메뉴 건너뛰기




Volumn 119, Issue 1, 1996, Pages 145-150

A mutation study of catalytic residue Asp 52 in hen egg lysozyme

Author keywords

Catalytic mechanism; Expression system; Hen lysozyme; Mutagenesis; X ray analysis

Indexed keywords

ASPARTIC ACID; BETA FRUCTOFURANOSIDASE; LYSOZYME; SIGNAL PEPTIDE;

EID: 0030047236     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a021199     Document Type: Article
Times cited : (47)

References (31)
  • 1
    • 0023398206 scopus 로고
    • Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: An application to overproduction of chicken lysozyme
    • Miki, T., Yasukouchi, T., Nagatani, H., Furuno, M., Orita, T., Yamada, H., Imoto, T., and Horiuchi, T. (1987) Construction of a plasmid vector for the regulatable high level expression of eukaryotic genes in Escherichia coli: An application to overproduction of chicken lysozyme. Protein Eng. 1, 327-332
    • (1987) Protein Eng. , vol.1 , pp. 327-332
    • Miki, T.1    Yasukouchi, T.2    Nagatani, H.3    Furuno, M.4    Orita, T.5    Yamada, H.6    Imoto, T.7    Horiuchi, T.8
  • 2
    • 0001203596 scopus 로고
    • Secretion of foreign proteins from Saccharomyces cerevisiae directed by α-factor gene fusions
    • Bitter, G.A., Chen, K.K., Banks, A.R., and Lai, P.H. (1984) Secretion of foreign proteins from Saccharomyces cerevisiae directed by α-factor gene fusions. Proc. Natl. Acad. Sci. USA 81, 5330-5334
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 5330-5334
    • Bitter, G.A.1    Chen, K.K.2    Banks, A.R.3    Lai, P.H.4
  • 4
    • 0022312788 scopus 로고
    • Expression of chicken egg white lysozyme by Saccharomyces cerevisiae
    • Oberto, J. and Davison, J. (1985) Expression of chicken egg white lysozyme by Saccharomyces cerevisiae. Gene 40, 57-65
    • (1985) Gene , vol.40 , pp. 57-65
    • Oberto, J.1    Davison, J.2
  • 6
    • 0023423761 scopus 로고
    • Conversion of Trp 62 of hen egg-white lysozyme to Tyr by site-directed mutagenesis
    • Kumagai, I., Kojima, S., Tamaki, E., and Miura, K. (1987) Conversion of Trp 62 of hen egg-white lysozyme to Tyr by site-directed mutagenesis. J. Biochem. 102, 733-740
    • (1987) J. Biochem. , vol.102 , pp. 733-740
    • Kumagai, I.1    Kojima, S.2    Tamaki, E.3    Miura, K.4
  • 7
    • 0022481842 scopus 로고
    • Expression of synthetic human-lysozyme gene in Saccharomyces cerevisiae: Use of a synthetic chicken-lysozyme signal sequence for secretion and processing
    • Jigami, I., Muraki, M., Harada, N., and Tanaka, H. (1986) Expression of synthetic human-lysozyme gene in Saccharomyces cerevisiae: Use of a synthetic chicken-lysozyme signal sequence for secretion and processing. Gene 43, 273-279
    • (1986) Gene , vol.43 , pp. 273-279
    • Jigami, I.1    Muraki, M.2    Harada, N.3    Tanaka, H.4
  • 8
    • 0023548385 scopus 로고
    • Engineering of the hydrophobic segment of the signal sequence for efficient secretion of human lysozyme by Saccharomyces cerevisiae
    • Yamamoto, Y., Taniyama, Y., Kikuchi, M., and Ikehara, M. (1987) Engineering of the hydrophobic segment of the signal sequence for efficient secretion of human lysozyme by Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 149, 431-436
    • (1987) Biochem. Biophys. Res. Commun. , vol.149 , pp. 431-436
    • Yamamoto, Y.1    Taniyama, Y.2    Kikuchi, M.3    Ikehara, M.4
  • 11
    • 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
  • 15
    • 0028794520 scopus 로고
    • The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue
    • Weaver, L.H., Grutter, M.G., and Matthews, B.W. (1995) The refined structures of goose lysozyme and its complex with a bound trisaccharide show that the "goose-type" lysozymes lack a catalytic aspartate residue. J. Mol. Biol. 245, 54-68
    • (1995) J. Mol. Biol. , vol.245 , pp. 54-68
    • Weaver, L.H.1    Grutter, M.G.2    Matthews, B.W.3
  • 17
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13 mp18 and pUC 19 vector
    • Vanish-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and host strains: Nucleotide sequences of the M13 mp18 and pUC 19 vector. Gene 33, 103-119
    • (1985) Gene , vol.33 , pp. 103-119
    • Vanish-Perron, C.1    Vieira, J.2    Messing, J.3
  • 19
    • 0020565542 scopus 로고
    • An amber replication mutant of F plasmid mapped in the minimal replication region
    • Maki, S., Kuribatashi, M., Miki, T., and Horiuchi, T. (1983) An amber replication mutant of F plasmid mapped in the minimal replication region. Mol. Gen. Genet. 191, 231-237
    • (1983) Mol. Gen. Genet. , vol.191 , pp. 231-237
    • Maki, S.1    Kuribatashi, M.2    Miki, T.3    Horiuchi, T.4
  • 20
    • 0015578109 scopus 로고
    • Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae
    • Toh-e, A., Ueda, Y., Kakimoto, S., and Oshima, Y. (1973) Isolation and characterization of acid phosphatase mutants in Saccharomyces cerevisiae. J. Bacteriol. 113, 727-738
    • (1973) J. Bacteriol. , vol.113 , pp. 727-738
    • Toh-e, A.1    Ueda, Y.2    Kakimoto, S.3    Oshima, Y.4
  • 21
    • 0023397166 scopus 로고
    • Point mutation of alanine (31) to valine prohibits the folding of reduced lysozyme by sulfhydryl-disulfide interchange
    • Imoto, T., Yamada, H., Yasukochi, T., Yamada, E., Ito, Y., Ueda, T., Nagatani, H., Miki, T., and Horiuchi, T. (1987) Point mutation of alanine (31) to valine prohibits the folding of reduced lysozyme by sulfhydryl-disulfide interchange. Protein Eng. 1, 333-338
    • (1987) Protein Eng. , vol.1 , pp. 333-338
    • Imoto, T.1    Yamada, H.2    Yasukochi, T.3    Yamada, E.4    Ito, Y.5    Ueda, T.6    Nagatani, H.7    Miki, T.8    Horiuchi, T.9
  • 23
    • 0023634094 scopus 로고
    • Production of single-stranded plasmid DNA
    • Vieira, J. and Messing, J. (1987) Production of single-stranded plasmid DNA. Methods Enzymol. 153, 3-11
    • (1987) Methods Enzymol. , vol.153 , pp. 3-11
    • Vieira, J.1    Messing, J.2
  • 25
    • 0017877721 scopus 로고
    • Mapping of the resistance genes of the R plasmid NRl
    • Miki, T., Easton, A.M., and Rownd, R.H. (1978) Mapping of the resistance genes of the R plasmid NRl. Mol. Gen. Genet. 158, 217-224
    • (1978) Mol. Gen. Genet. , vol.158 , pp. 217-224
    • Miki, T.1    Easton, A.M.2    Rownd, R.H.3
  • 26
    • 0023613953 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T.A., Roberts, J.D., and Zakour, R.A. (1987) Rapid and efficient site-specific mutagenesis without phenotypic selection. Methods Enzymol. 254, 367-382
    • (1987) Methods Enzymol. , vol.254 , pp. 367-382
    • Kunkel, T.A.1    Roberts, J.D.2    Zakour, R.A.3
  • 27
    • 0026650558 scopus 로고
    • Colorimetric assay for lysozyme using Micrococcus luteus labeled with a blue dye, remazol brilliant Blue R, as a substrate
    • Ito, Y., Yamada, H., and Imoto, T. (1992) Colorimetric assay for lysozyme using Micrococcus luteus labeled with a blue dye, remazol brilliant Blue R, as a substrate. Chem. Pharm. Bull. 40, 1523-1526
    • (1992) Chem. Pharm. Bull. , vol.40 , pp. 1523-1526
    • Ito, Y.1    Yamada, H.2    Imoto, T.3
  • 29
    • 0022588293 scopus 로고
    • Saccharomyces cerevisiae secretes and correctly processes human interferon hybrid proteins con-taining yeast invertase signal peptides
    • Chang, C.N., Matteucci, M., Perry, L.J., Wulf, J.J., Chen, C.Y., and Hitzeman, R.A. (1986) Saccharomyces cerevisiae secretes and correctly processes human interferon hybrid proteins con-taining yeast invertase signal peptides. Mol. Cell. Biol. 6, 1812-1819
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 1812-1819
    • Chang, C.N.1    Matteucci, M.2    Perry, L.J.3    Wulf, J.J.4    Chen, C.Y.5    Hitzeman, R.A.6
  • 30
    • 0022897178 scopus 로고
    • Expression of human salivary alpha-amylase gene in Saccharomyces cerevisiae and its secretion using the mammalian signal sequence
    • Nakamura, Y., Sato, T., Emi, M., Miyanohara, A., Nishida, T., and Matsubara, K. (1986) Expression of human salivary alpha-amylase gene in Saccharomyces cerevisiae and its secretion using the mammalian signal sequence. Gene 50, 239-245
    • (1986) Gene , vol.50 , pp. 239-245
    • Nakamura, Y.1    Sato, T.2    Emi, M.3    Miyanohara, A.4    Nishida, T.5    Matsubara, K.6
  • 31
    • 0026806898 scopus 로고
    • Expression of human soluble tissue factor in yeast and enzymatic properties of its complex with factor VIIa
    • Shigematsu, Y., Miyata, T., Higashi, S., Miki, T., Sadler, J.E., and Iwanaga, S. (1992) Expression of human soluble tissue factor in yeast and enzymatic properties of its complex with factor VIIa. J. Biol. Chem. 267, 21329-21337
    • (1992) J. Biol. Chem. , vol.267 , pp. 21329-21337
    • Shigematsu, Y.1    Miyata, T.2    Higashi, S.3    Miki, T.4    Sadler, J.E.5    Iwanaga, S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.