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Volumn 51, Issue 2, 2007, Pages 324-333

Heterologous expression and purification of kynurenine-3-monooxygenase from Pseudomonas fluorescens strain 17400

Author keywords

Aromatic; Expression; FAD; Flavin; Hydroxylase; Kynurenine; Monooxygenase; Oxygenase; Pseudomonas; Purification; Stroke

Indexed keywords

KYNURENINE 3 MONOOXYGENASE;

EID: 33751406135     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2006.07.024     Document Type: Article
Times cited : (19)

References (35)
  • 1
    • 0029497024 scopus 로고
    • Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism
    • Botting. Chemistry and neurochemistry of the kynurenine pathway of tryptophan metabolism. Chem. Soc. Rev. 24 (1995) 401-412
    • (1995) Chem. Soc. Rev. , vol.24 , pp. 401-412
    • Botting1
  • 3
    • 0033800790 scopus 로고    scopus 로고
    • The kynurenine pathway of tryptophan degradation as a target for neuroprotective therapies
    • Luthman J. The kynurenine pathway of tryptophan degradation as a target for neuroprotective therapies. Amino Acids 19 (2000) 273-274
    • (2000) Amino Acids , vol.19 , pp. 273-274
    • Luthman, J.1
  • 5
    • 3042760741 scopus 로고    scopus 로고
    • Pathological apoptosis by xanthurenic acid, a tryptophan metabolite: activation of cell caspases but not cytoskeleton breakdown
    • Malina H.Z., Richter C., Mehl M., and Hess O.M. Pathological apoptosis by xanthurenic acid, a tryptophan metabolite: activation of cell caspases but not cytoskeleton breakdown. BMC Physiol. 1 (2001) 7
    • (2001) BMC Physiol. , vol.1 , pp. 7
    • Malina, H.Z.1    Richter, C.2    Mehl, M.3    Hess, O.M.4
  • 7
    • 0029973593 scopus 로고    scopus 로고
    • Hydrogen peroxide-mediated neuronal cell death induced by an endogenous neurotoxin, 3-hydroxykynurenine
    • Okuda S., Nishiyama N., Saito H., and Katsuki H. Hydrogen peroxide-mediated neuronal cell death induced by an endogenous neurotoxin, 3-hydroxykynurenine. Proc. Natl. Acad. Sci. USA 93 (1996) 12553-12558
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12553-12558
    • Okuda, S.1    Nishiyama, N.2    Saito, H.3    Katsuki, H.4
  • 8
    • 15044338779 scopus 로고    scopus 로고
    • Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults
    • Lipton S.A. Failures and successes of NMDA receptor antagonists: molecular basis for the use of open-channel blockers like memantine in the treatment of acute and chronic neurologic insults. NeuroRx 1 (2004) 101-110
    • (2004) NeuroRx , vol.1 , pp. 101-110
    • Lipton, S.A.1
  • 9
    • 0030346562 scopus 로고    scopus 로고
    • Kynurenine hydroxylase and kynureninase inhibitors as tools to study the role of kynurenine metabolites in the central nervous system
    • Moroni F., Carpenedo R., and Chiarugi A. Kynurenine hydroxylase and kynureninase inhibitors as tools to study the role of kynurenine metabolites in the central nervous system. Adv. Exp. Med. Biol. 398 (1996) 203-210
    • (1996) Adv. Exp. Med. Biol. , vol.398 , pp. 203-210
    • Moroni, F.1    Carpenedo, R.2    Chiarugi, A.3
  • 10
    • 0033502043 scopus 로고    scopus 로고
    • Kynurenine hydroxylase inhibitors reduce ischemic brain damage: studies with (m-nitrobenzoyl)-alanine (mNBA) and 3,4-dimethoxy-[-N-4-(nitrophenyl)thiazol-2yl]-benzenesulfonamide (Ro 61-8048) in models of focal or global brain ischemia
    • Cozzi A., Carpenedo R., and Moroni F. Kynurenine hydroxylase inhibitors reduce ischemic brain damage: studies with (m-nitrobenzoyl)-alanine (mNBA) and 3,4-dimethoxy-[-N-4-(nitrophenyl)thiazol-2yl]-benzenesulfonamide (Ro 61-8048) in models of focal or global brain ischemia. J. Cereb. Blood Flow Metab. 19 (1999) 771-777
    • (1999) J. Cereb. Blood Flow Metab. , vol.19 , pp. 771-777
    • Cozzi, A.1    Carpenedo, R.2    Moroni, F.3
  • 11
    • 0018430643 scopus 로고
    • Purification of l-Kynurenine 3-hydroxylase by affinity chromatography
    • Nishimoto Y., Takeuchi F., and Shibata Y. Purification of l-Kynurenine 3-hydroxylase by affinity chromatography. J. Chromatogr. 169 (1979) 357-364
    • (1979) J. Chromatogr. , vol.169 , pp. 357-364
    • Nishimoto, Y.1    Takeuchi, F.2    Shibata, Y.3
  • 12
    • 0031887811 scopus 로고    scopus 로고
    • l-Kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver: purification, some properties, and monoclonal antibodies directed to the enzyme
    • Uemura T., and Hirai K. l-Kynurenine 3-monooxygenase from mitochondrial outer membrane of pig liver: purification, some properties, and monoclonal antibodies directed to the enzyme. J. Biochem. (Tokyo) 123 (1998) 253-262
    • (1998) J. Biochem. (Tokyo) , vol.123 , pp. 253-262
    • Uemura, T.1    Hirai, K.2
  • 13
    • 0030333445 scopus 로고    scopus 로고
    • Purification of l-Kynurenine 3-monooxygenase from pig liver mitochondrial outer membrane
    • Uemura T., and Hirai K. Purification of l-Kynurenine 3-monooxygenase from pig liver mitochondrial outer membrane. Adv. Exp. Med. Biol. 398 (1996) 527-530
    • (1996) Adv. Exp. Med. Biol. , vol.398 , pp. 527-530
    • Uemura, T.1    Hirai, K.2
  • 14
    • 0025945533 scopus 로고
    • Kynurenine 3-monooxygenase activity of rat brain mitochondria determined by high performance liquid chromatography with electrochemical detection
    • Uemura T., and Hirai K. Kynurenine 3-monooxygenase activity of rat brain mitochondria determined by high performance liquid chromatography with electrochemical detection. Adv. Exp. Med. Biol. 294 (1991) 531-534
    • (1991) Adv. Exp. Med. Biol. , vol.294 , pp. 531-534
    • Uemura, T.1    Hirai, K.2
  • 15
    • 0033977888 scopus 로고    scopus 로고
    • Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase
    • Breton J., Avanzi N., Magagnin S., Covini N., Magistrelli G., Cozzi L., and Isacchi A. Functional characterization and mechanism of action of recombinant human kynurenine 3-hydroxylase. Eur. J. Biochem. 267 (2000) 1092-1099
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1092-1099
    • Breton, J.1    Avanzi, N.2    Magagnin, S.3    Covini, N.4    Magistrelli, G.5    Cozzi, L.6    Isacchi, A.7
  • 17
    • 0020825965 scopus 로고
    • The purification and identification of flavin nucleotides by high-performance liquid chromatography
    • Entsch B., and Sim R.G. The purification and identification of flavin nucleotides by high-performance liquid chromatography. Anal. Biochem. 133 (1983) 401-408
    • (1983) Anal. Biochem. , vol.133 , pp. 401-408
    • Entsch, B.1    Sim, R.G.2
  • 18
    • 18544367825 scopus 로고    scopus 로고
    • Accumulation of multiple intermediates in the catalytic cycle of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis
    • Johnson-Winters K., Purpero V.M., Kavana M., and Moran G.R. Accumulation of multiple intermediates in the catalytic cycle of (4-hydroxyphenyl)pyruvate dioxygenase from Streptomyces avermitilis. Biochemistry 44 (2005) 7189-7199
    • (2005) Biochemistry , vol.44 , pp. 7189-7199
    • Johnson-Winters, K.1    Purpero, V.M.2    Kavana, M.3    Moran, G.R.4
  • 19
    • 0027488558 scopus 로고
    • Kynurenine 3-hydroxylase in brain: species activity differences and effect of gerbil cerebral ischemia
    • Saito K., Quearry B.J., Saito M., Nowak Jr. T.S., Markey S.P., and Heyes M.P. Kynurenine 3-hydroxylase in brain: species activity differences and effect of gerbil cerebral ischemia. Arch. Biochem. Biophys. 307 (1993) 104-109
    • (1993) Arch. Biochem. Biophys. , vol.307 , pp. 104-109
    • Saito, K.1    Quearry, B.J.2    Saito, M.3    Nowak Jr., T.S.4    Markey, S.P.5    Heyes, M.P.6
  • 21
    • 0025161951 scopus 로고
    • A radiometric kynurenine monooxygenase assay
    • Wiseman J.S., and Nichols J.S. A radiometric kynurenine monooxygenase assay. Anal. Biochem. 184 (1990) 55-58
    • (1990) Anal. Biochem. , vol.184 , pp. 55-58
    • Wiseman, J.S.1    Nichols, J.S.2
  • 22
    • 0019973924 scopus 로고
    • Inhibition of l-Kynurenine 3-hydroxylase from Saccharomyces carlsbergensis by alpha-keto acid derivatives of branched chain amino acids
    • Shin M., Sano K., and Umezawa C. Inhibition of l-Kynurenine 3-hydroxylase from Saccharomyces carlsbergensis by alpha-keto acid derivatives of branched chain amino acids. J. Nutr. Sci. Vitaminol. (Tokyo) 28 (1982) 191-201
    • (1982) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.28 , pp. 191-201
    • Shin, M.1    Sano, K.2    Umezawa, C.3
  • 23
    • 0025074882 scopus 로고
    • Decay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase
    • Taylor M.G., and Massey V. Decay of the 4a-hydroxy-FAD intermediate of phenol hydroxylase. J. Biol. Chem. 265 (1990) 13687-13694
    • (1990) J. Biol. Chem. , vol.265 , pp. 13687-13694
    • Taylor, M.G.1    Massey, V.2
  • 24
    • 0017188035 scopus 로고
    • Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase
    • Entsch B., Ballou D.P., and Massey V. Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase. J. Biol. Chem. 251 (1976) 2550-2563
    • (1976) J. Biol. Chem. , vol.251 , pp. 2550-2563
    • Entsch, B.1    Ballou, D.P.2    Massey, V.3
  • 25
    • 0030340832 scopus 로고    scopus 로고
    • Enantiospecific synthesis and in vitro activity of selective inhibitors of rat brain kynureninase and kynurenine-3-hydroxylase
    • Giordani A., Corti L., Cini M., Bormetti R., Marconi M., Veneroni O., Speciale C., and Varasi M. Enantiospecific synthesis and in vitro activity of selective inhibitors of rat brain kynureninase and kynurenine-3-hydroxylase. Adv. Exp. Med. Biol. 398 (1996) 531-534
    • (1996) Adv. Exp. Med. Biol. , vol.398 , pp. 531-534
    • Giordani, A.1    Corti, L.2    Cini, M.3    Bormetti, R.4    Marconi, M.5    Veneroni, O.6    Speciale, C.7    Varasi, M.8
  • 27
    • 33751415946 scopus 로고    scopus 로고
    • Heart Disease and Stroke Statistics 2005, The American Stroke Association.
  • 28
    • 0028305047 scopus 로고
    • Inhibitors of kynurenine hydroxylase and kynureninase increase cerebral formation of kynurenate and have sedative and anticonvulsant activities
    • Carpenedo R., Chiarugi A., Russi P., Lombardi G., Carla V., Pellicciari R., Mattoli L., and Moroni F. Inhibitors of kynurenine hydroxylase and kynureninase increase cerebral formation of kynurenate and have sedative and anticonvulsant activities. Neuroscience 61 (1994) 237-243
    • (1994) Neuroscience , vol.61 , pp. 237-243
    • Carpenedo, R.1    Chiarugi, A.2    Russi, P.3    Lombardi, G.4    Carla, V.5    Pellicciari, R.6    Mattoli, L.7    Moroni, F.8
  • 29
    • 0036734822 scopus 로고    scopus 로고
    • Kynurenine 3-mono-oxygenase inhibitors attenuate post-ischemic neuronal death in organotypic hippocampal slice cultures
    • Carpenedo R., Meli E., Peruginelli F., Pellegrini-Giampietro D.E., and Moroni F. Kynurenine 3-mono-oxygenase inhibitors attenuate post-ischemic neuronal death in organotypic hippocampal slice cultures. J. Neurochem. 82 (2002) 1465-1471
    • (2002) J. Neurochem. , vol.82 , pp. 1465-1471
    • Carpenedo, R.1    Meli, E.2    Peruginelli, F.3    Pellegrini-Giampietro, D.E.4    Moroni, F.5
  • 30
    • 0034647059 scopus 로고    scopus 로고
    • Early kynurenergic impairment in Huntington's disease and in a transgenic animal model
    • Guidetti P., Reddy P.H., Tagle D.A., and Schwarcz R. Early kynurenergic impairment in Huntington's disease and in a transgenic animal model. Neurosci. Lett. 283 (2000) 233-235
    • (2000) Neurosci. Lett. , vol.283 , pp. 233-235
    • Guidetti, P.1    Reddy, P.H.2    Tagle, D.A.3    Schwarcz, R.4
  • 31
    • 12444320333 scopus 로고    scopus 로고
    • The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction
    • Colabroy K.L., and Begley T.P. The pyridine ring of NAD is formed by a nonenzymatic pericyclic reaction. J. Am. Chem. Soc. 127 (2005) 840-841
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 840-841
    • Colabroy, K.L.1    Begley, T.P.2
  • 32
    • 33751395745 scopus 로고    scopus 로고
    • D.P. Ballou, in: Flavins and Flavoproteins, 1984, pp. 605-618.
  • 33
    • 0017188035 scopus 로고
    • Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase
    • Entsch B., Ballou D.P., and Massey V. Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase. J. Biol. Chem. 251 (1976) 2550-2563
    • (1976) J. Biol. Chem. , vol.251 , pp. 2550-2563
    • Entsch, B.1    Ballou, D.P.2    Massey, V.3
  • 34
    • 33751408558 scopus 로고    scopus 로고
    • B. Entsch, D.P. Ballou, V. Massey, in: Flavins and Flavoproteins (18/0/15, B., Ed.), Elsevier, Amsterdam, 1976, pp. 111-123.
  • 35
    • 0027415818 scopus 로고
    • On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies
    • Maeda-Yorita K., and Massey V. On the reaction mechanism of phenol hydroxylase. New information obtained by correlation of fluorescence and absorbance stopped flow studies. J. Biol. Chem. 268 (1993) 4134-4144
    • (1993) J. Biol. Chem. , vol.268 , pp. 4134-4144
    • Maeda-Yorita, K.1    Massey, V.2


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