메뉴 건너뛰기




Volumn 72, Issue 9, 2008, Pages 2467-2471

Enzymatic analysis of a thermostabilized mutant of an Escherichia coli hygromycin B phosphotransferase

Author keywords

CD analysis; Hygromycin B phosphotransferase; In vivo directed evolution; Thermostabilization

Indexed keywords

AMINES; AMINO ACIDS; BIOCHEMISTRY; ENZYMES; ESCHERICHIA COLI; FOOD ADDITIVES; ORGANIC ACIDS; THERMODYNAMIC STABILITY;

EID: 52649164004     PISSN: 09168451     EISSN: 13476947     Source Type: Journal    
DOI: 10.1271/bbb.80285     Document Type: Article
Times cited : (10)

References (25)
  • 1
    • 0015955554 scopus 로고
    • Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa
    • Oshima, T., and Imahori, K., Description of Thermus thermophilus (Yoshida and Oshima) comb. nov., a nonsporulating thermophilic bacterium from a Japanese thermal spa. Int. J. Syst. Bacteriol., 24, 102-112 (1974).
    • (1974) Int. J. Syst. Bacteriol , vol.24 , pp. 102-112
    • Oshima, T.1    Imahori, K.2
  • 2
    • 0022448655 scopus 로고
    • Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp
    • Koyama, Y., Hoshino, T., Tomizuka, N., and Furukawa, K., Genetic transformation of the extreme thermophile Thermus thermophilus and of other Thermus spp. J. Bacteriol., 166, 338-340 (1986).
    • (1986) J. Bacteriol , vol.166 , pp. 338-340
    • Koyama, Y.1    Hoshino, T.2    Tomizuka, N.3    Furukawa, K.4
  • 3
    • 0028314529 scopus 로고
    • A carotenogenic gene cluster exists on a large plasmid in Thermus thermophilus
    • Tabata, K., Ishida, S., Nakahara, T., and Hoshino, T., A carotenogenic gene cluster exists on a large plasmid in Thermus thermophilus. FEBS Lett., 341, 251-255 (1994).
    • (1994) FEBS Lett , vol.341 , pp. 251-255
    • Tabata, K.1    Ishida, S.2    Nakahara, T.3    Hoshino, T.4
  • 4
    • 0030762049 scopus 로고    scopus 로고
    • Characterization of a thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus
    • Kato, R., Hasegawa, K., Hidaka, Y., Kuramitsu, S., and Hoshino, T., Characterization of a thermostable DNA photolyase from an extremely thermophilic bacterium, Thermus thermophilus. J. Bacteriol., 179, 6499-6503 (1997).
    • (1997) J. Bacteriol , vol.179 , pp. 6499-6503
    • Kato, R.1    Hasegawa, K.2    Hidaka, Y.3    Kuramitsu, S.4    Hoshino, T.5
  • 6
    • 20444502976 scopus 로고    scopus 로고
    • Membrane-associated maturation of the heterotetrameric nitrate reductase of Thermus thermophilus
    • Zafra, O., Cava, F., Blasco, F., Magalon, A., and Berenguer, J., Membrane-associated maturation of the heterotetrameric nitrate reductase of Thermus thermophilus. J. Bacteriol., 187, 3990-3996 (2005).
    • (2005) J. Bacteriol , vol.187 , pp. 3990-3996
    • Zafra, O.1    Cava, F.2    Blasco, F.3    Magalon, A.4    Berenguer, J.5
  • 7
    • 40349108282 scopus 로고    scopus 로고
    • Characterization of three putative Lon proteases of Thermus thermophilus HB27 and use of their defective mutants as hosts for production of heterologous proteins
    • Maehara, T., Hoshino, T., and Nakamura, A., Characterization of three putative Lon proteases of Thermus thermophilus HB27 and use of their defective mutants as hosts for production of heterologous proteins. Extremophiles, 12, 285-296 (2008).
    • (2008) Extremophiles , vol.12 , pp. 285-296
    • Maehara, T.1    Hoshino, T.2    Nakamura, A.3
  • 8
    • 3142690593 scopus 로고    scopus 로고
    • Heterologous gene expression in Thermus thermophilus: β-galactosidase, dibenzothiophene monooxygenase, PNB carboxy esterase, 2-aminobiphenyl-2,3-diol dioxygenase, and chloramphenicol acetyl transferase
    • Park, H.-S., Kayser, K. J., Kwak, J.-H., and Kilbane II, J. J., Heterologous gene expression in Thermus thermophilus: β-galactosidase, dibenzothiophene monooxygenase, PNB carboxy esterase, 2-aminobiphenyl-2,3-diol dioxygenase, and chloramphenicol acetyl transferase. J. Ind. Microbiol. Biotechnol., 31, 189-197 (2004).
    • (2004) J. Ind. Microbiol. Biotechnol , vol.31 , pp. 189-197
    • Park, H.-S.1    Kayser, K.J.2    Kwak, J.-H.3    Kilbane II, J.J.4
  • 9
    • 1842425623 scopus 로고    scopus 로고
    • Functional analysis of the small subunit of the putative homoaconitase from Pyrococcus horikoshii in the Thermus lysine biosynthetic pathway
    • Lombo, T., Takaya, N., Miyazaki, J., Gotoh, K., Nishiyama, M., Kosuge, T., Nakamura, A., and Hoshino, T., Functional analysis of the small subunit of the putative homoaconitase from Pyrococcus horikoshii in the Thermus lysine biosynthetic pathway. FEMS Microbiol. Lett., 233, 315-324 (2004).
    • (2004) FEMS Microbiol. Lett , vol.233 , pp. 315-324
    • Lombo, T.1    Takaya, N.2    Miyazaki, J.3    Gotoh, K.4    Nishiyama, M.5    Kosuge, T.6    Nakamura, A.7    Hoshino, T.8
  • 10
    • 52649113418 scopus 로고    scopus 로고
    • Takayama, G., Kosuge, T., Sunamura, S., Matsui, I., Ishikawa, K., Nakamura, A., and Hoshino, T., Use of a Thermus thermophilus host-vector system for expression of genes from the hyperthermophilic archaeon Pyrococcus horikoshii. J. Jpn. Soc. Extremophiles, 3, 18-27 (2004).
    • Takayama, G., Kosuge, T., Sunamura, S., Matsui, I., Ishikawa, K., Nakamura, A., and Hoshino, T., Use of a Thermus thermophilus host-vector system for expression of genes from the hyperthermophilic archaeon Pyrococcus horikoshii. J. Jpn. Soc. Extremophiles, 3, 18-27 (2004).
  • 11
    • 0031935580 scopus 로고    scopus 로고
    • Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution
    • Akanuma, S., Yamagishi, A., Tanaka, N., and Oshima, T., Serial increase in the thermal stability of 3-isopropylmalate dehydrogenase from Bacillus subtilis by experimental evolution. Protein Sci., 7, 698-705 (1998).
    • (1998) Protein Sci , vol.7 , pp. 698-705
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 12
    • 0033106205 scopus 로고    scopus 로고
    • Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis
    • Akanuma, S., Yamagishi, A., Tanaka, N., and Oshima, T., Further improvement of the thermal stability of a partially stabilized Bacillus subtilis 3-isopropylmalate dehydrogenase variant by random and site-directed mutagenesis. Eur. J. Biochem., 260, 499-504 (1999).
    • (1999) Eur. J. Biochem , vol.260 , pp. 499-504
    • Akanuma, S.1    Yamagishi, A.2    Tanaka, N.3    Oshima, T.4
  • 13
    • 0035259956 scopus 로고    scopus 로고
    • Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus
    • Tamakoshi, M., Nakano, Y., Kakizawa, S., Yamagishi, A., and Oshima, T., Selection of stabilized 3-isopropylmalate dehydrogenase of Saccharomyces cerevisiae using the host-vector system of an extreme thermophile, Thermus thermophilus. Extremophiles, 5, 17-22 (2001).
    • (2001) Extremophiles , vol.5 , pp. 17-22
    • Tamakoshi, M.1    Nakano, Y.2    Kakizawa, S.3    Yamagishi, A.4    Oshima, T.5
  • 14
    • 0036267346 scopus 로고    scopus 로고
    • Thermoadaptation of α-galactosidase AgaB1 in Thermus thermophilus
    • Fridjonsson, O., Watzlawick, H., and Mattes, R., Thermoadaptation of α-galactosidase AgaB1 in Thermus thermophilus. J. Bacteriol., 184, 3385-3391 (2002).
    • (2002) J. Bacteriol , vol.184 , pp. 3385-3391
    • Fridjonsson, O.1    Watzlawick, H.2    Mattes, R.3
  • 16
    • 0022599340 scopus 로고
    • The nucleotide sequence of pUB110: Some salient features in relation to replication and its regulation
    • McKenzie, T., Hoshino, T., Tanaka, T., and Sueoka, N., The nucleotide sequence of pUB110: some salient features in relation to replication and its regulation. Plasmid, 15, 93-103 (1986).
    • (1986) Plasmid , vol.15 , pp. 93-103
    • McKenzie, T.1    Hoshino, T.2    Tanaka, T.3    Sueoka, N.4
  • 17
    • 0032730861 scopus 로고    scopus 로고
    • Directed evolution of thermostable kanamycin-resistance gene: A convenient selection marker for Thermus thermophilus
    • Hoseki, J., Yano, T., Koyama, Y., Kuramitsu, S., and Kagamiyama, H., Directed evolution of thermostable kanamycin-resistance gene: a convenient selection marker for Thermus thermophilus. J. Biochem. (Tokyo), 126, 951-956 (1999).
    • (1999) J. Biochem. (Tokyo) , vol.126 , pp. 951-956
    • Hoseki, J.1    Yano, T.2    Koyama, Y.3    Kuramitsu, S.4    Kagamiyama, H.5
  • 18
    • 27644459857 scopus 로고    scopus 로고
    • In vivo directed evolution for thermostabilization of Escherichia coli hygromycin B phosphotransferase and the use of the gene as a selection marker in the host-vector system of Thermus thermophilus
    • Nakamura, A., Takakura, Y., Kobayashi, H., and Hoshino, T., In vivo directed evolution for thermostabilization of Escherichia coli hygromycin B phosphotransferase and the use of the gene as a selection marker in the host-vector system of Thermus thermophilus. J. Biosci. Bioeng., 100, 158-163 (2005).
    • (2005) J. Biosci. Bioeng , vol.100 , pp. 158-163
    • Nakamura, A.1    Takakura, Y.2    Kobayashi, H.3    Hoshino, T.4
  • 19
    • 15744382276 scopus 로고    scopus 로고
    • Refolding and purification of non-fusion HPT protein expressed in Escherichia coli as inclusion bodies
    • Zhuo, Q., Piao, J.-H., Wang, R., and Yang, X.-G., Refolding and purification of non-fusion HPT protein expressed in Escherichia coli as inclusion bodies. Protein Expr. Purif., 41, 53-60 (2005).
    • (2005) Protein Expr. Purif , vol.41 , pp. 53-60
    • Zhuo, Q.1    Piao, J.-H.2    Wang, R.3    Yang, X.-G.4
  • 20
    • 0021083175 scopus 로고    scopus 로고
    • Rao, R. N., Allen, N. E., Hobbs, J. N., Jr., Alborn, W. E., Jr., Kirst, H. A., and Paschal, J. W., Genetic and enzymatic basis of hygromycin B resistance in Escherichia coli. Antimicrob. Agents Chemother., 24, 689-695 (1983).
    • Rao, R. N., Allen, N. E., Hobbs, J. N., Jr., Alborn, W. E., Jr., Kirst, H. A., and Paschal, J. W., Genetic and enzymatic basis of hygromycin B resistance in Escherichia coli. Antimicrob. Agents Chemother., 24, 689-695 (1983).
  • 21
    • 0027489832 scopus 로고
    • Thermodynamics of unfolding for turkey ovomucoid third domain: Thermal and chemical denaturation
    • Swint, L., and Robertson, A. D., Thermodynamics of unfolding for turkey ovomucoid third domain: thermal and chemical denaturation. Protein Sci., 2, 2037-2049 (1993).
    • (1993) Protein Sci , vol.2 , pp. 2037-2049
    • Swint, L.1    Robertson, A.D.2
  • 22
    • 0029026251 scopus 로고
    • Screening and analysis of DNA fragments that show promoter activities in Thermus thermophilus
    • Maseda, H., and Hoshino, T., Screening and analysis of DNA fragments that show promoter activities in Thermus thermophilus. FEMS Microbiol. Lett., 128, 127-134 (1995).
    • (1995) FEMS Microbiol. Lett , vol.128 , pp. 127-134
    • Maseda, H.1    Hoshino, T.2
  • 23
    • 0024287774 scopus 로고
    • Coupled spectrofluorometric assay for aminoglycoside phosphotransferases
    • Perlin, M. H., McCarty, S. C., and Greer, J. P., Coupled spectrofluorometric assay for aminoglycoside phosphotransferases. Anal. Biochem., 171, 145-149 (1988).
    • (1988) Anal. Biochem , vol.171 , pp. 145-149
    • Perlin, M.H.1    McCarty, S.C.2    Greer, J.P.3
  • 24
    • 0028358078 scopus 로고
    • Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: Overexpression, purification, and substrate specificity
    • McKay, G. A., Thompson, P. R., and Wright, G. D., Broad spectrum aminoglycoside phosphotransferase type III from Enterococcus: overexpression, purification, and substrate specificity. Biochemistry, 33, 6936-6944 (1994).
    • (1994) Biochemistry , vol.33 , pp. 6936-6944
    • McKay, G.A.1    Thompson, P.R.2    Wright, G.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.