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Volumn 161, Issue 2, 2006, Pages 138-144

Site-directed mutagenesis of gentisate 1,2-dioxygenases from Klebsiella pneumoniae M5a1 and Ralstonia sp. strain U2

Author keywords

Gentisate 1,2 dioxygenase; Klebsiella pneumoniae M5a1; Ralstonia sp. strain U2; Site directed mutagenesis

Indexed keywords

AMINO ACIDS; CATALYSIS; GENETIC ENGINEERING; MUTAGENESIS;

EID: 30944465384     PISSN: 09445013     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.micres.2005.07.004     Document Type: Article
Times cited : (8)

References (27)
  • 2
    • 0035899925 scopus 로고    scopus 로고
    • Identification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867
    • C.H. Chua, Y.M. Feng, C.C. Yeo, H.E. Khoo, and C.L. Poh Identification of amino acid residues essential for catalytic activity of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867 FEMS Microbiol. Lett. 204 2001 141 146
    • (2001) FEMS Microbiol. Lett. , vol.204 , pp. 141-146
    • Chua, C.H.1    Feng, Y.M.2    Yeo, C.C.3    Khoo, H.E.4    Poh, C.L.5
  • 3
    • 0016671272 scopus 로고
    • Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis
    • R.L. Crawford, S.W. Hutton, and P.J. Chapman Purification and properties of gentisate 1,2-dioxygenase from Moraxella osloensis J. Bacteriol. 121 1975 794 799
    • (1975) J. Bacteriol. , vol.121 , pp. 794-799
    • Crawford, R.L.1    Hutton, S.W.2    Chapman, P.J.3
  • 4
    • 0034096459 scopus 로고    scopus 로고
    • Microbial relatives of the seed storage proteins of higher plants: Conservation of structure and diversification of function during evolution of the cupin superfamily
    • J.M. Dunwell, S. Khuri, and P.J. Gane Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily Microbiol. Mol. Biol. Rev. 64 2000 153 179
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 153-179
    • Dunwell, J.M.1    Khuri, S.2    Gane, P.J.3
  • 5
    • 0039136118 scopus 로고    scopus 로고
    • Purification and characterization of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869
    • Y.M. Feng, H.E. Khoo, and C.L. Poh Purification and characterization of gentisate 1,2-dioxygenase from Pseudomonas alcaligenes NCIB 9867 and Pseudomonas putida NCIB 9869 Appl. Environ. Microbiol. 65 1999 946 950
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 946-950
    • Feng, Y.M.1    Khoo, H.E.2    Poh, C.L.3
  • 6
    • 0029132294 scopus 로고
    • Molecular characterization of a gene encoding a homogentisate dioxygenase from Aspergillus nidulans and indentification of its human and plant homologues
    • J.M. Fernandez-Canon, and M.A. Penaval Molecular characterization of a gene encoding a homogentisate dioxygenase from Aspergillus nidulans and indentification of its human and plant homologues J. Biol. Chem. 270 1995 21199 21205
    • (1995) J. Biol. Chem. , vol.270 , pp. 21199-21205
    • Fernandez-Canon, J.M.1    Penaval, M.A.2
  • 7
    • 0032213232 scopus 로고    scopus 로고
    • Gentisate 1,2-dioxygenase from Haloferax sp. D1227
    • W.J. Fu, and P. Oriel Gentisate 1,2-dioxygenase from Haloferax sp. D1227 Extremophiles 2 1998 439 446
    • (1998) Extremophiles , vol.2 , pp. 439-446
    • Fu, W.J.1    Oriel, P.2
  • 9
    • 30944437277 scopus 로고    scopus 로고
    • Gentisate pathway in aromatic catabolism
    • X.L. Gao, and N.Y. Zhou Gentisate pathway in aromatic catabolism Wei Sheng Wu Xue Tong Bao 30 2003 81 85 (in Chinese)
    • (2003) Wei Sheng Wu Xue Tong Bao , vol.30 , pp. 81-85
    • Gao, X.L.1    Zhou, N.Y.2
  • 10
    • 11844304935 scopus 로고    scopus 로고
    • The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)
    • B. Gopal, L.L. Madan, S.F. Betz, and A.A. Kossiakoff The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s) Biochemistry 44 2005 193 201
    • (2005) Biochemistry , vol.44 , pp. 193-201
    • Gopal, B.1    Madan, L.L.2    Betz, S.F.3    Kossiakoff, A.A.4
  • 11
    • 0028862027 scopus 로고
    • Crystal structure of the biphenyl-cleaving extradiol dioxygenase from a PCB-degrading Pseudomonad
    • S. Han, L.D. Eltis, K.N. Timmis, S.W. Muchmore, and J.T. Bolin 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
  • 12
    • 0025216788 scopus 로고
    • Gentisate 1,2-dioxygenase from Pseudomonas, purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans
    • M.R. Harpel, and J.D. Lipscomb Gentisate 1,2-dioxygenase from Pseudomonas, purification, characterization, and comparison of the enzymes from Pseudomonas testosteroni and Pseudomonas acidovorans J. Biol. Chem. 265 1990 6301 6311
    • (1990) J. Biol. Chem. , vol.265 , pp. 6301-6311
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 13
    • 0025676272 scopus 로고
    • Gentisate 1,2-dioxygenase from Pseudomonas, substrate coordination to active site Fe2+ and mechanism of turnover
    • M.R. Harpel, and J.D. Lipscomb Gentisate 1,2-dioxygenase from Pseudomonas, substrate coordination to active site Fe2+ and mechanism of turnover J. Biol. Chem. 265 1990 22187 22196
    • (1990) J. Biol. Chem. , vol.265 , pp. 22187-22196
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 14
    • 0029953163 scopus 로고    scopus 로고
    • Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: Potential mononuclear non-heme iron coordination sites
    • H. Jiang, R.E. Parales, N.A. Lynch, and D.T. Gibson Site-directed mutagenesis of conserved amino acids in the alpha subunit of toluene dioxygenase: potential mononuclear non-heme iron coordination sites J. Bacteriol. 178 1996 3133 3139
    • (1996) J. Bacteriol. , vol.178 , pp. 3133-3139
    • Jiang, H.1    Parales, R.E.2    Lynch, N.A.3    Gibson, D.T.4
  • 15
    • 0025130003 scopus 로고
    • Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1
    • D.C. Jones, and R.A. Cooper Catabolism of 3-hydroxybenzoate by the gentisate pathway in Klebsiella pneumoniae M5a1 Arch. Microbiol. 154 1990 489 495
    • (1990) Arch. Microbiol. , vol.154 , pp. 489-495
    • Jones, D.C.1    Cooper, R.A.2
  • 16
    • 0035065222 scopus 로고    scopus 로고
    • Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins
    • S. Khuri, F.T. Bakker, and J.M. Dunwell Phylogeny, function, and evolution of the cupins, a structurally conserved, functionally diverse superfamily of proteins Mol. Biol. Evol. 18 2001 593 605
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 593-605
    • Khuri, S.1    Bakker, F.T.2    Dunwell, J.M.3
  • 17
    • 0033556265 scopus 로고    scopus 로고
    • An archetypical extradiol-cleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrochatechase) from Pseudomonas putida mt-2
    • A. Kita, S.I. Kita, I. Fujisawa, K. Inaka, T. Ishida, K. Horiike, M. Nozaki, and K. Miki An archetypical extradiol-cleaving catecholic dioxygenase: the crystal structure of catechol 2,3-dioxygenase (metapyrochatechase) from Pseudomonas putida mt-2 Struct. Fold Des. 7 1999 25 34
    • (1999) Struct. Fold Des. , vol.7 , pp. 25-34
    • Kita, A.1    Kita, S.I.2    Fujisawa, I.3    Inaka, K.4    Ishida, T.5    Horiike, K.6    Nozaki, M.7    Miki, K.8
  • 19
    • 0029682161 scopus 로고    scopus 로고
    • In vitro recombination and mutagenesis by overlap extension PCR
    • R.J. Pogulis, A.N. Vallejo, and L.R. Pease In vitro recombination and mutagenesis by overlap extension PCR Methods Mol. Biol. 57 1996 167 176
    • (1996) Methods Mol. Biol. , vol.57 , pp. 167-176
    • Pogulis, R.J.1    Vallejo, A.N.2    Pease, L.R.3
  • 21
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • H. Schaggfr, and G.V. Jagow Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa Anal. Biochem. 166 1987 368 379
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schaggfr, H.1    Jagow, G.V.2
  • 22
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • F.W. Studier, and B.A. Moffatt Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes J. Mol. Biol. 189 1986 113 130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 23
    • 0030587575 scopus 로고    scopus 로고
    • Purification and biochemical characterization of gentisate 1,2-dioxygenase from Klebsiella pneumoniae M5a1
    • M. Suarez, E. Ferrer, and M. Martin Purification and biochemical characterization of gentisate 1,2-dioxygenase from Klebsiella pneumoniae M5a1 FEMS Microbiol. Lett. 143 1996 89 95
    • (1996) FEMS Microbiol. Lett. , vol.143 , pp. 89-95
    • Suarez, M.1    Ferrer, E.2    Martin, M.3
  • 24
    • 0033566802 scopus 로고    scopus 로고
    • Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions
    • K. Sugimoto, T. Senda, H. Aoshima, E. Masai, M. Fukuda, and Y. Mitsui Crystal structure of an aromatic ring opening dioxygenase LigAB, a protocatechuate 4,5-dioxygenase, under aerobic conditions Struct. Fold Des. 7 1999 953 965
    • (1999) Struct. Fold Des. , vol.7 , pp. 953-965
    • Sugimoto, K.1    Senda, T.2    Aoshima, H.3    Masai, E.4    Fukuda, M.5    Mitsui, Y.6
  • 25
    • 0031830170 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5
    • J. Werwath, H.A. Arfmann, D.H. Pieper, K.N. Timmis, and R.M. Wittich Biochemical and genetic characterization of a gentisate 1,2-dioxygenase from Sphingomonas sp. strain RW5 J. Bacteriol. 180 1998 4171 4176
    • (1998) J. Bacteriol. , vol.180 , pp. 4171-4176
    • Werwath, J.1    Arfmann, H.A.2    Pieper, D.H.3    Timmis, K.N.4    Wittich, R.M.5
  • 26
    • 30944440735 scopus 로고
    • Enzyme
    • J.Y. Wang S.G. Zhu C.F. Xu Higher Education Press Beijing
    • M.M. Yu Enzyme J.Y. Wang S.G. Zhu C.F. Xu Biochemistry 1990 Higher Education Press Beijing 274 279
    • (1990) Biochemistry , pp. 274-279
    • Yu, M.M.1
  • 27
    • 0035167509 scopus 로고    scopus 로고
    • Nag Genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism
    • N.Y. Zhou, S.L. Fuenmayor, and P.A. Williams nag Genes of Ralstonia (formerly Pseudomonas) sp. strain U2 encoding enzymes for gentisate catabolism J. Bacteriol. 183 2001 700 708
    • (2001) J. Bacteriol. , vol.183 , pp. 700-708
    • Zhou, N.Y.1    Fuenmayor, S.L.2    Williams, P.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.