Department of Biomolecular Sciences
Division of Biomolecular Chemistry

Functional Biomolecules 分野

Tomohisa Ogawa
キャンパス Katahira キャンパス
専攻分野 Biomolecular sciences
連絡先 022-217-6206

My research interests relate to the structure and function of proteins, which have been produced by nature through the evolutionary process of life to create new diversified functions with just the 20 amino acids found in nature. To understand the mysteries of proteins including their unique functions and properties, we focus on protein molecular evolution.

1986 Department of Chemistry, Faculty of Sciences, Kyushu University
1991 Research Fellowship for Young Scientists, JSPS Completed doctoral program and achieved Doctor of Science, Department of Chemistry, Graduate School of Sciences, Kyushu University Assistant professor, Faculty of Sciences, Kyushu University
1997 Associate Professor, Faculty of Agriculture, Tohoku University
2001 Associate Professor, Graduate School of Life Sciences, Tohoku University (present)
2002 Guest Associate Professor, Institute for Protein Research, Osaka University
2004 Project Leader, Center for Interdisciplinary International Advanced Research Program, Tohoku University
  1. Naganuma et al. (2014) Novel Matrix Proteins of Pteria penguin Pearl OysterShell Nacre Homologous to the Jacalin-Related β-PrismFold Lectins. PloS ONE 9(11): e112326. doi:10.1371/journal.pone.0112326.
  2. Ogawa & Shirai, (2013) Experimental Molecular Archeology: Reconstruction of Ancestral Mutants and Evolutionary History of Proteins as a New Approach in Protein Engineering. In: Protein Engineering - Technology and Application (Edited by Tomohisa Ogawa) ISBN 978-953-51-1138-2.
  3. Watanabe et al. (2012) Allosteric Regulation of the Carbohydrate-binding Ability of a Novel Conger Eel Galectin by D-Mannoside. J. Biol. Chem., 287 (37), 31061-31072.
  4. Konno et al. (2011) Tracing protein evolution through ancestral structures of fish galectin. Structure 19 (5): 711-721. (Selected by Faculty1000)
  5. Ogawa et al. (2011) Diversified carbohydrate-binding lectins from marine resources. J. Amino Acids, Article ID 838914 doi:10.4061/2011/838914
  6. Konno et al. (2010) Protein engineering of conger eel galectins by tracing of molecular evolution using probable ancestral mutants. BMC Evolutionary Biology, 10:43doi:10.1186/1471-2148-10-43.
  7. Shirai et al. (2009) Structure of Rhamnose-binding Lectin CSL3: Unique Pseudo-tetrameric Architecture of a Pattern Recognition Protein. J. Mol. Biol., 391 (2), 390-403. (Recommended by PubAdvanced)
  8. Ogawa (2009) Venomics: Venomous animal genome project. BIOClinica, 24 (6), 65-71. (Japanese)
  9. Seto et al. (2008) A novel recombinant system for functional expression of myonecrotic snake phospholipase A2 in Escherichia coli using a new fusion affinity tag. Protein Exp. Purif., 58 (2), 194-202.
  10. Konno et al. (2007) Reconstruction of a Probable Ancestral Form of Conger Eel Galectins Revealed Their Rapid Adaptive Evolution Process for Specific Carbohydrate Recognition. Mol. Biol. Evol., 24 (11), 2504-2514.
  11. Yamazaki, Yagi, & Oda. Ed. by Hatakeyama & Ogawa (2007) Seibutsu kagaku jikkenho 52 lectin kenkyuho.
  12. Ogawa (2006) Molecular diversity of proteins in biological offense and defense systems. Mol. Divers., 10 (4), 511-514.
  13. Ogawa et al. (2006) Kasoku shinka ni yoru tanpakushitsu no tainetsuka: shinka kogaku ni yoru tainetsuka kiko no kaimei kara. Seibutsu butsuri 46, 201-208.
  14. Ogawa et al. (2005) Molecular diversity and accelerated evolution of C-type lectin-like proteins from snake venom. Toxicon, 45, 1-14.
  15. Ogawa et al. (2004) The speciation of conger eel galectins by rapid adaptive evolution. Glycoconj. J., 19, 451-458.
  16. Nakashima et al. (1993) Accelerated Evolution of Trimeresurus flavoviridis Venom Gland Phospholipase-A2 Isozymes. Proc. Natl. Acad. Sci. USA, 90, 5964-5968.
  17. Ogawa et al. (1992) Unusually High Conservation of Untranslated Sequences in cDNAs for Trimeresurus flavoviridis Phospholipase-A2 Isozymes. Proc. Natl. Acad. Sci. USA, 89, 8557-8561.
所属学会 Japan Society for Bioscience, Biotechnology, and Agrochemistry; the Japanese Biochemical Society; the Chemical Society of Japan; the Japanese Society of Carbohydrate Research; International Society on Toxinology; the American Society for Biochemistry and Molecular Biology (ASBMB)
担当講義 Food protein chemistry (Faculty of Agriculture), student experiments (protein chemistry (Course of Biological Chemistry, Faculty of Agriculture); Seimei soshi kinogaku (Functional biomolecules) tokuron (graduate school)


The secrets of a pearl’s luster Pearl luster is one of major quality factors that determine the true beauty of pearl that charms many people. To understand the biomineralization mechanisms of the pearl shell, we focus on the matrix proteins, which regulate the lamellar nano-architechture structure composed of aragonite crystals, and especially on the molecular mechanism regulating the orientation distribution of aragonite crystals.

Experimental Molecular Archeology: Reconstruction of Ancestral Mutants and the Evolutionary History of Proteins To analyze the structure-function relationship of proteins and to design new functional proteins, we have developed a protein engineering system using reconstruction of ancestral mutants based on a phylogenetic tree.

A venomics project of the Protobothrops flavoviridis (Habu) snake Venomous animals produce multiple toxins, which specifically affect the biological systems of prey. We focus on the diverse functions of toxin genes, which demonstrate a unique evolutionary phenomenon: accelerated evolution. To elucidate the unique structural information of toxin-related genes and the mechanism of accelerated evolution, we are conducting whole genome analysis of the venomous snake, Protobothrops flavoviridis. Understanding the molecular mechanisms of accelerated evolution will provide us with a new concept of molecular evolution.


I believe that the skillful fusion of diverse ways of thinking, viewpoints, and research methods leads to unique new research programs. We study proteins from a variety of angles and enjoy the research; from protein structure, function, and evolution, to the application of this information to new materials and functional materials. I would like to encourage you to enjoy these research activities with us.