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Volumn 44, Issue 21, 2005, Pages 7623-7631

The mechanism of inactivation of 3-hydroxyanthranilate-3,4-dioxygenase by 4-Chloro-3-hydroxyanthranilate

Author keywords

[No Author keywords available]

Indexed keywords

2-AMINO-3-CARBOXYMUCONIC SEMIALDEHYDE; OXIDATIVE RING-OPENING; QUINOLINATE; SUPEROXIDES;

EID: 19644366181     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0473455     Document Type: Article
Times cited : (49)

References (50)
  • 1
    • 12444320333 scopus 로고    scopus 로고
    • The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction
    • Colabroy, K. L., and Begley, T. P. (2005) The Pyridine Ring of NAD Is Formed by a Nonenzymatic Pericyclic Reaction, J. Am. Chem. Soc. 127, 840-841.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 840-841
    • Colabroy, K.L.1    Begley, T.P.2
  • 3
    • 0036690151 scopus 로고    scopus 로고
    • Endogenous kynurenines as targets for drug discovery and development
    • Stone, T. W., and Darlington, G. L. (2002) Endogenous kynurenines as targets for drug discovery and development, Nat. Rev. Drug Discovery 1, 609-620.
    • (2002) Nat. Rev. Drug Discovery , vol.1 , pp. 609-620
    • Stone, T.W.1    Darlington, G.L.2
  • 4
    • 0742323784 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a drug target
    • Schwarcz, R. (2004) The kynurenine pathway of tryptophan degradation as a drug target, Curr. Opin. Pharmacol. 4, 12-17.
    • (2004) Curr. Opin. Pharmacol. , vol.4 , pp. 12-17
    • Schwarcz, R.1
  • 5
    • 0027225504 scopus 로고
    • Quantitation of human Immunodeficiency virus, immune activation factors, and quinolinic acid in AIDS brains
    • Achim, C., Heyes, M., and Wiley, C. (1993) Quantitation of Human Immunodeficiency Virus, Immune Activation Factors, and Quinolinic Acid in AIDS Brains, J. Clin. Invest. 91, 2769-2775.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2769-2775
    • Achim, C.1    Heyes, M.2    Wiley, C.3
  • 6
    • 0024024251 scopus 로고
    • 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims
    • Schwarcz, R., Okuno, E., White, R. J., Bird, E. D., and Whetsell, W. O., Jr. (1988) 3-Hydroxyanthranilate oxygenase activity is increased in the brains of Huntington disease victims, Proc. Natl. Acad. Sci. U.S.A. 85, 4079-4081.
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 4079-4081
    • Schwarcz, R.1    Okuno, E.2    White, R.J.3    Bird, E.D.4    Whetsell Jr., W.O.5
  • 7
    • 0027536709 scopus 로고
    • Metabolism and neuropathologic significance of quinolinic acid and kynurenic acid
    • Heyes, M. (1993) Metabolism and neuropathologic significance of quinolinic acid and kynurenic acid, Biochem. Soc. Trans. 21, 83-89.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 83-89
    • Heyes, M.1
  • 8
    • 0024208481 scopus 로고
    • 4-Chloro-3-hydroxyanthranilate inhibits brain 3-hydroxyanthranilate oxidase
    • Heyes, M., Hutto, B., and Markey, S. (1988) 4-Chloro-3- Hydroxyanthranilate Inhibits Brain 3-Hydroxyanthranilate Oxidase, Neurochem. Int. 13, 405-408.
    • (1988) Neurochem. Int. , vol.13 , pp. 405-408
    • Heyes, M.1    Hutto, B.2    Markey, S.3
  • 9
    • 19644363338 scopus 로고
    • 4-Chloro-3-hydroxyanthranilate, 6-chroro-tryptophan and norharmane attenuate quinolinic acid formation by interferon-y-stimulated monocytes (THP-1-cells)
    • Saito, K., Chen, C., Masana, M., Crowley, J., Markey, S., and Heyes, M. (1993) 4-Chloro-3-hydroxyanthranilate, 6-chroro-tryptophan and norharmane attenuate quinolinic acid formation by interferon-y-stimulated monocytes (THP-1-cells), Res. Commun., 12-14.
    • (1993) Res. Commun. , pp. 12-14
    • Saito, K.1    Chen, C.2    Masana, M.3    Crowley, J.4    Markey, S.5    Heyes, M.6
  • 10
    • 0025779659 scopus 로고
    • 4-Halo-3-hydroxyanthranilic acids: Potent competitive inhibitors of 3-hydroxy-anthranilic acid oxygenase in vitro
    • Walsh, J., Todd, W., Carpenter, B., and Schwarcz, R. (1991) 4-Halo-3-Hydroxyanthranilic Acids: Potent Competitive Inhibitors of 3-Hydroxy-Anthranilic Acid Oxygenase in Vitro, Biochem. Pharmacol. 42, 985-990.
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 985-990
    • Walsh, J.1    Todd, W.2    Carpenter, B.3    Schwarcz, R.4
  • 11
    • 0026009336 scopus 로고
    • 4-Halo-3-hydroxyanthranilates are potent inhibitors of 3-hydroxyanthranilate oxygenase in the rat brain in vitro and in vivo
    • Walsh, J., Todd, W., Carpenter, B., and Schwarcz, R. (1991) 4-Halo-3-Hydroxyanthranilates are Potent Inhibitors of 3-Hydroxyanthranilate Oxygenase in the Rat Brain in Vitro and in Vivo, Adv. Exp. Med. Biol. 294, 579-582.
    • (1991) Adv. Exp. Med. Biol. , vol.294 , pp. 579-582
    • Walsh, J.1    Todd, W.2    Carpenter, B.3    Schwarcz, R.4
  • 12
    • 0035822094 scopus 로고    scopus 로고
    • Solving the riddle of the intradiol and extradiol catechol dioxygenases: How do enzymes control hydroperoxide rearrangements
    • Bugg, T. D. H., and Lin, G. (2001) Solving the riddle of the intradiol and extradiol catechol dioxygenases: how do enzymes control hydroperoxide rearrangements, Chem. Commun. 941-952.
    • (2001) Chem. Commun. , pp. 941-952
    • Bugg, T.D.H.1    Lin, G.2
  • 13
    • 0034813032 scopus 로고    scopus 로고
    • Extradiol oxidative cleavage of catechols by ferrous and ferric complexes of 1,4,7-triazacyclononane: Insight into the mechanism of the extradiol catechol dioxygenases
    • Lin, G., Reid, G., and Bugg, T, D. H. (2001) Extradiol Oxidative Cleavage of Catechols by Ferrous and Ferric Complexes of 1,4,7-Triazacyclononane: Insight into the Mechanism of the Extradiol Catechol Dioxygenases, J. Am. Chem. Soc. 123, 5030-5039.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5030-5039
    • Lin, G.1    Reid, G.2    Bugg, T.D.H.3
  • 14
    • 0031767875 scopus 로고    scopus 로고
    • Enzymic cleavage of aromatic rings: Mechanistic aspects of the catechol dioxygenases and later enzymes of bacterial oxidative cleavage pathways
    • Bugg, T. D. H., and Winfield, C. (1998) Enzymic cleavage of aromatic rings: mechanistic aspects of the catechol dioxygenases and later enzymes of bacterial oxidative cleavage pathways, Nat. Prod. Rep. 15, 513-530.
    • (1998) Nat. Prod. Rep. , vol.15 , pp. 513-530
    • Bugg, T.D.H.1    Winfield, C.2
  • 15
    • 0037127253 scopus 로고    scopus 로고
    • The mechanism-based inactivation of 2.3-dihydroxy-biphenyl 1,2-dioxygenase by catecholic substrates
    • Vaillancourt, F., Labbe, G., Drouin, N., Fortin, P., and Eltis, L. (2002) The mechanism-based inactivation of 2.3-dihydroxy-biphenyl 1,2-dioxygenase by catecholic substrates, J. Biol. Chem. 277, 2019-2027.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2019-2027
    • Vaillancourt, F.1    Labbe, G.2    Drouin, N.3    Fortin, P.4    Eltis, L.5
  • 16
    • 0019294951 scopus 로고
    • Metabolism of 6-chlorotryptophan to 4-chloro-3-hydroxyanthranilic acid: A potent inhibitor of 3-hydroxyanthranilic acid oxidase
    • Parli, J. C., Krieter, P., and Schmidt, B. (1980) Metabolism of 6-chlorotryptophan to 4-chloro-3-hydroxyanthranilic acid: A potent inhibitor of 3-hydroxyanthranilic acid oxidase, Arch. Biochem. Biophys. 203, 161-166.
    • (1980) Arch. Biochem. Biophys. , vol.203 , pp. 161-166
    • Parli, J.C.1    Krieter, P.2    Schmidt, B.3
  • 17
    • 0037193195 scopus 로고    scopus 로고
    • Cloning of human 3-hydroxyanthranilic acid dioxygenase in Escherichia coli: Characterisation of the purified enzyme and its in vitro inhibition by Zn2+
    • Calderone, V., Trabucco, M., Menin, V., Negro, A., and Zanotti, G. (2002) Cloning of human 3-hydroxyanthranilic acid dioxygenase in Escherichia coli: characterisation of the purified enzyme and its in vitro inhibition by Zn2+, Biochim. Biophys. Acta 1596, 283-292.
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 283-292
    • Calderone, V.1    Trabucco, M.2    Menin, V.3    Negro, A.4    Zanotti, G.5
  • 18
    • 0017236996 scopus 로고
    • Beef kidney 3-hydroxy-anthranilic acid oxygenase
    • Koontz, W., and Shiman, R. (1976) Beef Kidney 3-Hydroxy-anthranilic Acid Oxygenase, J. Biol. Chem. 251, 368-377.
    • (1976) J. Biol. Chem. , vol.251 , pp. 368-377
    • Koontz, W.1    Shiman, R.2
  • 19
    • 0032513122 scopus 로고    scopus 로고
    • The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis
    • Kucharczyk, R., Zagulski, M., Rytka, J., and Herbert, C. (1998) The yeast gene YJR025c encodes a 3-hydroxyanthranilic acid dioxygenase and is involved in nicotinic acid biosynthesis, FEBS Lett. 424, 127-130.
    • (1998) FEBS Lett. , vol.424 , pp. 127-130
    • Kucharczyk, R.1    Zagulski, M.2    Rytka, J.3    Herbert, C.4
  • 21
    • 0023404040 scopus 로고
    • Rat 3-hydroxyanthranilic acid oxygenase: Purification from the liver and immunocytochemical localization in the brain
    • Okuno, E., Kohler, C., and Schwarcz, R. (1987) Rat 3-hydroxyanthranilic Acid Oxygenase: Purification from the Liver and Immunocytochemical Localization in the Brain, J. Neurochem. 49, 771-780.
    • (1987) J. Neurochem. , vol.49 , pp. 771-780
    • Okuno, E.1    Kohler, C.2    Schwarcz, R.3
  • 22
    • 0000773632 scopus 로고
    • Beef liver 3-hydroxyanthranilic acid oxidase
    • Stevens, C., and Henderson, L. (1959) Beef Liver 3-Hydroxyanthranilic Acid Oxidase, J. Biol. Chem. 234, 1188-1190.
    • (1959) J. Biol. Chem. , vol.234 , pp. 1188-1190
    • Stevens, C.1    Henderson, L.2
  • 24
    • 0025267280 scopus 로고
    • Regioselective synthesis of 4-chloro-3-hydroxyanthranilic acid, a potent in vitro inhibitor of 3-hydroxyanthranilic acid oxygenase activity from rate brain
    • Melikian, A., Boigegrain, R., Kan, J., and Soubrie, P. (1990) Regioselective synthesis of 4-chloro-3-hydroxyanthranilic acid, a potent in vitro inhibitor of 3-hydroxyanthranilic acid oxygenase activity from rate brain, Eur. J. Med Chem. 25, 267-270.
    • (1990) Eur. J. Med Chem. , vol.25 , pp. 267-270
    • Melikian, A.1    Boigegrain, R.2    Kan, J.3    Soubrie, P.4
  • 25
    • 0022931533 scopus 로고
    • Binding of oxygen-17-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site iron(2+) of extradiol dioxygenases
    • Arciero, D. M., and Lipscomb, J. D. (1986) Binding of oxygen-17-labeled substrate and inhibitors to protocatechuate 4,5-dioxygenase-nitrosyl complex. Evidence for direct substrate binding to the active site iron(2+) of extradiol dioxygenases, J. Biol. Chem. 261, 2170-2178.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2170-2178
    • Arciero, D.M.1    Lipscomb, J.D.2
  • 26
    • 0027997748 scopus 로고
    • Infrared multiphoton dissociation of large multiply charged ions for biomolecule sequencing
    • Little, D. P., Speir, J. P., Senko, M. W., O'Connor, P. B., and McLafferty, F. W. (1994) Infrared Multiphoton Dissociation of Large Multiply Charged Ions for Biomolecule Sequencing, Anal. Chem. 66, 2809-2815.
    • (1994) Anal. Chem. , vol.66 , pp. 2809-2815
    • Little, D.P.1    Speir, J.P.2    Senko, M.W.3    O'Connor, P.B.4    McLafferty, F.W.5
  • 27
    • 0037398265 scopus 로고    scopus 로고
    • Plasma electron capture dissociation for the characterization of large proteins by top down mass spectrometry
    • Sze, S. K., Ge, Y., Oh, H., and McLafferty, F. W. (2003) Plasma Electron Capture Dissociation for the Characterization of Large Proteins by Top Down Mass Spectrometry, Anal. Chem. 75, 1559-1603.
    • (2003) Anal. Chem. , vol.75 , pp. 1559-1603
    • Sze, S.K.1    Ge, Y.2    Oh, H.3    McLafferty, F.W.4
  • 28
    • 0033620364 scopus 로고    scopus 로고
    • Electron capture dissociation of gaseous multiply-charged proteins is favored at disulfide bonds and other sites of high hydrogen atom affinity
    • Zubarev, R. A., Kruger, N. A., Fridriksson, E. K., Lewis, M. A., Horn, D. M., Carpenter, B. K., and McLafferty, F. W. (1999) Electron Capture Dissociation of Gaseous Multiply-Charged Proteins is Favored at Disulfide Bonds and Other Sites of High Hydrogen Atom Affinity, J. Am. Chem. Soc. 121, 2857-2862.
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 2857-2862
    • Zubarev, R.A.1    Kruger, N.A.2    Fridriksson, E.K.3    Lewis, M.A.4    Horn, D.M.5    Carpenter, B.K.6    McLafferty, F.W.7
  • 30
    • 0034582319 scopus 로고    scopus 로고
    • Automated reduction and interpretation of high-resolution electrospray mass spectra of large molecules
    • Horn, D. M., Zubarev, R. A., and McLafferty, F. W. (2000) Automated reduction and interpretation of high-resolution electrospray mass spectra of large molecules, J. Am. Soc. Mass Spectrom. 11, 320-332.
    • (2000) J. Am. Soc. Mass Spectrom. , vol.11 , pp. 320-332
    • Horn, D.M.1    Zubarev, R.A.2    McLafferty, F.W.3
  • 34
    • 84894484215 scopus 로고
    • Spectroscopic and theoretical description of the electronic structure of the S = 3/2 nitrosyl complex of non-heme iron enzymes
    • Zhang, Y., Pavlosky, M. A., Brown, C. A., Westre, T. E., Hedman, B., Hodgson, K. O., and Solomon, E. I. (1992) Spectroscopic and theoretical description of the electronic structure of the S = 3/2 nitrosyl complex of non-heme iron enzymes J. Am. Chem. Soc. 114, 9189-9191.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 9189-9191
    • Zhang, Y.1    Pavlosky, M.A.2    Brown, C.A.3    Westre, T.E.4    Hedman, B.5    Hodgson, K.O.6    Solomon, E.I.7
  • 36
    • 0028774203 scopus 로고
    • Collisional activation of large multiply charged ions using fourier transform mass spectrometry
    • Senko, M. W., Speir, J. P., and McLafferty, F. W. (1994) Collisional Activation of Large Multiply Charged Ions Using Fourier Transform Mass Spectrometry, Anal. Chem. 66, 2801-2808.
    • (1994) Anal. Chem. , vol.66 , pp. 2801-2808
    • Senko, M.W.1    Speir, J.P.2    McLafferty, F.W.3
  • 37
    • 0037196338 scopus 로고    scopus 로고
    • Top down characterization of larger proteins (45 kDa) by electron capture dissociation mass spectrometry
    • Ge, Y., Lawhorn, B. G., ElNaggar, M., Strauss, E., Park, J.-H., Begley, T. P., and McLafferty, F. W. (2002) Top down characterization of larger proteins (45 kDa) by electron capture dissociation mass spectrometry, J. Am. Chem. Soc. 124, 672-678.
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 672-678
    • Ge, Y.1    Lawhorn, B.G.2    Elnaggar, M.3    Strauss, E.4    Park, J.-H.5    Begley, T.P.6    McLafferty, F.W.7
  • 38
    • 0025075792 scopus 로고
    • Determination of superoxide radical and singlet oxygen bases on chemiluminescence of luciferin analogs
    • Nakano, M. (1990) Determination of Superoxide Radical and Singlet Oxygen Bases on Chemiluminescence of Luciferin analogs, Methods Enzymol. 186, 585-591.
    • (1990) Methods Enzymol. , vol.186 , pp. 585-591
    • Nakano, M.1
  • 39
    • 0001460317 scopus 로고    scopus 로고
    • One-electron redox potentials of phenols in aqueous solution
    • Li, C., and Hoffman, M. Z. (1999) One-Electron Redox Potentials of Phenols in Aqueous Solution, J. Phys. Chem. B 103, 6653-6656.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 6653-6656
    • Li, C.1    Hoffman, M.Z.2
  • 40
    • 0013788501 scopus 로고
    • Rubredoxin: A new electron transfer protein from Clostridium pasteurianum
    • Lovenberg, W., and Sobel, B. E. (1965) Rubredoxin: A new electron transfer protein from Clostridium pasteurianum, Proc. Natl. Acad. Sci. U.S.A. 54, 193-199.
    • (1965) Proc. Natl. Acad. Sci. U.S.A. , vol.54 , pp. 193-199
    • Lovenberg, W.1    Sobel, B.E.2
  • 41
    • 33749300042 scopus 로고    scopus 로고
    • Kinetic Studies on the redox reactions of Clostridium pasteurianum Rubredoxin
    • Im, S.-C., and Sykes, G. A. (1996) Kinetic Studies on the redox reactions of Clostridium pasteurianum Rubredoxin, J. Chem. Soc., Dalton Trans. 11, 2219-2222.
    • (1996) J. Chem. Soc., Dalton Trans. , vol.11 , pp. 2219-2222
    • Im, S.-C.1    Sykes, G.A.2
  • 42
    • 0035476428 scopus 로고    scopus 로고
    • A role for rubredoxin in oxidative stress protection in desulfovibrio vulgaris: Catalytic electron transfer to rubrerythrin and two-iron superoxide reductase
    • Coulter, E. D., and Kurtz, D. M., Jr. (2001) A Role for Rubredoxin in Oxidative Stress Protection in Desulfovibrio vulgaris: Catalytic Electron Transfer to Rubrerythrin and Two-Iron Superoxide Reductase, Arch. Biochem. Biophys. 394, 76-86.
    • (2001) Arch. Biochem. Biophys. , vol.394 , pp. 76-86
    • Coulter, E.D.1    Kurtz Jr., D.M.2
  • 43
    • 0345109287 scopus 로고    scopus 로고
    • Anaerobic microbes: Oxygen detoxification without superoxide dismutase
    • Jenney, F. E., Jr., Verhagen, M. F., Cui, X., and Adams, M. W. (1999) Anaerobic microbes: oxygen detoxification without superoxide dismutase. Science 286, 306-309.
    • (1999) Science , vol.286 , pp. 306-309
    • Jenney Jr., F.E.1    Verhagen, M.F.2    Cui, X.3    Adams, M.W.4
  • 44
    • 0034646208 scopus 로고    scopus 로고
    • Structures of the Superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states
    • Yeh, A. P., Hu, Y., Jenney, F. E., Jr., Adams, M. W. W., and Rees, D. C. (2000) Structures of the Superoxide reductase from Pyrococcus furiosus in the oxidized and reduced states, Biochemistry 39, 2499-2508.
    • (2000) Biochemistry , vol.39 , pp. 2499-2508
    • Yeh, A.P.1    Hu, Y.2    Jenney Jr., F.E.3    Adams, M.W.W.4    Rees, D.C.5
  • 46
    • 0025678997 scopus 로고
    • Purification and characterization of desulfoferrodoxin, a novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center
    • Moura, I., Tavares, P., Moura, J. J. G., Ravi, N., Hanh, H. B., Liu, M. Y., and LeGall, J. (1990) Purification and characterization of desulfoferrodoxin, A novel protein from Desulfovibrio desulfuricans (ATCC 27774) and from Desulfovibrio vulgaris (strain Hildenborough) that contains a distorted rubredoxin center and a mononuclear ferrous center, J. Biol. Chem. 265, 21596-21602.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21596-21602
    • Moura, I.1    Tavares, P.2    Moura, J.J.G.3    Ravi, N.4    Hanh, H.B.5    Liu, M.Y.6    Legall, J.7
  • 47
    • 9444254650 scopus 로고    scopus 로고
    • Microbial detoxification of superoxide: The non-heme iron reductive paradigm for combating oxidative stress
    • Kurtz, D. M., Jr. (2004) Microbial Detoxification of Superoxide: The Non-Heme Iron Reductive Paradigm for Combating Oxidative Stress, Acc. Chem. Res. 37, 902-908.
    • (2004) Acc. Chem. Res. , vol.37 , pp. 902-908
    • Kurtz Jr., D.M.1
  • 48
    • 8644259915 scopus 로고    scopus 로고
    • Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the Superoxide reductase neelaredoxin
    • Auchere, F., Sikkink, R., Cordas, C., Raleiras, P., Tavares, P., Moura, I., and Moura, J. J. G. (2004) Overexpression and purification of Treponema pallidum rubredoxin; kinetic evidence for a superoxide-mediated electron transfer with the Superoxide reductase neelaredoxin, J. Biol. Inorg. Chem. 9, 839-849.
    • (2004) J. Biol. Inorg. Chem. , vol.9 , pp. 839-849
    • Auchere, F.1    Sikkink, R.2    Cordas, C.3    Raleiras, P.4    Tavares, P.5    Moura, I.6    Moura, J.J.G.7
  • 49
    • 4444294012 scopus 로고    scopus 로고
    • Structure of superoxide reductase bound to ferrocyanide and active site expansion upon X-ray-induced photo-reduction
    • Adam, V., Royant, A., Niviere, V., Molina-Heredia, F. P., and Bourgeois, D. (2004) Structure of Superoxide Reductase Bound to Ferrocyanide and Active Site Expansion upon X-Ray-Induced Photo-Reduction, Structure 12, 1729-1740.
    • (2004) Structure , vol.12 , pp. 1729-1740
    • Adam, V.1    Royant, A.2    Niviere, V.3    Molina-Heredia, F.P.4    Bourgeois, D.5
  • 50
    • 19644363211 scopus 로고    scopus 로고
    • Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of complex oxidation involved in NAD biosynthesis
    • Zhang, Y., Colabroy, K. L., Begley, T. P., and Ealick, S. E. (2005) Structural Studies on 3-Hydroxyanthranilate-3,4-dioxygenase: The Catalytic Mechanism of Complex Oxidation Involved in NAD Biosynthesis, Biochemistry 44, 7632-7643
    • (2005) Biochemistry , vol.44 , pp. 7632-7643
    • Zhang, Y.1    Colabroy, K.L.2    Begley, T.P.3    Ealick, S.E.4


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