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Coauthors
Yuta Mutaguchi Department of Biotechnology, Akita Prefectural University, Japan
2 protocols

Toshihisa Ohshima
  • Department of Biomedical Engineering, Osaka Institute of Technology, Japan
Contributions
  • 2 Author merit

Education

Ph.D. in Agricultural Chemistry, Kyoto University, Japan, 1975

Current position

Professor of Department of Biomedical Engineering, Osaka Institute of Technology, Osaka, Japan (04/2013- to date)

Publications

  1. Kawakami, R., Sakuraba, H. and Ohshima, T. (2014). Identification of catalytic residues of a very large NAD-glutamate dehydrogenase from Janthinobacterium lividum by site-directed mutagenesis. Biosci Biotechnol Biochem: 1-6.
  2. Akita, H., Imaizumi, Y., Suzuki, H., Doi, K. and Ohshima, T. (2014). Spectrophotometric assay of D-isoleucine using an artificially created D-amino acid dehydrogenase. Biotechnol Lett.
  3. Ogura, R., Wakamatsu, T., Mutaguchi, Y., Doi, K. and Ohshima, T. (2014). Biochemical characterization of an l-tryptophan dehydrogenase from the photoautotrophic cyanobacterium Nostoc punctiforme. Enzyme Microb Technol 60: 40-46.
  4. Akita, H., Suzuki, H., Doi, K. and Ohshima, T. (2014). Efficient synthesis of D-branched-chain amino acids and their labeled compounds with stable isotopes using D-amino acid dehydrogenase. Appl Microbiol Biotechnol 98(3): 1135-1143.
  5. Kanoh, Y., Uehara, S., Iwata, H., Yoneda, K., Ohshima, T. and Sakuraba, H. (2014). Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium. Acta Crystallogr D Biol Crystallogr 70(Pt 5): 1271-1280.
  6. H. Sakurab, T. Ohshima (2013) Thermostability mechanisms and application of extremozymes from hyperthermophiles, Bioindustry Vol. 8, pp. 3-11. (in Japanese, Review)
  7. H. Sakuraba、T. Ohshima (2013) Thermophiles in Environmental and Industrial Biotechnology, Thermophiles in Industrial Biotechnology, Chapter 34: Thermophiles in Industrial Biotechnology, Chapter 34: Heterogeneous Production of Thermostable Proteins and Enzymes, Springer, pp. 395-412, 2013
  8. Mutaguchi, Y., Ohmori, T., Akano, H., Doi, K. and Ohshima, T. (2013). Distribution of D-amino acids in vinegars and involvement of lactic acid bacteria in the production of D-amino acids. Springerplus 2: 691.
  9. Mutaguchi, Y., Ohmori, T., Wakamatsu, T., Doi, K. and Ohshima, T. (2013). Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species. J Bacteriol 195(22): 5207-5215.
  10. Wakamatsu, T., Higashi, C., Ohmori, T., Doi, K. and Ohshima, T. (2013). Biochemical characterization of two glutamate dehydrogenases with different cofactor specificities from a hyperthermophilic archaeon Pyrobaculum calidifontis. Extremophiles 17(3): 379-389.
  11. Doi, K., Mori, K., Tashiro, K., Fujino, Y., Nagayoshi, Y., Hayashi, Y., Kuhara, S. and Ohshima, T. (2013). Draft Genome Sequence of Pediococcus lolii NGRI 0510Q(T) Isolated from Ryegrass Silage. Genome Announc 1(1).
  12. Suzuki, H., Yoshida, K. and Ohshima, T. (2013). Polysaccharide-degrading thermophiles generated by heterologous gene expression in Geobacillus kaustophilus HTA426. Appl Environ Microbiol 79(17): 5151-5158.
  13. Doi, K., Mori, K., Mutaguchi, Y., Tashiro, K., Fujino, Y., Ohmori, T., Kuhara, S. and Ohshima, T. (2013). Draft genome sequence of D-branched-chain amino acid producer Lactobacillus otakiensis JCM 15040T, isolated from a traditional Japanese pickle. Genome announcements 1(4): e00546-00513.
  14. Suzuki, H., Wada, K., Furukawa, M., Doi, K. and Ohshima, T. (2013). A ternary conjugation system for the construction of DNA libraries for Geobacillus kaustophilus HTA426. Biosci Biotechnol Biochem 77(11): 2316-2318.
  15. Doi, K., Phuong, O. T. A., Kawatou, F., Nagayoshi, Y., Fujino, Y. and Ohshima, T. (2013). Identification and Characterization of Lactic Acid Bacteria Isolated from Fermented Rice Bran Product. Advances in Microbiology 3: 265.
  16. Kobayashi, J., Shimizu, Y., Mutaguchi, Y., Doi, K. and Ohshima, T. (2013). Characterization of d-amino acid aminotransferase from< i> Lactobacillus salivarius. Journal of Molecular Catalysis B: Enzymatic 94: 15-22.
  17. Erwan, E., Tomonaga, S., Ohmori, T., Mutaguchi, Y., Ohshima, T., Nagasawa, M., Yasuo, S., Tamura, Y. and Furuse, M. (2013). Oral Administration of D-aspartate, but not of L-aspartate, Reduces Food Intake in Chicks. The Journal of Poultry Science 50(2): 164-171.
  18. Yoneda, K., Sakuraba, H., Araki, T., Shibata, T., Nikki, T. and Ohshima, T. (2013). Crystallization and preliminary X-ray analysis of L-serine 3-dehydrogenase complexed with NADP+ from the hyperthermophilic archaeon Pyrobaculum calidifontis. Acta Crystallogr Sect F Struct Biol Cryst Commun 69(Pt 2): 134-136.
  19. Kawakami, R., Noguchi, C., Higashi, M., Sakuraba, H. and Ohshima, T. (2013). Comparative analysis of the catalytic components in the archaeal dye-linked L-proline dehydrogenase complexes. Appl Microbiol Biotechnol 97(8): 3419-3427.
  20. Esaki, K., Ohmori, T., Maebuchi, M., Nakamori, T., Ohshima, T. and Furuya, S. (2013). Increased tyrosine in the brain and serum of mice by orally administering dipeptide SY. Biosci Biotechnol Biochem 77(4): 847-849.
  21. Zhao, Y., Wakamatsu, T., Doi, K., Sakuraba, H. and Ohshima, T. (2012). A psychrophilic leucine dehydrogenase from< i> Sporosarcina psychrophila: Purification, characterization, gene sequencing and crystal structure analysis. Journal of Molecular Catalysis B: Enzymatic 83: 65-72.
  22. Ohshima, T. (2012). Structural characteristics of active and inactive glutamate dehydrogenases from the hyperthermophile Pyrobaculum islandicum. Biosci Biotechnol Biochem 76(9): 1601-1610.
  23. Akita, H., Doi, K., Kawarabayasi, Y. and Ohshima, T. (2012). Creation of a thermostable NADP(+)-dependent D-amino acid dehydrogenase from Ureibacillus thermosphaericus strain A1 meso-diaminopimelate dehydrogenase by site-directed mutagenesis. Biotechnol Lett 34(9): 1693-1699.
  24. Doi, K., Ohyama, Y., Yokoyama, E., Nishiyama, T., Fujino, Y., Nagayoshi, Y., Ohshima, T. and Ogata, S. (2012). Expression analysis of the spi gene in the pock-forming plasmid pSA1.1 from Streptomyces azureus and localization of its product during differentiation. Appl Microbiol Biotechnol 95(3): 707-716.
  25. Ohmori, T., Mutaguchi, Y., Doi, K. and Ohshima, T. (2012). Effects of alkali or acid treatment on the isomerization of amino acids. J Biosci Bioeng 114(4): 457-459.
  26. Sakuraba, H., Satomura, T., Kawakami, R., Kim, K., Hara, Y., Yoneda, K. and Ohshima, T. (2012). Crystal structure of novel dye-linked L-proline dehydrogenase from hyperthermophilic archaeon Aeropyrum pernix. J Biol Chem 287(24): 20070-20080.
  27. Satomura, T., Hara, Y., Suye, S., Sakuraba, H. and Ohshima, T. (2012). Gene expression and characterization of a third type of dye-linked L-proline dehydrogenase from the aerobic hyperthermophilic archaeon, Aeropyrum pernix. Biosci Biotechnol Biochem 76(3): 589-593.
  28. Satomura, T., Hiraki, A., Kawai, T., Kawakami, R., Ohshima, T. and Sakuraba, H. (2012). Expression, purification, crystallization and preliminary X-ray diffraction analysis of a galactose 1-phosphate uridylyltransferase from the hyperthermophilic archaeon Pyrobaculum aerophilum. Acta Crystallogr Sect F Struct Biol Cryst Commun 68(Pt 3): 330-332.
  29. Yoneda, K., Sakuraba, H., Araki, T. and Ohshima, T. (2012). Crystal structure of binary and ternary complexes of archaeal UDP-galactose 4-epimerase-like L-threonine dehydrogenase from Thermoplasma volcanium. J Biol Chem 287(16): 12966-12974.
2 Protocols published
Purification of a Protein Exhibiting Isoleucine 2-epimerase Activity from Lactobacillus otakiensis JCM 15040
Authors:  Yuta Mutaguchi and Toshihisa Ohshima, date: 10/20/2015, view: 2284, Q&A: 0
Prominent accumulation of D-leucine, D-allo-isoleucine and D-valine was observed in the culture medium of the heterofermentative bacterial species, Lactobacillus otakiensis (L. otakiensis) JCM 15040. The racemase enzyme ...
Analysis of L- and D-Amino Acids Using UPLC
Authors:  Yuta Mutaguchi and Toshihisa Ohshima, date: 09/05/2014, view: 4679, Q&A: 0
With the exception of glycine, α-amino acids are optically active, and two optical isomers (L- and D-) of each amino acid can be formed. Recent developments of analytical techniques have revealed that several free D-amino acids such as D-aspartate, ...