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Volumn 376, Issue 1, 2003, Pages 237-244

Aromatic residues within the substrate-binding cleft of Bacillus circulans chitinase A1 are essential for hydrolysis of crystalline chitin

Author keywords

Aromatic amino acid; Catalytic domain; Crystalline chitin hydrolysis; Site directed mutagenesis; Substrate binding cleft

Indexed keywords

AROMATIC COMPOUNDS; CATALYSIS; COLLOIDS; CRYSTALLINE MATERIALS; ENZYMES; HYDROLYSIS; MUTAGENESIS;

EID: 0344825227     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030419     Document Type: Article
Times cited : (106)

References (29)
  • 1
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. (1991) A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 280, 309-316
    • (1991) Biochem. J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 2
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B. and Bairoch, A. (1993) New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J. 293, 781-788
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 3
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies, G. and Henrissat, B. (1995) Structures and mechanisms of glycosyl hydrolases. Structure 3, 853-859
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 4
    • 0029835188 scopus 로고    scopus 로고
    • A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037
    • Ohno, T., Armand, S., Hata, T., Nikaidou, N., Henrissat, B., Mitsutomi, M. and Watanabe, T. (1996) A modular family 19 chitinase found in the prokaryotic organism Streptomyces griseus HUT 6037. J. Bacteriol. 178, 5065-5070
    • (1996) J. Bacteriol. , vol.178 , pp. 5065-5070
    • Ohno, T.1    Armand, S.2    Hata, T.3    Nikaidou, N.4    Henrissat, B.5    Mitsutomi, M.6    Watanabe, T.7
  • 6
    • 0033229842 scopus 로고    scopus 로고
    • Third chitinase gene (chiC) of Serratia marcescens 2170 and relationship of its product to other bacterial chitinases
    • Suzuki, K., Taiyoji, M., Sugawara, N., Nikaidou, N., Henrissat, B. and Watanabe, T. (1999) Third chitinase gene (chiC) of Serratia marcescens 2170 and relationship of its product to other bacterial chitinases. Biochem. J. 343, 587-596
    • (1999) Biochem. J. , vol.343 , pp. 587-596
    • Suzuki, K.1    Taiyoji, M.2    Sugawara, N.3    Nikaidou, N.4    Henrissat, B.5    Watanabe, T.6
  • 9
    • 0007151227 scopus 로고    scopus 로고
    • Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution
    • Matsumoto, T., Nonaka, T., Hashimoto, M., Watanabe, T. and Mitsui, Y. (1999) Three-dimensional structure of the catalytic domain of chitinase A1 from Bacillus circulans WL-12 at a very high resolution. Proc. Jpn. Acad. 75, 269-274
    • (1999) Proc. Jpn. Acad. , vol.75 , pp. 269-274
    • Matsumoto, T.1    Nonaka, T.2    Hashimoto, M.3    Watanabe, T.4    Mitsui, Y.5
  • 10
    • 9444272215 scopus 로고    scopus 로고
    • Three chitinase genes (chiA, chiC and chiD) comprise the chitinase system of Bacillus circulans WL-12
    • Alam, M. M., Mizutani, M., Isono, T., Nikaidou, N. and Watanabe, T. (1996) Three chitinase genes (chiA, chiC and chiD) comprise the chitinase system of Bacillus circulans WL-12. J. Ferment. Bioeng. 82, 28-36
    • (1996) J. Ferment. Bioeng. , vol.82 , pp. 28-36
    • Alam, M.M.1    Mizutani, M.2    Isono, T.3    Nikaidou, N.4    Watanabe, T.5
  • 11
    • 0025171327 scopus 로고
    • Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin
    • Watanabe, T., Suzuki, K., Oyanagi, W., Ohnishi, K. and Tanaka, H. (1990) Gene cloning of chitinase A1 from Bacillus circulans WL-12 revealed its evolutionary relationship to Serratia chitinase and to the type III homology units of fibronectin. J. Biol. Chem. 265, 15659-15665
    • (1990) J. Biol. Chem. , vol.265 , pp. 15659-15665
    • Watanabe, T.1    Suzuki, K.2    Oyanagi, W.3    Ohnishi, K.4    Tanaka, H.5
  • 12
    • 0027216435 scopus 로고
    • Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity
    • Watanabe, T., Kobori, K., Miyashita, K., Fujii, T., Sakai, H., Uchida, M. and Tanaka, H. (1993) Identification of glutamic acid 204 and aspartic acid 200 in chitinase A1 of Bacillus circulans WL-12 as essential residues for chitinase activity. J. Biol. Chem. 268, 18567-18572
    • (1993) J. Biol. Chem. , vol.268 , pp. 18567-18572
    • Watanabe, T.1    Kobori, K.2    Miyashita, K.3    Fujii, T.4    Sakai, H.5    Uchida, M.6    Tanaka, H.7
  • 13
    • 0034608015 scopus 로고    scopus 로고
    • Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1
    • Ikegami, T., Okada, T., Hashimoto, M., Seino, S., Walanabe, T. and Shirakawa, M. (2000) Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1. J. Biol. Chem. 275, 13654-13661
    • (2000) J. Biol. Chem. , vol.275 , pp. 13654-13661
    • Ikegami, T.1    Okada, T.2    Hashimoto, M.3    Seino, S.4    Walanabe, T.5    Shirakawa, M.6
  • 15
    • 0035815378 scopus 로고    scopus 로고
    • Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline-chitin hydrolysis by Bacillus circulans chitinase A1
    • Watanabe, T., Ishibashi, A., Ariga, Y., Hashimoto, M., Nikaidou, N., Sugiyama, J., Matsumoto, T. and Nonaka, T. (2001) Trp122 and Trp134 on the surface of the catalytic domain are essential for crystalline-chitin hydrolysis by Bacillus circulans chitinase A1. FEBS Lett. 494, 74-78
    • (2001) FEBS Lett. , vol.494 , pp. 74-78
    • Watanabe, T.1    Ishibashi, A.2    Ariga, Y.3    Hashimoto, M.4    Nikaidou, N.5    Sugiyama, J.6    Matsumoto, T.7    Nonaka, T.8
  • 16
    • 0035798612 scopus 로고    scopus 로고
    • Roles of the exposed aromatic residues in crystalline-chitin hydrolysis by chitinase a from Serratia marcescens 2170
    • Uchiyama, T., Katouno, F., Nikaidou, N., Nonaka, T., Sugiyama, J. and Watanabe, T. (2001) Roles of the exposed aromatic residues in crystalline-chitin hydrolysis by chitinase A from Serratia marcescens 2170. J. Biol. Chem. 276, 41343-41349
    • (2001) J. Biol. Chem. , vol.276 , pp. 41343-41349
    • Uchiyama, T.1    Katouno, F.2    Nikaidou, N.3    Nonaka, T.4    Sugiyama, J.5    Watanabe, T.6
  • 18
    • 0019883721 scopus 로고
    • A convenient synthesis of glycol chitin, a substrate of lysozyme
    • Yamada, H. and Imoto, T. (1981) A convenient synthesis of glycol chitin, a substrate of lysozyme. Carbohydr. Res. 92, 160-162
    • (1981) Carbohydr. Res. , vol.92 , pp. 160-162
    • Yamada, H.1    Imoto, T.2
  • 20
  • 21
    • 0023028051 scopus 로고
    • A genetic approach to analyzing membrane protein topology
    • Manoil, C. and Beckwith, J. (1986) A genetic approach to analyzing membrane protein topology. Science 233, 1403-1408
    • (1986) Science , vol.233 , pp. 1403-1408
    • Manoil, C.1    Beckwith, J.2
  • 22
    • 0031602025 scopus 로고    scopus 로고
    • Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170
    • Suzuki, K., Suzuki, M., Taiyoji, M., Nikaidou, N. and Watanabe, T. (1998) Chitin binding protein (CBP21) in the culture supernatant of Serratia marcescens 2170. Biosci. Biotechnol. Biochem. 62, 128-135
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 128-135
    • Suzuki, K.1    Suzuki, M.2    Taiyoji, M.3    Nikaidou, N.4    Watanabe, T.5
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227, 680-685
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T. and Yagishita, K. (1971) A simple activity measurement of lysozyme. Agr. Biol. Chem. 35, 1154-1156
    • (1971) Agr. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 25
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • Pace, C. N., Vajdos, F., Fee, L., Grimsley, G. and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4, 2411-2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 26
    • 0037116594 scopus 로고    scopus 로고
    • Directional degradation of β-chitin by chitinase A1 revealed by a novel reducing end labelling technique
    • Imai, T., Watanabe, T., Yui, Y. and Sugiyama, J. (2002) Directional degradation of β-chitin by chitinase A1 revealed by a novel reducing end labelling technique. FEBS Lett. 510, 201-205
    • (2002) FEBS Lett. , vol.510 , pp. 201-205
    • Imai, T.1    Watanabe, T.2    Yui, Y.3    Sugiyama, J.4
  • 27
    • 0036232796 scopus 로고    scopus 로고
    • Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes
    • Sasaki, C., Yokoyama, A., Itoh, Y., Hashimoto, M., Watanabe, T. and Fukamizo, T. (2002) Comparative study of the reaction mechanism of family 18 chitinases from plants and microbes. J. Biochem. 131, 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
  • 28
    • 0036186885 scopus 로고    scopus 로고
    • Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis
    • Bokma, E., Rozeboom, H. J., Sibbald, M., Dijkstra, B. W. and Beintema, J. J. (2002) Expression and characterization of active site mutants of hevamine, a chitinase from the rubber tree Hevea brasiliensis. Eur. J. Biochem. 269, 893-901
    • (2002) Eur. J. Biochem. , vol.269 , pp. 893-901
    • Bokma, E.1    Rozeboom, H.J.2    Sibbald, M.3    Dijkstra, B.W.4    Beintema, J.J.5
  • 29
    • 0035949643 scopus 로고    scopus 로고
    • High resolution structural analyses of mutant chitinase a complexes with substrates provide new insight into the mechanism of catalysis
    • Papanikolau, Y., Gali, P., Tavlas, G., Vorgias, C. E., Oppenheim, A. B. and Petratos, K. (2001) High resolution structural analyses of mutant chitinase A complexes with substrates provide new insight into the mechanism of catalysis. Biochemistry 40, 11338-11343
    • (2001) Biochemistry , vol.40 , pp. 11338-11343
    • Papanikolau, Y.1    Gali, P.2    Tavlas, G.3    Vorgias, C.E.4    Oppenheim, A.B.5    Petratos, K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.