Clostridium paraputrificum N-Acetyl-ꢀ-D-glucosaminidase
1133
Overexpression of a hydrogenase gene in Clostridium
paraputrificum to enhance hydrogen gas production.
FEMS Microbiol. Lett., 246, 229–234 (2005).
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.,
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 ꢀ-D-glucan glucohydrolase in
complex with a transition state mimic. J. Biol. Chem.,
279, 4970–4980 (2004).
14) Hrmova, M., Varghese, J. N., Gori, R. D., Smith, B. J.,
Driguez, H., and Fincher, G. B., Catalytic mechanism
and reaction intermediates along the hydrolytic pathway
of a plant ꢀ-D-glucan glucohydrolase. Structure, 9,
1005–1016 (2001).
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 ster-
corarium Xyn10B to xylan hydrolysis. Biosci. Biotech-
nol. 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-ꢀ-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).
19) Umekawa, H., Endo, T., and Hidaka, H., A rapid
separation of bovine brain S-100a and S-100b protein
and related conformation studies. Arch. Biochem. Bio-
phys., 227, 147–153 (1983).
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-ꢀ-D-
glucosaminidase using 2-acetamido-2-deoxy-5-fluoro-ꢁ-
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 muta-
genesis of the catalytic residues Asp-52 and Glu-35 of
chicken egg white lysozyme. Proc. Natl. Acad. Sci. USA,
86, 133–137 (1989).
4
)
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 ꢀ-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 ꢀ-N-acetylglucosaminidase
from hydrogen-producing Clostridium paraputrificum
M-21. J. Biosci. Bioeng., 96, 268–274 (2003).
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).
Tsujibo, H., Fujimoto, K., Tanno, H., Miyamoto, K.,
Imada, C., Okami, Y., and Inamori, Y., Gene sequence,
purification and characterization of N-acetyl-beta-gluco-
saminidase from a marine bacterium, Alteromonas sp.
strain O-7. Gene, 146, 111–115 (1994).
8
9)
1
1
1
0) Chitlaru, E., and Roseman, S., Molecular cloning and
characterization of a novel beta-N-acetyl-D-glucosami-
nidase from Vibrio furnissii. J. Biol. Chem., 271, 33433–
33439 (1996).
1) Cheng, Q., Li, H., Merdek, K., and Park, J. T., Molecular
characterization of the ꢀ-N-acetylglucosaminidase of
Escherichia coli and its role in cell wall recycling. J.
Bacteriol., 182, 4836–4840 (2000).
2) Varghese, J. N., Hrmova, M., and Fincher, G. B., Three-
dimensional structure of a barley ꢀ-D-glucan exohydro-
lase, a family 3 glycosyl hydrolase. Structure, 7, 179–
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).