메뉴 건너뛰기




Volumn 136, Issue 4, 2004, Pages 485-493

Bare-faced curassow lysozyme carrying amino acid substitutions at subsites E and F shows a change in activity against chitooligosaccharide caused by a local conformational change

Author keywords

Amino acid sequence; Bare faced curassow; Lysozyme; Molecular dynamics

Indexed keywords

BARE FACED CURASSOW LYSOZYME; LYSOZYME; N ACETYLGLUCOSAMINE; OLIGOSACCHARIDE; UNCLASSIFIED DRUG;

EID: 13644254584     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/jb/mvh148     Document Type: Article
Times cited : (4)

References (36)
  • 1
    • 0000385093 scopus 로고
    • The amino acid sequence of egg white lysozyme
    • Canfield, R.E. (1963) The amino acid sequence of egg white lysozyme. J. Biol. Chem. 238, 2698-2707
    • (1963) J. Biol. Chem. , vol.238 , pp. 2698-2707
    • Canfield, R.E.1
  • 2
    • 0000676684 scopus 로고
    • La structure chimique du lysozyme de blanc d'oeuf de poule: Etude detaillee
    • Jollès, J., Jauregui-Adell, J., Bernier, I., and Jollès, P. (1963) La structure chimique du lysozyme de blanc d'oeuf de poule: etude detaillee. Biochim. Biophys. Acta 78, 668-689
    • (1963) Biochim. Biophys. Acta , vol.78 , pp. 668-689
    • Jollès, J.1    Jauregui-Adell, J.2    Bernier, I.3    Jollès, P.4
  • 3
    • 0019143031 scopus 로고
    • Exons encode functional and structural units of chicken lysozyme
    • Jung, A., Sippel, A.E., Grez, M., and Schutz, G. (1980) Exons encode functional and structural units of chicken lysozyme. Proc. Natl Acad. Sci. USA 77, 5759-5763
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 5759-5763
    • Jung, A.1    Sippel, A.E.2    Grez, M.3    Schutz, G.4
  • 4
    • 0018570657 scopus 로고
    • X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme
    • Kelly, J.A., Sielecki, A.R., Sykes, B.D., James, M.N.G., and Phillips, D.C. (1979) X-ray crystallography of the binding of the bacterial cell wall trisaccharide NAM-NAG-NAM to lysozyme. Nature 282, 875-878
    • (1979) Nature , vol.282 , pp. 875-878
    • Kelly, J.A.1    Sielecki, A.R.2    Sykes, B.D.3    James, M.N.G.4    Phillips, D.C.5
  • 5
    • 0019874706 scopus 로고
    • Prediction of the three-dimensional structures of complexes of lysozyme with cell wall substrates
    • Pincus, M.R. and Scheraga, H.A. (1981) Prediction of the three-dimensional structures of complexes of lysozyme with cell wall substrates. Biochemistry 20, 3960-3965
    • (1981) Biochemistry , vol.20 , pp. 3960-3965
    • Pincus, M.R.1    Scheraga, H.A.2
  • 7
    • 0030856556 scopus 로고    scopus 로고
    • A covalent enzyme-substrate adduct in a mutant hen egg white lysozyme (D52E)
    • Kuroki, R., Ito, Y., Kato, Y., and Imoto, T. (1997) A covalent enzyme-substrate adduct in a mutant hen egg white lysozyme (D52E). J. Biol. Chem. 272, 19976-19981
    • (1997) J. Biol. Chem. , vol.272 , pp. 19976-19981
    • Kuroki, R.1    Ito, Y.2    Kato, Y.3    Imoto, T.4
  • 10
    • 0014593661 scopus 로고
    • The identification of aspartic acid residue 52 as being critical to lysozyme activity
    • Parsons, S.M. and Raftery, M.A. (1969) The identification of aspartic acid residue 52 as being critical to lysozyme activity. Biochemistry 8, 4199-4205
    • (1969) Biochemistry , vol.8 , pp. 4199-4205
    • Parsons, S.M.1    Raftery, M.A.2
  • 11
    • 0020492207 scopus 로고
    • Modification of catalytic groups in lysozyme with ethylenimine
    • Yamada, H., Imoto, T., and Noshita, G. (1982) Modification of catalytic groups in lysozyme with ethylenimine. Biochemistry 21, 2187-2192
    • (1982) Biochemistry , vol.21 , pp. 2187-2192
    • Yamada, H.1    Imoto, T.2    Noshita, G.3
  • 12
    • 0023001194 scopus 로고
    • Chemical mutations of the catalytic carboxyl groups in lysozyme to the corresponding amides
    • Kuroki, R., Yamada, H., Moriyama, T., and Imoto, T. (1986) Chemical mutations of the catalytic carboxyl groups in lysozyme to the corresponding amides. J. Biol. Chem. 261, 13571-13574
    • (1986) J. Biol. Chem. , vol.261 , pp. 13571-13574
    • Kuroki, R.1    Yamada, H.2    Moriyama, T.3    Imoto, T.4
  • 13
    • 0021772148 scopus 로고
    • Local effects of amino acid substitutions on the active site region of lysozyme: A comparison of physical and immunological results
    • Hornbeck, P.V. and Wilson, A.C. (1984) Local effects of amino acid substitutions on the active site region of lysozyme: a comparison of physical and immunological results. Biochemistry 23, 998-1002
    • (1984) Biochemistry , vol.23 , pp. 998-1002
    • Hornbeck, P.V.1    Wilson, A.C.2
  • 14
    • 0014967237 scopus 로고
    • Studies on the acceptor specificity of the lysozyme-catalyzed transglycosylation reaction
    • Pollock, J.J. and Sharon, N. (1970) Studies on the acceptor specificity of the lysozyme-catalyzed transglycosylation reaction. Biochemistry 9, 3913-3925
    • (1970) Biochemistry , vol.9 , pp. 3913-3925
    • Pollock, J.J.1    Sharon, N.2
  • 15
    • 0024801110 scopus 로고
    • Enhancement of transglycosylation activity of lysozyme by chemical modification
    • Fukamizo, T., Goto, S., Torikata, T., and Araki, T. (1989) Enhancement of transglycosylation activity of lysozyme by chemical modification. Agric. Biol. Chem. 53, 2641-2651
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2641-2651
    • Fukamizo, T.1    Goto, S.2    Torikata, T.3    Araki, T.4
  • 16
    • 0021772124 scopus 로고
    • Experimental identification of a theoretically predicted "left-sided" binding mode for (GlcNAc)6 in the active site of lysozyme
    • Smith-Gill, S.J., Rupley, J.A., Pincus, M.R., Carty, R.P., and Scheraga, H.A. (1984) Experimental identification of a theoretically predicted "left-sided" binding mode for (GlcNAc)6 in the active site of lysozyme. Biochemistry 23, 993-997
    • (1984) Biochemistry , vol.23 , pp. 993-997
    • Smith-Gill, S.J.1    Rupley, J.A.2    Pincus, M.R.3    Carty, R.P.4    Scheraga, H.A.5
  • 17
    • 0026490429 scopus 로고
    • Left-sided substrate binding of lysozyme: Evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme
    • Inoue, M., Yamada, H., Yasukochi, T., Miki, T., Horiuchi, T., and Imoto, T. (1992) Left-sided substrate binding of lysozyme: evidence for the involvement of asparagine-46 in the initial binding of substrate to chicken lysozyme. Biochemistry 31, 10322-10330
    • (1992) Biochemistry , vol.31 , pp. 10322-10330
    • Inoue, M.1    Yamada, H.2    Yasukochi, T.3    Miki, T.4    Horiuchi, T.5    Imoto, T.6
  • 18
    • 0031991117 scopus 로고    scopus 로고
    • Reptile lysozyme: The complete amino acid sequence of soft-shelled turtle lysozyme and its activity
    • Araki, T., Yamamoto, T., and Torikata, T. (1998) Reptile lysozyme: the complete amino acid sequence of soft-shelled turtle lysozyme and its activity. Biosci. Biotechnol. Biochem. 62, 316-324
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 316-324
    • Araki, T.1    Yamamoto, T.2    Torikata, T.3
  • 19
    • 0019631734 scopus 로고
    • Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides
    • Masaki, A., Fukamizo, T., Otakara, A., Torikata, T., Hayashi, K., and Imoto, T. (1981) Estimation of rate constants in lysozyme-catalyzed reaction of chitooligosaccharides. J. Biochem. 90, 1167-1175
    • (1981) J. Biochem. , vol.90 , pp. 1167-1175
    • Masaki, A.1    Fukamizo, T.2    Otakara, A.3    Torikata, T.4    Hayashi, K.5    Imoto, T.6
  • 20
    • 0020163235 scopus 로고
    • Estimation of the free energy change of substrate binding lysozyme-catalyzed reactions
    • Kuhara, S., Ezaki, E., Fukamizo, T., and Hayashi, K. (1982) Estimation of the free energy change of substrate binding lysozyme-catalyzed reactions. J. Biochem. 92, 121-127
    • (1982) J. Biochem. , vol.92 , pp. 121-127
    • Kuhara, S.1    Ezaki, E.2    Fukamizo, T.3    Hayashi, K.4
  • 21
    • 0026613757 scopus 로고
    • 1H-NMR study on the chitotrisaccharide binding to hen egg white lysozyme
    • Fukamizo, T., Ikeda, Y., Ohkawa, T., and Goto, S. (1992) 1H-NMR study on the chitotrisaccharide binding to hen egg white lysozyme. Eur. J. Biochem. 210, 351-357
    • (1992) Eur. J. Biochem. , vol.210 , pp. 351-357
    • Fukamizo, T.1    Ikeda, Y.2    Ohkawa, T.3    Goto, S.4
  • 23
    • 0345346100 scopus 로고
    • The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins
    • Crestfield, A.M., Moore, S., and Stein, W.H. (1963) The preparation and enzymatic hydrolysis of reduced and S-carboxymethylated proteins. J. Biol. Chem. 238, 622-627
    • (1963) J. Biol. Chem. , vol.238 , pp. 622-627
    • Crestfield, A.M.1    Moore, S.2    Stein, W.H.3
  • 24
    • 0018128519 scopus 로고
    • Micro-sequence analysis of peptides and proteins using 4-NN-dimethyl-aminoazobenzene 4′-isothiocyanate/phenylisothiocyanate double coupling method
    • Chang, J.Y., Brauer, D., and Wittmann-Liebold, B. (1978) Micro-sequence analysis of peptides and proteins using 4-NN-dimethyl-aminoazobenzene 4′-isothiocyanate/phenylisothiocyanate double coupling method. FEBS Lett. 93, 205-214
    • (1978) FEBS Lett. , vol.93 , pp. 205-214
    • Chang, J.Y.1    Brauer, D.2    Wittmann-Liebold, B.3
  • 25
    • 0018634979 scopus 로고
    • Die trennung der 4-[4-(dimethylamino) phenylazo] phenylthiohydantoin- derivate des leucins und isoleucins uber polyamid-dunnschichtplatten im picomol-bereich
    • Yang, C.Y. (1979) Die trennung der 4-[4-(dimethylamino) phenylazo] phenylthiohydantoin-derivate des leucins und isoleucins uber polyamid-dunnschichtplatten im picomol-bereich. Hoppe-Seyler's Z. Physiol. Chem. 360, 1673-1675
    • (1979) Hoppe-Seyler's Z. Physiol. Chem. , vol.360 , pp. 1673-1675
    • Yang, C.Y.1
  • 27
    • 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., Andersen, H.C., Berens, P.H., and Wilson, K.R. (1982) 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) J. Chem. Phys. , vol.76 , pp. 637-649
    • Swope, W.C.1    Andersen, H.C.2    Berens, P.H.3    Wilson, K.R.4
  • 28
    • 0025490494 scopus 로고
    • The amino acid sequence of lady Amherst's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes
    • Araki, T., Kuramoto, M., and Torikata, T. (1990) The amino acid sequence of lady Amherst's pheasant (Chrysolophus amherstiae) and golden pheasant (Chrysolophus pictus) egg-white lysozymes. Agric. Biol. Chem. 54, 2299-2308
    • (1990) Agric. Biol. Chem. , vol.54 , pp. 2299-2308
    • Araki, T.1    Kuramoto, M.2    Torikata, T.3
  • 29
    • 0026185391 scopus 로고
    • The amino acid sequence of lysozyme from kalij pheasant egg-white
    • Araki, T., Kudo, K., Kuramoto, M., and Torikata, T. (1991) The amino acid sequence of lysozyme from kalij pheasant egg-white. Agric. Biol. Chem. 55, 1701-1706
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1701-1706
    • Araki, T.1    Kudo, K.2    Kuramoto, M.3    Torikata, T.4
  • 30
    • 0026182768 scopus 로고
    • The amino acid sequence of reeves' pheasant lysozyme
    • Araki, T., Kuramoto, M., and Torikata, T. (1991) The amino acid sequence of reeves' pheasant lysozyme. Agric. Biol. Chem. 55, 1707-1713
    • (1991) Agric. Biol. Chem. , vol.55 , pp. 1707-1713
    • Araki, T.1    Kuramoto, M.2    Torikata, T.3
  • 31
    • 0043117158 scopus 로고
    • The amino acid sequence of Indian peafowl (Pavo cristatus) lysozyme and its comparison with lysozymes from phasianoid birds
    • Araki, T., Kudo, K., Kuramoto, M., and Torikata, T. (1989) The amino acid sequence of Indian peafowl (Pavo cristatus) lysozyme and its comparison with lysozymes from phasianoid birds. Agric. Biol. Chem. 53, 2955-2962
    • (1989) Agric. Biol. Chem. , vol.53 , pp. 2955-2962
    • Araki, T.1    Kudo, K.2    Kuramoto, M.3    Torikata, T.4
  • 33
    • 0032174603 scopus 로고    scopus 로고
    • The amino acid sequence of monal pheasant lysozyme and its activity
    • Araki, T., Matsumoto, T., and Torikata, T. (1998) The amino acid sequence of monal pheasant lysozyme and its activity. Biosci. Biotechnol. Biochem. 62, 1988-1994
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , pp. 1988-1994
    • Araki, T.1    Matsumoto, T.2    Torikata, T.3
  • 34
    • 0017165584 scopus 로고
    • Amino acid sequence and immunological properties of chalchalaca egg white lysozyme
    • Jollès, J., Schoentgen, F., Jollès, P., Prager, E.M., and Wilson, A.C. (1976) Amino acid sequence and immunological properties of chalchalaca egg white lysozyme. J. Mol. Evol. 8, 59-78
    • (1976) J. Mol. Evol. , vol.8 , pp. 59-78
    • Jollès, J.1    Schoentgen, F.2    Jollès, P.3    Prager, E.M.4    Wilson, A.C.5
  • 35
    • 0028174858 scopus 로고
    • Functional and structural role of a tryptophan generally observed in protein-carbohydrate interaction. TRP-62 of hen egg white lysozyme
    • Maenaka, K., Kawai, G., Watanabe, K., Sunada, F., and Kumagai, I. (1994) Functional and structural role of a tryptophan generally observed in protein-carbohydrate interaction. TRP-62 of hen egg white lysozyme. J. Biol. Chem. 269, 7070-7075
    • (1994) J. Biol. Chem. , vol.269 , pp. 7070-7075
    • Maenaka, K.1    Kawai, G.2    Watanabe, K.3    Sunada, F.4    Kumagai, I.5
  • 36
    • 0033072933 scopus 로고    scopus 로고
    • Resolution and characterization of tryptophyl fluorescence of hen egg-white lysozyme by quenching- and time-resolved spectroscopy
    • Nishimoto, E., Yamashita, S., Yamasaki, N., and Imoto, T. (1999) Resolution and characterization of tryptophyl fluorescence of hen egg-white lysozyme by quenching- and time-resolved spectroscopy. Biosci. Biotechnol. Biochem. 63, 329-336
    • (1999) Biosci. Biotechnol. Biochem. , vol.63 , pp. 329-336
    • Nishimoto, E.1    Yamashita, S.2    Yamasaki, N.3    Imoto, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.