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Volumn 34, Issue 3, 2008, Pages 455-464

Oxygen dependence of tyrosine hydroxylase

Author keywords

Catecholamines; Human; Hypoxia; Oxygen; Tyrosine hydroxylase

Indexed keywords

DOPA; FERRIC ION; FERROUS ION; ISOENZYME; OXYGEN; TYROSINE; TYROSINE 3 MONOOXYGENASE;

EID: 42449106099     PISSN: 09394451     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00726-007-0547-7     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0026731688 scopus 로고
    • Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications
    • B Almas B Le Bourdelles T Flatmark J Mallet J Haavik 1992 Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation. Structure/activity studies and mechanistic implications Eur J Biochem 209 249 255
    • (1992) Eur J Biochem , vol.209 , pp. 249-255
    • Almas, B.1    Le Bourdelles, B.2    Flatmark, T.3    Mallet, J.4    Haavik, J.5
  • 2
    • 0026776588 scopus 로고
    • Purification and characterization of the blue-green rat phaeochromocytoma (PC12) tyrosine hydroxylase with a dopamine-Fe(III) complex. Reversal of the endogenous feedback inhibition by phosphorylation of serine-40
    • KK Andersson C Vassort BA Brennan L Que Jr J Haavik T Flatmark F Gros J Thibault 1992 Purification and characterization of the blue-green rat phaeochromocytoma (PC12) tyrosine hydroxylase with a dopamine-Fe(III) complex. Reversal of the endogenous feedback inhibition by phosphorylation of serine-40 Biochem J 284 687 695
    • (1992) Biochem J , vol.284 , pp. 687-695
    • Andersson, K.K.1    Vassort, C.2    Brennan, B.A.3    Que Jr., L.4    Haavik, J.5    Flatmark, T.6    Gros, F.7    Thibault, J.8
  • 3
    • 0029595396 scopus 로고
    • Increase in carotid body sensitivity during sustained hypoxia
    • GE Bisgard 1995 Increase in carotid body sensitivity during sustained hypoxia Biol Signals 4 292 297
    • (1995) Biol Signals , vol.4 , pp. 292-297
    • Bisgard, G.E.1
  • 4
    • 0016433042 scopus 로고
    • Functional and biochemical aspects of catecholamine metabolism in brain under hypoxia
    • RM Brown W Kehr A Carlsson 1975 Functional and biochemical aspects of catecholamine metabolism in brain under hypoxia Brain Res 85 491 509
    • (1975) Brain Res , vol.85 , pp. 491-509
    • Brown, R.M.1    Kehr, W.2    Carlsson, A.3
  • 5
    • 0027979247 scopus 로고
    • Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells
    • MF Czyzyk-Krzeska BA Furnari EE Lawson DE Millhorn 1994 Hypoxia increases rate of transcription and stability of tyrosine hydroxylase mRNA in pheochromocytoma (PC12) cells J Biol Chem 269 760 764
    • (1994) J Biol Chem , vol.269 , pp. 760-764
    • Czyzyk-Krzeska, M.F.1    Furnari, B.A.2    Lawson, E.E.3    Millhorn, D.E.4
  • 6
    • 0017081242 scopus 로고
    • Brain tyrosine hydroxylation: Alteration of oxygen affinity in vivo by immobilization or electroshock in the rat
    • JN Davis 1976 Brain tyrosine hydroxylation: alteration of oxygen affinity in vivo by immobilization or electroshock in the rat J Neurochem 27 211 215
    • (1976) J Neurochem , vol.27 , pp. 211-215
    • Davis, J.N.1
  • 7
    • 0015829829 scopus 로고
    • Effect of hypoxia on tyrosine and tryptophan hydroxylation in unanaesthetized rat brain
    • JN Davis A Carlsson 1973 Effect of hypoxia on tyrosine and tryptophan hydroxylation in unanaesthetized rat brain J Neurochem 20 913 915
    • (1973) J Neurochem , vol.20 , pp. 913-915
    • Davis, J.N.1    Carlsson, A.2
  • 8
    • 0023144674 scopus 로고
    • Adaptations of neurotransmitter synthesis to chronic hypoxia in cell culture
    • SH Feinsilver R Wong DM Raybin 1987 Adaptations of neurotransmitter synthesis to chronic hypoxia in cell culture Biochim Biophys Acta 928 56 62
    • (1987) Biochim Biophys Acta , vol.928 , pp. 56-62
    • Feinsilver, S.H.1    Wong, R.2    Raybin, D.M.3
  • 9
    • 0015337871 scopus 로고
    • The inhibition of phenylalanine and tyrosine hydroxylases by high oxygen levels
    • DB Fisher S Kaufman 1972 The inhibition of phenylalanine and tyrosine hydroxylases by high oxygen levels J Neurochem 19 1359 1365
    • (1972) J Neurochem , vol.19 , pp. 1359-1365
    • Fisher, D.B.1    Kaufman, S.2
  • 10
    • 0025777217 scopus 로고
    • Steady-state kinetic mechanism of rat tyrosine hydroxylase
    • PF Fitzpatrick 1991 Steady-state kinetic mechanism of rat tyrosine hydroxylase Biochemistry 30 3658 3662
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 11
    • 0345492036 scopus 로고    scopus 로고
    • Mechanism of aromatic amino acid hydroxylation
    • PF Fitzpatrick 2003 Mechanism of aromatic amino acid hydroxylation Biochemistry 42 14083 14091
    • (2003) Biochemistry , vol.42 , pp. 14083-14091
    • Fitzpatrick, P.F.1
  • 12
    • 0025004130 scopus 로고
    • Expression of rat tyrosine hydroxylase in insect tissue culture cells and purification and characterization of the cloned enzyme
    • PF Fitzpatrick LJ Chlumsky SC Daubner KL O'Malley 1990 Expression of rat tyrosine hydroxylase in insect tissue culture cells and purification and characterization of the cloned enzyme J Biol Chem 265 2042 2047
    • (1990) J Biol Chem , vol.265 , pp. 2042-2047
    • Fitzpatrick, P.F.1    Chlumsky, L.J.2    Daubner, S.C.3    O'Malley, K.L.4
  • 13
    • 0001623810 scopus 로고    scopus 로고
    • Tyrosine hydroxylase binds tetrahydrobiopterin cofactor with negative cooperativity, as shown by kinetic analyses and surface plasmon resonance detection
    • T Flatmark B Almas PM Knappskog SV Berge RM Svebak R Chehin A Muga A Martinez 1999 Tyrosine hydroxylase binds tetrahydrobiopterin cofactor with negative cooperativity, as shown by kinetic analyses and surface plasmon resonance detection Eur J Biochem 262 840 849
    • (1999) Eur J Biochem , vol.262 , pp. 840-849
    • Flatmark, T.1    Almas, B.2    Knappskog, P.M.3    Berge, S.V.4    Svebak, R.M.5    Chehin, R.6    Muga, A.7    Martinez, A.8
  • 14
    • 22144450350 scopus 로고    scopus 로고
    • An oxygraphic method for determining kinetic properties and catalytic mechanism of aromatic amino acid hydroxylases
    • A Fossbakk J Haavik 2005 An oxygraphic method for determining kinetic properties and catalytic mechanism of aromatic amino acid hydroxylases Anal Biochem 343 100 105
    • (2005) Anal Biochem , vol.343 , pp. 100-105
    • Fossbakk, A.1    Haavik, J.2
  • 15
    • 33144475971 scopus 로고    scopus 로고
    • Reduction and oxidation of the active site iron in tyrosine hydroxylase: Kinetics and specificity
    • PA Frantom J Seravalli SW Ragsdale PF Fitzpatrick 2006 Reduction and oxidation of the active site iron in tyrosine hydroxylase: kinetics and specificity Biochemistry 45 4338
    • (2006) Biochemistry , vol.45 , pp. 4338
    • Frantom, P.A.1    Seravalli, J.2    Ragsdale, S.W.3    Fitzpatrick, P.F.4
  • 17
    • 0031010420 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase at 2.3 a and its implications for inherited neurodegenerative diseases
    • KE Goodwill C Sabatier C Marks R Raag PF Fitzpatrick RC Stevens 1997 Crystal structure of tyrosine hydroxylase at 2.3 A and its implications for inherited neurodegenerative diseases Nat Struct Biol 4 578 585
    • (1997) Nat Struct Biol , vol.4 , pp. 578-585
    • Goodwill, K.E.1    Sabatier, C.2    Marks, C.3    Raag, R.4    Fitzpatrick, P.F.5    Stevens, R.C.6
  • 19
    • 0023265418 scopus 로고
    • A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics
    • B Grima A Lamouroux C Boni JF Julien F Javoy-Agid J Mallet 1987 A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics Nature 326 707 711
    • (1987) Nature , vol.326 , pp. 707-711
    • Grima, B.1    Lamouroux, A.2    Boni, C.3    Julien, J.F.4    Javoy-Agid, F.5    Mallet, J.6
  • 20
    • 0023837249 scopus 로고
    • Soluble tyrosine hydroxylase (tyrosine 3-monooxygenase) from bovine adrenal medulla: Large-scale purification and physicochemical properties
    • J Haavik KK Andersson L Petersson T Flatmark 1988 Soluble tyrosine hydroxylase (tyrosine 3-monooxygenase) from bovine adrenal medulla: large-scale purification and physicochemical properties Biochim Biophys Acta 953 142 156
    • (1988) Biochim Biophys Acta , vol.953 , pp. 142-156
    • Haavik, J.1    Andersson, K.K.2    Petersson, L.3    Flatmark, T.4
  • 21
    • 0019123274 scopus 로고
    • Rapid and sensitive assay of tyrosine 3-monooxygenase activity by high-performance liquid chromatography using the native fluorescence of DOPA
    • J Haavik T Flatmark 1980 Rapid and sensitive assay of tyrosine 3-monooxygenase activity by high-performance liquid chromatography using the native fluorescence of DOPA J Chromatogr 198 511 515
    • (1980) J Chromatogr , vol.198 , pp. 511-515
    • Haavik, J.1    Flatmark, T.2
  • 22
    • 0020582527 scopus 로고
    • Isolation and characterization of quinonoid dihydropterins by high-performance liquid chromatography
    • J Haavik T Flatmark 1983 Isolation and characterization of quinonoid dihydropterins by high-performance liquid chromatography J Chromatogr 257 361 372
    • (1983) J Chromatogr , vol.257 , pp. 361-372
    • Haavik, J.1    Flatmark, T.2
  • 23
    • 0023430333 scopus 로고
    • Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3-monooxygenase (tyrosine hydroxylase) reaction
    • J Haavik T Flatmark 1987 Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3-monooxygenase (tyrosine hydroxylase) reaction Eur J Biochem 168 21 26
    • (1987) Eur J Biochem , vol.168 , pp. 21-26
    • Haavik, J.1    Flatmark, T.2
  • 24
    • 0025762292 scopus 로고
    • Recombinant human tyrosine hydroxylase isozymes. Reconstitution with iron and inhibitory effect of other metal ions
    • J Haavik B Le Bourdelles A Martinez T Flatmark J Mallet 1991 Recombinant human tyrosine hydroxylase isozymes. Reconstitution with iron and inhibitory effect of other metal ions Eur J Biochem 199 371 378
    • (1991) Eur J Biochem , vol.199 , pp. 371-378
    • Haavik, J.1    Le Bourdelles, B.2    Martinez, A.3    Flatmark, T.4    Mallet, J.5
  • 25
    • 0026466943 scopus 로고
    • The incorporation of divalent metal ions into recombinant human tyrosine hydroxylase apoenzymes studied by intrinsic fluorescence and 1H-NMR spectroscopy
    • J Haavik A Martinez S Olafsdottir J Mallet T Flatmark 1992 The incorporation of divalent metal ions into recombinant human tyrosine hydroxylase apoenzymes studied by intrinsic fluorescence and 1H-NMR spectroscopy Eur J Biochem 210 23 31
    • (1992) Eur J Biochem , vol.210 , pp. 23-31
    • Haavik, J.1    Martinez, A.2    Olafsdottir, S.3    Mallet, J.4    Flatmark, T.5
  • 27
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • M Hirsila P Koivunen V Gunzler KI Kivirikko J Myllyharju 2003 Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor J Biol Chem 278 30772 30780
    • (2003) J Biol Chem , vol.278 , pp. 30772-30780
    • Hirsila, M.1    Koivunen, P.2    Gunzler, V.3    Kivirikko, K.I.4    Myllyharju, J.5
  • 28
    • 0014011414 scopus 로고
    • A kinetic study of bovine adrenal tyrosine hydroxylase
    • M Ikeda LA Fahien S Udenfriend 1966 A kinetic study of bovine adrenal tyrosine hydroxylase J Biol Chem 241 4452 4456
    • (1966) J Biol Chem , vol.241 , pp. 4452-4456
    • Ikeda, M.1    Fahien, L.A.2    Udenfriend, S.3
  • 29
    • 0018973424 scopus 로고
    • Oxygen affinity of tyrosine and tryptophan hydroxylases in synaptosomes
    • IR Katz 1980 Oxygen affinity of tyrosine and tryptophan hydroxylases in synaptosomes J Neurochem 35 760 763
    • (1980) J Neurochem , vol.35 , pp. 760-763
    • Katz, I.R.1
  • 31
    • 0029806202 scopus 로고    scopus 로고
    • Tyrosine supplementation for phenylketonuria treatment
    • R Koch 1996 Tyrosine supplementation for phenylketonuria treatment Am J Clin Nutr 64 974 975
    • (1996) Am J Clin Nutr , vol.64 , pp. 974-975
    • Koch, R.1
  • 32
    • 0033499889 scopus 로고    scopus 로고
    • Peroxynitrite inactivation of tyrosine hydroxylase: Mediation by sulfhydryl oxidation, not tyrosine nitration
    • DM Kuhn CW Aretha TJ Geddes 1999 Peroxynitrite inactivation of tyrosine hydroxylase: mediation by sulfhydryl oxidation, not tyrosine nitration J Neurosci 19 10289 10294
    • (1999) J Neurosci , vol.19 , pp. 10289-10294
    • Kuhn, D.M.1    Aretha, C.W.2    Geddes, T.J.3
  • 34
    • 0029658895 scopus 로고    scopus 로고
    • Mossbauer, electron-paramagnetic-resonance and X-ray-absorption fine-structure studies of the iron environment in recombinant human tyrosine hydroxylase
    • W Meyer-Klaucke H Winkler V Schunemann AX Trautwein HF Nolting J Haavik 1996 Mossbauer, electron-paramagnetic-resonance and X-ray-absorption fine-structure studies of the iron environment in recombinant human tyrosine hydroxylase Eur J Biochem 241 432 439
    • (1996) Eur J Biochem , vol.241 , pp. 432-439
    • Meyer-Klaucke, W.1    Winkler, H.2    Schunemann, V.3    Trautwein, A.X.4    Nolting, H.F.5    Haavik, J.6
  • 35
    • 0017598779 scopus 로고
    • Effects of stereochemical structures of tetrahydrobiopterin on tyrosine hydroxylase
    • Y Numata T Kato T Nagatsu T Sugimoto S Matsuura 1977 Effects of stereochemical structures of tetrahydrobiopterin on tyrosine hydroxylase Biochim Biophys Acta 480 104 112
    • (1977) Biochim Biophys Acta , vol.480 , pp. 104-112
    • Numata, Y.1    Kato, T.2    Nagatsu, T.3    Sugimoto, T.4    Matsuura, S.5
  • 36
    • 0030568905 scopus 로고    scopus 로고
    • Characterization of the active site iron in tyrosine hydroxylase. Redox states of the iron
    • AJ Ramsey PJ Hillas PF Fitzpatrick 1996 Characterization of the active site iron in tyrosine hydroxylase. Redox states of the iron J Biol Chem 271 24395 24400
    • (1996) J Biol Chem , vol.271 , pp. 24395-24400
    • Ramsey, A.J.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 38
    • 0031913225 scopus 로고    scopus 로고
    • Catecholamines, hypoxia and high altitude
    • M Rostrup 1998 Catecholamines, hypoxia and high altitude Acta Physiol Scand 162 389 399
    • (1998) Acta Physiol Scand , vol.162 , pp. 389-399
    • Rostrup, M.1
  • 41
    • 0017372991 scopus 로고
    • The oxygen tension field within a discrete volume of cerebral cortex
    • RH Smith EJ Guilbeau DD Reneau 1977 The oxygen tension field within a discrete volume of cerebral cortex Microvasc Res 13 233 240
    • (1977) Microvasc Res , vol.13 , pp. 233-240
    • Smith, R.H.1    Guilbeau, E.J.2    Reneau, D.D.3
  • 42
    • 33748367238 scopus 로고    scopus 로고
    • Mutations in the BH4-metabolizing genes GTP cyclohydrolase I, 6-pyruvoyl-tetrahydropterin synthase, sepiapterin reductase, carbinolamine-4a-dehydratase, and dihydropteridine reductase
    • B Thony N Blau 2006 Mutations in the BH4-metabolizing genes GTP cyclohydrolase I, 6-pyruvoyl-tetrahydropterin synthase, sepiapterin reductase, carbinolamine-4a-dehydratase, and dihydropteridine reductase Hum Mutat 27 870 878
    • (2006) Hum Mutat , vol.27 , pp. 870-878
    • Thony, B.1    Blau, N.2
  • 43
    • 0021761501 scopus 로고
    • Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron
    • DE Wallick LM Bloom BJ Gaffney SJ Benkovic 1984 Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron Biochemistry 23 1295 1302
    • (1984) Biochemistry , vol.23 , pp. 1295-1302
    • Wallick, D.E.1    Bloom, L.M.2    Gaffney, B.J.3    Benkovic, S.J.4


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