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Volumn 43, Issue 3, 2004, Pages 663-674

Engineering p-Hydroxyphenylpyruvate Dioxygenase to a p-Hydroxymandelate Synthase and Evidence for the Proposed Benzene Oxide Intermediate in Homogentisate Formation

Author keywords

[No Author keywords available]

Indexed keywords

BENZENE; BIOASSAY; CATALYSIS; CHEMICAL MODIFICATION; CRYSTAL STRUCTURE; ENZYMES; FLUORESCENCE; IRON; METABOLISM; METABOLITES; OXIDATION; OXYGEN;

EID: 1642494902     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi035762w     Document Type: Article
Times cited : (69)

References (68)
  • 1
    • 0017646082 scopus 로고
    • Purification and some properties of human 4-hydroxyphenylpyruvate dioxygenase (1)
    • Lindblad, B., Lindstedt, G., Lindstedt, S., and Rundgren, M. (1977) Purification and some properties of human 4-hydroxyphenylpyruvate dioxygenase (1), J. Biol. Chem. 252, 5073-5084.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5073-5084
    • Lindblad, B.1    Lindstedt, G.2    Lindstedt, S.3    Rundgren, M.4
  • 3
    • 0032135179 scopus 로고    scopus 로고
    • Complementation of the Arabidopsis pds1 mutation with the gene encoding p-hydroxyphenylpyruvate dioxygenase
    • Norris, S. R., Shen, X., and DellaPenna, D. (1998) Complementation of the Arabidopsis pds1 mutation with the gene encoding p-hydroxyphenylpyruvate dioxygenase, Plant Physiol. 117, 1317-1323.
    • (1998) Plant Physiol. , vol.117 , pp. 1317-1323
    • Norris, S.R.1    Shen, X.2    DellaPenna, D.3
  • 4
    • 0027452908 scopus 로고
    • SC-0051, a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide, is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase
    • Schulz, A., Ort, O., Beyer, P., and Kleinig, H. (1993) SC-0051, a 2-benzoyl-cyclohexane-1,3-dione bleaching herbicide, is a potent inhibitor of the enzyme p-hydroxyphenylpyruvate dioxygenase, FEBS Lett. 318, 162-166.
    • (1993) FEBS Lett. , vol.318 , pp. 162-166
    • Schulz, A.1    Ort, O.2    Beyer, P.3    Kleinig, H.4
  • 5
    • 0037161587 scopus 로고    scopus 로고
    • Mode of action of 4-hydroxyphenylpyruvate dioxygenase inhibition by triketone-type inhibitors
    • Wu, C. S., Huang, J. L., Sun, Y. S., and Yang, D. Y. (2002) Mode of action of 4-hydroxyphenylpyruvate dioxygenase inhibition by triketone-type inhibitors, J. Med. Chem. 45, 2222-2228.
    • (2002) J. Med. Chem. , vol.45 , pp. 2222-2228
    • Wu, C.S.1    Huang, J.L.2    Sun, Y.S.3    Yang, D.Y.4
  • 6
    • 0026675589 scopus 로고
    • Treatment of hereditary tyrosinaemia type 1 by inhibition of 4-hydroxyphenylpyruvate dioxygenase
    • Lindstedt, S., Holme, E., Lock, E. A., Hjalmarson, O., and Strandvik, B. (1992) Treatment of hereditary tyrosinaemia type 1 by inhibition of 4-hydroxyphenylpyruvate dioxygenase, Lancet 340, 813-817.
    • (1992) Lancet , vol.340 , pp. 813-817
    • Lindstedt, S.1    Holme, E.2    Lock, E.A.3    Hjalmarson, O.4    Strandvik, B.5
  • 8
    • 0027177041 scopus 로고
    • Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene
    • Ruetschi, U., Dellsen, A., Sahlin, P., Stenman, G., Rymo, L., and Lindstedt, S. (1993) Human 4-hydroxyphenylpyruvate dioxygenase. Primary structure and chromosomal localization of the gene, Eur. J. Biochem. 213, 1081-1089.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1081-1089
    • Ruetschi, U.1    Dellsen, A.2    Sahlin, P.3    Stenman, G.4    Rymo, L.5    Lindstedt, S.6
  • 9
    • 0026486822 scopus 로고
    • Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. Evidence that the enzyme is a homodimer of identical subunits homologous to rat liver-specific alloantigen F
    • Endo, F., Awata, H., Tanoue, A., Ishiguro, M., Eda, Y., Titani, K., and Matsuda, I. (1992) Primary structure deduced from complementary DNA sequence and expression in cultured cells of mammalian 4-hydroxyphenylpyruvic acid dioxygenase. Evidence that the enzyme is a homodimer of identical subunits homologous to rat liver-specific alloantigen F, J. Biol. Chem. 267, 24235-24240.
    • (1992) J. Biol. Chem. , vol.267 , pp. 24235-24240
    • Endo, F.1    Awata, H.2    Tanoue, A.3    Ishiguro, M.4    Eda, Y.5    Titani, K.6    Matsuda, I.7
  • 10
    • 0344811560 scopus 로고    scopus 로고
    • Cloning and biochemical characterization of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis thaliana
    • Bartley, G. E., Maxwell, C. A., Hanna, W. S., Wittenbach, V. A., and Scolnik, P. A. (1997) Cloning and biochemical characterization of recombinant 4-hydroxyphenylpyruvate dioxygenase from Arabidopsis thaliana, Plant Physiol. 114, 1587-1587.
    • (1997) Plant Physiol. , vol.114 , pp. 1587-1587
    • Bartley, G.E.1    Maxwell, C.A.2    Hanna, W.S.3    Wittenbach, V.A.4    Scolnik, P.A.5
  • 11
    • 0030861598 scopus 로고    scopus 로고
    • Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA
    • Garcia, I., Rodgers, M., Lenne, C., Rolland, A., Sailland, A., and Matringe, M. (1997) Subcellular localization and purification of a p-hydroxyphenylpyruvate dioxygenase from cultured carrot cells and characterization of the corresponding cDNA, Biochem. J. 325, 761-769.
    • (1997) Biochem. J. , vol.325 , pp. 761-769
    • Garcia, I.1    Rodgers, M.2    Lenne, C.3    Rolland, A.4    Sailland, A.5    Matringe, M.6
  • 12
    • 0029163288 scopus 로고
    • Cloning and Expression of a Gene Encoding a T-Cell Reactive Protein from Coccidioides-Immitis-Homology to 4-Hydroxyphenylpyruvate Dioxygenase and the Mammalian F-Antigen
    • Wyckoff, E. E., Pishko, E. J., Kirkland, T. N., and Cole, G. T. (1995) Cloning and Expression of a Gene Encoding a T-Cell Reactive Protein from Coccidioides-Immitis-Homology to 4-Hydroxyphenylpyruvate Dioxygenase and the Mammalian F-Antigen, Gene 161, 107-111.
    • (1995) Gene , vol.161 , pp. 107-111
    • Wyckoff, E.E.1    Pishko, E.J.2    Kirkland, T.N.3    Cole, G.T.4
  • 13
    • 0027965019 scopus 로고
    • A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli
    • Denoya, C. D., Skinner, D. D., and Morgenstern, M. R. (1994) A Streptomyces avermitilis gene encoding a 4-hydroxyphenylpyruvic acid dioxygenase-like protein that directs the production of homogentisic acid and an ochronotic pigment in Escherichia coli, J. Bacteriol. 176, 5312-5319.
    • (1994) J. Bacteriol. , vol.176 , pp. 5312-5319
    • Denoya, C.D.1    Skinner, D.D.2    Morgenstern, M.R.3
  • 14
    • 0026544697 scopus 로고
    • Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme
    • Ruetschi, U., Odelhog, B., Lindstedt, S., Barros-Soderling, J., Persson, B., and Jornvall, H. (1992) Characterization of 4-hydroxyphenylpyruvate dioxygenase. Primary structure of the Pseudomonas enzyme, Eur. J. Biochem. 205, 459-466.
    • (1992) Eur. J. Biochem. , vol.205 , pp. 459-466
    • Ruetschi, U.1    Odelhog, B.2    Lindstedt, S.3    Barros-Soderling, J.4    Persson, B.5    Jornvall, H.6
  • 15
    • 0017381929 scopus 로고
    • Purification and some properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. P. J. 874
    • Lindstedt, S., Odelhog, B., and Rundgren, M. (1977) Purification and some properties of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. P. J. 874, Biochemistry 16, 3369-3377.
    • (1977) Biochemistry , vol.16 , pp. 3369-3377
    • Lindstedt, S.1    Odelhog, B.2    Rundgren, M.3
  • 16
    • 0033566995 scopus 로고    scopus 로고
    • Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: An enzyme involved in the tyrosine degradation pathway
    • Serre, L., Sailland, A., Sy, D., Boudec, P., Rolland, A., Pebay-Peyroula, E., and Cohen-Addad, C. (1999) Crystal structure of Pseudomonas fluorescens 4-hydroxyphenylpyruvate dioxygenase: an enzyme involved in the tyrosine degradation pathway, Struct. Fold Des. 7, 977-988.
    • (1999) Struct. Fold Des. , vol.7 , pp. 977-988
    • Serre, L.1    Sailland, A.2    Sy, D.3    Boudec, P.4    Rolland, A.5    Pebay-Peyroula, E.6    Cohen-Addad, C.7
  • 17
    • 0020422576 scopus 로고
    • Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874
    • Lindstedt, S., and Rundgren, M. (1982) Blue color, metal content, and substrate binding in 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874, J. Biol. Chem. 257, 11922-11931.
    • (1982) J. Biol. Chem. , vol.257 , pp. 11922-11931
    • Lindstedt, S.1    Rundgren, M.2
  • 18
    • 0030952515 scopus 로고    scopus 로고
    • A mechanistic rationalisation for the substrate specificity of recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase (4-HPPD)
    • Crouch, N. P., Adlington, R. M., Baldwin, J. E., Lee, M. H., and MacKinnon, C. H. (1997) A mechanistic rationalisation for the substrate specificity of recombinant mammalian 4-hydroxyphenylpyruvate dioxygenase (4-HPPD), Tetrahedron 53, 6993-7010.
    • (1997) Tetrahedron , vol.53 , pp. 6993-7010
    • Crouch, N.P.1    Adlington, R.M.2    Baldwin, J.E.3    Lee, M.H.4    MacKinnon, C.H.5
  • 19
    • 0037465347 scopus 로고    scopus 로고
    • (4-Hydroxyphenyl)pyruvate Dioxygenase from Streptomyces avermitilis: The Basis for Ordered Substrate Addition
    • Johnson-Winters, K., Purpero, V. M., Kavana, M., Nelson, T., and Moran, G. R. (2003) (4-Hydroxyphenyl)pyruvate Dioxygenase from Streptomyces avermitilis: The Basis for Ordered Substrate Addition, Biochemistry, 42, 2072-2080.
    • (2003) Biochemistry , vol.42 , pp. 2072-2080
    • Johnson-Winters, K.1    Purpero, V.M.2    Kavana, M.3    Nelson, T.4    Moran, G.R.5
  • 20
    • 0014952202 scopus 로고
    • The mechanism of enzymic formation of homogentisate from p-hydroxyphenylpyruvate
    • Lindblad, B., Lindstedt, G., and Lindstedt, S. (1970) The mechanism of enzymic formation of homogentisate from p-hydroxyphenylpyruvate, J. Am. Chem. Soc. 92, 7446-7449.
    • (1970) J. Am. Chem. Soc. , vol.92 , pp. 7446-7449
    • Lindblad, B.1    Lindstedt, G.2    Lindstedt, S.3
  • 21
    • 0019941570 scopus 로고
    • Tritium isotope effects in the reaction catalyzed by 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874
    • Rundgren, M. (1982) Tritium isotope effects in the reaction catalyzed by 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874, Biochim. Biophys. Acta 704, 59-65.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 59-65
    • Rundgren, M.1
  • 22
    • 0030594980 scopus 로고    scopus 로고
    • Identification and stereochemistry of the product of 4-HPPD catalyzed oxidation of the ketoacid of methionine
    • Adlington, R. M., Baldwin, J. E., Crouch, N. P., Lee, M. H., and MacKinnon, C. H. (1996) Identification and stereochemistry of the product of 4-HPPD catalyzed oxidation of the ketoacid of methionine, Bioorg. Med. Chem. Lett. 6, 2003-2006.
    • (1996) Bioorg. Med. Chem. Lett. , vol.6 , pp. 2003-2006
    • Adlington, R.M.1    Baldwin, J.E.2    Crouch, N.P.3    Lee, M.H.4    MacKinnon, C.H.5
  • 24
    • 0034523992 scopus 로고    scopus 로고
    • Biosynthesis of L-p-hydroxyphenylglycine, a nonproteinogenic amino acid constituent of peptide antibiotics
    • Hubbard, B. K., Thomas, M. G., and Walsh, C. T. (2000) Biosynthesis of L-p-hydroxyphenylglycine, a nonproteinogenic amino acid constituent of peptide antibiotics. Chem. Biol. 7, 931-942.
    • (2000) Chem. Biol. , vol.7 , pp. 931-942
    • Hubbard, B.K.1    Thomas, M.G.2    Walsh, C.T.3
  • 25
    • 0034616852 scopus 로고    scopus 로고
    • Biosynthesis of the vancomycin group of antibiotics: Involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine
    • Choroba, O. W., Williams, D. H., and Spencer, J. B. (2000) Biosynthesis of the vancomycin group of antibiotics: Involvement of an unusual dioxygenase in the pathway to (S)-4-hydroxyphenylglycine. J. Am. Chem. Soc. 122, 5389-5390.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 5389-5390
    • Choroba, O.W.1    Williams, D.H.2    Spencer, J.B.3
  • 26
    • 0017802490 scopus 로고
    • Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanine
    • Sheldrick, G. M., Jones, P. G., Kennard, O., Williams, D. H., and Smith, G. A. (1978) Structure of vancomycin and its complex with acetyl-D-alanyl-D-alanine, Nature 271, 223-225.
    • (1978) Nature , vol.271 , pp. 223-225
    • Sheldrick, G.M.1    Jones, P.G.2    Kennard, O.3    Williams, D.H.4    Smith, G.A.5
  • 27
    • 0024414215 scopus 로고
    • Structure of Complestatin, a Very Strong Inhibitor of Protease Activity of Complement in the Human-Complement System
    • Seto, H., Fujioka, T., Furihata, K., Kaneko, I., and Takahashi, S. (1989) Structure of Complestatin, a Very Strong Inhibitor of Protease Activity of Complement in the Human-Complement System, Tetrahedron Lett. 30, 4987-4990.
    • (1989) Tetrahedron Lett. , vol.30 , pp. 4987-4990
    • Seto, H.1    Fujioka, T.2    Furihata, K.3    Kaneko, I.4    Takahashi, S.5
  • 28
    • 0020539734 scopus 로고
    • Nocardicin A: Biosynthetic experiments with amino acid precursors
    • Townsend, C. A., and Brown, A. M. (1983) Nocardicin A: biosynthetic experiments with amino acid precursors, J. Am. Chem. Soc. 105, 913-918.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 913-918
    • Townsend, C.A.1    Brown, A.M.2
  • 33
    • 0345643323 scopus 로고    scopus 로고
    • Identification and analysis of the balhimycin biosynthetic gene cluster and its use for manipulating glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908
    • Pelzer, S., Sussmuth, R., Heckmann, D., Recktenwald, J., Huber, P., Jung, G., and Wohlleben, W. (1999) Identification and analysis of the balhimycin biosynthetic gene cluster and its use for manipulating glycopeptide biosynthesis in Amycolatopsis mediterranei DSM5908, Antimicrob. Agents Chemother. 43, 1565-1573.
    • (1999) Antimicrob. Agents Chemother. , vol.43 , pp. 1565-1573
    • Pelzer, S.1    Sussmuth, R.2    Heckmann, D.3    Recktenwald, J.4    Huber, P.5    Jung, G.6    Wohlleben, W.7
  • 35
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • Price, J. C., Barr, E. W., Tirupati, B., Bollinger, J. M., Jr., and Krebs, C. (2003) The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: a high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli, Biochemistry 42, 7497-7508.
    • (2003) Biochemistry , vol.42 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 36
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server, Bioinformatics 16, 404-405.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson, J. D., Gibson, T. J., Plewniak, F., Jeanmougin, F., and Higgins, D. G. (1997) The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools, Nucleic Acids Res. 25, 4876-4882.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 39
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • Saitou, N., and Nei, M. (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees, Mol. Biol. Evol. 4, 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 40
    • 0030203863 scopus 로고    scopus 로고
    • TreeView: An application to display phylogenetic trees on personal computers
    • Page, R. D. (1996) TreeView: an application to display phylogenetic trees on personal computers, Comput. Appl. Biosci. 12, 357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.1
  • 41
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction, Gene 77, 51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 42
    • 0030590525 scopus 로고    scopus 로고
    • The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity
    • Lee, M. H., Zhang, Z. H., MacKinnon, C. H., Baldwin, J. E., and Crouch, N. P. (1996) The C-terminal of rat 4-hydroxyphenylpyruvate dioxygenase is indispensable for enzyme activity, FEBS Lett. 393, 269-272.
    • (1996) FEBS Lett. , vol.393 , pp. 269-272
    • Lee, M.H.1    Zhang, Z.H.2    MacKinnon, C.H.3    Baldwin, J.E.4    Crouch, N.P.5
  • 43
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites
    • Que, L., Jr., and Ho, R. Y. (1996) Dioxygen Activation by Enzymes with Mononuclear Non-Heme Iron Active Sites, Chem. Rev. 96, 2607-2624.
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que Jr., L.1    Ho, R.Y.2
  • 44
    • 0034724670 scopus 로고    scopus 로고
    • Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/α-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding
    • Hogan, D. A., Smith, S. R., Saari, E. A., McCracken, J., and Hausinger, R. P. (2000) Site-directed mutagenesis of 2,4-dichlorophenoxyacetic acid/α-ketoglutarate dioxygenase. Identification of residues involved in metallocenter formation and substrate binding, J. Biol. Chem. 275, 12400-12409.
    • (2000) J. Biol. Chem. , vol.275 , pp. 12400-12409
    • Hogan, D.A.1    Smith, S.R.2    Saari, E.A.3    McCracken, J.4    Hausinger, R.P.5
  • 45
    • 0019980088 scopus 로고
    • Inhibition of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874 by the enol tautomer of the substrate
    • Lindstedt, S., and Rundgren, M. (1982) Inhibition of 4-hydroxyphenylpyruvate dioxygenase from Pseudomonas sp. strain P. J. 874 by the enol tautomer of the substrate, Biochim. Biophys. Acta 704, 66-74.
    • (1982) Biochim. Biophys. Acta , vol.704 , pp. 66-74
    • Lindstedt, S.1    Rundgren, M.2
  • 46
    • 0020493893 scopus 로고
    • Uncoupling in the γ-butyrobetaine hydroxylase reaction by D- and L-carnitine
    • Holme, E., Linstedt, S., and Nordin, I. (1982) Uncoupling in the γ-butyrobetaine hydroxylase reaction by D- and L-carnitine, Biochem. Biophys. Res. Commun. 107, 518-524.
    • (1982) Biochem. Biophys. Res. Commun. , vol.107 , pp. 518-524
    • Holme, E.1    Linstedt, S.2    Nordin, I.3
  • 47
    • 0019888157 scopus 로고
    • Uracil's uncoupling of the decarboxylation of α-ketoglutarate in the thymine 7-hydroxylase reaction of Neurospora crassa
    • Hsu, C. A., Saewert, M. D., Polsinelli, L. F., Jr., and Abbott, M. T. (1981) Uracil's uncoupling of the decarboxylation of α-ketoglutarate in the thymine 7-hydroxylase reaction of Neurospora crassa, J. Biol. Chem. 256, 6098-6101.
    • (1981) J. Biol. Chem. , vol.256 , pp. 6098-6101
    • Hsu, C.A.1    Saewert, M.D.2    Polsinelli Jr., L.F.3    Abbott, M.T.4
  • 48
    • 0025337148 scopus 로고
    • Purification and characterization of clavaminate synthase from Streptomyces clavuligerus: An unusual oxidative enzyme in natural product biosynthesis
    • Salowe, S. P., Marsh, E. N., and Townsend, C. A. (1990) Purification and characterization of clavaminate synthase from Streptomyces clavuligerus: an unusual oxidative enzyme in natural product biosynthesis, Biochemistry 29, 6499-6508.
    • (1990) Biochemistry , vol.29 , pp. 6499-6508
    • Salowe, S.P.1    Marsh, E.N.2    Townsend, C.A.3
  • 49
    • 0032481388 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate
    • Pavel, E. G., Zhou, J., Busby, R. W., Gunsior, M., Townsend, C. A., and Solomon. E. I. (1998) Circular dichroism and magnetic circular dichroism spectroscopic studies of the non-heme ferrous active site in clavaminate synthase and its interaction with α-ketoglutarate cosubstrate, J. Am. Chem. Soc. 120, 743-753.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 743-753
    • Pavel, E.G.1    Zhou, J.2    Busby, R.W.3    Gunsior, M.4    Townsend, C.A.5    Solomon, E.I.6
  • 52
    • 0032583527 scopus 로고    scopus 로고
    • Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation
    • Zhou, J., Gunsior, M., Bachmann, B. O., Townsend, C. A., and Solomon, E. I. (1998) Substrate binding to the α-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: Coupling mechanism of oxidative decarboxylation and hydroxylation, J. Am. Chem. Soc. 120, 13539-13540.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 13539-13540
    • Zhou, J.1    Gunsior, M.2    Bachmann, B.O.3    Townsend, C.A.4    Solomon, E.I.5
  • 53
    • 0017411774 scopus 로고
    • Steady-state kinetics of 4-hydroxyphenylpyruvate dioxygenase from human liver (III)
    • Rundgren, M. (1977) Steady-state kinetics of 4-hydroxyphenylpyruvate dioxygenase from human liver (III), J. Biol. Chem. 252, 5094-5099.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5094-5099
    • Rundgren, M.1
  • 55
    • 33947466148 scopus 로고
    • Quinol Intermediates in the Oxidation of Phenols and Their Rearrangements
    • Goodwin, S., and Witkop, B. (1957) Quinol Intermediates in the Oxidation of Phenols and Their Rearrangements, J. Am. Chem. Soc. 79, 179-185.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 179-185
    • Goodwin, S.1    Witkop, B.2
  • 56
    • 0002450846 scopus 로고
    • The proton in biological redox reactions
    • Hamilton, G. A. (1971) The proton in biological redox reactions, Prog. Bioorg. Chem. 1, 83-152.
    • (1971) Prog. Bioorg. Chem. , vol.1 , pp. 83-152
    • Hamilton, G.A.1
  • 57
    • 0343701106 scopus 로고
    • Non-heme dioxygenases: A unified mechanistic interpretation of their mode of action
    • Jefford, C. W. (1992) Non-heme dioxygenases: A unified mechanistic interpretation of their mode of action, Adv. Det. React. Mech. 2, 149-187.
    • (1992) Adv. Det. React. Mech. , vol.2 , pp. 149-187
    • Jefford, C.W.1
  • 58
    • 0018115590 scopus 로고
    • Excretion of cis- and trans-4-hydroxycyclohexylacetic acid in addition to hawkinsin in a family with a postulated defect of 4-hydroxyphenylpyruvate dioxygenase
    • Niederwieser, A., Wadman, S. K., and Danks, D. M. (1978) Excretion of cis- and trans-4-hydroxycyclohexylacetic acid in addition to hawkinsin in a family with a postulated defect of 4-hydroxyphenylpyruvate dioxygenase, Clin. Chim. Acta 90, 195-200.
    • (1978) Clin. Chim. Acta , vol.90 , pp. 195-200
    • Niederwieser, A.1    Wadman, S.K.2    Danks, D.M.3
  • 60
    • 0028596074 scopus 로고
    • Mechanism and Mechanism-Based Inactivation of 4-Hydroxyphenylpyruvate Dioxygenase
    • Forbes, B. J. R., and Hamilton, G. A. (1994) Mechanism and Mechanism-Based Inactivation of 4-Hydroxyphenylpyruvate Dioxygenase, Bioorg. Chem. 22, 343-361.
    • (1994) Bioorg. Chem. , vol.22 , pp. 343-361
    • Forbes, B.J.R.1    Hamilton, G.A.2
  • 61
    • 0021824504 scopus 로고
    • Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase
    • Pascal, R. A., Jr., Oliver, M. A., and Chen, Y. C. (1985) Alternate substrates and inhibitors of bacterial 4-hydroxyphenylpyruvate dioxygenase, Biochemistry 24, 3158-3165.
    • (1985) Biochemistry , vol.24 , pp. 3158-3165
    • Pascal Jr., R.A.1    Oliver, M.A.2    Chen, Y.C.3
  • 66
    • 1642530740 scopus 로고
    • Ketonization of 1,3-Cyclohexadienol, a Conjugated Enol
    • Pollack, R. M., Mack, J. P. G., and Blotny, G. (1987) Ketonization of 1,3-Cyclohexadienol, a Conjugated Enol, J. Am. Chem. Soc. 109, 3138-3139.
    • (1987) J. Am. Chem. Soc. , vol.109 , pp. 3138-3139
    • Pollack, R.M.1    Mack, J.P.G.2    Blotny, G.3
  • 67
    • 1642490167 scopus 로고
    • Kinetics and Mechanism of the Ketonization of a Conjugated Trienol
    • Dzingeleski, G. D., Bantia, S., Blotny, G., and Pollack, R. M. (1988) Kinetics and Mechanism of the Ketonization of a Conjugated Trienol, J. Org. Chem. 53, 1540-1544.
    • (1988) J. Org. Chem. , vol.53 , pp. 1540-1544
    • Dzingeleski, G.D.1    Bantia, S.2    Blotny, G.3    Pollack, R.M.4
  • 68
    • 0242585459 scopus 로고    scopus 로고
    • Aerobic Metabolism of 4-Hydroxybenzoic Acid in Archaea via an Unusual Pathway Involving an Intramolecular Migration (NIH Shift)
    • Fairley, D. J., Boyd, D. R., Sharma, N. D., Allen, C. C., Morgan, P., and Larkin, M. J. (2002) Aerobic Metabolism of 4-Hydroxybenzoic Acid in Archaea via an Unusual Pathway Involving an Intramolecular Migration (NIH Shift), Appl. Environ. Microbiol. 68, 6246-6255.
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6246-6255
    • Fairley, D.J.1    Boyd, D.R.2    Sharma, N.D.3    Allen, C.C.4    Morgan, P.5    Larkin, M.J.6


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