Research Topics

This laboratory works on microbial enzymes with protein engineering and genetic engineering at the molecular level. Collaborations with companies and academic organizations are conducted to disseminate our scientific outcomes oriented to diagnostic utility, environmental contribution, and wide application to foods and cosmetics. Microbes that can survive under extreme environments have unique and useful enzymes in their cells. We are focusing on the exploitation of those highly acid-tolerant and/or highly thermostable enzymes, which are allowed to be produced in E. coli cells through genetic engineering, and for structure elucidation by X-ray crystallography. Microbial enzymes can be used for many applications in the medicinal field. Some enzymes can induce apoptosis highly specifically to cancer cells. Enzymes that can be used for the diagnosis of liver functions with much higher sensitivity than the conventional chemical analysis. We study microbial enzymes related to some human diseases and for application to medicinal purposes. A novel approach to designing and modifying enzyme structures is being developed in this laboratory by exploiting the ability of cutting-edged computer chemistry. Molecular dynamics and quantum chemistry are introduced into real world bench chemistry, and the mathematical profession and speculation are put into practice by protein engineering and experimental evaluation.

Publication List

• Sato, D., Shiba, T., Yunoto, S., Furutani, K., Fukumoto, M., Kudou, D., Tamura, T., Inagaki, K., and Harada, S.: Structural and mechanistic insights into homocysteine degradation by a mutant of methionine γ-lyase based on substrate-assisted catalysis. Protein Science, 26, 1224-1230 (2017)
• Tamura, T., Tsunekawa, N., Nemoto, M., Inagaki, K., Hirano, T., Sato, F.: Molecular evolution of gas cavity in NiFeSe hydrogenases resurrected in silico. Scientific Reports 6, Article number: 19742 (2016)
• Fukuhara, T., Kobayashi, K., Kanayama, Y., Enomoto, S., Kondo, T., Tsunekawa, N., Nemoto, M., Ogasawara, N., Inagaki, K., and Tamura, T.: Identification and characterization of the zosA gene involved in copper uptake in Bacillus subtilis 168. 1)Biosci. Biotechnol. Biochem., 80, 600-609 (2016)
• Amano, M., Mizuguchi, H., Sano, T., Kondo, H., Shinyashiki, K., Inagaki, J., Tamura, T., Kawaguchi, T., Kusakabe, H., Imada, K., Inagaki, K.: Recombinant expression, molecular characterization and crystal structure of antitumor enzyme, L-lysine α-oxidase from Trichoderma viride. J. Biochem., 157, 549-559 (2015)
• Oshima, K., Hattori, M., Shimizu, H., Fukuda, K., Nemoto, M., Inagaki, K., and Tamura, T.: Draft Genome Sequence of Streptomyces incarnatus NRRL8089, which Produces the Nucleoside Antibiotic Sinefungin. Genome Announc., 3(4), e00715-15 (2015)
• Fukumoto, M., Kudou, D., Murano, S., Shiba, T., Sato, D., Tamura, T., Harada, S., Inagaki, K.: The role of amino acid residues in the active site of L-methionine γ-lyase from Pseudomonas putida. Biosci. Biotechnol. Biochem., 76, 1275-1284 (2012)
• Eguchi, Y., Makanae, K., Hasunuma, T., Ishibashi, Y., Kito, K., and Moriya, H.: Estimating the protein burden limit of yeast cells by measuring the expression limits of glycolytic proteins. Elife, 7, e34595 (2018)
• Ishikawa, K., Makanae, K., Iwasaki, S., Ingolia, N.T., and Moriya, H.: Post-Translational Dosage Compensation Buffers Genetic Perturbations to Stoichiometry of Protein Complexes. PLoS Genet., 13, e1006554 (2017)
• Kintaka, R., Makanae, K., and Moriya, H.: Cellular growth defects triggered by an overload of protein localization processes. Sci. Rep., 6, 31774 (2016)
• Moriya, H. Quantitative nature of overexpression experiments. Mol. Biol. Cell, 26(22), 3932-3939 (2015)
• Makanae, K., Kintaka, R., Makino, T., Kitano, H., and Moriya, H.: Identification of dosage-sensitive genes in Saccharomyces cerevisiae using the genetic tug-of-war method. Genome Res., 23(2), 300-311 (2013)

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