메뉴 건너뛰기




Volumn 38, Issue 6, 2006, Pages 765-771

Expression, characterization and mutagenesis of the gene encoding β-N-acetylglucosaminidase from Aeromonas caviae CB101

Author keywords

N Acetylglucosaminidase; Aeromonas caviae; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; GENES; HYDROLYSIS; MUTAGENESIS; OLIGOMERS; SUBSTITUTION REACTIONS;

EID: 32844462956     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.enzmictec.2005.08.003     Document Type: Article
Times cited : (8)

References (28)
  • 2
    • 0031866632 scopus 로고    scopus 로고
    • The molecular biology of chitin digestion
    • R. Cohen-Kupiec, and I. Chet The molecular biology of chitin digestion Curr Opin Biotechnol 9 1998 270 277
    • (1998) Curr Opin Biotechnol , vol.9 , pp. 270-277
    • Cohen-Kupiec, R.1    Chet, I.2
  • 3
    • 0003133857 scopus 로고
    • The ecology of chitin degradation
    • G.W. Gooday The ecology of chitin degradation Adv Microb Ecol 11 1990 387 430
    • (1990) Adv Microb Ecol , vol.11 , pp. 387-430
    • Gooday, G.W.1
  • 4
    • 0026350890 scopus 로고
    • Chitin utilization by marine bacteria
    • C. Yu, A.M. Lee, B.L. Bassler, and S. Roseman Chitin utilization by marine bacteria J Biol Chem 266 1991 24260 24266
    • (1991) J Biol Chem , vol.266 , pp. 24260-24266
    • Yu, C.1    Lee, A.M.2    Bassler, B.L.3    Roseman, S.4
  • 5
    • 0032714186 scopus 로고    scopus 로고
    • Physiological aspects of chitin catabolism in marine bacteria
    • N.O. Keyhani, and S. Roseman Physiological aspects of chitin catabolism in marine bacteria Biochim Biophys Acta 1473 1999 108 122
    • (1999) Biochim Biophys Acta , vol.1473 , pp. 108-122
    • Keyhani, N.O.1    Roseman, S.2
  • 6
    • 0030474759 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation and characterization of a periplasmic chitodextrinase
    • N.O. Keyhani, and S. Roseman The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation and characterization of a periplasmic chitodextrinase J Biol Chem 271 1996 33414 33424
    • (1996) J Biol Chem , vol.271 , pp. 33414-33424
    • Keyhani, N.O.1    Roseman, S.2
  • 7
    • 0030447616 scopus 로고    scopus 로고
    • The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation and characterization of a periplasmic beta-N-acetylglucosaminidase
    • N.O. Keyhani, and S. Roseman The chitin catabolic cascade in the marine bacterium Vibrio furnissii. Molecular cloning, isolation and characterization of a periplasmic beta-N-acetylglucosaminidase J Biol Chem 271 1996 33425 33432
    • (1996) J Biol Chem , vol.271 , pp. 33425-33432
    • Keyhani, N.O.1    Roseman, S.2
  • 8
    • 32044457718 scopus 로고    scopus 로고
    • Isolation and identification of a high-efficient chitin-degrading marine bacterium CB101 and studies on its chitinase system
    • X. Xiao, Y. Zhou, and F.P. Wang Isolation and identification of a high-efficient chitin-degrading marine bacterium CB101 and studies on its chitinase system Acta Oceanol Sinica 25 2003 138 142 (in Chinese and English Abstract)
    • (2003) Acta Oceanol Sinica , vol.25 , pp. 138-142
    • Xiao, X.1    Zhou, Y.2    Wang, F.P.3
  • 9
    • 31244433034 scopus 로고    scopus 로고
    • Structure of cloned chitinase and its truncate from A. caviae
    • Y. Zhou, F.P. Wang, and X. Xiao Structure of cloned chitinase and its truncate from A. caviae Prog Nat Sci 12 2002 587 591
    • (2002) Prog Nat Sci , vol.12 , pp. 587-591
    • Zhou, Y.1    Wang, F.P.2    Xiao, X.3
  • 10
    • 0345411954 scopus 로고    scopus 로고
    • The C-terminal module of Chi1 from Aeromonas caviae CB101 has function in substrate binding and hydrolysis
    • F.P. Wang, Q. Li, Y. Zhou, M.G. Li, and X. Xiao The C-terminal module of Chi1 from Aeromonas caviae CB101 has function in substrate binding and hydrolysis Proteins 53 2003 908 916
    • (2003) Proteins , vol.53 , pp. 908-916
    • Wang, F.P.1    Li, Q.2    Zhou, Y.3    Li, M.G.4    Xiao, X.5
  • 12
    • 0022516180 scopus 로고
    • Chitinase determinants of Vibrio vulnificus: Gene cloning and applications of a chitinase probe
    • A.T. Wortman, C.C. Somerville, and R.R. Colwell Chitinase determinants of Vibrio vulnificus: gene cloning and applications of a chitinase probe Appl Environ Microbiol 52 1986 142 145
    • (1986) Appl Environ Microbiol , vol.52 , pp. 142-145
    • Wortman, A.T.1    Somerville, C.C.2    Colwell, R.R.3
  • 13
    • 77049251255 scopus 로고
    • A modified colorimetric method for the estimation of N-acetylamino sugars
    • J.L. Reissig, J.L. Strominger, and L.F. Leloir A modified colorimetric method for the estimation of N-acetylamino sugars J Biol Chem 217 1955 959 966
    • (1955) J Biol Chem , vol.217 , pp. 959-966
    • Reissig, J.L.1    Strominger, J.L.2    Leloir, L.F.3
  • 14
    • 0031904683 scopus 로고    scopus 로고
    • A novel β-N-acetylhexosaminidase from streptomyces thermoviolaceus OPC-520: Gene cloning, expression and assignment to Family 3 of the glycosyl hydrolases
    • H. Tsujibo, N. Hatano, T. Mikami, A. Hirasawa, K. Miyamoto, and Y. Inamori A novel β-N-acetylhexosaminidase from streptomyces thermoviolaceus OPC-520: gene cloning, expression and assignment to Family 3 of the glycosyl hydrolases Appl Environ Microbiol 64 1998 2920 2924
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2920-2924
    • Tsujibo, H.1    Hatano, N.2    Mikami, T.3    Hirasawa, A.4    Miyamoto, K.5    Inamori, Y.6
  • 16
    • 0036187913 scopus 로고    scopus 로고
    • Extensive feature detection of N-terminal protein sorting signals
    • H. Bannai, Y. Tamada, O. Maruyama, K. Nakai, and S. Miyano Extensive feature detection of N-terminal protein sorting signals Bioinformatics 18 2002 298 305
    • (2002) Bioinformatics , vol.18 , pp. 298-305
    • Bannai, H.1    Tamada, Y.2    Maruyama, O.3    Nakai, K.4    Miyano, S.5
  • 17
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • H. Nielsen, J. Englebrecht, S. Brunak, and G. Heijne Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites Protein Eng 10 1997 1 6
    • (1997) Protein Eng , vol.10 , pp. 1-6
    • Nielsen, H.1    Englebrecht, J.2    Brunak, S.3    Heijne, G.4
  • 18
  • 19
    • 0023046815 scopus 로고
    • A new method for predicting signal sequence cleavage sites
    • G. von Heijne A new method for predicting signal sequence cleavage sites Nucleic Acids Res 14 1986 4683 4690
    • (1986) Nucleic Acids Res , vol.14 , pp. 4683-4690
    • Von Heijne, G.1
  • 20
    • 0029940470 scopus 로고    scopus 로고
    • Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease
    • I. Tews, A. Perrakis, A. Oppenheim, Z. Dauter, K.S. Wilson, and C.E. Vorgias Bacterial chitobiase structure provides insight into catalytic mechanism and the basis of Tay-Sachs disease Nat Struct Biol 3 1996 638 648
    • (1996) Nat Struct Biol , vol.3 , pp. 638-648
    • Tews, I.1    Perrakis, A.2    Oppenheim, A.3    Dauter, Z.4    Wilson, K.S.5    Vorgias, C.E.6
  • 21
    • 0034647424 scopus 로고    scopus 로고
    • Structures of chitobiase mutants complexed with the substrate di-N-acetyl-d-glucosamine: The catalytic role of the conserved acidic pair, Aspartate 539 and Glutamate 540
    • G. Prag, Y. Papanikolau, G. Tavlas, C.E. Vorgias, K. Petratos, and A.B. Oppenheim Structures of chitobiase mutants complexed with the substrate di-N-acetyl-d-glucosamine: the catalytic role of the conserved acidic pair, Aspartate 539 and Glutamate 540 J Mol Biol 300 2000 611 617
    • (2000) J Mol Biol , vol.300 , pp. 611-617
    • Prag, G.1    Papanikolau, Y.2    Tavlas, G.3    Vorgias, C.E.4    Petratos, K.5    Oppenheim, A.B.6
  • 22
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B. Henrissat A classification of glycosyl hydrolases based on amino-acid sequence similarities Biochem J 280 1991 309 316
    • (1991) Biochem J , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 23
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities
    • B. Henrissat, and A. Bairoch New families in the classification of glycosyl hydrolases based on amino-acid sequence similarities Biochem J 293 1993 781 788
    • (1993) Biochem J , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 24
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • G. Davies, and B. Henrissat Structures and mechanisms of glycosyl hydrolases Structure 3 1995 853 859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 25
    • 0029929874 scopus 로고    scopus 로고
    • Updating the sequence-based classification of glycosyl hydrolases
    • B. Henrissat, and A. Bairoch Updating the sequence-based classification of glycosyl hydrolases Biochem J 316 1996 695 696
    • (1996) Biochem J , vol.316 , pp. 695-696
    • Henrissat, B.1    Bairoch, A.2
  • 26
    • 0029988664 scopus 로고    scopus 로고
    • N-Acetylglucosaminidase (chitobiase) from Serratia marcescens: Gene sequence, and protein production and purification in Escherichia coli
    • I. Tews, R. Vincentelli, and C.E. Vorgias N-Acetylglucosaminidase (chitobiase) from Serratia marcescens: gene sequence, and protein production and purification in Escherichia coli Gene 170 1996 63 67
    • (1996) Gene , vol.170 , pp. 63-67
    • Tews, I.1    Vincentelli, R.2    Vorgias, C.E.3
  • 27
    • 4544264681 scopus 로고    scopus 로고
    • Purification, cloning and sequence analysis of β-N- acetylglucosaminidase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9
    • X. Lan, N. Ozawa, N. Nishiwaki, R. Kodaira, M. Okazaki, and M. Shimosaka Purification, cloning and sequence analysis of β-N-acetylglucosaminidase from the chitinolytic bacterium Aeromonas hydrophila strain SUWA-9 Biosci Biotechnol Biochem 68 2004 1082 1090
    • (2004) Biosci Biotechnol Biochem , vol.68 , pp. 1082-1090
    • Lan, X.1    Ozawa, N.2    Nishiwaki, N.3    Kodaira, R.4    Okazaki, M.5    Shimosaka, M.6
  • 28
    • 0024962415 scopus 로고
    • N,N′-Diacetylchitobiase of Vibrio harveyi primary structure, processing and evolutionary relationships
    • R.W. Soto-Gil, and J.W. Zyskind N,N′-Diacetylchitobiase of Vibrio harveyi primary structure, processing and evolutionary relationships J Biol Chem 264 1989 14778 14783
    • (1989) J Biol Chem , vol.264 , pp. 14778-14783
    • Soto-Gil, R.W.1    Zyskind, J.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.