Acids and Amino Acids on the Flocculation Activity of Chitosan-Like Bioflocculant-Producing Citrobacter freundii IFO13545 .  Japanese J. Wat. Treat. Biol. 50 ( 1 ) 23 - 31   2014.1Effects of Organic Acids and Amino Acids on the Flocculation Activity of Chitosan-Like Bioflocculant-Producing Citrobacter freundii IFO13545Reviewed

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  • K.Nagai, K.Yasuhira, Y.Tanaka, D.Kato, M.Takeo, Y.Higuchi, S.Negoro, N.Shibata .  Crystallization and X-ray diffraction analysis of nylon hydrolase (NylC) from Arthrobacter sp. KI72 .  Acta Cryst. F69   1151 - 1154   2013.9Crystallization and X-ray diffraction analysis of nylon hydrolase (NylC) from Arthrobacter sp. KI72Reviewed

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  • M.Takeo, A.Ohara, S.Sakae, Y.Okamoto, C.Kitamura, D.Kato, S.Negoro .  Function of a Glutamine Synthetase-Like Protein in Bacterial Aniline Oxidation via γ-Glutamylanilide .  J. Bacteriol.195 ( 19 ) 4406 - 4414   2013.7Function of a Glutamine Synthetase-Like Protein in Bacterial Aniline Oxidation via γ-GlutamylanilideReviewed

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  • V.R.Viviani, R.A.Prado, D.R.Neves, D.Kato,J.A.Barbosa .  A Route from Darkness to Light: Emergence and Evolution of Luciferase Activity in AMP-CoA-Ligases Inferred from a Mealworm Luciferase-like Enzyme .  Biochemistry52 ( 23 ) 3963 - 3973   2013.5A Route from Darkness to Light: Emergence and Evolution of Luciferase Activity in AMP-CoA-Ligases Inferred from a Mealworm Luciferase-like EnzymeReviewed

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  • D.Kato, Y.Hiraishi, M.Maenaka, K.Yokoyama, K.Niwa, Y.Ohmiya, M.Takeo, S.Negoro .  Interconversion of ketoprofen recognition in firefly luciferase-catalyzed enantioselective thioesterification reaction using from Pylocoeria miyako (PmL) and Hotaria parvura (HpL) just by mutating two amino acid residues .  J. Biotechnol. 168   277 - 283   2013.4Interconversion of ketoprofen recognition in firefly luciferase-catalyzed enantioselective thioesterification reaction using from Pylocoeria miyako (PmL) and Hotaria parvura (HpL) just by mutating two amino acid residuesReviewed

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  • K.Kimura, T.Inoue, D.Kato, S.Negoro, M.Ike, M.Takeo .  Distribution of chitin/chitosan-like bioflocculant-producing potential in the genus Citrobacter .  Appl. Microbiol. Biotechnol. 97   9569 - 9577   2013.3Distribution of chitin/chitosan-like bioflocculant-producing potential in the genus CitrobacterReviewed

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  • D.Kato, T.Kubo, M.Maenaka, K.Niwa, Y.Ohmiya, M.Takeoa, S.Negoro .  Confirmation of color determination factors for Ser286 derivatives of firefly luciferase from Luciola cruciata (LUC-G) .  J. Mol. Catal. B: Enzymatic87   18 - 23   2013.2Confirmation of color determination factors for Ser286 derivatives of firefly luciferase from Luciola cruciata (LUC-G)Reviewed

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  • D.Kato, Y.Hiraishi, K.Yokoyama, K.Niwa, Y.Ohmiya, M.Takeo, S.Negoro .  Enantioselective thioesterification activity in bioluminescent enzyme, firefly luciferase .  Luminescence27   124 - 125   2012.7Enantioselective thioesterification activity in bioluminescent enzyme, firefly luciferaseReviewed

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  • M.Maenaka, D.Kato, T.Kubo, K.Niwa, Y.Ohmiya, M.Takeo, S.Negoro .  Color tuning of bioluminescence reaction by modifying the hydrogen bond network around the active site in firefly luciferase .  Luminescence27   137 - 138   2012.7Color tuning of bioluminescence reaction by modifying the hydrogen bond network around the active site in firefly luciferaseReviewed

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  • K.Niwa, Y.Ichino, M.Maenaka, T.Kubo, Y.Hiraishi, D.Kato, Y.Ohmiya .  Quantum yield and kinetics of the bioluminescence reaction using various beetle luciferases .  Luminescence27   147 - 148   2012.7Quantum yield and kinetics of the bioluminescence reaction using various beetle luciferasesReviewed

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  • M.Takeo, Y.Maeda, J.Maeda, N.Nishiyama, C.Kitamura, D.Kato, S.Negoro .  Two identical nonylphenol monooxygenase genes linked to IS6100 and some putative IS elements in Sphingomonas sp. NP5 .  Microbiology 158   1796 - 1807   2012.6Two identical nonylphenol monooxygenase genes linked to IS6100 and some putative IS elements in Sphingomonas sp. NP5Reviewed

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  • S.Negoro, N.Shibata, Y.Tanaka, K.Yasuhira, H.Shibata, H.Hashimoto, Y.H.Lee, S.Oshima, R.Santa, S.Oshima, K.Mochiji, Y.Goto, T.Ikegami, K.Nagai, D.Kato, M.Takeo, Y.Higuchi .  Three-dimensional Structure of Nylon Hydrolase and Mechanism of Nylon-6 Hydrolysis .  J. Biol. Chem. 287   5079 - 5090   2012.3Three-dimensional Structure of Nylon Hydrolase and Mechanism of Nylon-6 HydrolysisReviewed

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  • D.Kato, K.Yokoyama, Y.Hiraishi, M.Takeo, S.Negoro .  Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly Luciferases .  Biosci. Biotech. Biochem.75   1758 - 1762   2011.10Comparison of Acyl-CoA Synthetic Activities and Enantioselectivity toward 2-Arylpropanoic Acids in Firefly LuciferasesReviewed

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  • K.Yasuhira, N.Shibata, Y.Tanaka, N.Kumagai, Y.Tanaka, K.Nagai, D.Kato, M.Takeo, S.Negoro, Y.Higuchi .  Crystallization and X-ray diffraction analysis of nylon oligomer hydrolase (NylC) from Agromyces sp. KY5R .  Acta Cryst.F67   892 - 895   2011.9Crystallization and X-ray diffraction analysis of nylon oligomer hydrolase (NylC) from Agromyces sp. KY5RReviewed

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  • K.Yamamoto, M.Nishimura, D.Kato, M.Takeo, S.Negoro .  Identification and characterization of another 4-nitrophenol degradation gene cluster, nps, in Rhodococcus sp. strain PN1 .  J. Biosci. Bioeng.111   687 - 694   2011.7Identification and characterization of another 4-nitrophenol degradation gene cluster, nps, in Rhodococcus sp. strain PN1Reviewed

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  • H.Liu, K.Nakagawa, D.Kato, D.Chaudhary, M.O.Tade .  Enzyme Encapsulation in Freeze-dried Bionanocomposites Prepared from Chitosan and Xanthan Gum Blend .  Mater. Chem. Phys.129   488 - 494   2011.5Enzyme Encapsulation in Freeze-dried Bionanocomposites Prepared from Chitosan and Xanthan Gum BlendReviewed

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  • K.Yamamoto, M.Sonoyama, K.Miyanaga, D.Kato, S.Negoro, R.K. Jain, M.Takeo .  Biodegradability of 3-Methyl-4-Nitrophenol by 4-Nitrophenol-Degrading Bacteria .  Japanese J. Wat. Treat. Biol. 47   19 - 27   2011.4Biodegradability of 3-Methyl-4-Nitrophenol by 4-Nitrophenol-Degrading BacteriaReviewed

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  • D.Kato, T.Tatsumi, A.Bansho, K.Teruya, H.Yoshida, M.Takeo, S.Negoro .  Enantiodifferentiation of Ketoprofen by Japanese Firefly Luciferase from Luciola lateralis .  J. Mol. Catal. B: Enzymatic 69   140 - 146   2011.3Enantiodifferentiation of Ketoprofen by Japanese Firefly Luciferase from Luciola lateralisReviewed

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  • D.Kato, A.Miura, M.Takeo, S.Negoro .  Preparation of enantiomerically pure (R)-ketoprofen using the enzymatic decarboxylation of Q11DV3 protein .  Rep. Grad. Sch. Eng., Univ. Hyogo63   24 - 28   2010.10Preparation of enantiomerically pure (R)-ketoprofen using the enzymatic decarboxylation of Q11DV3 proteinReviewed

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  • K.Niwa, Y.Ichino, S.Kumata, Y.Nakajima,Y.Hiraishi, D.Kato, Y.Ohmiya .  Quantum yield measurements of firefly bioluminescence reactions using a commercial luminometer .  Luminescence25   171 - 171   2010.7Quantum yield measurements of firefly bioluminescence reactions using a commercial luminometerReviewed

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  • D.Kato, H.Yoshida, M.Takeo, S.Negoro, H.Ohta .  Purification and Gene Cloning of an Enantioselective Thioesterification Enzyme from Brevibacterium ketoglutamicum KU1073, a Deracemization Bacterium of 2-(4-Chlorophenoxy)propanoic Acid .  Biosci. Biotech. Biochem.74   2405 - 2412   2010.6Purification and Gene Cloning of an Enantioselective Thioesterification Enzyme from Brevibacterium ketoglutamicum KU1073, a Deracemization Bacterium of 2-(4-Chlorophenoxy)propanoic AcidReviewed

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  • K.Niwa, Y.Ichino, S.Kumata, Y.Nakajima, Y.Hiraishi, D.Kato, V.R.Viviani, Y.Ohmiya .  Quantum Yields and Kinetics of the Firefly Bioluminescence Reaction of Beetle Luciferases .  Photochem. Photobiol. 86   1046 - 1049   2010.4Quantum Yields and Kinetics of the Firefly Bioluminescence Reaction of Beetle LuciferasesReviewed

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  • Y.Kawashima, K.Yasuhira, N.Shibata, Y.Matsuura, Y.Tanaka, M.Taniguchi, Y.Miyoshi, M.Takeo, D.Kato, Y.Higuchi, S.Negoro .  Enzymatic synthesis of nylon-6 units in organic solvents containing low concentrations of water .  J. Mol. Catal. B: Enzymatic64   81 - 88   2010.4Enzymatic synthesis of nylon-6 units in organic solvents containing low concentrations of waterReviewed

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  • K.Yasuhira, N.Shibata, G.Mongami, Y.Uedo, Y.Atsumi, Y.Kawashima, A.Hibino, Y.Tanaka, Y.-H.Lee, D.Kato, M.Takeo, Y.Higuchi, S.Negoro .  X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimmer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradation .  J. Biol. Chem.285   1239 - 1248   2010.3X-ray crystallographic analysis of the 6-aminohexanoate cyclic dimmer hydrolase: catalytic mechanism and evolution of an enzyme responsible for nylon-6 byproduct degradationReviewed

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  • K.Matsui, S.Morimoto, T.Asano, Y.Ukita, D.Kato, M.Takeo, Y.Utsumi, and S.Negoro .  Enzyme-Linked Immunosorbent Assay Using Vertical Micro Reactor Stack for the Deyection of Biomolecules .  Electron. Commun. Jpn.93   50 - 57   2010.2Enzyme-Linked Immunosorbent Assay Using Vertical Micro Reactor Stack for the Deyection of BiomoleculesReviewed

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  • D.Kato, J. Ohsako, T.Matsumoto, M.Takeo, S.Negoro .  Very simple method for the preparation of aminoacyl-tRNAs .  J. Mol. Catal. B: Enzymatic62 ( 1 ) 112   2010.2Very simple method for the preparation of aminoacyl-tRNAsReviewed

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  • T.Ohki, N.Shibata, Y.Higuchi, Y.Kawashima, M.Takeo, D.Kato, S.Negoro .  Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a β-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolase .  Protein Sci.18 ( 8 ) 1662 - 1673   2009.8Two alternative modes for optimizing nylon-6 byproduct hydrolytic activity from a carboxylesterase with a β-lactamase fold: X-ray crystallographic analysis of directly evolved 6-aminohexanoate-dimer hydrolaseReviewed

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  • A.Tagami, N.Ishibashi, D.Kato, N.Taguchi, Y.Mochizuki, H.Watanabe,M.Ito, S.Tanaka .  Ab initio quantum-chemical study on emission spectra of bioluminescent luciferases by fragment molecular orbital method .  Chem. Phys. Lett.472   118 - 123   2009.6Ab initio quantum-chemical study on emission spectra of bioluminescent luciferases by fragment molecular orbital methodReviewed

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  • Y.Kawashima, T.Ohki, N.Shibata, Y.Higuchi, Y.Wakitani, Y.Matsuura, Y.Nakata, M.Takeo, D.Kato, S.Negoro .  Molecular design of a nylon-6 byproduct-degrading enzyme from a carboxylesterase with a -lactamase fold .  FEBS J.276   2547 - 2556   2009.4Molecular design of a nylon-6 byproduct-degrading enzyme from a carboxylesterase with a -lactamase foldReviewed

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  • K.Sasa, D.Kato, T.Uno, H.Hayashi, H.Nakano .  Computational Chemical Analysis of Firefly Luciferase Catalyzed Enantioselective Thioester Formation toward Ketoprofen .  J. Comput. Chem. Jpn.7   143 - 150   2008.10Computational Chemical Analysis of Firefly Luciferase Catalyzed Enantioselective Thioester Formation toward KetoprofenReviewed

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  • M.Takeo, M.Murakami, S.Niihara, K.Yamamoto, M.Nishimura, D.Kato, S.Negoro .  Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. PN1: characterization of the two-component 4-nitrophenol hydroxylase and the regulation of its expression .  J. Bacteriol.190   7367 - 7374   2008.8Mechanism of 4-nitrophenol oxidation in Rhodococcus sp. PN1: characterization of the two-component 4-nitrophenol hydroxylase and the regulation of its expressionReviewed

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  • A.Tagami, N.Ishibashi, D.Kato, N.Taguchi, Y.Mochizuki, H.Watanabe, M.Ito, S.Tanaka .  Theoretical Study on Emission Spectra of Bioluminescent Luciferases by Fragment Molecular Orbital Method .  J. Com. Aid. Chem.9   47 - 54   2008.6Theoretical Study on Emission Spectra of Bioluminescent Luciferases by Fragment Molecular Orbital MethodReviewed

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  • K.Matsui, S.Morimoto, T.Asano, Y.Ukita, D.Kato, M.Takeo, Y.Utsumi, and S.Negoro .  Enzyme-Linked Immunosorbent Assay for nonylphenol using antibody-bound microfluid filters in vertical fluidic operation .  J. Biosci. Bioeng.104   347 - 350   2007.10Enzyme-Linked Immunosorbent Assay for nonylphenol using antibody-bound microfluid filters in vertical fluidic operationReviewed

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  • K. Yasuhira, Y. Uedo, M. Takeo, D. Kato, and S. Negoro .  Genetic organization of nylon-oligomer-degrading enzymes from an alkalophilic bacterium Agromyces sp. KY5R .  J. Biosci. Bioeng.104   521 - 542   2007.8Genetic organization of nylon-oligomer-degrading enzymes from an alkalophilic bacterium Agromyces sp. KY5RReviewed

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  • K.Yasuhira, Y.Tanaka, H.Shibata, Y.Kawashima, A.Ohara, D.Kato, M.Takeo, and S.Negoro .  6-Aminohexanoate-oligomer hydrolase from the alkalophilic bacteria Agromyces sp. KY5R and Kocuria sp. KY2 .  Appl. Environ. Microbiol.73   7099 - 7102   2007.66-Aminohexanoate-oligomer hydrolase from the alkalophilic bacteria Agromyces sp. KY5R and Kocuria sp. KY2Reviewed

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  • K. Matsui, I. Kawaji, Y. Utsumi, Y. Ukita,T. Asano, M. Takeo, D. Kato, and S. Negoro .  Immunoassay using microfluid filters constructed by deep X-ray lithography .  Biosci. Biotech. Biochem.71   3098 - 3101   2007.5Immunoassay using microfluid filters constructed by deep X-ray lithographyReviewed

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  • M.Takeo, M.Nishimura, H.Takahashi, C.Kitamura, D.Kato, and S.Negoro .  Purification and Characterization of Alkylcatechol 2,3-Dioxygenase from Butylphenol Degradation Pathway of Pseudomonas putida MT4 .  J. Biosci. Bioeng.104   309 - 314   2007.4Purification and Characterization of Alkylcatechol 2,3-Dioxygenase from Butylphenol Degradation Pathway of Pseudomonas putida MT4Reviewed

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  • D.Kato, K.Teruya, H.Yoshida, M.Takeo, S.Negoro, and H.Ohta .  New application of firefly luciferase - it can catalyze the enantioselective thioester formation of 2-arylpropanoic acid .  FEBS J.274   3877 - 3885   2007.2New application of firefly luciferase - it can catalyze the enantioselective thioester formation of 2-arylpropanoic acidReviewed

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  • S.Negoro, T.Ohki, N.Shibata, K.Sasa, H.Hayashi, H.Nakano, K.Yasuhira, D.Kato, M.Takeo, and Y.Higuchi .  Nylon-oligomer Degrading Enzyme/Substrate Complex: Catalytic Mechanism of 6-Aminohexanoate-dimer Hydrolase .  J. Mol. Biol.370   142 - 156   2007.2Nylon-oligomer Degrading Enzyme/Substrate Complex: Catalytic Mechanism of 6-Aminohexanoate-dimer HydrolaseReviewed

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  • K.Matsui, S.Morimoto, T.Asano, Y.Ukita, D.Kato, M.Takeo, Y.Utsumi, and S.Negoro .  Enzyme-Linked Immunosorbent Assay Using Vertical Micro Reactor Stack for the Deyection of Biomolecules .  IEEJ Trans. EIS127   204 - 209   2007.1Enzyme-Linked Immunosorbent Assay Using Vertical Micro Reactor Stack for the Deyection of BiomoleculesReviewed

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  • M.Takeo, S.K.Prabu, C.Kitamura, M.Hirai, H.Takahashi, D.Kato, and S.Negoro .  Characterization of Alkylphenol Degradation Gene Cluster in Pseudomonas putida MY4 and Evidence of Oxidation of Alkylphenols and Alkylcatechols with Medium-Length Alkyl Chain .  J. Biosci. Bioeng.102   352 - 361   2006.10Characterization of Alkylphenol Degradation Gene Cluster in Pseudomonas putida MY4 and Evidence of Oxidation of Alkylphenols and Alkylcatechols with Medium-Length Alkyl ChainReviewed

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  • T.Takanami, H.Tokoro, D.Kato, S.Nishiyama, and T.Sugai .  Chemo-enzymatic short-step total synthesis of symbioramide .  Tetrahedron Lett.46   3291 - 3295   2005.11Chemo-enzymatic short-step total synthesis of symbioramideReviewed

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  • S.Ohba, N.Ishida, D.Kato, K.Miyamoto, and H.Ohta .  (+)-(4aR, 9aS)-O-(4-Bromobenzoyl)-N-(3-methylanthracen-9-ylidene)hydroxyamine .  Acta Cryst. E61   o1620 - o1621   2005.8(+)-(4aR, 9aS)-O-(4-Bromobenzoyl)-N-(3-methylanthracen-9-ylidene)hydroxyamineReviewed

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  • D.Kato, K.Miyamoto, and H.Ohta .  Preparation of optically active 4-chlorophenylalanine from its racemate by deracemization technique using transformant Escherichia coli cells .  Biocat. Biotransform.23   375 - 379   2005.8Preparation of optically active 4-chlorophenylalanine from its racemate by deracemization technique using transformant Escherichia coli cellsReviewed

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  • D.Kato, K.Miyamoto, and H.Ohta .  Microbial deracemization of a-amino acids .  J. Mol. Catal. B: Enzymatic32   157 - 165   2005.6Microbial deracemization of a-amino acidsReviewed

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  • A.Kuboki, T.Tajimi, Y.Tokuda, D.Kato, T.Sugai, and S.Ohira .  Concious synthesis of 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) as a protected form based on a new transformation of a,b-unsaturated ester to a-oxocarboxylic acid ester via diol cyclic sulfite .  Tetrahedron Lett.45   4545 - 4548   2004.10Concious synthesis of 3-deoxy-D-manno-oct-2-ulosonic acid (KDO) as a protected form based on a new transformation of a,b-unsaturated ester to a-oxocarboxylic acid ester via diol cyclic sulfiteReviewed

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  • D.Kato, K.Miyamoto, and H.Ohta .  Microbial deracemization of a-substituted carboxylic acids: control of the reaction path .  Tetrahedron: Asymmetry15   2965 - 2973   2004.8Microbial deracemization of a-substituted carboxylic acids: control of the reaction pathReviewed

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  • D.Kato, S.Mitsuda, and H.Ohta .  Microbial Deracemization of a-Substituted Carboxylic Acids: Substrate Specificity and Mechanistic Inversigation .  J. Org. Chem.68   7234 - 7242   2003.8Microbial Deracemization of a-Substituted Carboxylic Acids: Substrate Specificity and Mechanistic InversigationReviewed

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  • D.Kato, S.Mitsuda, and H.Ohta .  Microbial Deracemization of a-Substituted Carboxylic Acids .  Org. Lett.4   371 - 373   2002.8Microbial Deracemization of a-Substituted Carboxylic AcidsReviewed

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Books

  • ナイロン分解酵素NylBの構造進化, 触媒機構とアミド合成への応用

    根来誠司, 武尾正弘, 柴田直樹, 樋口芳樹, 加藤太一郎, 重田育照( Role: Joint author ,  食品・バイオにおける最新の酵素応用, Ⅲバイオ産業への酵素応用編)

    シーエムシー出版  2019.7 

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    Responsible for pages:195-207   Language:Japanese Book type:Scholarly book

  • “Firefly Luciferase as Biocatalysts”, Editors: Tomoko Matsuda, Future Directions in Biocatalysis, 2nd Edition, Chapter 8

    D.Kato( Role: Sole author)

    Elsevier  2017.8 

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    Total pages:460   Responsible for pages:149-172   Language:English Book type:Scholarly book

  • 生体触媒によるカルボン酸の変換反応と光学活性体調製

    加藤太一郎( Role: Sole author)

    小宮山眞監修, 酵素利用技術体系~基礎・解析から改変・高機能化・産業利用まで~, 第5編 酵素を操る, 第1章 酵素を使った物質合成(エヌ・ティー・エス出版)  2010.6 

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    Language:Japanese Book type:Scholarly book

MISC

  • 続・生物工学基礎講座 バイオよもやま話 緩衝液のイロハ Invited Reviewed

    加藤 太一郎

    生物工学会誌   95 ( 8 )   476 - 479   2017.8

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    Authorship:Lead author, Corresponding author   Language:Japanese   Publishing type:Article, review, commentary, editorial, etc. (scientific journal)   Publisher:(公社)日本生物工学会