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Bioscience, Biotechnology, and Biochemistry Volume 70, 2006 - Issue 5
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Original Articles

Identification of a Catalytic Residue of Clostridium paraputrificumN-Acetyl-β-D-glucosaminidase Nag3A by Site-Directed Mutagenesis

Huazhong LISchool of Medicine, Southern Yangtze University
,
Guangshan ZHAOFaculty of Bioresources, Mie University
,
Hideo MIYAKEFaculty of Bioresources, Mie University
,
Hayato UMEKAWAFaculty of Bioresources, Mie University
,
Tetsuya KIMURAFaculty of Bioresources, Mie University
,
Kunio OHMIYAFaculty of Bioresources, Mie University
&
Kazuo SAKKAFaculty of Bioresources, Mie University
 show all
Pages 1127-1133 | Received 26 Aug 2005, Accepted 07 Jan 2006, Published online: 22 May 2014

  • 1) Evvyernie, D., Yamazaki, S., Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K., Identification and characterization of Clostridium paraputrificum M-21, a chitinolytic, mesophilic and hydrogen-producing bacterium. J. Biosci. Bioeng., 89, 596–601 (2000).
  • 2) Evvyernie, D., Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K., Conversion of chitinous wastes to hydrogen gas by Clostridium paraputrificum M-21. J. Biosci. Bioeng., 91, 339–343 (2001).
  • 3) Morimoto, K., Kimura, T., Sakka, K., and Ohmiya, K., Overexpression of a hydrogenase gene in Clostridium paraputrificum to enhance hydrogen gas production. FEMS Microbiol. Lett., 246, 229–234 (2005).
  • 4) Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K., Cloning, sequencing, and expression of the gene encoding Clostridium paraputrificum chitinase ChiB and analysis of the functions of novel cadherin-like domains and a chitin-binding domain. J. Bacteriol., 179, 7306–7314 (1997).
  • 5) Morimoto, K., Karita, S., Kimura, T., Sakka, K., and Ohmiya, K., Sequencing, expression, and transcription analysis of the Clostridium paraputrificum chiA gene encoding chitinase ChiA. Appl. Microbiol. Biotechnol., 51, 340–347 (1999).
  • 6) Li, H., Morimoto, K., Katagiri, N., Kimura, T., Sakka, K., and Ohmiya, K., A novel β-N-acetylglucosaminidase of Clostridium paraputrificum M-21 with high activity on chitobiose. Appl. Microbiol. Biotechnol., 60, 420–427 (2002).
  • 7) Li, H., Morimoto, K., Kimura, T., Sakka, K., and Ohmiya, K., A new type of β-N-acetylglucosaminidase from hydrogen-producing Clostridium paraputrificum M-21. J. Biosci. Bioeng., 96, 268–274 (2003).
  • 8) Coutinho, P. M., and Henrissat, B., The modular structure of cellulases and other carbohydrate-active enzymes: an integrated database approach. In “Genetics, Biochemistry and Ecology of Cellulose Degradation,” eds. Ohmiya, K., Hayashi, K., Sakka, K., Kobayashi, Y., Karita, S., and Kimura, T., Uni Publishers, Tokyo, pp. 15–23 (1999).
  • 9) Tsujibo, H., Fujimoto, K., Tanno, H., Miyamoto, K., Imada, C., Okami, Y., and Inamori, Y., Gene sequence, purification and characterization of N-acetyl-beta-glucosaminidase from a marine bacterium, Alteromonas sp. strain O-7. Gene, 146, 111–115 (1994).
  • 10) Chitlaru, E., and Roseman, S., Molecular cloning and characterization of a novel beta-N-acetyl-D-glucosaminidase from Vibrio furnissii. J. Biol. Chem., 271, 33433–33439 (1996).
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  • 12) Varghese, J. N., Hrmova, M., and Fincher, G. B., Three-dimensional structure of a barley β-D-glucan exohydrolase, a family 3 glycosyl hydrolase. Structure, 7, 179–190 (1999).
  • 13) Hrmova, M., Gori, R. D., Smith, B. J., Vasella, A., Varghese, J. N., and Fincher, G. B., Three-dimensional structure of the barley β-D-glucan glucohydrolase in complex with a transition state mimic. J. Biol. Chem., 279, 4970–4980 (2004).
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  • 15) Mursheda, K. A., Hayashi, H., Karita, S., Goto, M., Kimura, T., Sakka, K., and Ohmiya, K., Importance of the carbohydrate-binding module of Clostridium stercorarium Xyn10B to xylan hydrolysis. Biosci. Biotechnol. Biochem., 65, 41–47 (2001).
  • 16) Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R., Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene, 77, 51–59 (1989).
  • 17) O’Brien, M., and Colwell, R. R., A rapid test of chitinase activity that uses 4-methylumbelliferyl-N-acetyl-β-D-glucosaminide. Appl. Environ. Microbiol., 53, 1718–1720 (1987).
  • 18) Bradford, M. M., A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem., 72, 248–254 (1976).
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  • 20) Vocadlo, D. J., Mayer, C., He, S., and Withers, S. G., Mechanism of action and identification of Asp242 as the catalytic nucleophile of Vibrio furnisii N-acetyl-β-D-glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-α-L-idopyranosyl fluoride. Biochemistry, 39, 117–126 (2000).
  • 21) Malcolm, B. A., Rosenberg, S., Corey, M. J., Allen, J. S., Baetselier, A. D., and Kirsch, J. F., Site-directed mutagenesis of the catalytic residues Asp-52 and Glu-35 of chicken egg white lysozyme. Proc. Natl. Acad. Sci. USA, 86, 133–137 (1989).
  • 22) Hashimoto, Y., Yamada, K., Motoshima, H., Omura, T., Yamada, H., Yasukochi, T., Miki, T., Ueda, T., and Imoto, T., A mutation study of catalytic residue Asp 52 in hen egg lysozyme. J. Biochem., 119, 145–150 (1996).

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