메뉴 건너뛰기




Volumn 10, Issue 1, 1997, Pages 1-9

Cloning, overexpression, and mutagenesis of the gene for homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum

Author keywords

[No Author keywords available]

Indexed keywords


EID: 0031172842     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.1996.0703     Document Type: Article
Times cited : (30)

References (29)
  • 2
    • 0001615959 scopus 로고
    • Mechanistic aspects of dihydroxybenzoate dioxygenases
    • New York: Marcel Dekker. p. 243-298
    • Lipscomb J. D., Orville A. M. Mechanistic aspects of dihydroxybenzoate dioxygenases. Metal Ions in Biological Systems. 1992;Marcel Dekker, New York. p. 243-298.
    • (1992) Metal Ions in Biological Systems
    • Lipscomb, J.D.1    Orville, A.M.2
  • 3
  • 4
    • 0013791975 scopus 로고
    • Crystallization and some properties of 3,4-dihydroxyphenylacetate 2,3-dioxygenase fromPseudomonas ovalis
    • Kita H. Crystallization and some properties of 3,4-dihydroxyphenylacetate 2,3-dioxygenase fromPseudomonas ovalis. J. Biochem. 58:1965;116-122.
    • (1965) J. Biochem. , vol.58 , pp. 116-122
    • Kita, H.1
  • 5
    • 0015748395 scopus 로고
    • Studies on 3,4-dihydroxyphenylacetate 2,3-dioxygenase. I. Role of iron, substrate binding, and some other properties
    • Ono-Kamimoto M. Studies on 3,4-dihydroxyphenylacetate 2,3-dioxygenase. I. Role of iron, substrate binding, and some other properties. J. Biochem. 74:1973;1049-1059.
    • (1973) J. Biochem. , vol.74 , pp. 1049-1059
    • Ono-Kamimoto, M.1
  • 6
    • 0029883485 scopus 로고    scopus 로고
    • Homoprotocatechuate 2,3-dioxygenase fromBrevibacterium fuscum:
    • Miller M. A., Lipscomb J. D. Homoprotocatechuate 2,3-dioxygenase fromBrevibacterium fuscum: J. Biol. Chem. 271:1996;5524-5535.
    • (1996) J. Biol. Chem. , vol.271 , pp. 5524-5535
    • Miller, M.A.1    Lipscomb, J.D.2
  • 7
    • 0025115933 scopus 로고
    • Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene fromEscherichia coli
    • Roper D. I., Cooper R. A. Subcloning and nucleotide sequence of the 3,4-dihydroxyphenylacetate (homoprotocatechuate) 2,3-dioxygenase gene fromEscherichia coli. FEBS Lett. 275:1990;53-57.
    • (1990) FEBS Lett. , vol.275 , pp. 53-57
    • Roper, D.I.1    Cooper, R.A.2
  • 9
    • 0019778558 scopus 로고
    • 3,4-Dihydroxyphenylacetate 2,3-dioxygenase: A manganese (II) dioxygenase fromBacillus brevis
    • Que L., Widom J., Crawford R. L. 3,4-Dihydroxyphenylacetate 2,3-dioxygenase: A manganese (II) dioxygenase fromBacillus brevis. J. Biol. Chem. 256:1981;10941-10944.
    • (1981) J. Biol. Chem. , vol.256 , pp. 10941-10944
    • Que, L.1    Widom, J.2    Crawford, R.L.3
  • 11
    • 0001279038 scopus 로고
    • Preparation of genomic DNA from bacteria: Supplement 9
    • Ausubel New York: Wiley
    • Wilson K. Preparation of genomic DNA from bacteria: Supplement 9. Ausubel. Current Protocols in Molecular Biology. 1990;Wiley, New York.
    • (1990) Current Protocols in Molecular Biology
    • Wilson, K.1
  • 12
    • 0019186616 scopus 로고
    • A small cosmid for efficient cloning of large DNA fragments
    • Hohn B., Collins J. A small cosmid for efficient cloning of large DNA fragments. Gene. 11:1980;291-298.
    • (1980) Gene , vol.11 , pp. 291-298
    • Hohn, B.1    Collins, J.2
  • 15
    • 0025695782 scopus 로고
    • Single step large scale site-directed in vitro mutagenesis using multiple oligonucleotides
    • Perlak F. J. Single step large scale site-directed in vitro mutagenesis using multiple oligonucleotides. Nucleic. Acids Res. 18:1990;7457-7458.
    • (1990) Nucleic. Acids Res. , vol.18 , pp. 7457-7458
    • Perlak, F.J.1
  • 16
    • 0023777735 scopus 로고
    • Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins inEscherichia coli
    • Amann E., Ochs B., Abel K-J. Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins inEscherichia coli. Gene. 69:1988;301-315.
    • (1988) Gene , vol.69 , pp. 301-315
    • Amann, E.1    Ochs, B.2    Abel, K-J.3
  • 17
    • 0025005899 scopus 로고
    • Protocatechuate 3,4-dioxygenase fromBrevibacterium fuscum
    • Whittaker J. W., Orville A. M., Lipscomb J. D. Protocatechuate 3,4-dioxygenase fromBrevibacterium fuscum. Methods Enzymol. 188:1990;82-88.
    • (1990) Methods Enzymol. , vol.188 , pp. 82-88
    • Whittaker, J.W.1    Orville, A.M.2    Lipscomb, J.D.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 256:1976;248-254.
    • (1976) Anal. Biochem. , vol.256 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 49649145902 scopus 로고
    • EPR signal intensity and powder shapes: A reexamination
    • Aasa R., Vänngård T. EPR signal intensity and powder shapes: A reexamination. J. Magn. Reson. 19:1975;308-315.
    • (1975) J. Magn. Reson. , vol.19 , pp. 308-315
    • Aasa, R.1    Vänngård, T.2
  • 22
    • 0020560883 scopus 로고
    • Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid ofPseudomonas putida
    • Nakai C., Kagamiyama H., Nozaki M., Nakazawa T., Inouye S., Edina Y., Nakazawa A. Complete nucleotide sequence of the metapyrocatechase gene on the TOL plasmid ofPseudomonas putida. J. Biol. Chem. 258:1983;2923-2928.
    • (1983) J. Biol. Chem. , vol.258 , pp. 2923-2928
    • Nakai, C.1    Kagamiyama, H.2    Nozaki, M.3    Nakazawa, T.4    Inouye, S.5    Edina, Y.6    Nakazawa, A.7
  • 23
    • 0028324162 scopus 로고
    • The catechol 2,3-dioxygenase ofRhodococcus rhodochrous
    • Candidus S., van Pee K., Lingens F. The catechol 2,3-dioxygenase ofRhodococcus rhodochrous. Microbiology. 140:1994;321-330.
    • (1994) Microbiology , vol.140 , pp. 321-330
    • Candidus, S.1    Van Pee, K.2    Lingens, F.3
  • 25
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad
    • Han S., Eltis L. D., Timmis K. N., Muchmore S. W., Bolin J. T. Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad. Science. 270:1995;976-980.
    • (1995) Science , vol.270 , pp. 976-980
    • Han, S.1    Eltis, L.D.2    Timmis, K.N.3    Muchmore, S.W.4    Bolin, J.T.5
  • 27
    • 0029379752 scopus 로고
    • Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): Process control yielding high levels of metal-incorporated soluble proteinProtein Express
    • Hoffman B. J., Broadwater J. A., Johnson P., Harper J., Fox B. G., Kenealy W. R. Lactose fed-batch overexpression of recombinant metalloproteins in Escherichia coli BL21(DE3): Process control yielding high levels of metal-incorporated soluble proteinProtein Express. Purif. 6:1995;646-654.
    • (1995) Purif. , vol.6 , pp. 646-654
    • Hoffman, B.J.1    Broadwater, J.A.2    Johnson, P.3    Harper, J.4    Fox, B.G.5    Kenealy, W.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.