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研究室メンバー紹介MEMBERS


   准教授 山本 惠三

大阪大学 博士(工学)

略歴


1989 大阪大学大学院工学研究科醗酵工学専攻博士前期課程修了
1993 大阪大学大学院工学研究科醗酵工学専攻博士後期課程単位取得退学
2001 博士(工学)(大阪大学第16439号)

1993-    奈良県立医科大学助手
1994-1997 大阪大学蛋白質研究所共同研究員
1998-2001 大阪大学蛋白質研究所共同研究員
2001-    奈良県立医科大学講師
2012-    奈良県立医科大学准教授  現在に至る


専門分野


蛋白質工学
構造生物学

所属学会


日本生物工学会
日本結晶学会
日本農芸化学会
日本応用糖質科学会
高分子学会
日本応用糖質科学会近畿支部評議員(2002-)

研究テーマ


蛋白質の結晶構造解析

業績


[総説]
3. 松平崇, 山本惠三, 酒井宏水, 超分子重合を利用した人工酸素運搬体の構築, 人工血液, 29(1), 50-56 (2021).

2. 山田孫平, 松平崇, 山本惠三, 酒井宏水, NADH とヘモグロビンの共存による抗酸化的な擬似酵素活性と人工赤血球への応用, 人工血液, 28(1), 49-56 (2020).

1. 山本惠三, 花粉アレルゲンの遺伝子解析, 生物工学, 80, 148-152, (2002).


[論文(英文)]
31. K. Yamamoto, H. Tanaka, G. Kurisu, R. Nakano, H. Yano, H. Sakai, Structural insights into the substrate specificity of IMP-6 and IMP-1 metallo-β-lactamases. J. Biochem. 173(1), 21-30 (2022).

30. M. Yamada, T. Matsuhira, K. Yamamoto, H. Sakai, Antioxidative pseudo-enzymatic mechanism of NAD(P)H coexisting with oxyhemoglobin for suppressed methemoglobin formation. Biochemistry, 58(10), 1400-1410 (2019).

29. T. Matsuhira, K. Ymamoto, H. Sakai, Ring-opening polymerization of hemoglobin, Biomacromolecules 20(4), 1592-1602 (2019).

28. T. Matsuhira, T. Kure, K. Ymamoto, H. Sakai, Analysis of dimeric αβ subunit exchange between PEGylated and native hemoglobins (α2β2 tetramer) in an equilibrated state by intramolecular ββ-crosslinking, Biomacromolecules, 19(8), 3412-3420 (2018).

27. S. Osaki, K. Yamamoto, T. Matsuhira, H. Sakai, The effects of seasonal changes on the molecular weight of Nephila clavata spider silk, Polymer Journal, 48, 659-663 (2016).

26. T. Matsuhira, K. Yamamoto, S. Osaki, Effects of UV irradiation on the molecular weight of spider silk, Polymer Journal, 45, 1167-1169 (2013).

25. K. Yamamoto, H. Miyake, M. Kusunoki, S. Osaki, Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae, J. Biosci. Bioeng., 112, 545-550 (2011).

24. K. Yamamoto, H. Miyake, M. Kusunoki, S. Osaki, Crystal structure of isomaltase from Saccharomyces cerevisiae and in complex with its competitive inhibitor maltose, FEBS J.,277, 4205-4214 (2010).

23. K. Yamamoto, H. Miyake, M. Kusunoki, S. Osaki, Crystallization and preliminary X-ray analysis of isomaltase from Saccharomyces cerevisiae, Acta Crystallogr. Sect. F, 64, 1024-1026 (2008).

22. Y. Goto, T. Kondo, T. Ide, H. Yasueda, N. Kuramoto, K. Yamamoto, Cry j 1 isoforms derived from Cryptomeria japonica trees have different binding properties to monoclonal antibodies, Clin. Exp. Allergy, 34, 1754-1761 (2004).

21. K. Yamamoto, A. Nakayama, Y. Yamamoto, S. Tabata, Val216 decides the substrate specificity of α-glucosidase in Saccharomyces cerevisiae, Eur. J. Biochem., 271, 3414-3420 (2004).

20. S. Osaki, K. Yamamoto, A. Kajiwara, M. Murata, Evaluation of the resistance of spider silk to ultraviolet irradiation, Polymer J., 36, 623-627 (2004).

19. Y. Goto, T. Kondo, N. Kuramoto, T. Ide, K. Yamamoto, K. Inaoka, H. Yasueda, Mapping the gene encoding Cry j 1: a major Cryptomeria japonica pollen allergen, Silvae Genetica, 52, 97-99 (2003).

18. A. Nakayama, K. Yamamoto, S. Tabata, The amino acid residues involved in catalysis of the yeast glycogen debranching enzyme, J. Appl. Glycosci., 50, 299 (2003).

17. T. Nakaishi, K. Iio, K. Yamamoto, I. Urabe, T. Yomo, Kinetic properties of Qβ replicase, an RNA dependent RNA polymerase, J. Biosci. Bioeng., 93, 322-327 (2002).

16. A. Nakayama, K. Yamamoto, S. Tabata, The role of Asp-224 in conserved region I of yeast glycogen debranching enzyme, Appl. Biol. Sci, 7, 37-47 (2001).

15. A. Nakayama, K. Yamamoto, S. Tabata, Identification of the catalytic residues of bifunctional glycogen debranching enzyme, Journal of Biological Chemistry, 276, 28824-28828 (2001).

14. K. Yamamoto, G. Kurisu, M. Kusunoki, S. Tabata, I. Urabe, S. Osaki, Crystal structure of glucose dehydrogenase from Bacillus megaterium IWG3 at 1.7 Å resolution, Journal of Biochemistry, 129, 303-312 (2001).

13. K. Yamamoto, M. Kusunoki, I. Urabe, S. Tabata, S. Osaki, Crystallization and preliminary X-ray analysis of glucose dehydrogenase from Bacillus megaterium IWG3, Acta Crystallographica, D56, 1443-1445 (2000).

12. A. Nakayama, K. Yamamoto, S. Tabata, High expression of glycogen-debranching enzyme in Escherichia coli and its competent purification method, Protein Expression and Purification, 19, 298-303 (2000).

11. T. Nakaishi, M. Ishizuka, K. Iio, T. Yomo, Y. Inokuchi, M. Kajitani, K. Yamamoto, Y. Shima, I. Urabe, Purification and characterization of Qβ replicase with a His-tag, Journal of Molecular Catalysis, B10, 351-356 (2000).

10. M. Kameoka, Y. Tanaka, K. Ota, A. Itaya, K. Yamamoto, K. Yoshihara, HIV-1 Tat protein is poly(ADP-ribosyl)ated in vitro, Biochemical and Biophysical Research Communications, 261, 90-94 (1999).

9. T. Matsuura, K. Miyai, S. Trakulnaleamsai, T. Yomo, Y. Shima, S. Mini, K. Yamamoto, I. Urabe, Evolutionary molecular engineering by random elongation mutagenesis, Nature Biotechnology, 17, 58-61 (1999).

8. T. Matsuura, T. Yomo, S. Trakulnaleamsai, Y. Ohashi, K. Yamamoto, I. Urabe, Nonadditivity of mutational effects on the properties of catalase I and its application to efficient directed evolution, Protein Engineering, 11, 789-795 (1998).

7. A. Yamauchi, T. Yomo, F. Tanaka, I. D. Prijambada, S. Ohashi, K. Yamamoto, Y. Shima, K. Ogasahara, K. Yutani, M. Kataoka, I. Urabe, Characterization of soluble artificial proteins with random sequences, FEBS Letters, 421, 147-151 (1998).

6. T. Yomo, T. Hatanaka, H. Yamamoto, K. Yamamoto, Y. Shima, E. K Mitamura, I. Urabe, Kinetic equation for template-dependent polymerase reactions and its application toThermus thermophilus DNA polymerase, Journal of Fermentation and Bioengineering, 86, 379-384 (1998).

5. T. Yomo, T. Yamano, K. Yamamoto, I. Urabe, General equation of steady-state enzyme kinetics using net rate constants and its application to the kinetic analysis of catalase reaction, Journal of Theoretical Biology, 188, 301-312 (1997).

4. C. Kobayashi, Y. Suga, K. Yamamoto, T. Yomo, K. Ogasahara, K. Yutani, I. Urabe, Thermal conversion from low- to high-activity forms of catalase I from Bacillus stearothermophilus, Journal of Biological Chemistry, 272, 23011-23016 (1997).

3. I. D. Prijambada, T. Yomo, F. Tanaka, T. Kawama, K. Yamamoto, A. Hasegawa, Y. Shima, S. Negoro, I. Urabe, Solubility of artificial proteins with random sequences, FEBS Letters, 382, 21-25 (1996).

2. W. Z. Xu, J. Fukuhara, K. Yamamoto, T. Yomo, I. Urabe, Random mutagenesis of glutamine synthetase from Escherichia coli: Correlation between structure, activity, and fitness, Journal of Fermentation and Bioengineering, 77, 252-258 (1994).

1. N. Nagao, Y. Makino, K. Yamamoto, I. Urabe, H. Okada, Stability-increasing mutants of glucose dehydrogenase, FEBS Letters, 253, 113-116 (1989).


[論文(和文)]
2. 中山章文, 山本惠三, 稲岡心, 田端司郎, 酵母Glycogen debranching enzyme の2つの酵素作用とその触媒残基について, J. Appl. Glycosci., 49, 181-190 (2002).

1.井手武, 山本惠三, 田端司郎, 芦田恒男, ヒノキ花粉メジャーアレルゲン(Cha o 1)のN末端アミノ酸シークェンス, 日本花粉学会誌, 41, 69-72 (1995).


[その他]
11. 川井正雄, 山本惠三, 井本稔博士 卒寿の問い, 化学と工業, 75(3), 220-221, (2022).

10. Takashi Matsuhira, Keizo Yamamoto, Hiromi Sakai, Ring-opening polymerization of hemoglobin based on supramolecular chemistry. In: Nanobiotherapeutic Based Blood Substitutes (Regenerative Medicine, Artificial Cells and Nanomedicine), T.M.S. Chang, L. Bülow, J.S. Jahr, H. Sakai, C. Yang eds., World Scientific Publishing Co. Pte. Ltd., Singapore. Chapter 3.10, pp 433-445 (2021).

9. Takashi Matsuhira, Keizo Yamamoto, Hiromi Sakai, Analysis of dimeric αβ subunit exchange between bis-PEGylated and native hemoglobins. In: Nanobiotherapeutic Based Blood Substitutes (Regenerative Medicine, Artificial Cells and Nanomedicine), T.M.S. Chang, L. Bülow, J.S. Jahr, H. Sakai, C. Yang eds., World Scientific Publishing Co. Pte. Ltd., Singapore. Chapter 3.9, pp 417-431 (2021).

8. K. Yamamoto, H. Miyake, G. Kurisu, M. Kusunoki, Structural studies on subunit interaction of glucose dehydrogenase, Photon Factory Activity Report, 18B, 220 (2001).

7. T. Oyama, K. Yamamoto, Y. Nitta, M. Kusunoki, Crystal structure of Bacillus cereus b-amylase in complex with maltose, Glc-Glc-Xyl, and a-cyclodextrin, Photon Factory Activity Report, 16B, 256 (1998).

6. T. Yomo, I. D. Prijambada, K. Yamamoto, Y. Shima, S. Negoro, I. Urabe, Properties of artificial proteins with random sequences, Annals of New York Academy of Science, 864, 131-135 (1998).

5. T. Oyama, Y. Nitta, K. Yamamoto, M. Kusunoki, Crystal structure analysis of bacterial b-amylase at 3.0 Å, Photon Factory Activity Report, 14, 96 (1996).

4. T. Oyama, T. Kurino, Y. Nitta, K. Yamamoto, M. Kusunoki, X-ray crystallographic study of bacterial b-amylase, Photon Factory Activity Report, 13, 77 (1995).

3. K. Yamamoto, Y. Nitta, M. Kusunoki, X-ray crystal analysis of glucose dehydrogenase,Photon Factory Activity Report, 12, 87 (1994).

2. K. Yamamoto, Y. Nitta, M. Kusunoki, X-ray crystal analysis of glucose dehydrogenase,Photon Factory Activity Report, 11, 80 (1993).

1. K. Yamamoto, N. Nagao, Y. Makino, I. Urabe, H. Okada, Characterization of mutant glucose dehydrogenase with increasing stability, Annals of New York Academy of Science, 613, 362-365 (1990).


[特許]
2. Itaru Urabe, Tetsuya Yomo, Keizo Yamamoto, Hideaki Sonohara, Ryosei Kamaguchi, Yumi Hatano, Seamless capsule for synthesizing biopolymer and method for producing the same. United States Patent, Patent No. 6,251,661, Date of Patent: June 26, 2001.

1.卜部格, 四方哲也, 山本惠三, 生体高分子を合成するシームレスカプセル, (特許公開: H10-313861), 平成10年(1998)12月2日.

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