Papers - Miyamoto, Kenji

Fusion then fission: splitting and reassembly of an artificial fusion-protein nanocage

Ohara N., Kawakami N., Arai R., Adachi N., Ikeda A., Senda T., Miyamoto K.

Chemical Communications 60 ( 34 ) 4605 - 4608 2024.04

ISSN  13597345

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A split-protein system is a simple approach to introduce new termini which are useful as modification sites in protein engineering, but has been adapted mainly for monomeric proteins. Here we demonstrate the design of split subunits of the 60-mer artificial fusion-protein nanocage TIP60. The subunit fragments successfully reformed the cage structure in the same manner as prior to splitting. One of the newly introduced terminals at the interior surface can be modified using a tag peptide and green fluorescent protein. Therefore, the termini could serve as a versatile modification site for incorporating a wide variety of functional peptides and proteins.

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Thermally Reversible Gel-Sol Transition of Hydrogels via Dissociation and Association of an Artificial Protein Nanocage

Nasu E., Kawakami N., Takamura S., Hotta A., Arai R., Miyamoto K.

Biomacromolecules 25 ( 4 ) 2358 - 2366 2024.04

ISSN  15257797

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Oligomeric protein nanocages often disassemble into their subunits and reassemble by external stimuli. Thus, using these nanocages as cross-linkers for hydrogel network structures is a promising approach to allow hydrogels to undergo stimuli-responsive gel-sol transitions or self-healing. Here, we report hydrogels that show a reversible gel-sol transition resulting from the heat-induced dissociation and reassociation of protein nanocages. The hydrogel contained the 60-mer artificial protein nanocage, TIP60, as a supramolecular cross-linker for polyethylene glycol network structures. The hydrogel showed a gel-to-sol transition upon heating at a temperature above the melting point of TIP60 and immediately returned to a gel state upon cooling to room temperature. During the heating and cooling treatment of the hydrogel, small-angle X-ray scattering analysis suggested the dissociation and reassociation of TIP60. Furthermore, we demonstrated redox-responsive cargo release from TIP60 in the hydrogel. These results showed the potential of TIP60 as a component of multi-stimuli-responsive hydrogels.

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Alcanivorax bacteria as important polypropylene degraders in mesopelagic environments

Koike H., Miyamoto K., Teramoto M.

Applied and Environmental Microbiology 89 ( 12 )  2023.12

ISSN  00992240

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Plastics are causing serious problems in the sea and settling even to abyssal depths. Polypropylene (PP) is the second most common plastic product and thus would constitute a large fraction of plastics in the sea. The biodegradation of PP has not been clearly shown. In this study, Alcanivorax bacteria (mainly Alcanivorax borkumensis) were indicated to be enriched most abundantly on liquid PP and on its structurally similar branched alkane, pristane, in mesopelagic water. An Alcanivorax isolate probably of A. borkumensis showed the highest liquid PP-degrading activity among the isolates. These results indicate that Alcanivorax bacteria could be major degraders of PP in mesopelagic environments. Alcanivorax bacteria did not use liquid PP as the sole carbon and energy source. Short PP was preferentially degraded, and PP of all lengths appeared to be degraded. Liquid PP was degraded more efficientlyat 10°C than at 20°C, and correspondingly, higher concentrations of another carbon source were required at 10°C. Regarding the degradation of solid PP, an initial degradation sign, oxidation, was detected, but a weight loss of at least 1% was not detected. By using this study as a model, various PP-degrading microbes would start to be clarified.

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Column-free purification of an artificial protein nanocage, TIP60

Nasu E., Kawakami N., Ohara N., Hayashi K., Miyamoto K.

Protein Expression and Purification 205 2023.05

ISSN  10465928

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Protein nanocages, which have inner cavities and surface pores, are attractive materials for various applications, such as in catalysts and medicine. Recently, we produced an artificial protein nanocage, TIP60, and demonstrated its potential as a stimuli-responsive nanocarrier. In the present study, we report a simple purification method for TIP60 that can replace time-consuming and costly affinity chromatography purification. TIP60, which has an anionic surface charge, aggregated at mildly acidic pH and redissolved at neutral pH, maintaining its cage structure. This pH-responsive reversible precipitation allowed us to purify TIP60 from soluble fractions of the E. coli cell lysate by controlling the pH. Compared with conventional Ni-NTA column purification, the pH-responsive precipitation method provided purified TIP60 with similar purity (∼80%) and higher yield. This precipitation purification method should facilitate the large-scale investigation and practical use of TIP60 nanocages.

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Hydrophobization of a TIP60 Protein Nanocage for the Encapsulation of Hydrophobic Compounds

Yamashita M., Kawakami N., Miyamoto K.

ChemPlusChem (ChemPlusChem)  88 ( 3 )  2023.03

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Encapsulation of hydrophobic molecules in protein-based nanocages is a promising approach for dispersing these molecules in water. Here, we report a chemical modification approach to produce a protein nanocage with a hydrophobic interior surface based on our previously developed nanocage, TIP60. The large pores of TIP60 act as tunnels for small molecules, allowing modification of the interior surface by hydrophobic compounds without nanocage disassembly. We used four different hydrophobic compounds for modification. The largest modification group tested, pyrene, resulted in a modified TIP60 that could encapsulate aromatic photosensitizer zinc phthalocyanine (ZnPC) more efficiently than the other modification compounds. The encapsulated ZnPC generated singlet oxygen upon light activation in the aqueous phase, whereas ZnPC alone formed inert aggregates under the same experimental conditions. Given that chemical modification allows a wider diversity of modifications than mutagenesis, this approach could be used to develop more suitable nanocages for encapsulating hydrophobic molecules of interest.

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Reversible Assembly of an Artificial Protein Nanocage Using Alkaline Earth Metal Ions

Ohara N., Kawakami N., Arai R., Adachi N., Moriya T., Kawasaki M., Miyamoto K.

Journal of the American Chemical Society (Journal of the American Chemical Society)  145 ( 1 ) 216 - 223 2023.01

ISSN  00027863

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Protein nanocages are of increasing interest for use as drug capsules, but the encapsulation and release of drug molecules at appropriate times require the reversible association and dissociation of the nanocages. One promising approach to addressing this challenge is the design of metal-dependent associating proteins. Such designed proteins typically have Cys or His residues at the protein surface for connecting the associating proteins through metal-ion coordination. However, Cys and His residues favor interactions with soft and borderline metal ions, such as Au+ and Zn2+, classified by the hard and soft acids and bases concept, restricting the types of metal ions available to drive association. Here, we show the alkaline earth (AE) metal-dependent association of the recently designed artificial protein nanocage TIP60, which is composed of 60-mer fusion proteins. The introduction of a Glu (hard base) mutation to the fusion protein (K67E mutant) prevented the formation of the 60-mer but formed the expected cage structure in the presence of Ca, Sr, or Ba ions (hard acids). Cryogenic electron microscopy (cryo-EM) analysis indicated a Ba ion at the interface of the subunits. Furthermore, we demonstrated the encapsulation and release of single-stranded DNA molecules using this system. Our results provide insights into the design of AE metal-dependent association and dissociation mechanisms for proteins.

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Generation of Fusarium oxysporum-suppressive soil with non-soil carriers using a multiple-parallel-mineralization technique

Meeboon J., Ando A., Ogawa J., Miyamoto K., Kato Y., Shinohara M.

Scientific Reports 12 ( 1 )  2022.12

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Disease-suppressive soils exist worldwide. However, the disease-suppression mechanism is unknown, and it’s unclear how to produce such soils. The microbiota that develop in a multiple-parallel-mineralization system (MPM) can increase nutrient production efficiency and decrease root disease in hydroponic systems. Artificial media inoculated with MPM microorganisms can degrade organic matter to produce inorganic nutrients similarly to natural soil, but it’s unknown whether they can also suppress pathogen growth. Here, we produced an artificial medium that inhibited root disease similarly to disease-suppressive soils. Microbial MPM culture solution was inoculated into non-soil carriers (rockwool, rice husk charcoal, and vermiculite) to test whether it could suppress growth of Fusarium oxysporum f. sp. lactucae J. C. Hubb. & Gerik. We inoculated F. oxysporum f. sp. conglutinans (Wollenweber) Snyder et Hansen strain Cong:11 and F. oxysporum f. sp. lactucae J. C. Hubb. & Gerik into artificial media sown each with Arabidopsis thaliana (L.) Heynh. and Lactuca sativa L. var. capitata supplemented with MPM culture microbes. The MPM microorganisms suppressed F. oxysporum f. sp. lactucae J. C. Hubb. & Gerik growth and prevented plant disease. Thus, MPM-inoculated non-soil carriers that can generate inorganic nutrients from organic matter may also suppress disease in the absence of natural soil. Our study shows novel creation of a disease-suppressive effect in non-soil media using the microbial community from MPM culture solution.

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Icosahedral 60-meric porous structure of designed supramolecular protein nanoparticle TIP60

Obata J., Kawakami N., Tsutsumi A., Nasu E., Miyamoto K., Kikkawa M., Arai R.

Chemical Communications 57 ( 79 ) 10226 - 10229 2021.10

ISSN  13597345

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Supramolecular protein nanoparticles and nanocages have potential in a broad range of applications. Recently, we developed a uniform supramolecular protein nanoparticle, TIP60, symmmetrically self-assembled from fusion proteins of a pentameric Sm-like protein and a dimeric MyoX-coil domain. Herein, we report the icosahedral 60-meric structure of TIP60 solved using single-particle cryo-electron microscopy. Interestingly, the structure revealed 20 regular-triangle-like pores on the surface. TIP60 and its mutants have many modifiable sites on their exterior and interior surfaces. The TIP60 architecture will be useful in the development of biomedical and biochemical nanoparticles/nanocages for future applications.

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Nanopore-Controlled Dual-Surface Modifications on Artificial Protein Nanocages as Nanocarriers

Nasu E., Kawakami N., Miyamoto K.

ACS Applied Nano Materials (ACS Applied Nano Materials)  4 ( 3 ) 2434 - 2439 2021.03

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Chemical modification of the interior and exterior surfaces of protein nanocages holds promise for various applications such as cosmetics, pharmaceuticals, and catalysts. However, dual-surface modification of these surfaces using different chemicals remains challenging, particularly when the same substituents, such as cysteine thiols, are modified. We recently produced an artificial protein nanocage called TIP60 that has 20 large surface pores. Chemical modification of cysteine residues introduced in the interior surface of TIP60 showed that these pores allow the passage of small molecules from the outside environment to the inside of the nanocage. In this study, we found that the surface pores on TIP60 function as size-dependent molecular filters. Modification experiments using different-sized polymers containing maleimide groups, which specifically react with thiols, showed that macromolecules with diameters larger than that of the pores could not penetrate into the inner cavity. This molecular size discrimination by the pores prompted us to perform stepwise dual-surface functionalization of a double mutant of TIP60 presenting cysteine residues on the interior and exterior surfaces. This was achieved by modifying the exterior cysteine residues with a polymer containing a maleimide group that cannot penetrate to the inside of the nanocage, followed by modification of the interior cysteine residues using thiol-containing small molecules. Dual-functionalized TIP60 released internal small molecules in a redox-responsive manner. This simple approach for dual-surface modification would make TIP60 a useful nanocarrier for a broad range of applications including drug-delivery and molecular filtration systems.

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Apoptosis-inducing activity and antiproliferative effect of Paeoniflorigenone from moutan cortex

Ying Huang,Osamu Ohno, Kiyotake Suenaga, Kenji Miyamoto,

Bioscience, Biotechnology, and Biochemistry  2017

Joint Work, Accepted

5-keto-4-deoxy-D-Glucarate Dehydratase/Decarboxylase: Key role in the oxidative pathway towards α-keto-glutarate

André Pick, Barbara Beer, Risa Hemmi, Rena Momma, Jochen Schmid, Kenji Miyamoto and Volker Sieber

BMC Biotechnology 16 ( 1 )  2016.12

Joint Work, Accepted

Response to Comment on “A bacterium that degrades and assimilates poly(ethylene terephthalate)

S. Yoshida, K. Hiraga, T. Takehana, I. Taniguchi, H. Yamaji, Y. Maeda, K. Toyohara, K. Miyamoto, Y. Kimura and K. Oda

Science 353   759 2016.07

Joint Work, Accepted

Discovery of a poly(ethylene terephthalate) assimilation

S. Yoshida, K. Hiraga, T. Takehana, I. Taniguchi, H. Yamaji, Y. Maeda, K. Toyohara, K. Miyamoto, Y. Kimura and K. Oda

Science 351 ( 6278 ) 1196 - 1199 2016.03

Research paper (scientific journal), Joint Work, Accepted

Semiempirical QM/MM calculations reveal a step-wise proton transfer and an unusual thiolate pocket in the mechanism of the unique arylpropionate racemase AMDase G74C

F. Busch, J. Enoki, N. Hülsemann, K. Miyamoto, M. Bocola and R. Kourist

Catalysis Science & Technology  2016.03

Research paper (scientific journal), Accepted

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Arylmalonate decarboxylase-catalyzed asymmetric synthesis of both enantiomers of optically pure flurbiprofen

S. K. Gaßmeyer, J. Wetzig, C. Mügge, M. Assmann, J. Enoki, L. Hilterhaus, R. Zuhse, K. Miyamoto, A. Liese and R. Kourist

ChemCatChem 8   916 - 921 2016.01

Research paper (scientific journal), Joint Work, Accepted

ポリエチレンテレフタレート(PET)分解菌の発見、解析とその応用への展望

平賀和三、宮本憲二、吉田昭介、小田耕平

バイオサイエンストインダストリー 74   492 - 496 2016

Joint Work

Arylmalonate decarboxylase – a highly selective bacterial biocatalyst with unkown function

K. Miyamoto and R. Kourist

Appl. Microbiol. Biotechnol., 100   8621 - 8631 2016

Joint Work, Accepted

Improved enantioselectivity of thermostable esterase ST0071 from archaeon Sulforobus tokodaii by site-saturation mutagenesis

M. Ozaki, N. Kawakami, H. Ohta and K. Miyamoto

Biocatal. Biotransformation  2016

Joint Work, Accepted

Engineered hydrophobic pocket of (S)-selective arylmalonate decarboxylase variant by simultaneous saturation mutagenesis to improve catalytic performance

S. Yoshida, J. Enoki, R. Kourist and K. Miyamoto

Biosci. Biotechnol. Biochem. 79 ( 12 ) 1965 - 1971 2015.12

Research paper (scientific journal), Accepted

Modulating the catalytic activity and the substrate specificity of alcohol dehydrogenases using cyclic ethers

N. Kawakami, Y. Hara and K. Miyamoto

Catal. Sci. Technol. 5 ( 8 ) 3922 - 2925 2015.08

Research paper (scientific journal), Accepted

STD-NMR based protein engineering of the unique arylpropionate-racemase AMDase G74C

S. K. Gaßmeyer, H. Yoshikawa, J. Enoki, N. Hülsemann, R. Stoll, K. Miyamoto and R. Kourist

ChemBioChem 16 ( 13 ) 1943 - 1949 2015.05

Research paper (scientific journal), Joint Work, Accepted

Draft genome sequence of Bordetella bronchiseptica KU1201, the first isolation source of arylmalonate decarboxylase

Shosuke Yoshidaa, Junichi Enokia, Risa Hemmia, Robert Kouristb, Norifumi Kawakamia, and Kenji Miyamotoa.

Genome Announcements (May/June, 3 (3), e00373-15 (2015))  May/June, 3 ( 3 ) e00373 - 15 2015.05

Research paper (scientific journal), Accepted

Photosynthetic production of enantioselective biocatalysts

Maik Bartsch, Sarah K. Gaßmeyer, Katharina Köninger, Kosuke Igarashi, Pasqual Liauw, Nina Dyczmons-Nowaczyk, Kenji Miyamoto, Marc M. Nowaczyk, Robert Kourist

Microbial Cell Factories (14(1), 53 (2015))  14 ( 1 ) 53 2015.05

Research paper (scientific journal), Joint Work, Accepted

Substrate specificity of an archaeon Sulfolobus tokodaii esterase bearing a GGG(A)X motif

R. Wada, M. Ozaki, T. Kumon, H. Ohta and K. Miyamoto

Biocatalysis and Biotransformation 33 ( 3 ) 188 - 190 2015.05

Research paper (scientific journal), Joint Work, Accepted

Isolation of monovalerianester A, an inhibitor of fat accumulation, from Valeriana fauriei

K. Yuki, M. Ikeda, S. Yoshida, O. Ohno, K. Suenaga, K. Yamada, D. Uemura, and K. Miyamoto

Natural Product Communications 10 ( 8 ) 1333 - 1334 2015.05

Research paper (scientific journal), Joint Work, Accepted

Enzymatic Decarboxylation-An Emerging Reaction for Chemicals Production from Renewable Resources

Kourist, Robert; Guterl, Jan-Karl; Miyamoto, Kenji; Sieber, Volker

ChemCatChem 6 ( 3 ) 689 - 701 2014.06

Research paper (scientific journal), Joint Work

アリールマロン酸脱炭酸酵素の機能改変 －合理的デザインによる立体選択性の逆転と劇的活性向上－

MIYAMOTO KENJI

生物工学会誌 (8，424-4278 (2014))  8   424 - 427 2014

Research paper (scientific journal)

Draft genome sequence of Kozakia baliensis SR-745, the first sequenced Kozakia strain from the family Acetobacteraceae

Jochen Schmid, Steven Koenig, Andre; Pick, Fabian Steffler, Shosuke Yoshida, Kenji Miyamoto, and Volker Sieber

Genome Announcements (May/June, 2, e00594-14 (2014))  May/June, 2   e00594 - 14 2014

Research paper (scientific journal), Joint Work, Accepted

Thermally driven asymmetric domino reaction catalyzed by a thermostable esterase and its variants

Reina Wada, Takashi Kumon, Robert Kourist, Hiromichi Ohta, Daisuke Uemura, Shosuke Yoshida and Kenji Miyamoto

Tetrahedron Letters 54   1921-1923 2013.03

Research paper (scientific journal), Joint Work, Accepted

Isolation of 9-hydroxy-10E,12Z-octadecadienoic acid, an inhibitor of fat accumulation from Valeriana fauriei

Yuki, Keiji; Ikeda, Mariko; Miyamoto, Kenji; Ohno, Osamu; Yamada, Kaoru; Uemura, Daisuke

Bioscience, Biotechnology, and Biochemistry 76 ( 6 ) 1233-1235 2012

Research paper (scientific journal), Joint Work, Accepted

自然界に存在しない酵素をデザインする

MIYAMOTO KENJI

日本化学会バイオテクノロジー部会「研究紹介    4-6 2011.09

Research paper (scientific journal), Single Work

Biocatalytic strategies for the asymmetric synthesis of profens – recent trends and developments

MIYAMOTO KENJI

Green Chemistry 13 ( 10 ) 2607-2618 2011

Research paper (scientific journal), Single Work

Engineering the Promiscuous Racemase Activity of an Arylmalonate Decarboxylase

R. Kourist, Y. Miyauchi, D. Uemura and K. Miyamoto

Chemistry-A European Journal 17   557-563 2011

Research paper (scientific journal), Joint Work, Accepted

Protein engineering of Arylmalonate Decarboxylase G74C, an artificial racemase

R. Kourist and K. Miyamoto

Biotech international 23   6-11 2011

Research paper (scientific journal), Single Work

Dramatically improved catalytic activity of an artificial (S)-selective arylmalonate decarboxylase by structure-guided directed evolution

MIYAMOTO KENJI

Chemical Communications 47 ( 26 ) 7503-7505 2011

Research paper (scientific journal), Single Work

Inhibitory effects of bakuchiol, bavachin, and isobavachalcone isolated from Piper longum on melanin production in B16 mouse melanoma cells.

Ohno, Osamu; Watabe, Taeko; Nakamura, Kazuhiko; Kawagoshi, Masaru; Uotsu, Nobuo; Chiba, Tomohiro; Yamada, Masayoshi; Yamaguchi, Kohji; Yamada, Kaoru; Miyamoto, Kenji; Uemura, Daisuke

Bioscience, Biotechnology, and Biochemistry 74 ( 7 ) 1504-1506 2010

Research paper (scientific journal), Single Work, Accepted

アリールマロン酸脱炭酸酵素の機能改変

MIYAMOTO KENJI

酵素工学研究会「酵素工学ニュース」トピックス 64   5-10 2010

Research paper (scientific journal), Single Work

Microbial kinetic resolution of 2-substituted-1-propanol

MIYAMOTO KENJI

Biocatal. Biotransformation 27   66-70 2009

Research paper (scientific journal), Joint Work, Accepted

１種類の酵素による多段階反応は可能か？

MIYAMOTO KENJI

生物工学会誌 87 ( 8 ) 394 2009

Research paper (scientific journal), Single Work

Purification and characterization of thermostable H2O2-forming NADH oxidase from 2-phenylethanol-assimilating Brevibacterium sp. KU1309

MIYAMOTO KENJI

Applied Microbiology and Biotechnology 80 ( 1 ) 71-78 2008

Research paper (scientific journal), Joint Work, Accepted

Asymmetric decarboxylation of  -hydroxy- and  -amino- -phenylmalonate catalyzed by arylmalonate decarboxylase from Alcaligenes bronchisepticus

MIYAMOTO KENJI

Biocatalysis and Biotransformation 26 ( 4 )  2008

Research paper (scientific journal), Joint Work, Accepted

Screening, cloning, expression, and purification of an acidic arylmalonate decarboxylase from Enterobacter cloacae KU1313

MIYAMOTO KENJI

Applied Microbiology and Biotechnology 78 ( 5 ) 793-799 2008

Research paper (scientific journal), Joint Work, Accepted

The green and effective oxidation of alcohols to carboxylic acids with molecular oxygen via biocatalytic reaction

MIYAMOTO KENJI

Tetrahedron Letters 49 ( 7 ) 1217-1219 2008

Research paper (scientific journal), Joint Work, Accepted

Crystallization and preliminary X-ray diffraction experiments of arylmalonate decarboxylase from Alcaligenes bronchisepticus

MIYAMOTO KENJI

Acta Crystallographica, Section F: Structural Biology and Crystallization Communications F64 ( 7 ) 610-613 2008

Research paper (scientific journal), Joint Work, Accepted

Purification and characterization of aldehyde dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU1309

MIYAMOTO KENJI

Appl. Microbiol. Biotechnol. 76 ( 2 ) 357-363 2007

Research paper (scientific journal), Joint Work, Accepted

Stereochemistry of decarboxylation of arylmalonate catalyzed by mutant enzymes.

MIYAMOTO KENJI

Chem. Lett. 36 ( 5 ) 656-657 2007

Research paper (scientific journal), Joint Work, Accepted

Substrate specificity and reaction mechanism of recombinant styrene oxide isomerase from Pseudomonas putida S12.

MIYAMOTO KENJI

Tetrahedron Lett. 48 ( 18 ) 3255-3257 2007

Research paper (scientific journal), Joint Work, Accepted

Conversion of a-methyltropate to optically active a-phenylpropionate by tropate-degrading Rhodococcus sp. KU1314.

MIYAMOTO KENJI

J. Mol. Catal., B Enzym. 46 ( 1-4 ) 14-19 2007

Research paper (scientific journal), Joint Work, Accepted

The aldol type reaction catalyzed by arylmalonate decarboxylasea decarboxylase can catalyze an entirely different reaction, aldol reaction-.

MIYAMOTO KENJI

Chem. Lett. 36 ( 3 ) 420-421 2007

Research paper (scientific journal), Joint Work, Accepted

Inversion of enantioselectivity of arylmalonate decarboxylase via site-directed mutation based on the proposed reaction mechanism.

MIYAMOTO KENJI

J. Mol. Catal., B Enzym. 45( ( 1-2 ) 15-20 2007

Research paper (scientific journal), Joint Work, Accepted

Purification and Characterization of Arylmalonate Decarboxylase from Achromobacter sp. KU1311

MIYAMOTO KENJI

J. Biosci. Bioeng.    in press 2007

Research paper (scientific journal), Joint Work, Accepted

Microbial kinetic resolution of 2-substituted-1-propanol

MIYAMOTO KENJI

Biocatal. Biotransformation    in press 2007

Research paper (scientific journal), Joint Work, Accepted

Improvement of the activity of arylmalonate decarboxylase by random mutagenesis

MIYAMOTO KENJI

Appl. Microbiol. Biotechnol. 73 ( 3 ) 647-653 2006

Research paper (scientific journal), Joint Work, Accepted

Introduction of single mutation changes arylmalonate decarboxylase to racemase

MIYAMOTO KENJI

Chem. Commun.  ( 34 ) 3600-3602 2006

Research paper (scientific journal), Joint Work, Accepted

Microbial deracemization of a-amino acids

Dai-Ichiro Kato, Kenji Miyamoto and Hiromichi Ohta

Journal of Molecular Catalysis B: Enzymatic 32 ( 4 ) 157-165 2005

Research paper (scientific journal), Joint Work, Accepted

(R)-1-Phenyl-1-ethylammonium (R)-2-hydroxymethyl-2-(2-naphthyl)propanoate

Shigeru Ohba, Tomomi Tsutsumi, Yosuke Terao, Kenji Miyamoto and Hiromichi Ohta

Acta Crystallographica. Section E: Structure Reports E61   o1283-o1285 2005

Research paper (scientific journal), Joint Work, Accepted

(+)-(4a R,9a S)-O-(4-Bromobenzoyl)-N-(3-methylanthracen-9-ylidene)hydroxylamine

Shigeru Ohba, Naoyuki Ishida, Dai-ichiro Kato, Kenji Miyamoto and HiromichiOhta

Acta Crystallographica. Section E: Structure Reports E61   o1620-o1621 2005

Research paper (scientific journal), Joint Work, Accepted

Purification and characterization of the alcohol dehydrogenase with a broad substrate specificity originated from 2-phenylethanol-assimilating Brevibacterium sp. KU 1309

MIYAMOTO KENJI

J. Biosci. Bioeng. 100 ( 3 ) 318-322 2005

Research paper (scientific journal), Joint Work, Accepted

Preparation of optically active 4-chlorophenylalanine from its racemate by deracemization technique using transformant Escherichia coli cells.

MIYAMOTO KENJI

Biocatal. Biotransformation 23 ( 5 ) 375-379 2005

Research paper (scientific journal), Joint Work, Accepted

変異１個で異なる機能を付与、変異２個で酵素のエナンチオ選択性逆転

MIYAMOTO KENJI

バイオサイエンスとインダストリー 63 ( 9 ) 583-586 2005

Research paper (scientific journal), Joint Work

Efficient oxidation of alcohols by a 2-phenylethanol-degrading Brevibacterium sp.

Kenji Miyamoto, Jun-ichiro Hirano and Hiromichi Ohta

Biotechnology Letters 26 ( 17 ) 1385-1388 2004

Research paper (scientific journal), Joint Work, Accepted

A novel thermostable esterase from the thermoacidophilic archaeon Sulfolobus tokodaii strain 7.

Yoichi Suzuki, Kenji Miyamoto and Hiromichi Ohta

FEMS Microbiology Letters 236 ( 1 ) 97-102 2004

Research paper (scientific journal), Single Work, Accepted

Mechanism of asymmetric decarboxylation of a-aryl-a-methylmalonate catalyzed by arylmalonate decarboxylase originated from Alcaligenes bronchisepticus.

Kaori Matoishi, Minoru Ueda, Kenji Miyamoto and Hiromichi Ohta

Journal of Molecular Catalysis B: Enzymatic 27 ( 4-6 ) 161-168 2004

Research paper (scientific journal), Single Work, Accepted

Microbial deracemization of a-substituted carboxylic acids: control of the reaction path

Dai-ichiro Kato, Kenji Miyamoto and Hiromichi Ohta

Tetrahedron: Asymmetry, 15, 2965-2973(2004) 15 ( 1 ) 2965-2973 2004

Research paper (scientific journal), Single Work, Accepted

生体触媒反応と有機化学

宮本憲二、太田博道

化学工業 54 ( 3 ) 48-51 2003

Research paper (scientific journal), Single Work

Enzymatically Enantioselective Hydrolysis of Prochiral 1,3-Diacyloxyglycerol

Biosci. Biotechnol. Biochem.  2001.09

Joint Work

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1,3-ジアシルグリセロール誘導体のリパーゼによる加水分解を検討し、条件の最適化を行った

A Practical Chemoenzymatic Synthesis of a Key Intermediate of a Antifungal Agents

Tetrahedron Lett.  2001.08

Joint Work

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酵素反応を鍵反応とする抗真菌剤中間体の新規製法を検討した

Effect of Comformation of the Sub- strate on Enzumatic Decarboxy- lation of a-Arylmalonic Acid

Bioorg.Medicinal Chem.  1994.06

Joint Work

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アリールマロン酸脱炭酸酵素の活性中心での基質のコンフォメーションを推定した

Highly Efficient Conversion of (±)-Mandelic Acid to Its (R)-Enantiomer By Conbination of Enzyme-Mediated Oxidation and Reduction

Biotechnol. Lett  1992.12

Joint Work

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フェニルマロン酸資化性菌Alcaligenes bronchisepticusの酸化酵素とベンゾイルギ酸還元酵素を利用して、ラセミ体のマンデル酸から高収率で光学活性マンデル酸を得た

Stereochemistry of Enzyme- Catalyzed Decarboxylation of a-Methyl-a-phenylmalonic acids

J. Am. Chem. Soc.  1992.07

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１３Ｃでラベルした光学活性な基質を合成し、脱炭酸反応が立体反転を伴って進行することを明らかとした

Enantioselective Oxidation of Mandelic Acid Using a Phenyl- malonate Metabolizing Pathway of a Soil Bacterium Alcaligenes bronchisepticus KU1201

Biotechnol. Lett  1992.05

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フェニルマロン酸資化性菌Alcaligenes bronchisepticusの代謝経路を推定し、その代謝経路を利用して光学活性なマンデル酸を得ることに成功した

Microbial Asymmetric Decarboxy- lation of Fluorine-containing Arylmalonic Acid

J. Fluorine Chem.  1992.03

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含フッ素アリールマロン酸を基質として脱炭酸反応により光学活性な２－アリールプロピオン酸を得た

Purification and Properties of a Novel Arylmalonate Decarboxylase from Alcaligenes bronchisepticus KU1201

Eur. J. Biochem.  1992.01

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フェニルマロン酸資化性菌Alcaligenes bronchisepticusから新規アリールマロン酸脱炭酸酵素を精製し諸性質を明らかとした

Cloning and Heterologous Expression of a Novel Arylmalonate Decar- boxylase Gene from Alcaligenes bronchisepticus KU1201

Appl. Microbiol. Biotechnol.  1992.01

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フェニルマロン酸資化性菌Alcaligenes bronchisepticusからアリールマロン酸脱炭酸酵素の遺伝子をクローニングし、大腸菌での発現に成功した

Asymmetric Decarboxylation of Disubstituted Malonic Acid by Alcaligenes bronchisepticus KU1201

Biocatalysis  1991.01

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２置換マロン酸を不斉脱炭酸反応を触媒する微生物を見いだし、反応条件や各種基質への応用を検討した

Enzyme-Mediated Asymmetric Decar- boxylation of Disubstituted Malonic Acids

J. Am. Chem. Soc.  1990.06

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２置換マロン酸を不斉脱炭酸反応を触媒する微生物を見いだした

Asymmetric Hydrolysis of 1-Cyano- alkyl Acetate

Agric. Biol. Chem.  1988.12

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１－シアノアルキルアセテートの微生物による加水分解により光学活性体を得た