메뉴 건너뛰기




Volumn 336, Issue 2, 2005, Pages 514-520

Purification and characterization of a chitinase from Amycolatopsis orientalis with N-acetyllactosamine-repeating unit releasing activity

Author keywords

Chitinase; Glycosides; Glycosyl hydrolase; Kinetics; N Acetyllactosamine

Indexed keywords

AMMONIUM SULFATE; CHITINASE; CHROMOGENIC SUBSTRATE; NITROPHENOL; OLIGOSACCHARIDE;

EID: 24644432576     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.123     Document Type: Article
Times cited : (9)

References (31)
  • 1
    • 0028566913 scopus 로고
    • Human serum contains a chitinase: Identification of an enzyme, formerly described as 4-methylumberyferyl-tetra-N-acetylchitotorioside hydrolase (MU-TACT hydrolase)
    • B. Overdijk, and G.J. Van Steijn Human serum contains a chitinase: identification of an enzyme, formerly described as 4-methylumberyferyl-tetra-N- acetylchitotorioside hydrolase (MU-TACT hydrolase) Glycobiology 4 1994 797 803
    • (1994) Glycobiology , vol.4 , pp. 797-803
    • Overdijk, B.1    Van Steijn, G.J.2
  • 2
    • 0028911536 scopus 로고
    • Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins
    • G.H. Renkema, R.F. Boot, A.O. Muijsers, W.E. Donker-Koopman, and J.M.F.G. Aerts Purification and characterization of human chitotriosidase, a novel member of the chitinase family of proteins J. Biol. Chem. 270 1995 2198 2202
    • (1995) J. Biol. Chem. , vol.270 , pp. 2198-2202
    • Renkema, G.H.1    Boot, R.F.2    Muijsers, A.O.3    Donker-Koopman, W.E.4    Aerts, J.M.F.G.5
  • 3
    • 0028822746 scopus 로고
    • Chitinase activity in human serum and leukocytes
    • G.M. Escott, and D.J. Adams Chitinase activity in human serum and leukocytes Infect. Immun. 63 1995 4770 4773
    • (1995) Infect. Immun. , vol.63 , pp. 4770-4773
    • Escott, G.M.1    Adams, D.J.2
  • 5
    • 0031585572 scopus 로고    scopus 로고
    • Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encodes chitinase and cathepsin genes
    • R.E. Hawtin, T. Zarkowska, K. Arnold, C.J. Thomas, G.W. Gooday, L.A. King, J.A. Kuzio, and R.D. Possee Liquefaction of Autographa californica nucleopolyhedrovirus-infected insects is dependent on the integrity of virus-encodes chitinase and cathepsin genes Virology 238 1997 243 253
    • (1997) Virology , vol.238 , pp. 243-253
    • Hawtin, R.E.1    Zarkowska, T.2    Arnold, K.3    Thomas, C.J.4    Gooday, G.W.5    King, L.A.6    Kuzio, J.A.7    Possee, R.D.8
  • 8
    • 0029854392 scopus 로고    scopus 로고
    • Chitinase levels in guinea pig blood are increased after systemic infection with Aspergillus fumigatus
    • B. Overdijk, G.J. Van Steiji, and F.C. Odds Chitinase levels in guinea pig blood are increased after systemic infection with Aspergillus fumigatus Glycobiology 6 1996 627 634
    • (1996) Glycobiology , vol.6 , pp. 627-634
    • Overdijk, B.1    Van Steiji, G.J.2    Odds, F.C.3
  • 10
    • 0028220472 scopus 로고
    • Marked elevation of plasma chitotriosidase activity, a novel hallmark of Gaucher disease
    • C.E.M. Hollak, S. van Weely, M.H.J. van Oers, and J.M.F.G. Aerts Marked elevation of plasma chitotriosidase activity, a novel hallmark of Gaucher disease J. Clin. Invest. 93 1994 1288 1292
    • (1994) J. Clin. Invest. , vol.93 , pp. 1288-1292
    • Hollak, C.E.M.1    Van Weely, S.2    Van Oers, M.H.J.3    Aerts, J.M.F.G.4
  • 12
    • 0027225980 scopus 로고
    • New families in classification of glycosyl hydrolases based on amino acid sequence similarities
    • B. Henrissat, and A. Bairoch New families in 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
  • 13
    • 0000122560 scopus 로고
    • Properties and transglycosylation reaction of a chitinase from Nocardia orientalis
    • F. Nanjo, K. Sakai, M. Ishikawa, K. Isobe, and T. Usui Properties and transglycosylation reaction of a chitinase from Nocardia orientalis Agric. Biol. Chem. 53 1989 2189 2195
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2189-2195
    • Nanjo, F.1    Sakai, K.2    Ishikawa, M.3    Isobe, K.4    Usui, T.5
  • 14
    • 0001330973 scopus 로고
    • Purification, properties, and transglycosylation reaction of β-N-acetylhexosaminidase from Nocardia orientalis
    • F. Nanjo, M. Ishikawa, R. Katsumi, and K. Sakai Purification, properties, and transglycosylation reaction of β-N-acetylhexosaminidase from Nocardia orientalis Agric. Biol. Chem. 54 1990 899 906
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 899-906
    • Nanjo, F.1    Ishikawa, M.2    Katsumi, R.3    Sakai, K.4
  • 15
    • 0025329913 scopus 로고
    • Purification and characterization of exo-β-d-glucosaminidase, a novel type of enzyme, from Nocardia orientalis
    • F. Nanjo, R. Katsumi, and K. Sakai Purification and characterization of exo-β-d-glucosaminidase, a novel type of enzyme, from Nocardia orientalis J. Biol. Chem. 256 1990 10088 10094
    • (1990) J. Biol. Chem. , vol.256 , pp. 10088-10094
    • Nanjo, F.1    Katsumi, R.2    Sakai, K.3
  • 16
    • 0023137199 scopus 로고
    • Transglycosylation reaction of a chitinase purified from Nocardia orientalis
    • T. Usui, Y. Hayashi, F. Nanjo, K. Sakai, and Y. Ishido Transglycosylation reaction of a chitinase purified from Nocardia orientalis Biochim. Biophys. Acta 923 1987 302 309
    • (1987) Biochim. Biophys. Acta , vol.923 , pp. 302-309
    • Usui, T.1    Hayashi, Y.2    Nanjo, F.3    Sakai, K.4    Ishido, Y.5
  • 17
    • 0025471599 scopus 로고
    • Enzymatic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate
    • T. Usui, H. Matsui, and K. Isobe Enzymatic synthesis of useful chito-oligosaccharides utilizing transglycosylation by chitinolytic enzymes in a buffer containing ammonium sulfate Carbohydr. Res. 203 1990 65 77
    • (1990) Carbohydr. Res. , vol.203 , pp. 65-77
    • Usui, T.1    Matsui, H.2    Isobe, K.3
  • 18
  • 19
    • 0030913877 scopus 로고    scopus 로고
    • Enzymic synthesis of 3′-O- and 6′-O-N-acetylglucosaminyl-N- acetyllactosaminide glycosides catalyzed by β-N-acetyl-d-hexosaminidase from Nocardia orientalis
    • T. Murata, A. Tashiro, T. Itoh, and T. Usui Enzymic synthesis of 3′-O- and 6′-O-N-acetylglucosaminyl-N-acetyllactosaminide glycosides catalyzed by β-N-acetyl-d-hexosaminidase from Nocardia orientalis Biochim. Biophys. Acta 1335 1997 326 334
    • (1997) Biochim. Biophys. Acta , vol.1335 , pp. 326-334
    • Murata, T.1    Tashiro, A.2    Itoh, T.3    Usui, T.4
  • 20
    • 0031825608 scopus 로고    scopus 로고
    • 2-p as a carbohydrate unit of mucin-type 2 core
    • 2-p as a carbohydrate unit of mucin-type 2 core Glycoconjug. J. 15 1998 575 582
    • (1998) Glycoconjug. J. , vol.15 , pp. 575-582
    • Murata, T.1    Itoh, T.2    Usui, T.3
  • 21
    • 0141558968 scopus 로고    scopus 로고
    • Kinetic studies of endo-β-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosamine-repeating oligosaccharide β-glycosides using its transglycosylation activity
    • T. Murata, T. Hattori, S. Amarume, A. Koichi, and T. Usui Kinetic studies of endo-β-galactosidase by a novel colorimetric assay and synthesis of N-acetyllactosamine-repeating oligosaccharide β-glycosides using its transglycosylation activity Eur. J. Biochem. 270 2003 3709 3719
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3709-3719
    • Murata, T.1    Hattori, T.2    Amarume, S.3    Koichi, A.4    Usui, T.5
  • 24
    • 0027607298 scopus 로고
    • A convenient synthesis of β-d-galactosyl disaccharide derivatives using the β-d-galactosidase from Bacillus circulans
    • T. Usui, S. Kubota, and H. Ohi A convenient synthesis of β-d-galactosyl disaccharide derivatives using the β-d-galactosidase from Bacillus circulans Carbohydr. Res. 244 1993 315 323
    • (1993) Carbohydr. Res. , vol.244 , pp. 315-323
    • Usui, T.1    Kubota, S.2    Ohi, H.3
  • 25
    • 0031178553 scopus 로고    scopus 로고
    • Galactosyl transfer onto p-nitrophenyl β-d-glucoside using β-d-galactosidase from Bacillus circulans
    • T. Murata, S. Akimoto, M. Horimoto, and T. Usui Galactosyl transfer onto p-nitrophenyl β-d-glucoside using β-d-galactosidase from Bacillus circulans Biosci. Biotechnol. Biochem. 61 1997 1118 1120
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1118-1120
    • Murata, T.1    Akimoto, S.2    Horimoto, M.3    Usui, T.4
  • 26
    • 0001378427 scopus 로고
    • Enzymatic synthesis of N-acetyllactosamine and N-acetylallolactosamine by the use of β-d-galactosidase
    • K. Sakai, R. Kastumi, H. Ohi, T. Usui, and Y. Ishido Enzymatic synthesis of N-acetyllactosamine and N-acetylallolactosamine by the use of β-d-galactosidase J. Carbohydr. Chem. 11 1992 553 565
    • (1992) J. Carbohydr. Chem. , vol.11 , pp. 553-565
    • Sakai, K.1    Kastumi, R.2    Ohi, H.3    Usui, T.4    Ishido, Y.5
  • 27
    • 9744227158 scopus 로고    scopus 로고
    • Differential recognition of animal type β-4-galactosylated and α3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum
    • H. Boer, N. Munck, J. Natunen, G. Wohlfahrt, H. Söderlund, O. Renkonen, and A. Koivula Differential recognition of animal type β-4-galactosylated and α3-fucosylated chito-oligosaccharides by two family 18 chitinases from Trichoderma harzianum Glycobiology 14 2004 1303 1313
    • (2004) Glycobiology , vol.14 , pp. 1303-1313
    • Boer, H.1    Munck, N.2    Natunen, J.3    Wohlfahrt, G.4    Söderlund, H.5    Renkonen, O.6    Koivula, A.7
  • 29
    • 0036232796 scopus 로고    scopus 로고
    • Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes
    • C. Sasaki, A. Yokoyama, Y. Itoh, M. Hashimoto, T. Watanabe, and T. Fukamizo Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes J. Biochem. 131 2002 557 564
    • (2002) J. Biochem. , vol.131 , pp. 557-564
    • Sasaki, C.1    Yokoyama, A.2    Itoh, Y.3    Hashimoto, M.4    Watanabe, T.5    Fukamizo, T.6
  • 31
    • 0034617366 scopus 로고    scopus 로고
    • Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides
    • Y. Honda, S. Tanimoto, M. Kirihara, S. Kaneko, K. Tokuyasu, M. Hashimoto, T. Watanabe, and T. Fukamizo Kinetic analysis of the reaction catalyzed by chitinase A1 from Bacillus circulans WL-12 toward the novel substrates, partially N-deacetylated 4-methylumbelliferyl chitobiosides FEBS Lett. 476 2000 194 197
    • (2000) FEBS Lett. , vol.476 , pp. 194-197
    • Honda, Y.1    Tanimoto, S.2    Kirihara, M.3    Kaneko, S.4    Tokuyasu, K.5    Hashimoto, M.6    Watanabe, T.7    Fukamizo, T.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.