메뉴 건너뛰기




Volumn 59, Issue 4, 1998, Pages 520-523

Alteration of the substrate range of haloalkane dehalogenase by site- directed mutagenesis

Author keywords

Bioremediation; Haloalkane dehalogenase; Protein engineering

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CHLORINE COMPOUNDS; ENZYMES; MUTAGENESIS; ORGANIC SOLVENTS; SUBSTRATES;

EID: 0032552222     PISSN: 00063592     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0290(19980820)59:4<520::AID-BIT16>3.0.CO;2-D     Document Type: Article
Times cited : (35)

References (17)
  • 1
    • 0003181453 scopus 로고    scopus 로고
    • Facts and figures for the chemical industry
    • Anonymous. 1996. Facts and figures for the chemical industry. Chem. Eng. News 74: 38-77.
    • (1996) Chem. Eng. News , vol.74 , pp. 38-77
  • 2
    • 0001588040 scopus 로고
    • Biodegradation of haloalkanes
    • Belkin, S. 1992. Biodegradation of haloalkanes. Biodegradation 3: 299-313.
    • (1992) Biodegradation , vol.3 , pp. 299-313
    • Belkin, S.1
  • 3
    • 0025734772 scopus 로고
    • Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes
    • Franken, S. M., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W. 1991. Crystal structure of haloalkane dehalogenase: An enzyme to detoxify halogenated alkanes. EMBO J. 10: 1297-1302.
    • (1991) EMBO J. , vol.10 , pp. 1297-1302
    • Franken, S.M.1    Rozeboom, H.J.2    Kalk, K.H.3    Dijkstra, B.W.4
  • 4
    • 0024358064 scopus 로고
    • Cloning of the 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression of the dhlA gene
    • Janssen, D. B., Pries, F., van der Ploeg, J., Kazemier, B., Terpstra, P., Withold, B. 1989. Cloning of the 1,2-dichloroethane degradation genes of Xanthobacter autotrophicus GJ10 and expression of the dhlA gene. J. Bacteriol. 171: 6791-6799.
    • (1989) J. Bacteriol. , vol.171 , pp. 6791-6799
    • Janssen, D.B.1    Pries, F.2    Van der Ploeg, J.3    Kazemier, B.4    Terpstra, P.5    Withold, B.6
  • 5
    • 0021966251 scopus 로고
    • Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10
    • Janssen, D. B., Scheper, A., Dijkhuizen, L., Witholt, B. 1985. Degradation of halogenated aliphatic compounds by Xanthobacter autotrophicus GJ10. Appl. Environ. Microbiol. 49: 673-677.
    • (1985) Appl. Environ. Microbiol. , vol.49 , pp. 673-677
    • Janssen, D.B.1    Scheper, A.2    Dijkhuizen, L.3    Witholt, B.4
  • 6
    • 0028942983 scopus 로고
    • Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity
    • Kennes, C., Pries, F., Krooshof, G. H., Bokma, E., Kingma, J., Janssen, D. B. 1995. Replacement of tryptophan residues in haloalkane dehalogenase reduces halide binding and catalytic activity. Eur. J. Biochem. 228: 403-407.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 403-407
    • Kennes, C.1    Pries, F.2    Krooshof, G.H.3    Bokma, E.4    Kingma, J.5    Janssen, D.B.6
  • 7
    • 0021798672 scopus 로고
    • Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus
    • Keuning, S., Janssen, D. B. Witholt, B. 1985. Purification and characterization of hydrolytic haloalkane dehalogenase from Xanthobacter autotrophicus. J. Bacteriol. 163: 635-639.
    • (1985) J. Bacteriol. , vol.163 , pp. 635-639
    • Keuning, S.1    Janssen, B.D.2    Witholt, B.3
  • 8
    • 0025888264 scopus 로고
    • Efficient site-directed mutagenesis using uracil-containing DNA
    • Kunkel, T. A., Bebenek, K., McClary, J. 1991. Efficient site-directed mutagenesis using uracil-containing DNA. Methods Enzymol. 204: 125-139.
    • (1991) Methods Enzymol. , vol.204 , pp. 125-139
    • Kunkel, T.A.1    Bebenek, K.2    McClary, J.3
  • 9
    • 0020454481 scopus 로고
    • C1 and C2 halocarbons
    • O. Hutzinger (ed.). Springer-Verlag, Berlin
    • Pearson, C. R. 1982. C1 and C2 halocarbons, pp. 69-116. In: O. Hutzinger (ed.), The Handbook of Environmental Chemistry. Springer-Verlag, Berlin.
    • (1982) The Handbook of Environmental Chemistry , pp. 69-116
    • Pearson, C.R.1
  • 10
    • 0028242876 scopus 로고
    • The role of spontaneous mutations in haloalkane dehalogenase specificity and evolution
    • Pries, F., van den Wijngaard, A. J., Bos, R., Pentenga, M., Janssen, D. B. 1994. The role of spontaneous mutations in haloalkane dehalogenase specificity and evolution. J. Biol. Chem. 269: 17490-17494.
    • (1994) J. Biol. Chem. , vol.269 , pp. 17490-17494
    • Pries, F.1    Van den Wijngaard, A.J.2    Bos, R.3    Pentenga, M.4    Janssen, D.B.5
  • 11
    • 0028915619 scopus 로고
    • Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase
    • Pries, F., Kingma, J., Krooshof, G., Jeronimus-Stratingh, C. M., Bruins, A. P., Janssen, D. B. 1995. Histidine 289 is essential for hydrolysis of the alkyl-enzyme intermediate of haloalkane dehalogenase. J. Biol. Chem. 270: 10405-10411.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10405-10411
    • Pries, F.1    Kingma, J.2    Krooshof, G.3    Jeronimus-Stratingh, C.M.4    Bruins, A.P.5    Janssen, D.B.6
  • 12
    • 0024278449 scopus 로고
    • Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10
    • Rozeboom, H. J., Kingma, J., Janssen, D. B., Dijkstra, B. W. 1988. Crystallization of haloalkane dehalogenase from Xanthobacter autotrophicus GJ10. J. Mol. Biol. 200: 611-612.
    • (1988) J. Mol. Biol. , vol.200 , pp. 611-612
    • Rozeboom, H.J.1    Kingma, J.2    Janssen, D.B.3    Dijkstra, B.W.4
  • 14
    • 0029800609 scopus 로고    scopus 로고
    • Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range
    • Schanstra, J. P., Ridder, I. S., Heimeriks, G. J., Rink, R., Poelarends, G. J., Kalk, H. K., Dijkstra, B. W., Janssen, D. B. 1996. Kinetic characterization and X-ray structure of a mutant of haloalkane dehalogenase with higher catalytic activity and modified substrate range. Biochemistry 35: 13186-13195.
    • (1996) Biochemistry , vol.35 , pp. 13186-13195
    • Schanstra, J.P.1    Ridder, I.S.2    Heimeriks, G.J.3    Rink, R.4    Poelarends, G.J.5    Kalk, H.K.6    Dijkstra, B.W.7    Janssen, D.B.8
  • 15
    • 0027674250 scopus 로고
    • Construction of an expression and site-directed mutagenesis system of haloalkane dehalogenase in Escherichia coli
    • Schanstra, J. P., Rink, R., Pries, F., Janssen, D. B. 1993. Construction of an expression and site-directed mutagenesis system of haloalkane dehalogenase in Escherichia coli. Protein Expression Purif. 4: 479-489.
    • (1993) Protein Expression Purif. , vol.4 , pp. 479-489
    • Schanstra, J.P.1    Rink, R.2    Pries, F.3    Janssen, D.B.4
  • 16
    • 0027337615 scopus 로고
    • Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase
    • Verschueren, K. H. G., Selje, F., Rozeboom, H. J., Kalk, K. H., Dijkstra, B. W. 1993a. Crystallographic analysis of the catalytic mechanism of haloalkane dehalogenase. Nature 363: 693-698.
    • (1993) Nature , vol.363 , pp. 693-698
    • Verschueren, K.H.G.1    Selje, F.2    Rozeboom, H.J.3    Kalk, K.H.4    Dijkstra, B.W.5
  • 17
    • 0027819259 scopus 로고
    • Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions: Studies with halide compounds reveal a halide binding site in the active site
    • Verschueren, K. H. G., Kingma, J., Rozeboom, H. J., Kalk, K. H., Janssen, D. B., Dijkstra, B. W. 1993b. Crystallographic and fluorescence studies of the interaction of haloalkane dehalogenase with halide ions: Studies with halide compounds reveal a halide binding site in the active site. Biochemistry 32: 9031-9037.
    • (1993) Biochemistry , vol.32 , pp. 9031-9037
    • Verschueren, K.H.G.1    Kingma, J.2    Rozeboom, H.J.3    Kalk, K.H.4    Janssen, D.B.5    Dijkstra, B.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.