메뉴 건너뛰기




Volumn 67, Issue 2, 2003, Pages 341-346

Mutational analysis of amino acid residues involved in catalytic activity of a family 18 chitinase from tulip bulbs

Author keywords

Chitinase; Site directed mutagenesis; Tulip bulb; Tulipa bakeri

Indexed keywords

AMINO ACID; CHITIN; CHITINASE; DRUG DERIVATIVE; GLYCOLCHITIN; HEVAMINE; LYSOZYME; PRIMER DNA; RECOMBINANT PROTEIN; VEGETABLE PROTEIN;

EID: 0041626165     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.67.341     Document Type: Article
Times cited : (9)

References (21)
  • 1
    • 0001519173 scopus 로고
    • Plant chitinases are potent inhibitors of fungal growth
    • Schlumbaum, A., Mauxh, F., Vogeli, U., and Boiler, T., Plant chitinases are potent inhibitors of fungal growth. Nature, 324, 365-367 (1986).
    • (1986) Nature , vol.324 , pp. 365-367
    • Schlumbaum, A.1    Mauxh, F.2    Vogeli, U.3    Boiler, T.4
  • 2
    • 0342972186 scopus 로고
    • Comparison of some molecular, enzymatic, and antifungal properties of chitinases from thorn-apple, tobacco, and wheat
    • Brochaert, W. F., Van Pariji, J., Allen, A. K., and Peumans, W. J., Comparison of some molecular, enzymatic, and antifungal properties of chitinases from thorn-apple, tobacco, and wheat. Physiol. Mol. Plant Pathol., 33, 319-331 (1988).
    • (1988) Physiol. Mol. Plant Pathol. , vol.33 , pp. 319-331
    • Brochaert, W.F.1    Van Pariji, J.2    Allen, A.K.3    Peumans, W.J.4
  • 4
    • 0027225980 scopus 로고
    • New families in the classification of glycosyl hydrolases based on amino acid sequence similarities
    • Henrissat, B., and Bairoch, A., New families in the classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem. J., 293, 781-788 (1993).
    • (1993) Biochem. J. , vol.293 , pp. 781-788
    • Henrissat, B.1    Bairoch, A.2
  • 5
    • 0031299672 scopus 로고    scopus 로고
    • Purification and characterization of two chitinase isoforms from the bulbs of gladiolus (Gladiolus gandavensis)
    • Yamagami, T., Mine, Y., Aso, Y., and Ishiguro, M., Purification and characterization of two chitinase isoforms from the bulbs of gladiolus (Gladiolus gandavensis). Biosci. Biotechnol. Biochem., 61, 2140-2142 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 2140-2142
    • Yamagami, T.1    Mine, Y.2    Aso, Y.3    Ishiguro, M.4
  • 6
    • 0032013706 scopus 로고    scopus 로고
    • Isolation and characterization of chitinase isoforms from the bulbs of four species of the genus
    • Yamagami, T., Taira, T., Aso, Y., and Ishiguro, M., Isolation and characterization of chitinase isoforms from the bulbs of four species of the genus Tulipa. Biosci. Biotechnol. Biochem., 62, 584-587 (1998).
    • (1998) Tulipa. Biosci. Biotechnol. Biochem. , vol.62 , pp. 584-587
    • Yamagami, T.1    Taira, T.2    Aso, Y.3    Ishiguro, M.4
  • 7
    • 0031989683 scopus 로고    scopus 로고
    • Complete amino acid sequence of chitinase-a from bulbs of gladiolus (Gladiolus gandavensis)
    • Yamagami, T., Mine, Y., and Ishiguro, M., Complete amino acid sequence of chitinase-a from bulbs of gladiolus (Gladiolus gandavensis). Biosci. Biotechnol. Biochem., 62, 386-389 (1998).
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 386-389
    • Yamagami, T.1    Mine, Y.2    Ishiguro, M.3
  • 8
    • 0032087899 scopus 로고    scopus 로고
    • Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus
    • Yamagami, T., and Ishiguro, M., Complete amino acid sequences of chitinase-1 and -2 from bulbs of genus Tulipa. Biosci. Biotechnol. Biochem., 62, 1253-1257 (1998).
    • (1998) Tulipa. Biosci. Biotechnol. Biochem. , vol.62 , pp. 1253-1257
    • Yamagami, T.1    Ishiguro, M.2
  • 9
    • 85007797432 scopus 로고
    • The complete amino acid sequence of chitinase-B from the leaves of pokeweed (Phytolacca americana)
    • Tanigawa, M., Yamagami, T., and Funatsu, G., The complete amino acid sequence of chitinase-B from the leaves of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem., 59, 841-847 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 841-847
    • Tanigawa, M.1    Yamagami, T.2    Funatsu, G.3
  • 10
    • 0025739769 scopus 로고
    • The primary structure of hevamine, an enzyme with lysozyme /chitinase activity from Hevea brasiliensis
    • Jeckel, P. A., Hartmann, J. B. H., and Beintema, J. J., The primary structure of hevamine, an enzyme with lysozyme /chitinase activity from Hevea brasiliensis. Eur. J. Biochem., 200, 123-130 (1991).
    • (1991) Eur. J. Biochem. , vol.200 , pp. 123-130
    • Jeckel, P.A.1    Hartmann, J.B.H.2    Beintema, J.J.3
  • 11
    • 0029278071 scopus 로고
    • Purification and characterization of two chitinases from the leaves of pokeweed (Phytolacca americana)
    • Ohta, M., Yamagami, T., and Funatsu, G., Purification and characterization of two chitinases from the leaves of pokeweed (Phytolacca americana). Biosci. Biotechnol. Biochem., 59, 656-661 (1995).
    • (1995) Biosci. Biotechnol. Biochem. , vol.59 , pp. 656-661
    • Ohta, M.1    Yamagami, T.2    Funatsu, G.3
  • 12
    • 0034222241 scopus 로고    scopus 로고
    • Cloning, sequencing, and expression of the tulip bulb chitinase-1 cDNA
    • Yamagami, T., Tsutsumi, K., and Ishiguro, M., Cloning, sequencing, and expression of the tulip bulb chitinase-1 cDNA. Biosci. Biotechnol. Biochem., 64, 1394-1401 (2000).
    • (2000) Biosci. Biotechnol. Biochem. , vol.64 , pp. 1394-1401
    • Yamagami, T.1    Tsutsumi, K.2    Ishiguro, M.3
  • 13
    • 78651143374 scopus 로고
    • The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular weight substrates for lysozyme
    • Rupley, J. A., The hydrolysis of chitin by concentrated hydrochloric acid, and the preparation of low-molecular weight substrates for lysozyme. Biochim. Biophys. Acta, 83, 245-255 (1964).
    • (1964) Biochim. Biophys. Acta , vol.83 , pp. 245-255
    • Rupley, J.A.1
  • 14
    • 19544381690 scopus 로고
    • A simple activity measurement of lysozyme
    • Imoto, T., and Yagishita, K., A simple activity measurement of lysozyme. Agric. Biol. Chem., 35, 1154-1156 (1971).
    • (1971) Agric. Biol. Chem. , vol.35 , pp. 1154-1156
    • Imoto, T.1    Yagishita, K.2
  • 15
    • 36749110571 scopus 로고
    • A computer simulation method for the calculation of equilibrium constants for the formation of physical clusters of molecules: Application to small water clusters
    • Swope, W. C., Anderson, H. C., Berens, P. H., and Wilson, K. R., A computer simulation method for the calculation of equilibrium constants for the formation of physical clusters of molecules: application to small water clusters. J. Chem. Phys., 76, 637-649 (1982).
    • (1982) J. Chem. Phys. , vol.76 , pp. 637-649
    • Swope, W.C.1    Erson, H.C.2    Berens, P.H.3    Wilson, K.R.4
  • 17
    • 0028774705 scopus 로고
    • Crystal structures of hevamine: A plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor
    • Terwisscha van Scheltinga, A. C., Kalk, K. H., Beintema, J. J., and Dijkstra, B. W., Crystal structures of hevamine: a plant defense protein with chitinase and lysozyme activity, and its complex with an inhibitor. Structure, 2, 1181-1189 (1994).
    • (1994) Structure , vol.2 , pp. 1181-1189
    • Terwisscha Van Scheltinga, A.C.1    Kalk, K.H.2    Beintema, J.J.3    Dijkstra, B.W.4
  • 18
    • 0028828695 scopus 로고
    • Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: Evidence for substrate assisted catalysis
    • Terwisscha van Scheltinga, A. C., Armand, S., Kalk, K. H., Isogai, A., Henrissat, B., and Dijkstra, B. W., Stereochemistry of chitin hydrolysis by a plant chitinase/lysozyme and X-ray structure of a complex with allosamidin: evidence for substrate assisted catalysis. Biochemistry, 34, 15619-15623 (1995).
    • (1995) Biochemistry , vol.34 , pp. 15619-15623
    • Terwisscha Van Scheltinga, A.C.1    Armand, S.2    Kalk, K.H.3    Isogai, A.4    Henrissat, B.5    Dijkstra, B.W.6
  • 19
    • 0034236249 scopus 로고    scopus 로고
    • Chitinolytic enzymes: Catalysis, substrate binding, and their application
    • Fukamizo, T., Chitinolytic enzymes: catalysis, substrate binding, and their application. Curr. Proteins Peptide Sci., 1, 105-124 (2000).
    • (2000) Curr. Proteins Peptide Sci. , vol.1 , pp. 105-124
    • Fukamizo, T.1
  • 20
    • 0005795835 scopus 로고    scopus 로고
    • Involvements of Trp23 in the chitin-binding and of Trp131 in the chitinase activity of rye seed chitinase-a
    • Yamagami, T., and Funatsu, G., Involvements of Trp23 in the chitin-binding and of Trp131 in the chitinase activity of rye seed chitinase-a. Biosci. Biotechnol. Biochem., 61, 1819-1825 (1997).
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 1819-1825
    • Yamagami, T.1    Funatsu, G.2
  • 21
    • 0015217634 scopus 로고
    • The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions
    • Nozaki, Y., and Tanford, C., The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. J. Biol. Chem., 246, 2211-2217 (1971)
    • (1971) J. Biol. Chem. , vol.246 , pp. 2211-2217
    • Nozaki, Y.1    Tanford, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.