京都工芸繊維大学

著書および学術論文目録

原著論文

  1. H. Suzuki, Y. Nakafuji, and T. Tamura. New Method To Produce Kokumi Seasoning from Protein Hydrolysates Using Bacterial Enzymes. Journal of Agricultural and Food Chemistry, 65, 10514-10519 (2017).
  2. Y. Sugiyama, A. Nakamura, M. Matsumoto, A. Kanbe, H. Suzuki, M. Sakanaka, K. Higashi, K. Igarashi, T. Katayama, and S. Kurihara. A novel putrescine exporter SapBCDF of Escherichia coli. Journal of Biological Chemistry, 291(51), 26343-26351 (2016).
  3. A. Kamiyama, M. Nakajima, L. Hana, K. Wada, M. Mizutania, Y. Tabuchia, A. K.-Yuasa, I. M.-Yuasa, H. Suzuki, K. Fukuyama, B. Watanabe, and J. Hiratake. Phosphonate-based irreversible inhibitors 1 of human γ-glutamyl transpeptidase (GGT). GGsTop is a non-toxic and highly selective inhibitor with critical electrostatic interaction with an active-site residue Lys562 for enhanced inhibitory activity. Bioorganic and Medicinal Chemistry, 24(21), 5340-5352 (2016).
  4. A. Sakamoto, Y. Terui, T. Yoshida, T. Yamamoto, H. Suzuki, K. Yamamoto, A. Ishihama, K. Igarashi, and K. Kashiwagi. Three members of polyamine modulon under oxidative stress conditions: Two transcription factors (SoxR and EmrR) and a glutathione synthetic enzyme (GshA). PLoS ONE 10(4): e0124883 (2015). doi:10.1371/ journal.pone.0124883.
  5. R. Kibe, S. Kurihara, Y. Sakai, H. Suzuki, T. Ooga, E. Sawaki, K. Muramatsu, A. Nakamura, A. Yamashita, Y. Kitada, M. Kakeyama, Y. Benno, and M. Matsumoto. Upregulation of colonic luminal polyamines produced by intestinal microbiota delays senescence in mice. Scientific Reports, 4, article number 4548, (2014). Doi:10.1038/srep04548.
  6. M. Nakajima, B. Watanabe, L. Han, B. Shimizu, K. Wada, K. Fukuyama, H. Suzuki, and J. Hiratake. Glutathione-analogous peptidyl phosphorus esters as mechanism-based inhibitors of γ-glutamyl transpeptidase for probing cysteinyl-glycine binding site. Bioorganic and Medicinal Chemistry, 22(3), 1176-1194 (2014).
  7. T. Ida, H. Suzuki, K. Fukuyama, J. Hiratake and K. Wada. Structure of Bacillus subtilis γ-glutamyltranspeptidase in complex with acivicin: diversity of the binding mode of a classical and electrophilic active-site directed glutamate analogue. Acta Crystallographica Section D, D70, 607-614 (2014).
  8. Y. Terui, S. D. Saroj, A. Sakamoto, T. Yoshida, K. Higashi, S. Kurihara, H. Suzuki, T. Toida, K. Kashiwagi, K. Igarashi. Properties of putrescine uptake by PotFGHI and PuuP and their physiological significance in Escherichia coli. Amino Acids, 46(3), 661-670 (2014). DOI 10.1007/s00726-013-1517-x
  9. S. Kurihara, Y. Sakai, H. Suzuki, A. Muth, O. Phanstiel, and P. N. Rather. Putrescine importer PlaP contributes to swarming motility and urothelial cell invasion in Proteus mirabilis. Journal of Biological Chemistry, 288(22), 15668-15676 (2013).
  10. T. V. Ho, K. Kamei, K. Wada, K. Fukuyama, and H. Suzuki. Thermal denaturation and renaturation of γ-glutamyltranspeptidase of Escherichia coli. Bioscience, Biotechnology, and Biochemistry, 77(2), 409-412 (2013).
  11. T. V. Ho, and H. Suzuki. Increase of “umami” and “kokumi” compounds in miso, fermented soybeans, by the addition of bacterial γ-glutamyltranspeptidase. International Journal of Food Studies, 2(1), 39-47 (2013).
  12. N. Nemoto, S. Kurihara, Y. Kitahara, K. Asada, K. Kato, and H. Suzuki. Mechanism for regulation of the putrescine utilization pathway by the transcription factor PuuR in Escherichia coli K-12. Journal of Bacteriology, 194(13), 3437-3447 (2012).
  13. K. Kitadokoro, U. Thumarat, R. Nakamura, K. Nishimura, H. Karatani, H. Suzuki, and F. Kawai. Crystal structure of cutinase Est119 from Thermobifida alba AHK119 that can degrade modified polyethylene terephthalate at 1.76 Å resolution. Polymer Degradation and Stability, 97(5), 771-775 (2012).
  14. U. Thumarat, R. Nakamura, T. Kawabata, H. Suzuki and F. Kawai. Biochemical and genetic analysis of a cutinase-type polyesterase from a thermophilic Thermobifida alba AHK119. Applied Microbiology and Biotechnology, 95(2), 419-430 (2012).
  15. M. Kiyohara, T. Nakatomi, S. Kurihara, S. Fushinobu, H. Suzuki, T. Tanaka, S. Shoda, M. Kitaoka, T. Katayama, K. Yamamoto, and H. Ashida. An α-N-acetylgalactosaminidase from infant-associated bifidobacteria belonging to a novel glycoside hydrolase family 129 is implicated in an alternative mucin degradation pathway. Journal of Biological Chemistry, 287(1), 693-700 (2012).
  16. S. Kurihara, H. Suzuki, M. Oshida, and Y. Benno. A novel putrescine importer required for type 1 pili-driven surface motility induced by extracellular putrescine in Escherichia coli K-12. Journal of Biological Chemistry, 286(12), 10185-10192 (2011).
  17. P. Powedchagun, H. Suzuki, and S. Rengpipat. Characterization of a probiotic Bacillus S11 bacterium of black tiger shrimp Penaeus monodon. Songklanakarin Journal of Science and Technology, 33(1), 1-8 (2011).
  18. A. S. A. F. El Sayed, S. Fujimoto, C. Yamada, and H. Suzuki. Enzymatic synthesis of γ-glutamylglutamine, a stable glutamine analogue, by γ-glutamyltranspeptidase from Escherichia coli K-12. Biotechnology Letters, 32(12), 1877-1881 (2010).
  19. S. Kurihara, K. Kato, K. Asada, H. Kumagai, and H. Suzuki. A putrescine-inducible pathway comprising PuuE-YneI in which γ-aminobutyrate (GABA) is degraded into succinate in Escherichia coli K-12. Journal of Bacteriology, 192(18), 4582-4591 (2010).
  20. H. Suzuki, C. Yamada, K. Kijima, S. Ishihara, K. Wada, K. Fukuyama, and H. Kumagai. Enhancement of glutaryl-7-aminocephalosporanic acid acylase activity of γ-glutamyltranspeptidase of Bacillus subtilis. Biotechnology Journal, 5(8), 829-837 (2010).
  21. K. Wada, M. Irie, H. Suzuki, and K. Fukuyama. Crystal structure of the halotolerant γ-glutamyltranspeptidase from Bacillus subtilis in complex with glutamate reveals its unique architecture of the solvent-exposed catalytic pocket. FEBS Journal, 277(4), 1000-1009 (2010). および表紙
  22. T. Koyanagi, T. Katayama, H. Suzuki, A. Onishi, K. Yokozeki, and H. Kumagai. Hyperproduction of 3,4-dihydroxyphenyl-L-alanine (L-dopa) using Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR. Bioscience, Biotechnology, and Biochemistry, 73(5), 1221-1223 (2009).
  23. S. Kurihara, Y. Tsuboi, S. Oda, H. G. Kim, H. Kumagai, and H. Suzuki. The putrescine importer PuuP of Escherichia coli K-12. Journal of Bacteriology, 191(8), 2776-2782 (2009).
  24. S. Kurihara, H. Suzuki, Y. Tsuboi, and Y. Benno. Dependence of swarming in Escherichia coli K-12 on spermidine and the spermidine importer. FEMS Microbiology Letters, 294(1), 97-101 (2009).
  25. S. Kurihara, S. Oda, Y. Tsuboi, H. G. Kim, M. Oshida, H. Kumagai, and H. Suzuki. γ-Glutamylputrescine synthetase in the putrescine utilization pathway of Escherichia coli K-12. Journal of Biological Chemistry, 283(29), 19981-19990 (2008).
  26. T. Koyanagi, T. Katayama, H. Suzuki, and H. Kumagai. Altered oligomerization properties of N316 mutants of Escherichia coli TyrR. Journal of Bacteriology, 190(24), 8238-8243 (2008).
  27. C. Yamada, K. Kijima, S. Ishihara, C. Miwa, K. Wada, T. Okada, K. Fukuyama, H. Kumagai, and H. Suzuki. Improvement of the glutaryl-7-aminocephalosporanic acid acylase activity of a bacterial γ-glutamyltranspeptidase. Applied and Environmental Microbiology, 74(11), 3400-3409 (2008).
  28. K. Wada, J. Hiratake, M. Irie, T. Okada, C. Yamada, H. Kumagai, H. Suzuki, and K. Fukuyama. Crystal structures of Escherichia coli γ-glutamyltranspeptidase in complex with azaserine and acivicin: Covalently bound inhibitors with the catalytic Thr391 in a novel manner and mechanistic implication for inhibition by glutamine antagonists. Journal of Molecular Biology, 380(2), 361-372 (2008).
  29. T. Okada, H. Suzuki, K. Wada, H. Kumagai, and K. Fukuyama. Crystal structure of the γ-glutamyltranspeptidase precursor protein from Escherichia coli: Structural changes upon autocatalytic processing and implications for the maturation mechanism. Journal of Biological Chemistry, 282(4), 2433-2439 (2007).
  30. G. Boanca, A. Sand, T. Okada, H. Suzuki, H. Kumagai, K. Fukuyama, and J. J. Barycki. Autoprocessing of H. pylori γ-glutamyltranspeptidase leads to the formation of a threonine-threonine catalytic dyad. Journal of Biological Chemistry, 282(1), 534-541 (2007).
  31. H. Suzuki, C. Yamada, and K. Kato. γ-Glutamyl compounds and their enzymatic production using bacterial γ-glutamyltranspeptidase. Amino Acids, 32(3), 333-340 (2007).
  32. K. Kijima and H. Suzuki. Improving the umami taste of soy sauce by the addition of bacterial γ-glutamyltranspeptidase as a glutaminase to the fermentation mixture. Enzyme and Microbial Technology, 41(1-2), 80-84 (2007).
  33. T. Okada, H. Suzuki, K. Wada, H. Kumagai, and K. Fukuyama. Crystal structures of γ-glutamyltranspeptidase from E. coli, a key enzyme in glutathione metabolism, and its reaction intermediate. Proceedings of the National Academy of Sciences, USA, 103(17), 6471-6476 (2006).
  34. S. Kurihara, S. Oda, H. Kumagai, and H. Suzuki. γ-Glutamyl-γ-aminobutyrate hydrolase in the putrescine utilization pathway of Escherichia coli K-12. FEMS Microbiology Letters, 256(2), 318-323 (2006).
  35. L. Han, J. Hiratake, N. Tachi, H. Suzuki, H. Kumagai, and K. Sakata. γ-(Monophenyl)phosphono glutamate analogues as mechanism-based inhibitors of γ-glutamyl transpeptidase. Bioorganic and Medical Chemistry, 14(17), 6043-6054 (2006).
  36. T. Koyanagi, T. Katayama, A. Hirao, H. Suzuki, and H. Kumagai. Construction of an efficient protein expression system using the tpl promoter. Biotechnology Letters, 27(17), 1267-1271 (2005).
  37. H. Suzuki, T. Koyanagi, S. Izuka, A. Onishi, and H. Kumagai. The yliA, B, C, and D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. Journal of Bacteriology, 187(17), 5861-5867 (2005).
  38. S. Kurihara, S. Oda, K. Kato, H. G. Kim, T. Koyanagi, H. Kumagai, and H. Suzuki. A novel putrescine utilization pathway involves γ-glutamylated intermediates of Escherichia coli K-12. Journal of Biological Chemistry, 280(6), 4602-4608 (2005).
  39. T. Koyanagi, T. Katayama, H. Suzuki, H. Nakazawa, K. Yokozeki, and H. Kumagai. Effective production of 3,4-dihydroxyphenyl-L-alanine (L-DOPA) with Erwinia herbicola cells carrying a mutant transcriptional regulator TyrR. Journal of Biotechnology, 115(3), 303-306 (2005).
  40. H. Suzuki, C. Miwa, S. Ishihara, and H. Kumagai. A single amino acid substitution converts γ-glutamyltranspeptidase to class IV cephalosporin acylase (glutaryl-7-amino-cephalosporanic acid acylase). Applied and Environmental Microbiology, 70(10), 6324-6328 (2004).
  41. T. Koyanagi, T. Katayama, H. Suzuki, and H. Kumagai. The LIV-I/LS system as a determinant of azaserine sensitivity of Escherichia coli K-12. FEMS Microbiology Letters, 237(1), 73-77 (2004).
  42. H. Suzuki, K. Kato, and H. Kumagai. Development of an efficient enzymatic production of γ-D-glutamyl-L-tryptophan (SCV-07), a prospective medicine for tuberculosis, with bacterial γ-glutamyltranspeptidase. Journal of Biotechnology, 111(3), 291-295 (2004).
  43. H. Suzuki, K. Kato, and H. Kumagai. Enzymatic synthesis of γ-glutamylvaline to improve the bitter taste of valine. Journal of Agricultural and Food Chemistry, 52(3), 577-580 (2004).
  44. H. Minami, H. Suzuki, and H. Kumagai. γ-Glutamyltranspeptidase, but not YwrD, is important in utilizing extracellular glutathione as a sulfur source in Bacillus subtilis. Journal of Bacteriology, 186(4), 1213-1214 (2004).
  45. T. Koyanagi, T. Katayama, H. Suzuki, and H. Kumagai. Identification of the LIV-I/LS system as the third phenylalanine transporter in Escherichia coli K-12. Journal of Bacteriology, 186(2), 343-350 (2004).
  46. H. Suzuki, S. Izuka, H. Minami, N. Miyakawa, S. Ishihara, and H. Kumagai. Use of bacterial γ-glutamyltranspeptidase for enzymatic synthesis of γ-D-glutamyl compounds. Applied and Environmental Microbiology, 69(11), 6399-6404 (2003).
  47. H. Minami, H. Suzuki, and H. Kumagai. Salt-tolerant γ-glutamyltranspeptidase from Bacillus subtilis 168 with glutaminase activity. Enzyme and Microbial Technology, 32(3-4), 431-438 (2003).
  48. H. Minami, H. Suzuki, and H. Kumagai. A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity. FEMS Microbiology Letters, 224(2), 169-173 (2003).
  49. H. Suzuki, and H. Kumagai. Autocatalytic processing of γ-glutamyltranspeptidase. Journal of Biological Chemistry, 277(45), 43536-43543 (2002).
  50. H. Suzuki, S. Izuka, N. Miyakawa, and H. Kumagai. Enzymatic production of theanine, an “umami” component of tea, from glutamine and ethylamine with bacterial γ-glutamyltranspeptidase. Enzyme and Microbial Technology, 31(6), 884-889 (2002).
  51. T. Katayama, H. Suzuki, T. Koyanagi, and H. Kumagai. Functional analysis of the Erwinia herbicola tutB gene and its product. Journal of Bacteriology, 184(11), 3135-3141 (2002).
  52. H. Suzuki, N. Miyakawa, and H. Kumagai. Enzymatic production of γ-L-glutamyltaurine through the transpeptidation reaction of γ-glutamyltranspeptidase from Escherichia coli K-12. Enzyme and Microbial Technology, 30(7), 883-888 (2002).
  53. H. Suzuki, Y. Kajimoto, and H. Kumagai. Improvement of the bitter taste of amino acids through the transpeptidation reaction of bacterial γ-glutamyltranspeptidase. Journal of Agricultural and Food Chemistry, 50(2), 313-318 (2002).
  54. H. Suzuki, S. Kamatani, and H. Kumagai. Purification and characterization of aminopeptidase B from Escherichia coli K-12. Bioscience, Biotechnology, and Biochemistry, 65(7), 1549-1558 (2001).
  55. H. Suzuki, S. Kamatani, E.-S. Kim, and H. Kumagai. Aminopeptidases A, B and N, and dipeptidase D are the four cysteinylglycinases of Escherichia coli K-12. Journal of Bacteriology, 183(4), 1489-1490 (2001).
  56. T. Katayama, H. Suzuki, T. Koyanagi, and H. Kumagai. Cloning and random mutagenesis of the Erwinia herbicola tyrR gene for high-level expression of tyrosine phenol-lyase. Applied and Environmental Microbiology, 66(11), 4764-4771 (2000).
  57. M. Inoue, J. Hiratake, H. Suzuki, H. Kumagai, and K. Sakata. Identification of catalytic nucleophile of Escherichia coli γ-glutamyltranspeptidase by γ-monofluorophosphono derivative of glutamic acid: N-terminal Thr-391 in small subunit is the nucleophile. Biochemistry, 39(26), 7764-7771 (2000).
  58. J. H. Roh, J. Wouters, E. Depiereux, H. Yukawa, M. Inui, H. Minami, H. Suzuki, and H. Kumagai. Purification, cloning, and 3-dimensional structure prediction of Micrococcus luteus FAD-containing tyramine oxidase. Biochemical and Biophysical Research Communications, 268(2), 293-297 (2000).
  59. H. Suzuki, W. Hashimoto, and H. Kumagai. Glutathione metabolism in Escherichia coli. Journal of Molecular Catalysis B: Enzymatic, 6(3), 175-184 (1999).
  60. T. Katayama, H. Suzuki, K. Yamamoto, and H. Kumagai. Transcriptional regulation of tyrosine phenol-lyase gene mediated through TyrR and cAMP receptor protein. Bioscience, Biotechnology and Biochemistry, 63(10), 1823-1827 (1999).
  61. W. Hashimoto, H. Suzuki, K. Yamamoto, and H. Kumagai. Analysis of low temperature inducible mechanism of γ-glutamyltranspeptidase of Escherichia coli K-12. Bioscience, Biotechnology and Biochemistry, 61(1), 34-39 (1997).
  62. Y. Takenaka, J.-H. Roh, H. Suzuki, K. Yamamoto, and H. Kumagai. Metal ionic induction; expression of monoamine oxidase gene of Escherichia coli is induced by copper ion. Journal of Fermentation and Bioengineering, 83(2), 174-176 (1997).
  63. S. Kawai, H. Suzuki, K. Yamamoto, and H. Kumagai. Characterization of the L-malate permease gene (maeP) of Streptococcus bovis ATCC 15352. Journal of Bacteriology, 179(12), 4056-4060 (1997).
  64. P. Xu, T. Yano, K. Yamamoto, H. Suzuki, and H. Kumagai. Characterization of a lactate oxidase from a strain of gram negative bacterium from soil. Applied Biochemistry and Biotechnology, 56(3), 277-288 (1996).
  65. P. Xu, T. Yano, K. Yamamoto, H. Suzuki, and H. Kumagai. Screening for bacterial strains producing lactate oxidase. Journal of Fermentation and Bioengineering, 81(4), 357-359 (1996).
  66. M. Yamashita, H. Azakami, N. Yokoro, J.-H. Roh, H. Suzuki, H. Kumagai, and Y. Murooka. maoB, a gene that encodes a positive regulator of the monoamine oxidase gene (maoA) in Escherichia coli. Journal of Bacteriology, 178(10), 2941-2947 (1996).
  67. H. Sakai, N. Sakabe, K. Sasaki, W. Hashimoto, H. Suzuki, H. Tachi, H. Kumagai, and K. Sakabe. A preliminary description of the crystal structure of γ-glutamyltranspeptidase from E. coli K-12. Journal of Biochemistry, 120(1), 26-28 (1996).
  68. A. K. North, D. S. Weiss, H. Suzuki, Y. Flashner, and S. Kustu. Repressor forms of the enhancer-binding protein NtrC: some fail in coupling ATP hydrolysis to open complex formation by σ54-holoenzyme. Journal of Molecular Biology, 260(3), 317-331 (1996).
  69. S. Kawai, H. Suzuki, K. Yamamoto, M. Inui, H. Yukawa, and H. Kumagai. Purification and characterization of a malic enzyme from the ruminal bacterium Streptococcus bovis ATCC 15352 and cloning and sequening of its gene. Applied and Environmental Microbiology, 62(8), 2692-2700 (1996).
  70. H. Suzuki, E.-S. Kim, N. Yamamoto, W. Hashimoto, K. Yamamoto, and H. Kumagai. Mapping, cloning, and DNA sequencing of pepB gene which encodes peptidase B of Escherichia coli K-12. Journal of Fermentation and Bioengineering, 82(4), 392-397 (1996).
  71. W. Hashimoto, H. Suzuki, K. Yamamoto, and H. Kumagai. Effect of site-directed mutations on processing and activity of γ-glutamyltranspeptidase of Escherichia coli K-12. Journal of Biochemistry, 118(1), 75-80 (1995).
  72. J. H. Roh, Y. Takenaka, H. Suzuki, K. Yamamoto, and H. Kumagai. Escherichia coli K-12 copper containing monoamine oxidase: Investigation of the copper binding ligands by site directed mutagenesis, elemental analysis and TOPA quinone formation. Biochemical and Biophysical Research Communications, 212(3), 1107-1114 (1995).
  73. H. Suzuki, T. Katayama, K. Yamamoto, and H. Kumagai. Transcriptional regulation of tyrosine phenol-lyase gene of Erwinia herbicola AJ2985. Bioscience, Biotechnology and Biochemistry, 59(12), 2339-2341 (1995).
  74. W. Hashimoto, H. Suzuki, S. Nohara, H. Tachi, K. Yamamoto, and H. Kumagai. Subunit association of γ-glutamyltranspeptidase of Escherichia coli K-12. Journal of Biochemistry, 118(6), 1216-1223 (1995).
  75. H. Azakami, M. Yamashita, J.-H. Roh, H. Suzuki, H. Kumagai, and Y. Murooka. Nucleotide sequence of the gene for monoamine oxidase (maoA) from Escherichia coli. Journal of Fermentation and Bioengineering, 77(3), 315-319 (1994).
  76. J.-H. Roh, H. Suzuki, H. Kumagai, M. Yamashita, H. Azakami, Y. Murooka, and B. Mikami. Crystallization and preliminary X-ray analysis of copper amine oxidase from Escherichia coli K-12. Journal of Molecular Biology, 238(4), 635-637 (1994).
  77. J.-H. Roh, H. Suzuki, H. Azakami, M. Yamashita, Y. Murooka, and H. Kumagai. Purification, characterization, and crystallization of monoamine oxidase from Escherichia coli K-12. Bioscience, Biotechnology and Biochemistry, 58(9), 1652-1656 (1994).
  78. H. Suzuki, W. Hashimoto, and H. Kumagai. Escherichia coli K-12 can utilize an exogenous γ-glutamyl peptide as an amino acid source, for which γ-glutamyltranspeptidase is essential. Journal of Bacteriology, 175(18), 6038-6040 (1993).
  79. H. Kumagai, S. Nohara, H. Suzuki, W. Hashimoto, K. Yamamoto, H. Sakai, K. Sakabe, K. Fukuyama, and N. Sakabe. Crystallization and preliminary X-ray analysis of γ-glutamyltranspeptidase from Escherichia coli K-12. Journal of Molecular Biology, 234(4), 1259-1262 (1993).
  80. L. M. Heisler, H. Suzuki, R. Landick, and C. A. Gross. Four contiguous amino acids in the β subunit of Escherichia coli RNA polymerase define the target for streptolydigin resistance. Journal of Biological Chemistry, 268(34), 25369-25375 (1993).
  81. H. Suzuki, K. Nishihara, N. Usui, H. Matsui, and H. Kumagai. Cloning and nucleotide sequence of Erwinia herbicola AJ2982 tyrosine phenol-lyase gene. Journal of Fermentation and Bioengineering, 75(2), 145-148(1993).
  82. W. Hashimoto, H. Suzuki, S. Nohara, and H. Kumagai. Escherichia coli γ-glutamyltranspeptidase mutants deficient in processing to subunits. Biochemical and Biophysical Research Communications, 189(1), 173-178 (1992).
  83. J. O. Claudio, H. Suzuki, H. Kumagai, and T. Tochikura. Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli K-12. Journal of Fermentation and Bioengineering, 72(2), 125-127 (1991).
  84. H. Kumagai, H. Suzuki, M. Shimizu, and T. Tochikura. Utilization of the Escherichia coli K-12 γ-glutamyltranspeptidase reaction for glutathione synthesis. Journal of Biotechnology, 9(2), 129-138 (1989).
  85. H. Kumagai, T. Echigo, H. Suzuki, and T. Tochikura. Enzymatic synthesis of γ-glutamyltyrosine methyl ester from L-glutamine and L-tyrosine methyl ester with Escherichia coli K-12 γ-glutamyltranspeptidase. Agricultural and Biological Chemistry, 53(5), 1429-1430 (1989).
  86. H. Kumagai, H. Suzuki, H. Shigematsu, and T. Tochikura. S-Carboxymethylcysteine synthetase from Escherichia coli. Agricultural and Biological Chemistry, 53(9), 2481-2487 (1989).
  87. H. Kumagai, T. Echigo, H. Suzuki, and T. Tochikura. Enzymatic synthesis of γ-glutamyl-L-histidine by γ-glutamyltranspeptidase from Escherichia coli K-12. Letters in Applied Microbiology, 8(4), 143-146 (1989).
  88. H. Suzuki, H. Kumagai, T. Echigo, and T. Tochikura. DNA sequence of the Escherichia coli K-12 γ-glutamyltranspeptidase gene, ggt . Journal of Bacteriology, 171(9), 5169-5172 (1989).
  89. H. Suzuki, H. Kumagai, T. Echigo, and T. Tochikura. Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase. Biochemical and Biophysical Research Communications, 150(1), 33-38 (1988).
  90. H. Kumagai, H. Tamaki, Y. Koshino, H. Suzuki, and T. Tochikura. Distribution, formation and stabilization of yeast glutathione S-transferase. Agricultural and Biological Chemistry, 52(6), 1377-1382 (1988).
  91. H. Kumagai, T. Echigo, H. Suzuki, and T. Tochikura. Synthesis of γ-glutamyl-DOPA from L-glutamine and L-DOPA by γ-glutamyltranspeptidase of Escherichia coli K-12. Agricultural and Biological Chemistry, 52(7), 1741-1745 (1988).
  92. H. Suzuki, H. Kumagai, and T. Tochikura. Isolation, genetic mapping, and characterization of Escherichia coli K-12 mutants lacking γ-glutamyltranspeptidase. Journal of Bacteriology, 169(9), 3926-3931 (1987).
  93. T. Tachiki, H. Suzuki, S. Wakisaka, T. Yano, and T. Tochikura. Production of γ-glutamylmethylamide and γ-glutamylethylamide by coupling of baker's yeast preparations and bacterial glutamine synthetase. Journal of General and Applied Microbiology, 32(6), 545-548 (1986).
  94. H. Suzuki, H. Kumagai, and T. Tochikura. γ-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. Journal of Bacteriology, 168(3), 1325-1331 (1986).
  95. H. Suzuki, H. Kumagai, and T. Tochikura. γ-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. Journal of Bacteriology, 168(3), 1332-1335 (1986).
  96. T. Tachiki, H. Suzuki, S. Wakisaka, T. Yano, and T. Tochikura. Glutamine production in high concentrations with energy transfer employing glutamine synthetase from Micrococcus glutamicus. Journal of General and Applied Microbiology, 29(5), 355-363 (1983).
  97. T. Tachiki, S. Wakisaka, H. Suzuki, H. Kumagai, and T. Tochikura. Variation of properties of Micrococcus glutamicus glutamine synthetase brought about by divalent cations. Agricultural and Biological Chemistry, 47(2), 287-292 (1983).

総説など

  1. 鈴木秀之、中藤裕子、田村友規. コク味調味料の新規調製法〜プロテアーゼ処理で得られたタンパク加水分解物のγ-グルタミル化. 醸協, 113(6), 353-362 (2018).
  2. H. Suzuki, and S. Kurihara. Polyamine catabolism in prokaryotes. In Polyamines: A universal molecular nexus for growth, survival and specialized metabolism. Ed. by T. Kusano, and H. Suzuki, pp. 47-59, Springer, Tokyo (2015).
  3. S. Kurihara, and H. Suzuki. Bacterial polyamine transporters. In Polyamines: A universal molecular nexus for growth, survival and specialized metabolism. Ed. by T. Kusano, and H. Suzuki, pp. 171-178, Springer, Tokyo (2015).
  4. 鈴木秀之、栗原新. 大腸菌のポリアミン代謝. ポリアミン, 1, 47-54 (2014).
  5. 和田啓、鈴木秀之. 「Part II 8章 塩耐性タンパク質」 In CSJカレントレビュー第17号「極限環境の生体分子 過酷な環境下での機能を科学する」日本化学会編、跡見晴幸、大野弘幸、杉本直己(編集)、化学同人, 京都, pp. 89-94 (2014).
  6. H. Suzuki. Microbial production of amino acids and their derivatives for use in foods, nutraceuticals, and medications. In Microbial production of food ingredients, enzymes and nutraceuticals, Ed. by B McNeil, D Archer, I Giavasis, and L Harvey, pp. 385-412, Woodhead Publishing, Cambridge, UK (2013).
  7. H. Suzuki. Microbial production of amino acids and their derivatives for use in foods, nutraceuticals, and medications. In Microbial production of food ingredients, enzymes and nutraceuticals. Ed. by B. McNeil, D. Archer, I. Giavasis, and L. Harvey, pp. 385-412. Woodhead Publishing, Cambridge, UK (2013).
  8. J. Hiratake, H. Suzuki, K. Fukuyama, K. Wada, and H. Kumagai. γ-Glutamyl transpeptidase and its precursor. In Handbook of Proteolytic Enzymes. 3rd ed. Vol. 1, ed. by N. D. Rawlings and G. S. Salvesen, pp. 3712-3719, Academic Press, Oxford, UK (2013).
  9. H. Suzuki, Y. Sato, I. Sato, S. Izuka, A. Onishi, and Y. Kajimoto. Direct fermentation process for production of glutathione: A kokumi-enhancing substance. In Advances and Challenges in Flavor Chemistry & Biology. Ed. by T. Hofmann, W. Meyerhof, and P. Shieberle, pp. 229-234. Deutsche Forschungsanstalt für Lebensmittelchemie (2011).
  10. 栗原新、鈴木秀之. γ-グルタミル中間体を経る大腸菌の新規ポリアミン代謝系と取り込み系の発見:プトレッシンの効率的な発酵生産に資するか? 化学と生物, 48(10), 664-666 (2010).
  11. 鈴木秀之、和田啓、福山恵一. γ-グルタミルトランスペプチダーゼの立体構造に基づいた成熟化と酵素反応機構. 蛋白質核酸酵素, 54(3), 245-251 (2009).
  12. 鈴木秀之、和田啓、福山恵一. γ-グルタミルトランスペプチダーゼのグルタリル-7-アミノセファロスポラン酸アシラーゼへの変換~立体構造に基づく効果的変異導入. バイオサイエンスとインダストリー, 66(12), 660-666 (2008).
  13. H. Suzuki, and C. Yamada. Improvement of the flavor of amino acids and peptides using bacterial γ-glutamyltranspeptidase. In Recent Highlights in Flavor Chemistry & Biology. Ed. by T. Hofmann, W. Meyerhof, and P. Shieberle, pp. 227-232. Deutsche Forschungsanstalt für Lebensmittelchemie (2008).
  14. K. Kijima, and H. Suzuki. Improvement of the umami taste in soy sauce by the addition of bacterial γ-glutamyltranspeptidase to the fermentation mixture. In Recent Highlights in Flavor Chemistry & Biology. Ed. by T. Hofmann, W. Meyerhof, and P. Shieberle, pp. 399-402. Deutsche Forschungsanstalt für Lebensmittelchemie (2008).
  15. 和田啓、鈴木秀之、福山恵一. γ-グルタミルトランスペプチダーゼはどのように成熟化し、反応を触媒するか? 日本応用酵素協会誌, 43, 23-31 (2008).
  16. H. Suzuki, C. Yamada, and K. Kato. γ-Glutamyl compounds and their enzymatic production using bacterial γ-glutamyltranspeptidase. Amino Acids, 32(3), 333-340 (2007).
  17. H. Suzuki, H. Minami, S. Izuka, N. Miyakawa, Y. Kajimoto, K. Kato, S. Ishihara, and H. Kumagai. Effective use of bacterial γ-glutamyltranspeptidase to improve the taste of food. In State-of The Art in Flavour Chemistry And Biology. Ed. by T. Hofmann, M. Rothe, and P. Schieberle, pp. 205-212. Deutsche Forschungsanstalt für Lebensmittelchemie (2005).
  18. J. Hiratake, H. Suzuki, and H. Kumagai. γ-Glutamyltranspeptidase and its precursor. In Handbook of Proteolytic Enzymes. 2nd ed. Ed. by A. J. Barrett, N. D. Rawlings, and J. F. Woessner, pp. 2090-2094. Academic Press, Oxford, UK (2004).
  19. H. Suzuki, and H. Kumagai. Application of bacterial γ-glutamyltranspeptidase to improve the taste of food. In Challenges in Taste Chemistry and Biology. Ed by T. Hofmann, W. Pickenhagen, and C.-T. Ho, pp. 223-237. American Chemical Society, Washington, D.C. (2004).
  20. 南博道、鈴木秀之、熊谷英彦. 枯草菌のγ-グルタミルトランスペプチダーゼに関する研究. 応用微生物学研究, 1, 109-114 (2003).
  21. 片山高嶺、小柳喬、鈴木秀之、熊谷英彦. L-ドーパ生産酵素チロシンフェノールリアーゼ(TPL)の発現調節機構の解明と転写調節因子の改変によるTPLの高発現. 応用微生物学研究, 1, 130-137 (2003).
  22. 鈴木秀之、熊谷英彦. [分解系] γ-グルタミルトランスフェラーゼ.(〈シリーズ〉バイオファクター研究のブレイクスルー:グルタチオン) ビタミン, 76, 521-524 (2002).
  23. 鈴木秀之、熊谷英彦. γ-グルタミルトランスペプチダーゼ:Ntn-ヒドロラーゼスーパーファミリーの新しいメンバー. 蛋白質核酸酵素, 46, 105-111 (2001).
  24. 片山高嶺、鈴木秀之、熊谷英彦. 転写調節因子TyrRの改変によるチロシンフェノールリアーゼの高発現. バイオサイエンスとインダストリー, 59, 759-762 (2001).
  25. 鈴木秀之. グルタチオン代謝の細胞生理の酵素分子生物学的解明と代謝酵素の構造と機能に関する研究. 日本農芸化学会誌, 71(10), 987-994 (1997).
  26. 鈴木秀之、熊谷英彦 大腸菌のγ-グルタミルトランスペプチダーゼ. ビタミン, 28(9), 485-499 (1994).
  27. 鈴木秀之、熊谷英彦 細菌のγ-グルタミルトランスペプチダーゼ. 日本農芸化学会誌, 66(10), 1497-1500 (1992).
  28. 鈴木秀之、熊谷英彦 Escherichia coli K-12のγ-グルタミルトランスペプチダーゼ. 生化学, 61(6), 491-496 (1989).
  29. H. Kumagai, H. Suzuki, T. Echigo, M. Shimizu, and T. Tochikura. Escherichia coli K-12 mutants lacking γ-glutamyltranspeptidase and molecular cloning of ggt gene. In Glutathione Centennial: Molecular Perspectives and Clinical Implications. Ed. by N. Taniguchi, T. Higashi, Y. Sakamoto, and A. Meister, Academic Press, pp. 161-175 (1989).

紀要・報告書など

  1. 鈴木秀之、中藤裕子. γ-グルタミル化による食品の塩味・甘味の増強効果を利用した塩分・糖分制限食の開発. 日本食品化学研究振興財団平成27年度研究成果報告書. 22, 123-127 (2016).
  2. 鈴木秀之、田村友規. 微生物酵素によるプロテアーゼ処理たん白質分解酵素の呈味性改良法の開発. 大豆たん白質研究, 17, 42-45 (2015).
  3. 鈴木秀之、山田千晶、Ho Van Thao. Bacillus属細菌のγ-グルタミルトランスペプチダーゼをグルタミナーゼとして醗酵食品の醪に添加することにより、うま味を向上させる方法に関連する研究. 中央味噌研究所報告, 32, 51-54 (2011).
  4. 鈴木秀之. 米や麦を原料とする食品製造残渣を有効利用するための微生物菌株に関する研究. 平成24年度飯島藤十郎記念食品科学振興財団年報, 28, pp. 146-149 (2012).
  5. 鈴木秀之、渡邉美子. おからを原料とした納豆菌による生分解性プラスチック素材:ポリγ-グルタミン酸の製造法の開発. 大豆たん白質研究, 13, 62-65 (2010).
  6. 鈴木秀之、林田果乃子. 乳酸菌による豆乳の大豆臭除去法の開発. 大豆たん白質研究, 12, 75-77 (2009).
  7. 鈴木秀之、富山大輔. 大豆の青臭さの原因であるn-ヘキサナールを分解できるアルデヒドデヒドロゲナーゼのスクリーニング. 大豆たん白質研究, 11, 67-70 (2008).
  8. 鈴木秀之. 大豆タンパク質に由来するうま味成分の捕捉改善法の実用化を目指した細菌のγ-グルタミルトランスペプチダーゼの簡易調製法の開発. 飯島記念食品科学振興財団平成17年度年報, 207-210 (2007).
  9. 鈴木秀之、木嶋恭子. γ-グルタミルトランスペプチダーゼをグルタミナーゼとして醤油醸造時に添加することによる呈味性改善法の開発(第二報). 大豆たん白質研究, 9, 42-46 (2006).
  10. 鈴木秀之. 食品を微生物の酵素でおいしくする. 三島海雲記念財団-平成15年度受賞者研究報告書, 41, 13-19 (2004).
  11. 鈴木秀之、南博道、井塚俊介、宮川展和、梶本陽子、加藤健二、石原清香、熊谷英彦. 細菌のγ-グルタミルトランスペプチダーゼによる食品の呈味性改善に関する研究. すかいらーくフードサイエンス研究所-平成15年度食に関する助成研究調査報告書, 17, 23-30 (2004).
  12. 鈴木秀之. γ-グルタミルトランスペプチダーゼの自己触媒的プロセシングの分子機構. 長瀬科学技術振興財団研究報告集, 15, 119-126 (2003).
  13. H. Suzuki. Creation of novel tastes. Memoirs of Asahi Brewery Foundation, 16, 21-25 (2003).
  14. H. Suzuki. Salt-tolerant γ-glutamyltranspeptidase: to utilize soy protein as a source of umami taste. 大豆たん白質研究, 5, 31-35 (2002).
  15. H. C. Seo, H. Suzuki, K. Yamamoto, and H. Kumagai. Screening for Aspergillus oryzae strains producing large amount of salt tolerant and heat stable glutaminase. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 20, 143-154 (1997).
  16. P. Xu, T. Yano, K. Yamamoto, H. Suzuki, and H. Kumagai. Screening of bacteria producing a lactate oxidase and characterization of the enzyme. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 16, 201-214 (1993).
  17. H. Kumagai, H. Suzuki, and W. Hashimoto. γ-Glutamyltranspeptidase is essential for Escherichia coli K-12 to utilize an exogenous γ-glutamyl peptide as an amino acid source. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 16, 556-559 (1993).
  18. H. Kumagai, H. Suzuki, W. Hashimoto, and S. Nohara. Structure-function relationship and regulation of biosynthesis of γ-glutamyltranspeptidase of Escherichia coli K-12. 長瀬科学技術振興財団研究報告集, 4, 97-107 (1993).
  19. H. Suzuki, P. Pinphanichakarn, S. Thaniyavarn, S. Rengpipat, and H. Kumagai. Screening of high γ-glutamyltranspeptidase producing strains from fermented food in Thailand. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 15, 367-370 (1992).
  20. W. Hashimoto, H. Suzuki, S. Nohara, and H. Kumagai. γ-Glutamyltranspeptidase mutants of E. coli deficient in processing to subunits. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 15, 460-464 (1992).
  21. H. Suzuki, H. Kumagai, W. Hashimoto, J. O. Claudio, and T. Tochikura. Molecular cloning and DNA sequence of Escherichia coli K-12 γ-glutamyltranspeptidase gene, ggt, and excretion of γ-glutamyltranspeptidase. In Frontiers and New Horizons in Amino Acid Research. Ed. by K. Takai, Elsevier, pp. 589-593 (1992).
  22. H. Kumagai, H. Suzuki, T. Echigo, and T. Tochikura. Syntheses of γ-glutamyl peptides by γ-glutamyltranspeptidase from Escherichia coli K-12. Annals of the New York Academy of Sciences, 613, 647-651 (1990).
  23. J. O. Claudio, H. Suzuki, H. Kumagai, and T. Tochikura. Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli K-12. Annual Reports of International Center of Cooperative Research in Biotechnology, Japan, 13, 129-143 (1990).
  24. H. Kumagai, R. Nakayama, H. Suzuki, and T. Tochikura. Bacterial γ-glutamyltranspeptidase: properties and γ-glutamy amino acids synthesis. Proceedings of 4th European Congress on Biotechnology, Vol.2, p.68 (1987).
  25. H. Kumagai, H. Suzuki, H. Shigematsu, and T. Tochikura. S-Carboxymethylcysteine synthase from Escherichia coli. In Biochemistry of Vitamin B6. Ed. by T. Korpela and P. Christen, Birkhauser Verlag Basel, Boston, pp. 239-241 (1987).
  26. T. Tachiki, H. Suzuki, T. Yano, H. Kumagai, and T. Tochikura. Glutamine production by coupling with energy transfer: employing dried baker's yeast cells and bacterial glutamine synthetase. Proceedings of 3rd European Congress on Biotechnology, Vol.1, p.313 (1984).