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Matsuda Kenichi

Faculty of Pharmaceutical Sciences　Molecular Pharmaceutical Sciences　Chemistry and Medicinal ChemistryAssociate Professor
Office of AdmissionsAssociate Professor

Researcher basic information

■ Degree
  • 博士（農学）, 東京大学
■ URL
researchmap URLホームページURL■ Various IDs
Researcher number
  • 50812301
ORCID IDJ-Global ID■ Research Keywords and Fields
Research Keyword
  • Actinomycetes
  • Genome mining
  • Biosynthesis
  • Natural product chemistry
Research Field
  • Life Science, Bioorganic chemistry, natural product chemistry
■ Educational Organization

Career

■ Career
Career
  • Sep. 2024 - Present
    Hokkaido University, Faculty of Pharmaceutical Sciences, 准教授
  • Sep. 2021 - Aug. 2024
    Hokkaido University, Faculty of Pharmaceutical Sciences, 講師
  • Sep. 2017 - Aug. 2021
    Hokkaido University, Faculty of Pharmaceutical Sciences, 助教
  • Jun. 2017 - Aug. 2017
    Hokkaido University, Faculty of Pharmaceutical Sciences, 特任助教
  • Apr. 2017 - May 2017
    次世代天然物化学技術研究組合, 博士研究員

Research activity information

■ Awards
  • Apr. 2026, 令和８年度 科学技術分野の文部科学大臣表彰 若手科学者賞
  • Aug. 2025, 天然物化学談話会, 2025年度（第24回） 天然物化学談話会奨励賞
    天然物生合成酵素を活用した修飾環状ペプチドの化学－酵素合成
    松田研一
  • Jun. 2025, 天野エンザイム 科学技術振興財団, 第26回酵素応用シンポジウム 研究奨励賞
    天然物生合成酵素を用いた複雑修飾ペプチドの化学－酵素合成
  • Apr. 2025, 化学情報協会, JAICI賞
  • Mar. 2025, 日本薬学会, 日本薬学会奨励賞
    天然物生合成酵素の開拓と有用化合物合成への応用
  • Oct. 2024, 日本放線菌学会, 浜田賞 (研究奨励賞)
    放線菌由来天然物生合成酵素を用いた環状ペプチドの化学-酵素合成
  • Sep. 2023, 生体触媒化学シンポジウム, 第23回 生体触媒化学シンポジウム The company spotlight presentation award
    松田研一
  • Sep. 2022, 日本生薬学会, 学術奨励賞
    天然物生合成におけるペプチド修飾反応に関する研究
    松田研一
  • Oct. 2021, 第58回ペプチド討論会, 第58回ペプチド討論会 若手優秀発表賞
    Enzymatic basis of guanidine bis-prenylation in argicyclamide biosynthesis
    Kenichi Matsuda;Chin-Soon Phan;Nandani Balloo;Kei Fujita;Tatsufumi Okino;Toshiyuki Wakimoto
  • Oct. 2021, 第63回天然有機化合物討論会, 第63回天然有機化合物討論会 奨励賞 口頭発表の部
    窒素－窒素結合含有天然物のゲノムマイニング
    松田研一;有馬陸;秋山智子;阿部葉;城内航;新家一男;脇本敏幸
  • Oct. 2021, 日本薬学会生薬天然物部会, 令和3年度 日本薬学会生薬天然物部会 奨励研究
    松田研一
■ Papers
  • A Pseudokinase Catalyzes Nitrile Formation in the Biosynthesis of a Potent Marine Toxin
    Yuito Yamada; Hiromi Yokoyama; Stefan Leopold‐Messer; Kenichi Matsuda; Jörn Piel; Toshiyuki Wakimoto
    Angewandte Chemie International Edition, 14 Apr. 2026, [Peer-reviewed]
    Scientific journal
  • An atypical non-ribosomal peptide cyclase catalyzing homochiral coupling with cyclic amine nucleophile
    Mitsuo Aono; Yuito Yamada; Kenichi Matsuda; Toshiyuki Wakimoto
    The Journal of Antibiotics, Mar. 2026, [Peer-reviewed], [Invited], [Corresponding author]
    Scientific journal
  • Non-ribosomal peptide cyclase-directed chemoenzymatic synthesis of lariat lipopeptides
    Masakazu Kobayashi; Kenichi Matsuda; Yuito Yamada; Rintaro Ichihara; Naho Onozawa; Hanako Fukano; Yoshihiko Hoshino; Aki Hirabayashi; Masato Suzuki; Akira Katsuyama; Satoshi Ichikawa; Toshiyuki Wakimoto
    Nature Chemistry, 18, 1, 180, 188, Springer Science and Business Media LLC, 04 Nov. 2025, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal
  • High-throughput prediction of protein–protein interactions uncovers hidden molecular networks in biosynthetic gene clusters
    Yoshitaka Moriwaki; Taro Shiraishi; Yohei Katsuyama; Kenichi Matsuda; Toyoyuki Ose; Atsushi Minami; Hideaki Oikawa; Tomohisa Kuzuyama; Ryuichiro Ishitani; Tohru Terada
    biorxiv, 27 Oct. 2025
  • Non-canonical thioesterases in bacterial non-ribosomal peptide biosynthesis
    Kenichi Matsuda
    The Journal of Antibiotics, Oct. 2025, [Peer-reviewed], [Invited], [Lead author, Last author, Corresponding author]
    Scientific journal
  • Diol as a New Pantetheine Surrogate for Chemoenzymatic Synthesis of Cyclic Peptides via Nonribosomal Peptide Cyclases
    Kei Fujita; Rintaro Ichihara; Masakazu Kobayashi; Kenichi Matsuda; Toshiyuki Wakimoto
    Methods in Molecular Biology, 105, 121, Springer US, 19 Jun. 2025, [Invited], [Corresponding author]
    In book
  • Arginine-N,N′-bisprenyltransferases: Switchable Catalysis in Consecutive Guanidine-N-prenylation
    Kei Fujita; Yuito Yamada; Tomo Taniguchi; Daisuke Fujinami; Takahiro Mori; Kenichi Matsuda; Ikuro Abe; Toshiyuki Wakimoto
    Journal of the American Chemical Society, American Chemical Society (ACS), 12 Jun. 2025, [Peer-reviewed], [Corresponding author]
    Scientific journal
  • Facile Synthesis of 15N-Labeled Amino Acids Using 15N-Ammonium Salt
    Kuga Arima; Kenichi Matsuda; Toshiyuki Wakimoto
    Tetrahedron Letters, 157, 155490, 155490, Elsevier BV, Feb. 2025, [Peer-reviewed], [Corresponding author]
    Scientific journal
  • Enzymatic peptide macrocyclization via indole-N-acylation
    Hiroto Maruyama; Yuito Yamada; Yasuhiro Igarashi; Kenichi Matsuda; Toshiyuki Wakimoto
    Chemical Science, 16, 9, 3872, 3877, Royal Society of Chemistry (RSC), 2025, [Peer-reviewed], [Corresponding author]
    Scientific journal, BulbE TE, identified as a unique non-ribosomal peptide macrocyclizing thioesterase that catalyzes an N-acylindole linkage formation, offers valuable insight into the pivotal role of its catalytic residue in dictating nucleophile specificity.
  • Doubly Homologated Tyrosine-Containing Peptides from the Cyanobacterium Microcystis aeruginosa NIES-4285 and Their Biosynthesis
    Chin-Soon Phan; Zhengyi Ling; Jakia Jerin Mehjabin; Kenichi Matsuda; Nurcahyo Iman Prakoso; Taiki Umezawa; Toshiyuki Wakimoto; Tatsufumi Okino
    Journal of Natural Products, 87, 11, 2629, 2639, American Chemical Society (ACS), 30 Oct. 2024, [Peer-reviewed]
    Scientific journal
  • Synthesis and Cytotoxicity of Cyclic Octapeptide Surugamides with Varied N-Acyl Moieties
    Kenichi Matsuda; Shinya Niikura; Rintaro Ichihara; Kei Fujita; Anna M. Strasser; Rokusuke Yoshikawa; Jiro Yasuda; Yoshiki Hiramatsu; Hironori Hayashi; Eiichi N. Kodama; Toshiyuki Wakimoto
    Chemical and Pharmaceutical Bulletin, 72, 9, 826, 830, Pharmaceutical Society of Japan, 20 Sep. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal
  • Macrocyclizing-thioesterases in bacterial non-ribosomal peptide biosynthesis
    Kenichi Matsuda
    Journal of Natural Medicines, 79, 1, 1, 14, Springer Science and Business Media LLC, 30 Aug. 2024, [Peer-reviewed], [Invited], [Lead author, Last author, Corresponding author]
    Scientific journal, Abstract

    Macrocyclization of peptides reduces conformational flexibilities, potentially leading to improved drug-like properties. However, side reactions such as epimerization and oligomerization often pose synthetic challenges. Peptide-cyclizing biocatalysts in the biosynthesis of non-ribosomal peptides (NRPs) have remarkable potentials as chemoenzymatic tools to facilitate more straightforward access to complex macrocycles. This review highlights the biocatalytic potentials of NRP cyclases, especially those of cis-acting thioesterases, the most general cyclizing machinery in NRP biosynthesis. Growing insights into penicillin-binding protein-type thioesterases, a relatively new group of trans-acting thioesterases, are also summarized.

    Graphical abstract
  • FlkO, a penicillin-binding protein-type thioesterase in cyclofaulknamycin biosynthesis
    Kenichi Matsuda; Rintaro Ichihara; Toshiyuki Wakimoto
    Organic & Biomolecular Chemistry, 22, 33, 6713, 6717, Royal Society of Chemistry (RSC), Aug. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal, In vitro studies of FlkO, a new penicillin-binding protein thioesterase, demonstrated its peptide-cyclizing activity and substrate scope.
  • Penicillin-binding protein-type thioesterases: An emerging family of non-ribosomal peptide cyclases with biocatalytic potentials
    Kenichi Matsuda; Toshiyuki Wakimoto
    Current Opinion in Chemical Biology, 80, 102465, 102465, Elsevier BV, Jun. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal
  • Chemoenzymatic tandem cyclization for the facile synthesis of bicyclic peptides
    Masakazu Kobayashi; Naho Onozawa; Kenichi Matsuda; Toshiyuki Wakimoto
    Communications Chemistry, 7, 1, Springer Science and Business Media LLC, 28 Mar. 2024, [Peer-reviewed], [Corresponding author]
    Scientific journal, Abstract

    Bicyclic peptides exhibit improved metabolic stabilities and target specificities when compared to their linear or mono-cyclic counterparts; however, efficient and straightforward synthesis remains challenging due to their intricate architectures. Here, we present a highly selective and operationally simple one-pot chemoenzymatic tandem cyclization approach to synthesize bicyclic peptides with small to medium ring sizes. Penicillin-binding protein-type thioesterases (PBP-type TEs) efficiently cyclized azide/alkyne-containing peptides in a head-to-tail manner. Successive copper (I)-catalyzed azide-alkyne cycloaddition generated bicyclic peptides in one-pot, thus omitting the purification of monocyclic intermediates. This chemoenzymatic strategy enabled the facile synthesis of bicyclic peptides bearing hexa-, octa-, and undecapeptidyl head-to-tail cyclic scaffolds.
  • Bacterial Hydrazine Biosynthetic Pathways Featuring Cupin/Methionyl tRNA Synthetase‐like Enzymes
    Kenichi Matsuda; Toshiyuki Wakimoto
    ChemBioChem, 25, 9, Wiley, 25 Mar. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal, Abstract

    Nitrogen‐Nitrogen (N−N) bond‐containing functional groups in natural products and synthetic drugs play significant roles in exerting biological activities. The mechanisms of N−N bond formation in natural organic molecules have garnered increasing attention over the decades. Recent advances have illuminated various enzymatic and nonenzymatic strategies, and our understanding of natural N−N bond construction is rapidly expanding. A group of didomain proteins with zinc‐binding cupin/methionyl‐tRNA synthetase (MetRS)‐like domains, also known as hydrazine synthetases, generates amino acid‐based hydrazines, which serve as key biosynthetic precursors of diverse N−N bond‐containing functionalities such as hydrazone, diazo, triazene, pyrazole, and pyridazinone groups. In this review, we summarize the current knowledge on hydrazine synthetase mechanisms and the various pathways employing this unique bond‐forming machinery.
  • Phylogeny‐guided Characterization of Bacterial Hydrazine Biosynthesis Mediated by Cupin/methionyl tRNA Synthetase‐like Enzymes
    Kenichi Matsuda; Yuto Nakahara; Atina Rizkiya Choirunnisa; Kuga Arima; Toshiyuki Wakimoto
    ChemBioChem, 25, 7, Wiley, 12 Mar. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal, Abstract

    Cupin/methionyl‐tRNA synthetase (MetRS)‐like didomain enzymes catalyze nitrogen‐nitrogen (N−N) bond formation between Nω‐hydroxylamines and amino acids to generate hydrazines, key biosynthetic intermediates of various natural products containing N−N bonds. While the combination of these two building blocks leads to the creation of diverse hydrazine products, the full extent of their structural diversity remains largely unknown. To explore this, we herein conducted phylogeny‐guided genome‐mining of related hydrazine biosynthetic pathways consisting of two enzymes: flavin‐dependent Nω‐hydroxylating monooxygenases (NMOs) that produce Nω‐hydroxylamine precursors and cupin/MetRS‐like enzymes that couple the Nω‐hydroxylamines with amino acids via N−N bonds. A phylogenetic analysis identified the largely unexplored sequence spaces of these enzyme families. The biochemical characterization of NMOs demonstrated their capabilities to produce various Nω‐hydroxylamines, including those previously not known as precursors of N−N bonds. Furthermore, the characterization of cupin/MetRS‐like enzymes identified five new hydrazine products with novel combinations of building blocks, including one containing non‐amino acid building blocks: 1,3‐diaminopropane and putrescine. This study substantially expanded the variety of N−N bond forming pathways mediated by cupin/MetRS‐like enzymes.
  • Actinobacterial chalkophores: the biosynthesis of hazimycins
    Kenichi Matsuda; Hiroto Maruyama; Kumiko Imachi; Haruo Ikeda; Toshiyuki Wakimoto
    The Journal of Antibiotics, 77, 4, 228, 237, Springer Science and Business Media LLC, 20 Feb. 2024, [Peer-reviewed], [Lead author, Corresponding author]
    Scientific journal
  • Carrier Protein Mediated Formation of the Dihydropyridazinone Ring in Actinopyridazinone Biosynthesis
    Kuga Arima; Satoko Akiyama; Kazuo Shin‐ya; Kenichi Matsuda; Toshiyuki Wakimoto
    Angewandte Chemie International Edition, 62, 29, Wiley, 06 Jun. 2023, [Peer-reviewed], [Corresponding author]
    Scientific journal, Abstract

    Heterocycles with nitrogen‐nitrogen (N−N) bonds are privileged building blocks of synthetic drugs. They are also found in natural products, although the biosynthetic logic behind them is poorly understood. Actinopyridazinones produced by Streptomyces sp. MSD090630SC‐05 possess unique dihydropyridazinone rings that have been studied as core nuclei in several approved synthetic therapeutics. Herein, we performed gene knockouts and in vitro biochemical experiments to elucidate the major steps in actinopyridazinone biosynthesis, including the unprecedented carrier protein mediated machinery for dihydropyridazinone formation.
  • Streamlined Chemoenzymatic Synthesis of Cyclic Peptides by Non-ribosomal Peptide Cyclases
    Masakazu Kobayashi; Kei Fujita; Kenichi Matsuda; Toshiyuki Wakimoto
    Journal of the American Chemical Society, 145, 6, 3270, 3275, American Chemical Society (ACS), 13 Jan. 2023, [Peer-reviewed], [Corresponding author]
    Scientific journal
  • Chemo-Enzymatic Synthesis of Non-ribosomal Macrolactams by a Penicillin-Binding Protein-Type Thioesterase.
    Masakazu Kobayashi; Kei Fujita; Kenichi Matsuda; Toshiyuki Wakimoto
    Methods in molecular biology (Clifton, N.J.), 2670, 127, 144, 2023, [Peer-reviewed], [Invited], [Corresponding author], [International Magazine]
    English, Scientific journal, Penicillin-binding protein-type thioesterases (PBP-type TEs) are an emerging family of non-ribosomal peptide cyclases. PBP-type TEs exhibit distinct substrate scopes from the well-exploited ribosomal peptide cyclases and traditional non-ribosomal peptide cyclases. Their unique properties, as well as their stand-alone nature, highlight PBP-type TEs as valuable candidates for development as biocatalysts for peptide macrocyclization. Here in this chapter, we describe the scheme for the chemoenzymatic synthesis of non-ribosomal macrolactam by SurE, a representative member of PBP-type TEs.
  • Characterization of the surugamide biosynthetic gene cluster of TUA-NKU25, aStreptomyces diastaticusstrain isolated from Kusaya, and its effects on salt-dependent growth
    Aoi Takeuchi; Asahi Hirata; Aiko Teshima; Miu Ueki; Takumi Satoh; Kenichi Matsuda; Toshiyuki Wakimoto; Kenji Arakawa; Morio Ishikawa; Toshihiro Suzuki
    Bioscience, Biotechnology, and Biochemistry, 87, 3, 320, 329, Oxford University Press (OUP), 10 Dec. 2022, [Peer-reviewed]
    Scientific journal, ABSTRACT

    Kusaya, a traditional Japanese fermented fish product, is known for its high preservability, as it contains natural antibiotics derived from microorganisms, and therefore molds and yeasts do not colonize it easily. In this study, the Streptomyces diastaticus strain TUA-NKU25 was isolated from Kusaya, and its growth as well as the production of antibiotics were investigated. Strain TUA-NKU25 showed advantageous growth characteristics in the presence, but not in the absence, of sodium chloride (NaCl). Antimicrobial assay, high-performance liquid chromatography, and electrospray ionization-mass spectrometry analysis showed that this strain produced surugamide A and uncharacterized antimicrobial compound(s) during growth in the presence of NaCl, suggesting that the biosynthesis of these compounds was upregulated by NaCl. Draft genomic analysis revealed that strain TUA-NKU25 possesses a surugamide biosynthetic gene cluster (sur BGC), although it is incomplete, lacking surB/surC. Phylogenetic analysis of strain TUA-NKU25 and surugamide-producing Streptomyces showed that sur BGC formed a clade distinct from other known groups.
  • Molecular Basis for Enzymatic Aziridine Formation via Sulfate Elimination
    Sumire Kurosawa; Fumihito Hasebe; Hironori Okamura; Ayako Yoshida; Kenichi Matsuda; Yusuke Sone; Takeo Tomita; Tetsuro Shinada; Hirosato Takikawa; Tomohisa Kuzuyama; Saori Kosono; Makoto Nishiyama
    Journal of the American Chemical Society, 144, 35, 16164, 16170, American Chemical Society (ACS), 23 Aug. 2022, [Peer-reviewed], [International Magazine]
    English, Scientific journal, Natural products containing an aziridine ring, such as mitomycin C and azinomycin B, exhibit antitumor activities by alkylating DNA via their aziridine rings; however, the biosynthetic mechanisms underlying the formation of these rings have not yet been elucidated. We herein investigated the biosynthesis of vazabitide A, the structure of which is similar to that of azinomycin B, and demonstrated that Vzb10/11, with no similarities to known enzymes, catalyzed the formation of the aziridine ring via sulfate elimination. To elucidate the detailed reaction mechanism, crystallization of Vzb10/11 and the homologous enzyme, AziU3/U2, in the biosynthesis of azinomycin B was attempted, and the structure of AziU3/U2, which had a new protein fold overall, was successfully determined. The structural analysis revealed that these enzymes adjusted the dihedral angle between the amino group and the adjacent sulfate group of the substrate to almost 180° and enhanced the nucleophilicity of the C6-amino group temporarily, facilitating the SN2-like reaction to form the aziridine ring. The present study reports for the first time the molecular basis for aziridine ring formation.
  • New azodyrecins identified by a genome mining-directed reactivity-based screening
    Atina Rizkiya Choirunnisa; Kuga Arima; Yo Abe; Noritaka Kagaya; Kei Kudo; Hikaru Suenaga; Junko Hashimoto; Manabu Fujie; Noriyuki Satoh; Kazuo Shin-ya; Kenichi Matsuda; Toshiyuki Wakimoto
    Beilstein Journal of Organic Chemistry, 18, 1017, 1025, Beilstein Institut, 10 Aug. 2022, [Peer-reviewed], [Corresponding author]
    English, Scientific journal, Only a few azoxy natural products have been identified despite their intriguing biological activities. Azodyrecins D–G, four new analogs of aliphatic azoxides, were identified from two Streptomyces species by a reactivity-based screening that targets azoxy bonds. A biological activity evaluation demonstrated that the double bond in the alkyl side chain is important for the cytotoxicity of azodyrecins. An in vitro assay elucidated the tailoring step of azodyrecin biosynthesis, which is mediated by the S-adenosylmethionine (SAM)-dependent methyltransferase Ady1. This study paves the way for the targeted isolation of aliphatic azoxy natural products through a genome-mining approach and further investigations of their biosynthetic mechanisms.
  • A Natural Dihydropyridazinone Scaffold Generated from a Unique Substrate for a Hydrazine-Forming Enzyme
    Kenichi Matsuda; Kuga Arima; Satoko Akiyama; Yuito Yamada; Yo Abe; Hikaru Suenaga; Junko Hashimoto; Kazuo Shin-ya; Makoto Nishiyama; Toshiyuki Wakimoto
    Journal of the American Chemical Society, 144, 28, 12954, 12960, American Chemical Society (ACS), 30 Jun. 2022, [Peer-reviewed], [Lead author, Corresponding author], [International Magazine]
    English, Scientific journal, Nitrogen-nitrogen bond-containing functional groups are rare, but they are found in a considerably wide class of natural products. Recent clarifications of the biosynthetic routes for such functional groups shed light onto overlooked biosynthetic genes distributed across the bacterial kingdom, highlighting the presence of yet-to-be identified natural products with peculiar functional groups. Here, the genome-mining approach targeting a unique hydrazine-forming gene led to the discovery of actinopyridazinones A (1) and B (2), the first natural products with dihydropyridazinone rings. The structure of actinopyridazinone A was unambiguously established by total synthesis. Biosynthetic studies unveiled the structural diversity of natural hydrazines derived from this family of N-N bond-forming enzymes.
  • Argicyclamides A–C Unveil Enzymatic Basis for Guanidine Bis-prenylation
    Chin-Soon Phan; Kenichi Matsuda; Nandani Balloo; Kei Fujita; Toshiyuki Wakimoto; Tatsufumi Okino
    Journal of the American Chemical Society, 143, 27, 10083, 10087, American Chemical Society (ACS), 28 Jun. 2021, [Peer-reviewed], [Lead author]
    Scientific journal
  • PenA, a penicillin-binding protein-type thioesterase specialized for small peptide cyclization.
    Kenichi Matsuda; Kei Fujita; Toshiyuki Wakimoto
    Journal of industrial microbiology & biotechnology, 48, 3-4, 13 Mar. 2021, [Peer-reviewed], [Lead author], [International Magazine]
    English, Scientific journal, Penicillin binding protein-type thioesterases (PBP-type TEs) are a recently identified group of peptide cyclases that catalyze head-to-tail macrolactamization of non-ribosomal peptides. PenA, a new member of this group, is involved in the biosyntheses of cyclic pentapeptides. In this study, we demonstrated the enzymatic activity of PenA in vitro, and analyzed its substrate scope with a series of synthetic substrates. A comparison of the reaction profiles between PenA and SurE, a representative PBP-type TE, showed that PenA is more specialized for small peptide cyclization. A computational model provided a possible structural rationale for the altered specificity for substrate chain lengths.
  • Insights into phosphatase-activated chemical defense in a marine sponge holobiont
    Takahiro Jomori; Kenichi Matsuda; Yoko Egami; Ikuro Abe; Akira Takai; Toshiyuki Wakimoto
    RSC Chemical Biology, 2, 6, 1600, 1607, Royal Society of Chemistry (RSC), 2021, [Peer-reviewed]
    Scientific journal, The phosphatase that activates calyculin biogenesis in the sponge Discodermia calyx turned out to originate from the bacterial symbiont Entotheonella.
  • Recent advance in the biosynthesis of nitrogen–nitrogen bond–containing natural products
    Yohei Katsuyama; Kenichi Matsuda
    Current Opinion in Chemical Biology, 59, 62, 68, Elsevier {BV}, Dec. 2020, [Peer-reviewed], [Invited]
    English, Scientific journal
  • Total Synthesis and Structural Revision of Kasumigamide, and Identification of a New Analogue
    Takefumi Kuranaga; Kenichi Matsuda; Masachika Takaoka; Chisato Tachikawa; Ayae Sano; Kosei Itoh; Ayumu Enomoto; Kei Fujita; Ikuro Abe; Toshiyuki Wakimoto
    ChemBioChem, Wiley, 21 Jul. 2020, [Peer-reviewed]
    Scientific journal
  • Guanidyl modification of the 1-azabicyclo[3.1.0]hexane ring in ficellomycin essential for its biological activity.
    Sumire Kurosawa; Kenichi Matsuda; Fumihito Hasebe; Taro Shiraishi; Kazuo Shin-Ya; Tomohisa Kuzuyama; Makoto Nishiyama
    Organic & biomolecular chemistry, 18, 27, 5137, 5144, 15 Jul. 2020, [Peer-reviewed], [International Magazine]
    English, Scientific journal, The 1-azabicyclo[3.1.0]hexane ring is a key moiety in natural products for biological activities against bacteria, fungi, and tumor through DNA alkylation. Ficellomycin is a dipeptide that consists of l-valine and a non-proteinogenic amino acid with the 1-azabicyclo[3.1.0]hexane ring structure. Although the biosynthetic gene cluster of ficellomycin has been identified, the biosynthetic pathway currently remains unclear. We herein report the final stage of ficellomycin biosynthesis involving ring modifications and successive dipeptide formation. After the ring is formed, the hydroxy group of the ring is converted into the guanidyl unit by three enzymes, which include an aminotransferase with a novel inter ω-ω amino-transferring activity. In the last step, the resulting 1-azabicyclo[3.1.0]hexane ring-containing amino acid is connected with l-valine by an amino acid ligase to yield ficellomycin. The present study revealed a new machinery that expands the structural and biological diversities of natural products.
  • Heterochiral coupling in non-ribosomal peptide macrolactamization
    Kenichi Matsuda; Rui Zhai; Takahiro Mori; Masakazu Kobayashi; Ayae Sano; Ikuro Abe; Toshiyuki Wakimoto
    Nature Catalysis, 3, 6, 507, 515, Springer Science and Business Media LLC, 04 May 2020, [Peer-reviewed], [Lead author]
    Scientific journal
  • A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria.
    Kei Sakaki; Keita Ohishi; Tetsu Shimizu; Ikki Kobayashi; Naoki Mori; Kenichi Matsuda; Takeo Tomita; Hidenori Watanabe; Kan Tanaka; Tomohisa Kuzuyama; Makoto Nishiyama
    Nature chemical biology, 16, 4, 415, 422, 10 Feb. 2020, [Peer-reviewed], [International Magazine]
    English, Scientific journal, In biotin biosynthesis, the conversion of pimeloyl intermediates to biotin is catalyzed by a universal set of four enzymes: BioF, BioA, BioD and BioB. We found that the gene homologous to bioA, the product of which is involved in the conversion of 8-amino-7-oxononanoate (AON) to 7,8-diaminononanoate (DAN), is missing in the genome of the cyanobacterium Synechocystis sp. PCC 6803. We provide structural and biochemical evidence showing that a novel dehydrogenase, BioU, is involved in biotin biosynthesis and functionally replaces BioA. This enzyme catalyzes three reactions: formation of covalent linkage with AON to yield a BioU-DAN conjugate at the ε-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+. In this biosynthetic pathway, BioU is a suicide enzyme that loses the Lys124 amino group after a single round of reaction.
  • A New Cyclase Family Catalyzing Head-to-Tail Macrolactamization of Non-ribosomal Peptides
    Kenichi Matsuda; Takefumi Kuranaga; Toshiyuki Wakimoto
    Journal of Synthetic Organic Chemistry, Japan, 77, 11, 1106, 1115, 01 Nov. 2019, [Peer-reviewed], [Invited], [Lead author]
    Scientific journal
  • Immunosuppressive effect of a non-proteinogenic amino acid from Streptomyces through inhibiting allogeneic T cell proliferation
    Takuya Yashiro; Fumiya Sakata; Takahiro Sekimoto; Tomohiro Shirai; Fumihito Hasebe; Kenichi Matsuda; Sumire Kurosawa; Shodai Suzuki; Kazuki Nagata; Kazumi Kasakura; Makoto Nishiyama; Chiharu Nishiyama
    Bioscience, Biotechnology, and Biochemistry, 83, 6, 1111, 1116, Informa UK Limited, 03 Jun. 2019, [Peer-reviewed]
    Scientific journal, ABSTRACT

    The immunosuppressive activity of myriocin (ISP-1), a lead compound of fingolimod (FTY720), is derived from its 2-amino-1,3-propandiol structure. A non-proteinogenic amino acid, (2S,6R)-diamino-(5R,7)-dihydroxy-heptanoic acid (DADH), that contains this structure, was recently identified as a biosynthetic intermediate of a dipeptide secondary metabolite, vazabitide A, in Streptmyces sp. SANK 60404; however its effect on adaptive immunity has not yet been examined. In this study, we examined whether DADH suppresses mixed lymphocyte reaction using mouse bone marrow-derived dendritic cells (BMDCs) and allogeneic splenic T cells. Although T cell proliferation induced by cross-linking CD3 and CD28 were not suppressed by DADH unlike ISP-1, the pre-incubation of BMDCs with DADH but not ISP-1 significantly decreased allogeneic CD8+ T cell expansion. Based on these results, we concluded that DADH suppresses DC-mediated T cell activation by targeting DCs.
  • Scrobiculosides A and B from the deep-sea sponge Pachastrella scrobiculosa
    Takahiro Jomori; Shuji Shiroyama; Yuji Ise; Hisanori Kohtsuka; Kenichi Matsuda; Takefumi Kuranaga; Toshiyuki Wakimoto
    Journal of Natural Medicines, 73, 4, 814, 819, Springer Science and Business Media LLC, 03 May 2019, [Peer-reviewed]
    Scientific journal
  • The Revised Structure of the Cyclic Octapeptide Surugamide A
    Kenichi Matsuda; Takefumi Kuranaga; Ayae Sano; Akihiro Ninomiya; Kentaro Takada; Toshiyuki Wakimoto
    Chemical and Pharmaceutical Bulletin, 67, 5, 476, 480, Pharmaceutical Society of Japan, 01 May 2019, [Peer-reviewed], [Lead author]
    Scientific journal
  • SurE is a trans-acting thioesterase cyclizing two distinct non-ribosomal peptides
    Kenichi Matsuda; Masakazu Kobayashi; Takefumi Kuranaga; Kentaro Takada; Haruo Ikeda; Shigeki Matsunaga; Toshiyuki Wakimoto
    Organic & Biomolecular Chemistry, 17, 5, 1058, 1061, Royal Society of Chemistry (RSC), 2019, [Peer-reviewed], [Lead author]
    Scientific journal,

    A new stand-alone thioesterase, SurE, is capable of offloading two different NRPS assembly lines to generate two structurally unrelated cyclopeptides.

  • Discovery of Unprecedented Hydrazine-Forming Machinery in Bacteria
    Kenichi Matsuda; Takeo Tomita; Kazuo Shin-ya; Toshiyuki Wakimoto; Tomohisa Kuzuyama; Makoto Nishiyama
    Journal of the American Chemical Society, 140, 29, 9083, 9086, American Chemical Society (ACS), 12 Jul. 2018, [Peer-reviewed], [Lead author]
    Scientific journal
  • Total Synthesis of the Nonribosomal Peptide Surugamide B and Identification of a New Offloading Cyclase Family
    Takefumi Kuranaga; Kenichi Matsuda; Ayae Sano; Masakazu Kobayashi; Akihiro Ninomiya; Kentaro Takada; Shigeki Matsunaga; Toshiyuki Wakimoto
    Angewandte Chemie International Edition, 57, 30, 9447, 9451, Wiley, 25 Jun. 2018, [Peer-reviewed]
    Scientific journal, Abstract

    The cathepsin B inhibitor surugamide B (2), along with structurally related derivatives (A and C–E), has previously been isolated from the marine actinomycete Streptomyces sp. JAMM992. The biosynthetic genes are unexpectedly part of a cluster of four non‐ribosomal peptide synthetase (NRPS) genes, two of which are responsible for the biosynthesis of the additional linear decapeptide surugamide F. However, the thioesterase domain required for the later stage of the biosynthesis of the cyclic peptides surugamides A–E is not present in any module architecture of the surugamide NRPSs. Herein, we report the first total synthesis of surugamide B (2) through the macrocyclization at the biomimetic position, which not only alleviated the Cα epimerization in the macrolactamization process, but also efficiently provided 2 in 34 % yield for 18 steps. Furthermore, both the chemical and enzymatic studies with the biosynthetic precursor mimics revealed that the stand‐alone enzyme SurE, which belongs to the penicillin‐binding protein family, is responsible for macrocyclization of the tethered octapeptidyl intermediate.
  • Genome Mining of Amino Group Carrier Protein-Mediated Machinery: Discovery and Biosynthetic Characterization of a Natural Product with Unique Hydrazone Unit
    Kenichi Matsuda; Fumihito Hasebe; Yuh Shiwa; Yu Kanesaki; Takeo Tomita; Hirofumi Yoshikawa; Kazuo Shin-ya; Tomohisa Kuzuyama; Makoto Nishiyama
    ACS CHEMICAL BIOLOGY, 12, 1, 124, 131, Jan. 2017, [Peer-reviewed], [Lead author]
    English, Scientific journal
  • Amino-group carrier-protein-mediated secondary metabolite biosynthesis in Streptomyces
    Fumihito Hasebe; Kenichi Matsuda; Taro Shiraishi; Yushi Futamura; Takeshi Nakano; Takeo Tomita; Ken Ishigami; Hikari Taka; Reiko Mineki; Tsutomu Fujimura; Hiroyuki Osada; Tomohisa Kuzuyama; Makoto Nishiyama
    NATURE CHEMICAL BIOLOGY, 12, 11, 967, +, Nov. 2016, [Peer-reviewed]
    English, Scientific journal
  • Crystallization and preliminary X-ray diffraction analysis of cyclolavandulyl diphosphate synthase, a new member of the cis-isoprenyl diphosphate synthase superfamily
    Takeo Tomita; Taro Ozaki; Kenichi Matsuda; Makoto Nishiyama; Tomohisa Kuzuyama
    Acta Crystallographica Section F:Structural Biology Communications, 70, 1410, 1413, International Union of Crystallography, 01 Oct. 2014, [Peer-reviewed]
    English, Scientific journal
■ Other Activities and Achievements
■ Lectures, oral presentations, etc.
  • 環状二級アミンを求核基とする非リボソームペプチド環化酵素の機能解析
    青野満夫、山田惟人、松田研一、脇本敏幸
    日本薬学会第146年会, 27 Mar. 2026
  • 非リボソームペプチド環化酵素PBP-type TEファミリーの探索と機能解析
    横山光海、新倉慎也、上田龍聖、市原凛太郎、小林雅和、松田研一、脇本敏幸
    日本薬学会第146年会, 27 Mar. 2026
  • カリクリンAのニトリル形成を担うシュードキナーゼの機能解析
    山田惟人、横山光海、松田研一、脇本敏幸
    日本薬学会第146年会, 27 Mar. 2026
  • 天然物生合成酵素の探索と複雑分子の化学ー酵素合成
    松田研一
    日本農芸化学会 2026年度京都大会 ランチョンセミナー 3LS1A3, 11 Mar. 2026
    [Invited]
  • N-N結合含有ヘテロ環形成に関わるアシルヒドラゾン 加水分解酵素Apy4の機能解析
    福井秀弥、有馬陸、山田惟人、松田研一、脇本敏幸
    日本農芸化学会 2026年度京都大会, 11 Mar. 2026
  • 窒素−窒素共有結合を形成する金属酵素を用いたα-ヒドラジノ酸の化学酵素合成
    有馬陸、松田研一、脇本敏幸
    日本農芸化学会 2026年度京都大会, 10 Mar. 2026
  • 環状ペプチドの化学ー酵素合成
    松田研一
    25-2 高分子学会講演会 ペプチド合成・解析の最前線, 18 Feb. 2026
    [Invited]
  • Exploring Bacterial Hydrazine Biosynthetic Pathways Featuring Cupin/Methionyl tRNA Synthetase-like Enzymes
    Kenichi Matsuda, Toshiyuki Wakimoto
    Pacifichem2025, 17 Dec. 2025
  • Functional analysis of a new nitrile synthase in calyculin biosynthesis
    Hiromi Yokoyama, Yuito Yamada, Kenichi Matsuda, Jörn Piel, Toshiyuki Wakimoto
    Pacifichem2025, 17 Dec. 2025
  • Flavin-dependent α-ketoamide forming enzyme in the biosynthesis of NRPS-PKS hybrid-type natural products
    Yuito Yamada, Huibin Wang, Takahiro Mori, Kenichi Matsuda, Ikuro Abe, Toshiyuki Wakimoto
    Pacifichem2025, 17 Dec. 2025
  • Enzymatic peptide macrocyclization via indole-N-acylation
    Hiroto Maruyama, Yuito Yamada, Yasuhiro Igarashi, Kenichi Matsuda, Toshiyuki Wakimoto
    Pacifichem2025, 17 Dec. 2025
  • 二級アミンを求核基とする非リボソームペプチド環化ドメインの機能解析
    青野満夫、松田研一、脇本敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • Calyculin生合成における末端ニトリル形成機構の解明
    横山光海、山田惟人、松田研一、脇本敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • N-N結合含有天然物の鍵中間体であるヒドラジン生合成経路の探索
    中原悠斗、有馬陸、松田研一、脇本敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • NRPS-PKS ハイブリッド型天然物の生合成においてα-ケトアミド形成を担う新規フラビン酵素に関する研究
    山田 惟人, 王匯濱, 森 貴裕, 松田 研一, 阿部 郁朗, 脇本 敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • インドールN-アシル化を介したペプチド環化機構
    丸山 広大,山田惟人,五十嵐 康弘,松田研一,脇本敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • 金属酵素を用いた α‑ヒドラジノ酸の化学酵素合成
    有馬陸、松田研一、脇本敏幸
    第25回 天然薬物の開発と応用シンポジウム, 11 Oct. 2025
  • 系統解析に基づく新規ヒドラジン生合成経路の探索
    中原悠斗、有馬陸、松田研一、脇本敏幸
    第71回日本生薬学会, 14 Sep. 2025
  • Calyculinにおける末端ニトリル生合成機構の解明
    横山光海、山田惟人、松田研一、脇本敏幸
    第71回日本生薬学会, 14 Sep. 2025
  • 金属酵素を用いた α‑ヒドラジノ酸の合成
    有馬陸、松田研一、脇本敏幸
    第71回日本生薬学会, 14 Sep. 2025
  • 海綿動物由来環状ペプチドのα-ケトアミド⽣合成機構
    山田 惟人, 王匯濱, 森 貴裕, 松田 研一, 阿部 郁朗, 脇本 敏幸
    第71回日本生薬学会, 14 Sep. 2025
  • アルギニン選択的ペプチドビスプレニル化酵素における連続プレニル基転移反応機構の解明と制御
    藤田慧、山田惟人、森貴裕、松田研一、阿部郁朗、脇本敏幸
    第71回日本生薬学会, 14 Sep. 2025
  • アルギニン側鎖選択的ペプチドビスプレニル化酵素の同定と連続プレニル化反応の制御
    藤田慧、山田惟人、森貴裕、Phan Chin-Soon、沖野龍文、松田研一、阿部郁朗、脇本敏幸
    第67回天然有機化合物討論会, 11 Sep. 2025
  • Bulbiferamide 生合成におけるインドール N -アシル化を伴うペプチド環化反応
    丸山 広大,山田惟人,五十嵐 康弘,松田研一,脇本敏幸
    学術変革領域研究（A)予知生合成科学2025年若手合宿勉強会, 07 Sep. 2025
  • 海綿動物由来 α-ketoamide 含有環状ペプチドの生合成機構
    山田 惟人, 王匯濱, 森 貴裕, 松田 研一, 阿部 郁朗, 脇本 敏幸
    学術変革領域研究（A)予知生合成科学2025年若手合宿勉強会, 07 Sep. 2025
  • 金属酵素を用いた α‑ヒドラジノ酸の合成
    有馬陸、松田研一、脇本敏幸
    学術変革領域研究（A)予知生合成科学2025年若手合宿勉強会, 07 Sep. 2025
  • アルギニン側鎖選択的ビスプレニル化酵素における連続プレニル基転移反応機構の解明と制御
    藤田慧、山田惟人、森貴裕、松田研一、阿部郁朗、脇本敏幸
    学術変革領域研究（A)予知生合成科学2025年若手合宿勉強会, 07 Sep. 2025
  • 主鎖アミドアルキル化環状ペプチドの化学ー酵素合成に向けた非リボソームペプチド環化酵素の機能解析
    青野満夫、松田研一、脇本敏幸
    2025年度 (第39回) 日本放線菌学会大会, 03 Sep. 2025
  • ペプチド–ペプチド核酸ハイブリッド環状化合物の化学–酵素合成
    小野澤 菜帆, 松田 研一, 脇本 敏幸
    2025年度 (第39回) 日本放線菌学会大会, 03 Sep. 2025
  • Biosynthesis of Natural Products Featuring Bacterial Hydrazine Synthetases: Cupin/Methionyl tRNA Synthetase-like Enzymes
    Kenichi Matsuda, Toshiyuki Wakimoto
    1st Japanese-Australian Symposium on the Biosynthesis of Natural Products, 29 Aug. 2025
    [Invited]
  • Biosynthesis of Natural Products Featuring Bacterial Hydrazine Synthetases: Cupin/Methionyl tRNA Synthetase-like Enzymes
    Kenichi Matsuda, Toshiyuki Wakimoto
    32nd International Symposium on the Chemistry of Natural Products, 24 Aug. 2025
  • Arginine-N,N’-bisprenyltransferases: Switchable Catalysis in Consecutive Guanidine-N-prenylation
    Kei Fujita, Yuito Yamada, Takahiro Mori, Kenichi Matsuda, Ikuro Abe, Toshiyuki Wakimoto
    32nd International Symposium on the Chemistry of Natural Products, 24 Aug. 2025
  • Phylogeny-guided exploration of bacterial hydrazine biosynthetic pathways mediated by cupin/methionyl-tRNA synthetase-like enzymes
    Yuto Nakahara, Kuga Arima, Kenichi Matsuda, Toshiyuki Wakimoto
    32nd International Symposium on the Chemistry of Natural Products, 24 Aug. 2025
  • 天然物生合成酵素を活用した修飾ペプチドの化学－酵素合成
    松田研一
    第58回 天然物化学談話会, 14 Jul. 2025
  • Bulbiferamide生合成におけるインドールN-アシル化を伴うペプチド環化反応
    丸山 広大,山田惟人,五十嵐 康弘,松田研一,脇本敏幸
    第37回万有札幌シンポジウム, 05 Jul. 2025
  • A SIMPLIFIED PANTETHEINE SURROGATE FACILITATES CHEMOENZYMATIC CYCLIC PEPTIDES SYNTHESIS VIA NON-RIBOSOMAL PEPTIDE CYCLASES
    Kenichi Matsuda, Toshiyuki Wakimoto
    BIOTRANS - 17th International Symposium on Biocatalysis and Biotransformations, 03 Jul. 2025
  • Exploring Bacterial Hydrazine Biosynthetic Pathways Featuring Cupin/Methionyl tRNA Synthetase-like Enzymes
    Kenichi Matsuda, Toshiyuki Wakimoto
    REPARTZYME2025, 29 Jun. 2025
  • Bulbiferamide生合成におけるインドールN-アシル化を伴うペプチド環化反応
    丸山 広大,山田惟人,五十嵐 康弘,松田研一,脇本敏幸
    第51回生体分子科学討論会, 26 Jun. 2025
  • 窒素−窒素結合形成を触媒する金属酵素を用いた α‑ヒドラジノ酸の合成
    有馬陸、松田研一、脇本敏幸
    第51回生体分子科学討論会, 26 Jun. 2025
  • 天然物生合成酵素を用いた複雑修飾ペプチドの化学－酵素合成
    松田研一
    第26回酵素応用シンポジウム, 14 Jun. 2025
    [Invited]
  • Calyculin生合成における新規ニトリル合成酵素の機能解析
    横山光海、山田惟人、松田研一、脇本敏幸
    第49回日本生薬学会北海道支部例会, 17 May 2025
  • 二級アミンを求核基とするペプチド環化酵素の機能解析
    青野満夫、松田研一、脇本敏幸
    第49回日本生薬学会北海道支部例会, 17 May 2025
  • Bacterial Hydrazine Biosynthetic Pathways Featuring Cupin/Methionyl tRNA Synthetase-like Enzymes
    Kenichi Matsuda
    AmineBioCat2025, 01 Apr. 2025
    [Invited]
  • 天然物生合成酵素の開拓と有用化合物合成への応用
    松田研一
    日本薬学会第145年会, 29 Mar. 2025
    [Invited]
  • 窒素−窒素結合形成を触媒する金属酵素を用いたα-ヒドラジノ酸の合成
    有馬陸、松田研一、脇本敏幸
    日本薬学会第145年会, 27 Mar. 2025
  • 系統解析に基づくヒドラジンの構造多様性の開拓
    中原悠斗、有馬陸、Atina Rizkiya Choirunnisa、松田研一、脇本敏幸
    日本農芸化学会2025年度大会, 07 Mar. 2025
  • 非リボソームヘキサペプチド環化酵素WolJ/FlkOの比較機能解析
    市原 凜太郎,松田 研一,脇本 敏幸
    日本農芸化学会2025年度大会, 07 Mar. 2025
  • 非リボソームペプチド生合成におけるインドールN-アシル化を介した環化反応
    丸山 広大,山田惟人,森内良太,小谷 真也,五十嵐 康弘,松田研一,脇本敏幸
    日本農芸化学会2025年度大会, 07 Mar. 2025
  • NRPS-PKSハイブリッド型環状ペプチドのα-ケトアミド構造生合成研究
    山田 惟人, 王匯濱, 森 貴裕, 松田 研一, 阿部 郁朗, 脇本 敏幸
    日本農芸化学会2025年度大会, 06 Mar. 2025
  • 新規Arg選択的ビスプレニル化酵素の同定と構造機能解析
    藤田慧, 山田惟人, 森貴裕, 松田研一, 阿部郁朗, 脇本敏幸
    日本農芸化学会2025年度大会, 06 Mar. 2025
  • 2-6 - DIOL AS A NEW PANTETHEINE SURROGATE FOR CHEMOENZYMATIC SYNTHESIS OF CYCLIC PEPTIDES VIA NON-RIBOSOMAL PEPTIDE CYCLASES
    Kenichi Matsuda
    the 5th International Conference on Natural Products Discovery and Development in the Genomic Era, 05 Jan. 2025
    [Invited]
  • Bacterial Hydrazine Biosynthetic Pathways Featured by Cupin/methionyl-tRNA synthetase-like Enzymes
    Kenichi Matsuda, Toshiyuki Wakimoto
    2024 The 2nd Taiwan-Japan Bilateral Symposium on Natural Products Biosynthesis, 15 Nov. 2024
    [Invited]
  • 系統解析に基づくヒドラジン生合成経路の多様性の開拓
    中原 悠斗, 有馬 陸, Choirunnisa Atina, 松田 研一, 脇本 敏幸
    第10回食品薬学シンポジウム, 12 Oct. 2024
  • ヘキサペプチドに特化した非リボソームペプチド環化酵素FlkO/WolJの比較機能解析
    市原凜太郎, 松田研一, 脇本敏幸
    第10回食品薬学シンポジウム, 12 Oct. 2024
  • インドールN-アシル化による環状ペプチドの生合成
    丸山広大、山田惟人、森内良太、小谷真也、五十嵐康弘、松田研一、脇本敏幸
    第10回食品薬学シンポジウム, 12 Oct. 2024
  • 新規アルギニンビスプレニル化酵素の構造と反応機構解析
    藤田慧, 山田惟人, 森貴裕, 松田研一, 阿部郁朗, 脇本敏幸
    第10回食品薬学シンポジウム, 12 Oct. 2024
  • Cyclofaulknamycin生合成においてペプチド環化反応を触媒する新規PBP型チオエステラーゼFlkOの機能解析
    市原凜太郎, 松田研一, 脇本敏幸
    第70回日本生薬学会, 15 Sep. 2024
  • Bulbiferamide生合成におけるインドールN-アシル化を伴うペプチド環化反応
    丸山 広大,山田惟人,森内良太,小谷 真也,五十嵐 康弘,松田研一,脇本敏幸
    第70回日本生薬学会, 15 Sep. 2024
  • 天然物生合成酵素を活用した環状中分子の化学−酵素合成
    松田研一
    第6回BINDS合成勉強会 @名古屋大学創薬科学研究科, 14 Sep. 2024
  • 系統解析に基づくヒドラジン生合成経路の多様性の開拓
    中原 悠斗, 有馬 陸, Choirunnisa Atina, 松田 研一, 脇本 敏幸
    2024年度（第38回）日本放線菌学会大会 東京, 10 Sep. 2024
  • 放線菌由来天然物生合成酵素を用いた環状ペプチドの化学−酵素合成
    松田研一
    2024年度（第38回）日本放線菌学会大会 東京, 10 Sep. 2024
    [Invited]
  • インドールN-アシル化による環状ペプチドの生合成
    丸山 広大,山田惟人,森内良太,小谷 真也,五十嵐 康弘,松田研一,脇本敏幸
    第66回天然有機化合物討論会, 09 Sep. 2024
  • NRPS-PKS ハイブリッド型天然物生合成におけるα-ケトアミド形成機構
    山田 惟人, Huibin Wang, 森 貴裕, 松田 研一, 阿部 郁朗, 脇本 敏幸
    学術変革領域研究（A)予知生合成科学2024年若手合宿勉強会, 24 Aug. 2024
  • 酵素を用いたグリシンのN-アミノ化反応
    有馬陸、松田研一、脇本敏幸
    学術変革領域研究（A)予知生合成科学2024年若手合宿勉強会, 24 Aug. 2024
  • インドールN-アシル化を介したペプチド環化機構
    丸山 広大、山田 惟人、森内 良太、小谷 真也、五十嵐 康弘、松田 研一、脇本敏幸
    学術変革領域研究（A)予知生合成科学2024年若手合宿勉強会, 24 Aug. 2024
  • 天然物生合成酵素の開拓と触媒利用
    松田研一
    第19回薬学研究院研究発表会, 09 Aug. 2024
  • ヒドラジン合成酵素を介するN－N 結合含有天然物生合成経路の開拓
    松田研一
    学術変革領域研究（A)予知生合成第4回公開シンポジウム, 20 Jul. 2024
  • NRPS-PKS ハイブリッド型天然物の生合成におけるα-ケトアミド形成機構に関する研究
    山田惟人, 松田研一, 脇本敏幸
    万有札幌, 13 Jul. 2024
  • A New Family of Non-ribosomal Peptide Cyclases Facilitate Streamlined Chemoenzymatic Synthesis of Cyclic Peptides
    Kenichi Matsuda, Masakazu Kobayashi, Naho Onozawa, Kei Fujita, Toshiyuki Wakimoto
    2024 Biocatalysis Conference GRC, 07 Jul. 2024
  • 非リボソームペプチド環化酵素FlkOの機能解析
    市原 凜太郎、松田 研一、脇本 敏幸
    第48回日本生薬学会北海道支部例会, 06 Jul. 2024
  • Exploration and biocatalytic application of enzymes in specialized metabolism in bacteria
    Kenichi Matsuda
    Gangneung, KIST, 04 Jul. 2024
    [Invited]
  • A New Family of Peptide Cyclases Enabled Streamlined Chemoenzymatic Synthesis of Cyclic Peptides
    Kenichi Matsuda
    KSABC International symposium 2024, 02 Jul. 2024
    [Invited]
  • 天然物生合成酵素を活用した環状中分子の化学－酵素合成
    松田研一、小林雅和、藤田慧、小野澤菜帆、脇本敏幸
    創薬懇話会2024 in 札幌, 20 Jun. 2024
  • Identification of A New Family of Peptide Cyclases Facilitating Streamlined Chemoenzymatic Synthesis of Cyclic Peptides
    Kenichi Matsuda, Toshiyuki Wakimoto
    2024 US-Japan Seminar on the biosynthesis of Natural Products, 22 May 2024
    [Invited]
  • 特異な複素環形成を含むactinopyridazinone生合成経路の解明
    有馬陸、秋山智子、松田研一、脇本敏幸
    第35回万有仙台シンポジウム, 18 May 2024
  • 海綿動物由来α-ケトアミド含有環状ペプチドの生合成研究
    山田惟人, 松田研一, 脇本敏幸
    第35回海洋生物活性談話会, 18 May 2024
  • 天然物生合成におけるN−N結合形成酵素の機能解析
    有馬 陸、中原 悠斗、秋山 智子、Atina Rizkiya Choirunnisa、松田 研一、脇本 敏幸
    第35回万有仙台ミニシンポジウム, 17 May 2024
  • Exploration and biocatalytic application of enzymes in specialized metabolism
    Kenichi Matsuda
    日本薬学会第144年会（横浜） [IS01] 次世代薬学アジアシンポジウム ケミカルバイオロジー1, 30 Mar. 2024
    [Invited]
  • [S19-3] 天然物生合成酵素を活用した環状中分子の化学－酵素合成
    松田研一
    日本薬学会第144年会（横浜） [S19] 中分子創薬研究のフロンティア －中分子創薬に資する次世代分子技術－, 30 Mar. 2024
    [Invited]
  • シアノバクチン生合成におけるグアニジンビスプレニル化酵素の網羅的探索と機能解析
    藤田慧、山田惟人、松田研一、脇本敏幸
    日本薬学会第144年会（横浜）, 30 Mar. 2024
  • ヒドラジン生合成に関わるN-水酸化酵素の系統解析と新規ヒドラジン化合物の同定
    中原 悠斗; Choirunnisa Atina; 有馬 陸; 松田 研一; 脇本 敏幸
    日本薬学会第144年会（横浜）, 30 Mar. 2024
  • インドールN-アシル化によるペプチド環化機構
    丸山 広大; 松田 研一; 小谷 真也; 五十嵐 康弘; 脇本敏幸
    日本薬学会第144年会（横浜）, 30 Mar. 2024
  • 二環性ペプチドの化学-酵素合成
    小野澤菜帆、小林 雅和、松田 研一、脇本 敏幸
    日本薬学会第144年会（横浜）, 30 Mar. 2024
  • [30-411-am04] 非リボソームペプチド環化酵素を用いたラリアット型環状ペプチドの化学－酵素合成
    小林 雅和、松田 研一、脇本 敏幸
    日本薬学会第144年会（横浜）, 30 Mar. 2024
  • 非リボソームペプチオ環化酵素を用いたhead-to-side chain型環状ペプチドの化学－酵素合成
    小林 雅和、松田 研一、脇本 敏幸
    日本農芸化学会2024年度大会, 27 Mar. 2024
  • A New Family of Peptide Cyclases Enabled Streamlined Chemoenzymatic Synthesis of Cyclic Peptides
    Kenichi Matsuda; Toshiyuki Wakimoto
    2023 The 1st Taiwan-Japan Bilateral Symposium on Natural Products Biosynthesis, 25 Dec. 2023
    [Invited]
  • 有用な天然物生合成酵素の探索とその触媒利用
    松田研一
    9th BROGHT Symposium, 26 Oct. 2023
    [Invited]
  • Actinopyridazinone 生合成における複素環形成機構の解明
    有馬陸、秋山智子、松田研一、脇本敏幸
    第24回天然薬物の開発と応用シンポジウム, 15 Oct. 2023
  • 二環性ペプチドの化学-酵素合成
    小野澤菜帆、小林 雅和、松田 研一、脇本 敏幸
    第24回天然薬物の開発と応用シンポジウム, 14 Oct. 2023
  • 抗結核菌活性環状ヘキサペプチド wollamide 生合成における環化酵素 WolJの機能解析
    市原 凜太郎、小林 雅和、藤田 慧、松田 研一、脇本 敏幸
    第24回天然薬物の開発と応用シンポジウム, 14 Oct. 2023
  • NRPS-PKSハイブリッド型天然物の生合成におけるα-ケトアミド形成機構に関する研究
    山田惟人; 福場淳生; 松田研一; 脇本敏幸
    第24回天然薬物の開発と応用シンポジウム, 14 Oct. 2023
  • アルギニン選択的環状ペプチドビスプレニル化酵素の網羅的探索と機能解析
    藤田慧、松田研一、脇本敏幸
    第24回天然薬物の開発と応用シンポジウム, 14 Oct. 2023
  • チロシンイソシアニド化酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本敏幸
    第24回天然薬物の開発と応用シンポジウム, 14 Oct. 2023
  • A New Family of Peptide Cyclases Enabled Streamlined Chemoenzymatic Synthesis of Cyclic Peptide
    Kenichi Matsuda; Masakazu Kobayashi; Kei Fujita; Toshiyuki Wakimoto
    The 23rd Symposium of the Society of Biocatalysis Japan, 29 Sep. 2023
  • 窒素-窒素共有結合を含むヘテロ環の生合成機構の解明とその分光学的測定法の開発
    有馬陸、秋山智子、福士江里、松田研一、脇本敏幸
    第65回天然有機化合物討論会, 14 Sep. 2023
  • 非リボソームペプチド環化酵素を利用した環状ペプチドの効率的合成法の開発
    小林雅和、市原凛太朗、藤田慧、松田研一、脇本敏幸
    第65回天然有機化合物討論会, 14 Sep. 2023
  • NRPS-PKSハイブリッド型天然物の生合成におけるα-ketoamide形成機構に関する研究
    山田惟人; 福場淳生; 松田研一; 脇本敏幸
    日本生薬学会第69年会, 10 Sep. 2023
  • 非リボソームペプチド環化酵素 WolJ を用いた抗結核菌活性環状ペプチドの構造展開
    市原 凜太郎、小林 雅和、藤田 慧、松田 研一、脇本 敏幸
    日本生薬学会第69年会, 10 Sep. 2023
  • 二環性ペプチドの化学-酵素合成
    小野澤菜帆、小林 雅和、松田 研一、脇本 敏幸
    日本生薬学会第69年会, 10 Sep. 2023
  • A New Family of Peptide Cyclases Enabled Streamlined Chemoenzymatic Synthesis of Cyclic Peptides
    Kenichi Matsuda; Masakazu Kobayashi; Kei Fujita; Toshiyuki Wakimoto
    3rd Japan-Switzerland-Germany Workshop on Biocatalysis and Bioprocess Development, 10 Sep. 2023
  • チロシンイソシアニド化酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本敏幸
    第37回放線菌学会大会, 07 Sep. 2023
  • Actinopyridazinone生合成における特異な複素環形成機構の解明
    有馬陸、秋山智子、松田研一、脇本敏幸
    予知生合成科学2023年若手合宿勉強会, 26 Aug. 2023
  • NRPS-PKSハイブリッド型天然物生合成におけるフラビン依存性酸化酵素によるα-ケトアミド形成
    山田惟人; 福場淳生; 松田研一; 脇本敏幸
    予知生合成科学2023年若手合宿勉強会, 26 Aug. 2023
  • ハジマイシン生合成におけるイソシアニド合成酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本敏幸
    予知生合成科学2023年若手合宿勉強会, 26 Aug. 2023
  • アルギニンビスプレニル化酵素の探索と機能解析
    藤田慧、松田研一、脇本敏幸
    第55回若手ペプチド夏の勉強会, 09 Aug. 2023
  • 非リボソームペプチド環化酵素WolJを用いた抗結核菌活性環状ペプチドWollamideの構造展開
    市原 凜太郎、小林 雅和、藤田 慧、松田 研一、脇本 敏幸
    第55回若手ペプチド夏の勉強会, 09 Aug. 2023
  • Actinopyridazinone生合成における特異な複素環形成機構の解明
    有馬陸、秋山智子、松田研一、脇本敏幸
    第35回万有札幌シンポジウム, 01 Jul. 2023
  • Streamlined Chemoenzymatic Synthesis of Cyclic Peptides by Non-ribosomal Peptide Cyclases
    Kenichi Matsuda; Masakazu Kobayashi; Kei Fujita; Toshiyuki Wakimoto
    Biotrans2023, 27 Jun. 2023
  • アルギニンビスプレニル化酵素の探索と機能解析
    藤田慧、松田研一、脇本敏幸
    第15回化学生態学研究会, 16 Jun. 2023
  • イソシアニド生合成酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本敏幸
    第15回化学生態学研究会, 16 Jun. 2023
  • イソシアニド生合成酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本敏幸
    第47回日本生薬学会北海道支部例会, 20 May 2023
  • 二環性ペプチドの化学-酵素合成
    小野澤菜帆、小林 雅和、松田 研一、脇本 敏幸
    第47回日本生薬学会北海道支部例会, 20 May 2023
  • Streamlined chemoenzymatic synthesis of cyclic peptides by non-ribosomal peptide cyclases
    Kenichi Matsuda; Masakazu Kobayashi; Kei Fujita; Toshiyuki Wakimoto
    NextGenBiocat 2023, 18 Apr. 2023
  • Identification of the Gene Cluster Involved in Doubly Homologated Tyrosine Biosynthesis from Microcystis aeruginosa
    Zhengyi Ling; Chin-Soon Phan; Jakia Jerin Mehjabin; Kenichi Matsuda; Prakoso Nurcahyo Iman; Taiki Umezawa; Toshiyuki Wakimoto; Tatsufumi Okino
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • Carrier protein-mediated heterocyclization in actinopyridazinone biosynthesis
    Kuga Arima; Satoko Akiyama; Kenichi Matsuda; Toshiyuki Wakimoto
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • 非リボソームペプチド環化酵素WolJの基質選択性に関する研究
    市原 凜太郎; 小林 雅和; 藤田 慧; 松田 研一; 脇本 敏幸
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • イソシアニド生合成酵素HzmAの機能解析
    丸山 広大; 井町 久美子; 松田 研一; 脇本 敏幸
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • Actinopyridazinone生合成における特異な複素環形成機構の解明
    有馬 陸; 秋山 智子; 松田 研一; 脇本 敏幸
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • NRPS-PKSハイブリッド型天然物の生合成におけるα-ケトアミド形成を担う新規酸化酵素に関する研究
    山田 惟人; 福場 淳生; 松田 研一; 脇本 敏幸
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • 寛容な基質選択性を有するアルギニンビスプレニル化酵素AnzFの同定
    藤田 慧; 松田 研一; 脇本 敏幸
    , 日本薬学会第143年会（札幌）, 26 Mar. 2023
  • 非リボソームペプチド環化酵素を利用した環状ペプチドの効率的な化学-酵素合成法の開発
    小林 雅和; 藤田 慧; 松田 研一; 脇本 敏幸
    日本薬学会第143年会（札幌）, 26 Mar. 2023
  • 伝統水産発酵食品くさやから分離した放線菌Streptomyces diastaticus TUA-NKU25株の塩依存的Surugamide A生産と生合成遺伝子の特徴
    鈴木 敏弘; 竹内 葵; 平田 朝陽; 手島 愛子; 植木 美羽; 松田 研一; 脇本 敏幸; 荒川 賢治; 石川 森夫
    日本農芸化学会2023年度大会, 14 Mar. 2023
  • 寛容な基質選択性を有するアルギニンビスプレニル化酵素AnzFの同定
    藤田 慧; 松田 研一; 脇本 敏幸
    日本農芸化学会2023年度大会, 14 Mar. 2023
  • Actinopyridazinone生合成におけるキャリアタンパク質を介したジヒドロピリダジノン環形成機構の解明
    有馬 陸; 秋山 智子; 松田 研一; 脇本 敏幸
    日本農芸化学会2023年度大会, 14 Mar. 2023
  • STREAMLINED CHEMOENZYMATIC SYNTHESIS OF CYCLIC PEPTIDES BY NON-RIBOSOMAL PEPTIDE CYCLASES
    Masakazu Kobayashi; Kei Fujita; Kenichi Matsuda; Toshiyuki Wakimoto
    International Conference on Natural Product Discovery and Development in the Genomic Era, SIMB, 08 Jan. 2023
  • IDENTIFICATION OF ANZF, ARG-BISPRENYLTRANSFERASE WITH BROAD SUBSTRATE SELECTIVITY
    Kei Fujita; Kenichi Matsuda; Toshiyuki Wakimoto
    International Conference on Natural Product Discovery and Development in the Genomic Era, SIMB 2023, 08 Jan. 2023
  • EXPLORING THE HYDRAZINE BIOSYNTHETIC PATHWAYS IN BACTERIAL SECONDARY METABOLISM
    Kenichi Matsuda; Kuga Arima; Satoko Akiyama; Yo Abe; Yuito Yamada; Toshiyuki Wakimoto
    International Conference on Natural Product Discovery and Development in the Genomic Era, SIMB, 08 Jan. 2023
  • Exploring amine-modifying enzymes in bacterial hydrazine synthetic pathways
    Kenichi Matsuda; Arima Kuga; Satoko Akiyama; Toshiyuki Wakimoto
    Amine Biocat 5.0, 28 Nov. 2022
  • Identification of guanidine bis-prenyltransferase with broad substrate tolerance
    Kei Fujita; Kenichi Matsuda; Toshiyuki Wakimoto
    The 59th Japanese Peptide Symposium, 26 Oct. 2022
  • アルギニンビスプレニル化酵素の探索と機能解析
    藤田慧; 松田研一; 脇本敏幸
    第34回 万有札幌シンポジウム, 08 Oct. 2022
  • Exploring the hydrazine biosynthetic pathways in bacteria
    Kenichi Matsuda; Kuga Arima; Satoko Akiyama; Kazuo Shin-ya; Makoto Nishiyama; Toshiyuki Wakimoto
    JNU-UTokyo Joint Seminar on Natural Product Biosynthesis, 25 Sep. 2022
    [Invited]
  • 細胞外⼩胞が⽣産誘導する放線菌由来新規抗菌性天然物の探索
    本田拓⺒; 吉村彩; 中田隆介; 松田研一; 脇本敏幸
    第 36 回（2022 年度）⽇本放線菌学会⼤会, 14 Sep. 2022
  • ジヒドロピリダジノン環含有天然物 actinopyridazinone A の⽣合成経路の解明
    有馬 陸; 秋山 智子; 松田 研一; 脇本 敏幸
    第 36 回（2022 年度）⽇本放線菌学会⼤会, 14 Sep. 2022
  • 天然物生合成におけるペプチド修飾反応に関する研究
    松田研一
    日本生薬学会第68回年会, 10 Sep. 2022
  • ジヒドロピリダジノン環含有天然物, actinopyridazinone Aの生合成機構の解明
    有馬陸; 秋山智子; 松田研一; 脇本敏幸
    日本生薬学会第68回年会, 10 Sep. 2022
  • 環状ペプチドを基質とするグアニジンビスプレニルトランスフェラーゼの機能解析
    藤田慧; 松田研一; 脇本敏幸
    日本生薬学会第68回年会, 10 Sep. 2022
  • α-ketoamide形成を担う新規酸化酵素の同定及び機能解析
    山田惟人; 福場淳生; 松田研一; 脇本敏幸
    日本生薬学会第68回年会, 10 Sep. 2022
  • 細菌が放出する細胞外小胞による二次代謝産物生産誘導に関する研究
    吉村彩; 佐伯梨緒; 中田隆介; 冨本将汰; 松田研一; 脇本敏幸
    第64回天然有機化合物討論会, 07 Sep. 2022
  • Exploring the hydrazine biosynthetic pathways in bacteria
    Kenichi Matsuda
    Sapporo Summer Seminar on Natural Product Biosynthesis, 16 Aug. 2022
  • PBP型チオエステラーゼSurEによるペプチドライゲーション反応
    市原凜太郎; 小林雅和; 松田研一; 脇本敏幸
    日本生薬学会第46回北海道支部例会, 21 May 2022
  • 窒素―窒素共有結合形成酵素の機能解析
    伊藤楓; 有馬陸; 松田研一; 脇本敏幸
    日本生薬学会第46回北海道支部例会, 21 May 2022
  • 非リボソームペプチド環化酵素SurEの基質選択性の合理的改変
    日本薬学; 名古
    25 Mar. 2022
  • NRPS-PKSハイブリッド型天然物の生合成におけるα-ketoamide形成機構に関する研究
    山田 惟人; 福場 淳生; 松田 研一; 脇本 敏幸
    日本薬学会第142年会（名古屋）, 25 Mar. 2022
  • 環状ペプチドを基質とするグアニジンプレニル化酵素AgcFの機能解析
    藤田 慧; 松田 研一; 脇本 敏幸
    日本薬学会第142年会（名古屋）, 25 Mar. 2022
  • 特異なdihydropyridazinone環を有する新規天然物actinopyridazinone Aに関する研究
    有馬 陸; 秋山 智子; 松田 研一; 脇本 敏幸
    日本薬学会第142年会（名古屋）, 25 Mar. 2022
  • ペプチド環化酵素ファミリーPBP-type TEの発見・機能解析・応用
    松田研一
    日本薬学会第142年会 一般シンポジウム「[S08] タンパク質工学による創薬化学の新展開」, 23 Mar. 2022, Nominated symposium
    [Invited]
  • PBP-type TE, a new family of offloading cyclase in biosynthesis of non-ribosomal macrolactam
    Kenichi Matsuda; Rui Zhai; Takahiro Mori; Masakazu Kobayashi; Ayae Sano; Ikuro Abe; Toshiyuki Wakimoto
    Pacifichem 2021, 16 Dec. 2021
  • Enzymatic basis of guanidine bis-prenylation in argicyclamide biosynthesis
    Kenichi Matsuda; Chin-Soon Phan; Nandani Balloo; Kei Fujita; Okino Tatsufumi; Toshiyuki Wakimoto
    第58回ペプチド討論会, 21 Oct. 2021, Oral presentation
  • 非リボソームペプチド生合成における新規ペプチド環化酵素の発見と機能解析
    松田研一
    第23回天然薬物の開発と応用シンポジウム, 17 Oct. 2021, Invited oral presentation
    [Invited]
  • ゲノム情報と比色法を利用した稀少天然物の開拓
    松田研一
    日本生薬学会第67回年会 若手シンポジウム, 20 Sep. 2021, Nominated symposium
    [Invited]
  • 窒素－窒素結合含有天然物のゲノムマイニング
    松田研一; 有馬陸; 秋山智子; 阿部葉; 城内航; 新家一男; 脇本敏幸
    第63回天然有機化合物討論会, 16 Sep. 2021, Oral presentation
  • Argicyclamide revealed enzymatic basis for guanidine bis-prenylation
    Matsuda, K; Phan, C.-S; Balloo, N; Fujita, K; Okino, T; Wakimoto, T
    第53回若手ペプチド夏の勉強会, 09 Aug. 2021, Poster presentation
  • A marine-derived biocatalyst for cyclic peptide production
    Kenichi Matsuda
    The 4th international symposium on marine and fisheries research, 28 Jul. 2021, Invited oral presentation
    [Invited]
  • 海洋放線菌に見出した新規ペプチド環化酵素ファミリーの機能解析と応用可能性
    松田研一
    第21回マリンバイオテクノロジー学会ミニシンポジウム（若手の会）, 16 May 2021, Nominated symposium
    [Invited]
  • 新規ペプチド環化酵素の発見と機能解析
    松田研一
    第3回「生体適合化学の進歩」インタラクティブフォーラム, 23 Apr. 2021, Invited oral presentation
    [Invited]
  • A new off-loading cyclase in non-ribosomal peptide biosynthesis
    Matsuda, K; Wakimoto, T
    2nd German-Japanese Symposium on Natural Product Biosynthesis, 02 Apr. 2020, Nominated symposium
  • trans-TE NRPS の発見と機能改変
    松田研一
    若手研究者のための有機化学札幌セミナー, 20 Nov. 2019, Invited oral presentation
    [Invited]
  • Penicillin-binding protein-type thioesterases; scope, limitation and its application
    Kenichi Matsuda
    13th Australian Peptide Conference, 09 Sep. 2019, Invited oral presentation
    [Invited]
  • Identification of a new family of offloading cyclase in biosynthesis of non-ribosomal peptide
    Kenichi Matsuda
    7th Modern Solid Phase Peptide Synthesis & Its Application Symposium, 07 Sep. 2019, Invited oral presentation
    [Invited]
  • 非リボソームペプチドの環化反応を触媒するペニシリン結合タンパク質ファミリーの発見と機能解析
    松田研一
    新学術領域生合成リデザイン特別講演会, 13 Jun. 2019, Invited oral presentation
    [Invited]
  • ペニシリン結合タンパク質による非リボソームペプチドの環化反応
    松田研一
    日本薬学会、第139年会, シンポジウムS43 「生体分子骨格リデザインで挑む次世代創薬研究」, 22 Mar. 2019, Nominated symposium
    [Invited]
  • Structural Basis for the Consecutive Guanidine-Nω-prenylation catalyzed by Arginine-N,N'-bisprenyltransferases
    Kei Fujita, Yuito Yamada, Takahiro Mori, Kenichi Matsuda, Ikuro Abe, Toshiyuki Wakimoto
    GRC Marine Natural Products
  • ペプチド環化酵素SurEの生産菌が有する新規ペプチド環化酵素FalKOの機能解析
    市原 凜太郎、松田 研一、脇本 敏幸
    第48回日本生薬学会北海道支部例会
■ Syllabus
  • 天然物化学特論, 2024年, 修士課程, 生命科学院
  • 天然物化学, 2024年, 学士課程, 薬学部
  • 有機化学実習Ⅰ, 2024年, 学士課程, 薬学部
  • 有機化学実習Ⅱ, 2024年, 学士課程, 薬学部
■ Affiliated academic society
  • Oct. 2022 - Present
    日本化学会
  • THE JAPANESE SOCIETY OF PHARMACOGNOSY
  • SOCIETY FOR ACTINOMYCETES JAPAN
  • JAPAN SOCIETY FOR BIOSCIENCE, BIOTECHNOLOGY, AND AGROCHEMISTRY
  • 日本薬学会
■ Research Themes
  • 新規窒素代謝で実現するバイオヒドラジン生産
    2023創発的研究支援事業
    2024 - 2031
    JST, Principal investigator
  • 微生物－酵素触媒複合系によるバイオヒドラジン生産
    科学研究費助成事業
    Apr. 2024 - Mar. 2027
    松田 研一
    日本学術振興会, 基盤研究(B), 北海道大学, Principal investigator, 24K01659
  • 複雑修飾中分子の固相化学酵素合成
    科学研究費助成事業
    Jun. 2023 - Mar. 2027
    松田 研一
    日本学術振興会, 挑戦的研究(開拓), 北海道大学, 23K17410
  • 新規ペプチド修飾酵素の機能拡張による大環状複雑骨格の創出
    Grants-in-Aid for Scientific Research Grant-in-Aid for Transformative Research Areas (A)
    Jun. 2022 - Mar. 2027
    脇本 敏幸; 松田 研一
    Japan Society for the Promotion of Science, Grant-in-Aid for Transformative Research Areas (A), Hokkaido University, Coinvestigator, 22H05128
  • 感染症治療薬の新モダリティー天然物2.0
    AMED-CREST
    2022 - 2027
    浅井禎吾
    日本医療研究開発機構(AMED), Coinvestigator
  • 短鎖環状ペプチドの酵素・生物合成
    戦略的な研究開発の推進 戦略的創造研究推進事業 ACT-X 加速フェーズ
    Apr. 2023 - Mar. 2024
    松田 研一
    短鎖環状ペプチドは優れた代謝安定性・組織移行性を示します。本研究では、短鎖環状ペプチドの合成に特化した新規なペプチド環化酵素ファミリーに着目し、その機能解析に基づく論理的な酵素改良を行い、生体触媒として開発すると共に、本酵素の合成生物学的利用法を提案します。これによりこれまで効率的な合成が困難であった短鎖環状ペプチドを、精度よく安定してかつ大量に合成できる環境調和性の技術の開発を目指します。
    科学技術振興機構, 北海道大学, Principal investigator
  • 複雑修飾ペプチドのフロー生体触媒合成
    2022 年度 Ⅲ研究助成金
    Apr. 2023 - Mar. 2024
    公益財団法人 テルモ生命科学振興財団, Principal investigator
  • 合成終盤における酵素的構造多様化を基盤とする複雑修飾ペプチド創成プラットフォーム
    Grants-in-Aid for Scientific Research Grant-in-Aid for Early-Career Scientists
    Apr. 2022 - Mar. 2024
    松田 研一
    Japan Society for the Promotion of Science, Grant-in-Aid for Early-Career Scientists, Hokkaido University, 22K15302
  • PBP-type TEを基軸とした環状ペプチドの新規供給法の確立
    次世代育成支援研究助成
    Apr. 2020 - Mar. 2023
    松田研一
    公益財団法人 内藤記念科学振興財団, Principal investigator
  • PBP type-TEのペプチド環化触媒能の解明と環状ペプチドの多様性拡張
    Grants-in-Aid for Scientific Research Grant-in-Aid for Early-Career Scientists
    Apr. 2019 - Mar. 2022
    Matsuda Kenichi
    SurE, a novel peptide cyclase involved in the biosynthesis of nonribosomal macrolactams produced by actinomycetes, was analyzed to elucidate its substrate selectivity and its structural basis; biochemical and structural comparison between SurE and two homologous enzymes was performed to clarify the structure that generates differences in substrate selectivity. Based on the findings obtained, we succeeded in logically modifying the substrate selectivity of the enzyme. Furthermore, we investigated the synthesis scheme of the enzyme substrate and established a highly efficient synthetic method. The modified solid phase peptide synthesis combined with sequential enzymatic cyclization realized seamless chemoenzymatic synthesis of cyclic peptides.
    Japan Society for the Promotion of Science, Grant-in-Aid for Early-Career Scientists, Hokkaido University, Principal investigator, 19K16390
  • 短鎖環状ペプチドの酵素・生物合成
    戦略的な研究開発の推進 戦略的創造研究推進事業 ACT-X
    2020 - 2022
    松田 研一
    短鎖環状ペプチドは優れた代謝安定性・組織移行性を示します。本研究では、短鎖環状ペプチドの合成に特化した新規なペプチド環化酵素ファミリーに着目し、その機能解析に基づく論理的な酵素改良を行い、生体触媒として開発すると共に、本酵素の合成生物学的利用法を提案します。これによりこれまで効率的な合成が困難であった短鎖環状ペプチドを、精度よく安定してかつ大量に合成できる環境調和性の技術の開発を目指します。
    北海道大学, Principal investigator, 20345138
  • PBP type-TEによる環状ペプチドの化学・生物生産
    研究奨励金
    Apr. 2020 - Mar. 2021
    松田研一
    上原記念生命科学財団, Principal investigator
  • PBP type-TEを基軸とする環状ペプチドの革新的生産法の確立
    若手研究加速事業
    Sep. 2019 - Mar. 2020
    北海道大学, Principal investigator
  • 新規ペプチド環化酵素ファミリーPBP-type TE における特異性発現メカニズムの解明
    研究助成
    松田研一
    第一三共生命科学研究振興財団, Principal investigator
  • ペプチド環化酵素PBP-type TEの基質選択性発現メカニズムの解明と改変
    2020年度 基礎科学研究助成
    松田研一
    住友財団, Principal investigator
■ Industrial Property Rights
  • 環状ペプチドの効率的な化学－酵素合成方法
    Patent right, 脇本敏幸; 松田研一; 小林雅和, 国立大学法人北海道大学
    特願2022-24966, 21 Feb. 2022
  • 新規プレニル化酵素
    Patent right, 脇本敏幸; 沖野龍文; 松田研一; パンチンスン, 国立大学法人北海道大学
    特願PCT/JP2022/004501, 04 Feb. 2022
  • 酵素を用いたペプチドライゲーション
    Patent right, 脇本敏幸; 松田研一; 小林雅和, 国立大学法人北海道大学
    特願2021-157054, 27 Sep. 2021
  • ペプチド類の大環状化酵素
    Patent right, 脇本敏幸; 倉永健史; 松田研一
    特願2018-89287, 07 May 2018
  • 化合物、その製造方法、抗菌剤及び銅キレート剤医薬
    Patent right, 高田雅親; 砂原博文; 脇本敏幸; 松田研一, 株式会社村田製作所, 国立大学法人北海道大学
    特願2021-109058
  • 銅キレート剤、抗がん剤及びウィルソン病の予防又は治療剤
    Patent right, 高田雅親; 砂原博文; 脇本敏幸; 松田研一, 株式会社村田製作所, 国立大学法人北海道大学
    特願2021-109057