메뉴 건너뛰기




Volumn 74, Issue , 2000, Pages 235-294

The aromatic amino acid hydroxylases

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; NONHEME IRON PROTEIN; PHENYLALANINE 4 MONOOXYGENASE; TRYPTOPHAN HYDROXYLASE; TYROSINE 3 MONOOXYGENASE;

EID: 0033660818     PISSN: 0065258X     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article
Times cited : (87)

References (198)
  • 1
    • 0025929715 scopus 로고
    • Limited proteolysis of rat brain tyrosine hydroxylase defines an N-terminal region required for regulation of cofactor binding and directing substrate specificity
    • Abate C, Joh tH (1991): Limited proteolysis of rat brain tyrosine hydroxylase defines an N-terminal region required for regulation of cofactor binding and directing substrate specificity. J Mol Neurosci 2: 203-215.
    • (1991) J Mol Neurosci , vol.2 , pp. 203-215
    • Abate, C.1    Th, J.2
  • 2
    • 0017178796 scopus 로고
    • In vitro activation of rat liver phenylalanine hydroxylase by phosphorylation
    • Abita J-P, Milstien S, Chang N, Kaufman S (1976): In vitro activation of rat liver phenylalanine hydroxylase by phosphorylation. J Biol Chem 251: 5310-5314.
    • (1976) J Biol Chem , vol.251 , pp. 5310-5314
    • Abita, J.-P.1    Milstien, S.2    Chang, N.3    Kaufman, S.4
  • 3
    • 0021682831 scopus 로고
    • The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties
    • Abita J-P, Parniak M, Kaufman S (1984): The activation of rat liver phenylalanine hydroxylase by limited proteolysis, lysolecithin, and tocopherol phosphate. Changes in conformation and catalytic properties. J Biol Chem 259: 14560-14566.
    • (1984) J Biol Chem , vol.259 , pp. 14560-14566
    • Abita, J.-P.1    Parniak, M.2    Kaufman, S.3
  • 4
    • 0030248429 scopus 로고    scopus 로고
    • 14-3-3 and its possible role in co-ordinating multiple signalling pathways
    • Aitken A (1996): 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol 6: 341-347.
    • (1996) Trends Cell Biol , vol.6 , pp. 341-347
    • Aitken, A.1
  • 6
    • 0026731688 scopus 로고
    • Regulation of recombinant human tyrosine hydroxylase isozymes by catecholamine binding and phosphorylation structure/activity studies and mechanistic implications
    • Almas B, Le Bourdelles B, Flatmark T, Mallet J, Haavik J (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
  • 8
    • 0018264496 scopus 로고
    • Tyrosine hydroxylase. Activation by protein phosphorylation and end product inhibition
    • Ames MM, Lerner P, Lovenberg W (1978): Tyrosine hydroxylase. Activation by protein phosphorylation and end product inhibition. J Biol Chem 253: 27-31.
    • (1978) J Biol Chem , vol.253 , pp. 27-31
    • Ames, M.M.1    Lerner, P.2    Lovenberg, W.3
  • 9
    • 0024232648 scopus 로고
    • Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron
    • Andersson KK, Cox DD, Que L Jr, Flatmark T, Haavik J (1988): Resonance Raman studies on the blue-green-colored bovine adrenal tyrosine 3-monooxygenase (tyrosine hydroxylase). Evidence that the feedback inhibitors adrenaline and noradrenaline are coordinated to iron. J Biol Chem 263: 18621-18626.
    • (1988) J Biol Chem , vol.263 , pp. 18621-18626
    • Andersson, K.K.1    Cox, D.D.2    Que Jr., L.3    Flatmark, T.4    Haavik, J.5
  • 10
    • 0024451831 scopus 로고
    • Evidence from EPR spectroscopy that phosphorylation of Ser-40 in bovine adrenal tyrosine hydroxylase facilitates the reduction of high-spin Fe(III) under turnover conditions
    • Andersson KK, Haavik J, Martinez A, Flatmark T, Petersson L (1989): Evidence from EPR spectroscopy that phosphorylation of Ser-40 in bovine adrenal tyrosine hydroxylase facilitates the reduction of high-spin Fe(III) under turnover conditions. FEBS Letts 258: 9-12.
    • (1989) FEBS Letts , vol.258 , pp. 9-12
    • Andersson, K.K.1    Haavik, J.2    Martinez, A.3    Flatmark, T.4    Petersson, L.5
  • 11
    • 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
    • Andersson KK, Vassort C, Brennan BA, Que L Jr, Haavik J, Flatmark T, Gros F, Thibault J (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
  • 12
    • 0014753020 scopus 로고
    • Rearrangement of quinonoid dihydropteridines to 7,8-dihydropteridines
    • Archer MC, Scrimgeour KG (1970): Rearrangement of quinonoid dihydropteridines to 7,8-dihydropteridines. Can J Biochem 48: 278-287.
    • (1970) Can J Biochem , vol.48 , pp. 278-287
    • Archer, M.C.1    Scrimgeour, K.G.2
  • 14
    • 0018279224 scopus 로고
    • Pyrimidines as cofactors for phenylalanine hydroxylase
    • Bailey SW, Ayling JE (1978): Pyrimidines as cofactors for phenylalanine hydroxylase. Biochem Biophys Res Commun 85: 1614-1621.
    • (1978) Biochem Biophys Res Commun , vol.85 , pp. 1614-1621
    • Bailey, S.W.1    Ayling, J.E.2
  • 15
    • 0019332839 scopus 로고
    • Cleavage of the 5-amino substituent of pyrimidine cofactors by phenylalanine hydroxylase
    • Bailey SW, Ayling JE (1980): Cleavage of the 5-amino substituent of pyrimidine cofactors by phenylalanine hydroxylase. J Biol Chem 255: 7774-7781.
    • (1980) J Biol Chem , vol.255 , pp. 7774-7781
    • Bailey, S.W.1    Ayling, J.E.2
  • 16
    • 0020490927 scopus 로고
    • Incorporation of molecular oxygen into pyrimidine cofactors by phenylalanine hydroxylase
    • Bailey SW, Weintraub ST, Hamilton SM, Ayling JE (1982): Incorporation of molecular oxygen into pyrimidine cofactors by phenylalanine hydroxylase. J Biol Chem 257: 8253-8260.
    • (1982) J Biol Chem , vol.257 , pp. 8253-8260
    • Bailey, S.W.1    Weintraub, S.T.2    Hamilton, S.M.3    Ayling, J.E.4
  • 17
    • 0024585931 scopus 로고
    • Changes in the cofactor binding domain of bovine striatal tyrosine hydroxylase at physiological pH upon cAMP-dependent phosphorylation mapped with tetrahydrobiopterin analogues
    • Bailey SW, Dillard SB, Thomas KB, Ayling JE (1989): Changes in the cofactor binding domain of bovine striatal tyrosine hydroxylase at physiological pH upon cAMP-dependent phosphorylation mapped with tetrahydrobiopterin analogues. Biochemistry 28: 494-504.
    • (1989) Biochemistry , vol.28 , pp. 494-504
    • Bailey, S.W.1    Dillard, S.B.2    Thomas, K.B.3    Ayling, J.E.4
  • 18
    • 0028834765 scopus 로고
    • Synthesis of 4a-hydroxytetrahydropterins and the mechanism of their nonenzymatic dehydration to quinoid dihydropterins
    • Bailey SW, Rebrin I, Boerth SR, Ayling JE (1995): Synthesis of 4a-hydroxytetrahydropterins and the mechanism of their nonenzymatic dehydration to quinoid dihydropterins. J Am Chem Soc 117: 10203-10211.
    • (1995) J Am Chem Soc , vol.117 , pp. 10203-10211
    • Bailey, S.W.1    Rebrin, I.2    Boerth, S.R.3    Ayling, J.E.4
  • 19
    • 0028070247 scopus 로고
    • Identification of metal ligands in Cu(II)-inhibited Chromobacterium violaceum phenylalanine hydroxylase by electron spin echo envelope modulation analysis of histidine to serine mutations
    • Balasubramanian S, Carr RT, Bender CJ, Peisach J, Benkovic SJ (1994): Identification of metal ligands in Cu(II)-inhibited Chromobacterium violaceum phenylalanine hydroxylase by electron spin echo envelope modulation analysis of histidine to serine mutations. Biochemistry 33: 8532-8537.
    • (1994) Biochemistry , vol.33 , pp. 8532-8537
    • Balasubramanian, S.1    Carr, R.T.2    Bender, C.J.3    Peisach, J.4    Benkovic, S.J.5
  • 22
    • 0026721593 scopus 로고
    • X-ray absorption studies of the Cudependent phenylalanine hydroxylase from Chromobacterium violaceum. Comparison of the copper coordination in oxidized and dithionite-reduced enzymes
    • Blackburn NJ, Strange RW, Carr RT, Benkovic SJ (1992): X-ray absorption studies of the Cudependent phenylalanine hydroxylase from Chromobacterium violaceum. Comparison of the copper coordination in oxidized and dithionite-reduced enzymes. Biochemistry 31: 5298-5303.
    • (1992) Biochemistry , vol.31 , pp. 5298-5303
    • Blackburn, N.J.1    Strange, R.W.2    Carr, R.T.3    Benkovic, S.J.4
  • 23
    • 37049120826 scopus 로고
    • Kinetics and mechanism of the autoxidation of the 2-amino-4-hydroxy-5,6, 7,8-tetrahydropteridines
    • Blair JA, Pearson AJ (1974): Kinetics and mechanism of the autoxidation of the 2-amino-4-hydroxy-5,6,7,8-tetrahydropteridines. J C S Perkin II 80-88.
    • (1974) J C S Perkin , vol.2 , pp. 80-88
    • Blair, J.A.1    Pearson, A.J.2
  • 24
    • 0022467392 scopus 로고
    • Characterization of phenylalanine hydroxylase
    • Bloom LM, Benkovic SJ, Gaffney BJ (1986): Characterization of phenylalanine hydroxylase. Biochemistry 25: 4204-4210.
    • (1986) Biochemistry , vol.25 , pp. 4204-4210
    • Bloom, L.M.1    Benkovic, S.J.2    Gaffney, B.J.3
  • 26
    • 0001710455 scopus 로고
    • Solution chemistry of arene oxides
    • Bruice TC, Bruice PY (1976): Solution chemistry of arene oxides. Acc Chem Res 9: 378-384.
    • (1976) Acc Chem Res , vol.9 , pp. 378-384
    • Bruice, T.C.1    Bruice, P.Y.2
  • 27
    • 0000561889 scopus 로고
    • Monooxygen donation potential of 4a-hydroperoxyflavins as compared with those of a percarboxylic acid and other hydroperoxides. Monooxygen donation to olefin, tertiary amine, alkyl sulfide, and iodide ion
    • Bruice TC, Noar JB, Ball SS, Venkatara UV (1983): Monooxygen donation potential of 4a-hydroperoxyflavins as compared with those of a percarboxylic acid and other hydroperoxides. Monooxygen donation to olefin, tertiary amine, alkyl sulfide, and iodide ion. J Am Chem Soc 105: 2452-2465.
    • (1983) J Am Chem Soc , vol.105 , pp. 2452-2465
    • Bruice, T.C.1    Noar, J.B.2    Ball, S.S.3    Venkatara, U.V.4
  • 28
    • 0027442475 scopus 로고
    • Abnormal behavior associated with point mutation in the structural gene for monoamine oxidase a
    • Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA (1993): Abnormal behavior associated with point mutation in the structural gene for monoamine oxidase A. Science 262: 578-580.
    • (1993) Science , vol.262 , pp. 578-580
    • Brunner, H.G.1    Nelen, M.2    Breakefield, X.O.3    Ropers, H.H.4    Van Oost, B.A.5
  • 30
    • 0023025693 scopus 로고
    • Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase
    • Campbell DG, Hardie DG, Vulliet PR (1986): Identification of four phosphorylation sites in the N-terminal region of tyrosine hydroxylase. J Biol Chem 261: 10489-10492.
    • (1986) J Biol Chem , vol.261 , pp. 10489-10492
    • Campbell, D.G.1    Hardie, D.G.2    Vulliet, P.R.3
  • 31
    • 0027716531 scopus 로고
    • An examination of the copper requirement of phenylalanine hydroxylase from Chromobacterium violaceum
    • Carr RT, Benkovic SJ (1993): An examination of the copper requirement of phenylalanine hydroxylase from Chromobacterium violaceum. Biochemistry 32: 14132-14138.
    • (1993) Biochemistry , vol.32 , pp. 14132-14138
    • Carr, R.T.1    Benkovic, S.J.2
  • 32
    • 0029047711 scopus 로고
    • Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase
    • Carr RT, Balasubramanian S, Hawkins PCD, Benkovic SJ (1995): Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34: 7525-7532.
    • (1995) Biochemistry , vol.34 , pp. 7525-7532
    • Carr, R.T.1    Balasubramanian, S.2    Hawkins, P.C.D.3    Benkovic, S.J.4
  • 33
    • 0032475980 scopus 로고    scopus 로고
    • Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation
    • Chen D, Frey P (1998): Phenylalanine hydroxylase from Chromobacterium violaceum. Uncoupled oxidation of tetrahydropterin and the role of iron in hydroxylation. J Biol Chem 273: 25594-25601.
    • (1998) J Biol Chem , vol.273 , pp. 25594-25601
    • Chen, D.1    Frey, P.2
  • 35
    • 0014278161 scopus 로고
    • Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase
    • Daly J, Guroff G (1968): Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase. Arch Biochem Biophys 125: 136-141.
    • (1968) Arch Biochem Biophys , vol.125 , pp. 136-141
    • Daly, J.1    Guroff, G.2
  • 36
    • 0014322138 scopus 로고
    • Isotope studies on the mechanism of action of adrenal tyrosine hydroxylase
    • Daly J, Levitt M, Guroff G, Udenfriend S (1968): Isotope studies on the mechanism of action of adrenal tyrosine hydroxylase. Arch Biochem Biophys 126: 593-598.
    • (1968) Arch Biochem Biophys , vol.126 , pp. 593-598
    • Daly, J.1    Levitt, M.2    Guroff, G.3    Udenfriend, S.4
  • 37
    • 0015510826 scopus 로고
    • Arene oxides and the NIH shift: The metabolism, toxicity and carcinogenicity of aromatic compounds
    • Daly JW, Jerina DM, Witkop B (1972): Arene oxides and the NIH shift: the metabolism, toxicity and carcinogenicity of aromatic compounds. Experientia 28: 1129-1264.
    • (1972) Experientia , vol.28 , pp. 1129-1264
    • Daly, J.W.1    Jerina, D.M.2    Witkop, B.3
  • 38
    • 3643077110 scopus 로고    scopus 로고
    • Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine
    • Daubner SC, Fitzpatrick PF (1998): Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine. Biochemistry 37: 16440-16444.
    • (1998) Biochemistry , vol.37 , pp. 16440-16444
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 39
    • 0033528728 scopus 로고    scopus 로고
    • Site-directed mutants of charged residues in the active site of tyrosine hydroxylase
    • Daubner SC, Fitzpatrick PF (1999): Site-directed mutants of charged residues in the active site of tyrosine hydroxylase. Biochemistry 38: 4448-4454.
    • (1999) Biochemistry , vol.38 , pp. 4448-4454
    • Daubner, S.C.1    Fitzpatrick, P.F.2
  • 40
    • 0026776269 scopus 로고
    • Site-directed mutagenesis of Serine 40 of rat tyrosine hydroxylase. Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity
    • Daubner SC, Lauriano C, Haycock JW, Fitzpatrick PF (1992): Site-directed mutagenesis of Serine 40 of rat tyrosine hydroxylase. Effects of dopamine and cAMP-dependent phosphorylation on enzyme activity. J Biol Chem 267: 12639-12646.
    • (1992) J Biol Chem , vol.267 , pp. 12639-12646
    • Daubner, S.C.1    Lauriano, C.2    Haycock, J.W.3    Fitzpatrick, P.F.4
  • 41
    • 0030848479 scopus 로고    scopus 로고
    • Characterization of chimeric pterin dependent hydroxylases: Contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity
    • Daubner SC, Hillas PJ, Fitzpatrick PF (1997a): Characterization of chimeric pterin dependent hydroxylases: contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity. Biochemistry 36: 11574-11582.
    • (1997) Biochemistry , vol.36 , pp. 11574-11582
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 42
    • 0031574292 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic domain of human phenylalanine hydroxylase
    • Daubner SC, Hillas PJ, Fitzpatrick PF (1997b): Expression and characterization of the catalytic domain of human phenylalanine hydroxylase. Arch Biochem Biophys 348: 295-302.
    • (1997) Arch Biochem Biophys , vol.348 , pp. 295-302
    • Daubner, S.C.1    Hillas, P.J.2    Fitzpatrick, P.F.3
  • 43
    • 0024413420 scopus 로고
    • Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase
    • Davis MD, Kaufman S (1989): Evidence for the formation of the 4a-carbinolamine during the tyrosine-dependent oxidation of tetrahydrobiopterin by rat liver phenylalanine hydroxylase. J Biol Chem 264: 8585-8596.
    • (1989) J Biol Chem , vol.264 , pp. 8585-8596
    • Davis, M.D.1    Kaufman, S.2
  • 44
    • 0025768831 scopus 로고
    • Studies on the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase
    • Davis MD, Kaufman S (1991): Studies on the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase. Neurochem Res 16: 813-819.
    • (1991) Neurochem Res , vol.16 , pp. 813-819
    • Davis, M.D.1    Kaufman, S.2
  • 46
    • 0028109263 scopus 로고
    • Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function
    • Dickson PW, Jennings IG, Cotton RGH (1994): Delineation of the catalytic core of phenylalanine hydroxylase and identification of glutamate 286 as a critical residue for pterin function. J Biol Chem 269: 20369-20375.
    • (1994) J Biol Chem , vol.269 , pp. 20369-20375
    • Dickson, P.W.1    Jennings, I.G.2    Cotton, R.G.H.3
  • 47
    • 0022380807 scopus 로고
    • Mechanism of "uncoupled" tetrahydropterin oxidation by phenylalanine hydroxylase
    • Dix TA, Benkovic SJ (1985): Mechanism of "uncoupled" tetrahydropterin oxidation by phenylalanine hydroxylase. Biochemistry 24: 5839-5846.
    • (1985) Biochemistry , vol.24 , pp. 5839-5846
    • Dix, T.A.1    Benkovic, S.J.2
  • 48
    • 0022418789 scopus 로고
    • Phenylalanine hydroxylase: Absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species
    • Dix TA, Bollag G, Domanico PL, Benkovic SJ (1985): Phenylalanine hydroxylase: absolute configuration and source of oxygen of the 4a-hydroxytetrahydropterin species. Biochemistry 24: 2955-2958.
    • (1985) Biochemistry , vol.24 , pp. 2955-2958
    • Dix, T.A.1    Bollag, G.2    Domanico, P.L.3    Benkovic, S.J.4
  • 49
    • 0023657759 scopus 로고
    • Mechanism of oxygen activation by tyrosine hydroxylase
    • Dix TA, Kuhn DM, Benkovic SJ (1987): Mechanism of oxygen activation by tyrosine hydroxylase. Biochemistry 26: 3354-3361.
    • (1987) Biochemistry , vol.26 , pp. 3354-3361
    • Dix, T.A.1    Kuhn, D.M.2    Benkovic, S.J.3
  • 50
    • 0021127277 scopus 로고
    • The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme
    • Doskeland AP, Doskeland SO, Ogreid D, Flatmark T (1984a): The effect of ligands of phenylalanine 4-monooxygenase on the cAMP-dependent phosphorylation of the enzyme. J Biol Chem 259: 11242-11248.
    • (1984) J Biol Chem , vol.259 , pp. 11242-11248
    • Doskeland, A.P.1    Doskeland, S.O.2    Ogreid, D.3    Flatmark, T.4
  • 52
    • 0021093567 scopus 로고
    • The chemistry of a 1,5-diblocked flavin. 2. Proton and electron transfer steps in the reaction of dihydroflavins with oxygen
    • Eberlein G, Bruice TC (1983): The chemistry of a 1,5-diblocked flavin. 2. Proton and electron transfer steps in the reaction of dihydroflavins with oxygen. J Am Chem Soc 105: 6685-6697.
    • (1983) J Am Chem Soc , vol.105 , pp. 6685-6697
    • Eberlein, G.1    Bruice, T.C.2
  • 53
    • 0000575758 scopus 로고
    • The interconversion of the 5,6,7,8-tetrahydro-, 7,8-dihydro-, and radical forms of 6,6,7,7-teiramethyldihydropterin. a model for the biopterin center of aromatic amino acid mixed function oxidases
    • Eberlein GA, Bmice TC, Lazarus RA, Henrie R, Benkovic SJ (1984): The interconversion of the 5,6,7,8-tetrahydro-, 7,8-dihydro-, and radical forms of 6,6,7,7-teiramethyldihydropterin. A model for the biopterin center of aromatic amino acid mixed function oxidases. J Am Chem Soc 106: 7916-7924.
    • (1984) J Am Chem Soc , vol.106 , pp. 7916-7924
    • Eberlein, G.A.1    Bmice, T.C.2    Lazarus, R.A.3    Henrie, R.4    Benkovic, S.J.5
  • 54
    • 0041808002 scopus 로고
    • Laser flash photolysis studies of intramolecular electron transfer between the FAD and iron-sulfur II centers in xanthine oxidase
    • Edmondson DE, McCormick DB (eds): Hawthorne, N.Y.: Walter de Gruyter
    • Edmondson DE, Hazzard JT, Tollin G (1987): Laser flash photolysis studies of intramolecular electron transfer between the FAD and iron-sulfur II centers in xanthine oxidase. In Edmondson DE, McCormick DB (eds): "Flavins and Flavoproteins." Hawthorne, N.Y.: Walter de Gruyter, pp. 403-408.
    • (1987) Flavins and Flavoproteins , pp. 403-408
    • Edmondson, D.E.1    Hazzard, J.T.2    Tollin, G.3
  • 55
    • 0033600563 scopus 로고    scopus 로고
    • Conserved phenylalanine residues in the active-site of tyrosine hydroxylase: Mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe 300
    • Ellis HR, Daubner SC, McCulloch RI, Fitzpatrick PF (1999): Conserved phenylalanine residues in the active-site of tyrosine hydroxylase: mutagenesis of Phe300 and Phe309 to alanine and metal ion-catalyzed hydroxylation of Phe 300. Biochemistry 38: 10909-10914.
    • (1999) Biochemistry , vol.38 , pp. 10909-10914
    • Ellis, H.R.1    Daubner, S.C.2    McCulloch, R.I.3    Fitzpatrick, P.F.4
  • 57
    • 0029001623 scopus 로고
    • Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator
    • Endrizzi JA, Cronk JD, Wang W, Crabtree GR, Alber T (1995): Crystal structure of DCoH, a bifunctional, protein-binding transcriptional coactivator. Science 268: 556-559.
    • (1995) Science , vol.268 , pp. 556-559
    • Endrizzi, J.A.1    Cronk, J.D.2    Wang, W.3    Crabtree, G.R.4    Alber, T.5
  • 58
    • 0017188035 scopus 로고
    • Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase
    • Entsch B, Ballou DP, Massey V (1976): Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase. J Biol Chem 251: 2550-2563.
    • (1976) J Biol Chem , vol.251 , pp. 2550-2563
    • Entsch, B.1    Ballou, D.P.2    Massey, V.3
  • 59
    • 0031303781 scopus 로고    scopus 로고
    • Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria
    • Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC (1997): Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat Struct Biol 4: 995-1000.
    • (1997) Nat Struct Biol , vol.4 , pp. 995-1000
    • Erlandsen, H.1    Fusetti, F.2    Martinez, A.3    Hough, E.4    Flatmark, T.5    Stevens, R.C.6
  • 60
    • 0032506049 scopus 로고    scopus 로고
    • Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 Å resolution
    • Erlandsen H, Flatmark T, Stevens RC, Hough E (1998): Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 Å resolution. Biochemistry 37: 15638-15646.
    • (1998) Biochemistry , vol.37 , pp. 15638-15646
    • Erlandsen, H.1    Flatmark, T.2    Stevens, R.C.3    Hough, E.4
  • 61
    • 0019425499 scopus 로고
    • Activation of tyrosine 3-monooxygenase in pheochromocytoma cells by adenosine
    • Erny RE, Berezo MW, Perlman RL (1981): Activation of tyrosine 3-monooxygenase in pheochromocytoma cells by adenosine. J Biol Chem 256: 1335-1339.
    • (1981) J Biol Chem , vol.256 , pp. 1335-1339
    • Erny, R.E.1    Berezo, M.W.2    Perlman, R.L.3
  • 62
    • 0015830432 scopus 로고
    • The stimulation of rat liver phenylalanine hydroxylase by lysolecithin and α-chymotrypsin
    • Fisher DB, Kaufman S (1973a): The stimulation of rat liver phenylalanine hydroxylase by lysolecithin and α-chymotrypsin. J Biol Chem 248: 4345-4353.
    • (1973) J Biol Chem , vol.248 , pp. 4345-4353
    • Fisher, D.B.1    Kaufman, S.2
  • 63
    • 0015798237 scopus 로고
    • Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase
    • Fisher DB, Kaufman S (1973b): Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase. J Biol Chem 248: 4300-4304.
    • (1973) J Biol Chem , vol.248 , pp. 4300-4304
    • Fisher, D.B.1    Kaufman, S.2
  • 64
    • 0024324003 scopus 로고
    • The metal requirement of rat tyrosine hydroxylase
    • Fitzpatrick PF (1989): The metal requirement of rat tyrosine hydroxylase. Biochem Biophys Res Commun 161: 211-215.
    • (1989) Biochem Biophys Res Commun , vol.161 , pp. 211-215
    • Fitzpatrick, P.F.1
  • 65
    • 0025777217 scopus 로고
    • The steady state kinetic mechanism of rat tyrosine hydroxylase
    • Fitzpatrick PF (1991a): The steady state kinetic mechanism of rat tyrosine hydroxylase. Biochemistry 30: 3658-3662.
    • (1991) Biochemistry , vol.30 , pp. 3658-3662
    • Fitzpatrick, P.F.1
  • 66
    • 0025900994 scopus 로고
    • Studies of the rate-limiting step in the tyrosine hydroxylase reaction: Alternate substrates, solvent isotope effects, and transition state analogs
    • Fitzpatrick PF (1991b): Studies of the rate-limiting step in the tyrosine hydroxylase reaction: alternate substrates, solvent isotope effects, and transition state analogs. Biochemistry 30: 6386-6391.
    • (1991) Biochemistry , vol.30 , pp. 6386-6391
    • Fitzpatrick, P.F.1
  • 67
    • 0028039678 scopus 로고
    • Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate
    • Fitzpatrick PF (1994): Kinetic isotope effects on hydroxylation of ring-deuterated phenylalanines by tyrosine hydroxylase provide evidence against partitioning of an arene oxide intermediate. J Am Chem Soc 116: 1133-1134.
    • (1994) J Am Chem Soc , vol.116 , pp. 1133-1134
    • Fitzpatrick, P.F.1
  • 68
    • 0032490094 scopus 로고    scopus 로고
    • Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: Evidence of rate limiting oxygen activation
    • Francisco WA, Tian G, Fitzpatrick PF, Klinman JP (1998): Oxygen-18 kinetic isotope effect studies of the tyrosine hydroxylase reaction: evidence of rate limiting oxygen activation. J Am Chem Soc 120: 4057-4062.
    • (1998) J Am Chem Soc , vol.120 , pp. 4057-4062
    • Francisco, W.A.1    Tian, G.2    Fitzpatrick, P.F.3    Klinman, J.P.4
  • 69
    • 0025339139 scopus 로고
    • Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells
    • Fukami MH, Haavik J, Flatmark T (1990): Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells. Biochem J 268: 525-528.
    • (1990) Biochem J , vol.268 , pp. 525-528
    • Fukami, M.H.1    Haavik, J.2    Flatmark, T.3
  • 70
    • 0026049417 scopus 로고
    • Different effects on activity caused by phosphorylation of tyrosine hydroxylase at serine 40 by three multifunctional protein kinases
    • Funakoshi H, Okuno S, Fujisawa H (1991): Different effects on activity caused by phosphorylation of tyrosine hydroxylase at serine 40 by three multifunctional protein kinases. J Biol Chem 266: 15614-15620.
    • (1991) J Biol Chem , vol.266 , pp. 15614-15620
    • Funakoshi, H.1    Okuno, S.2    Fujisawa, H.3
  • 71
    • 0027201574 scopus 로고
    • Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein
    • Funikawa Y, Ikuta N, Omata S, Yamauchi T, Isobe T, Ichimura T (1993): Demonstration of the phosphorylation-dependent interaction of tryptophan hydroxylase with the 14-3-3 protein. Biochem Biophys Res Commun 194: 144-149.
    • (1993) Biochem Biophys Res Commun , vol.194 , pp. 144-149
    • Funikawa, Y.1    Ikuta, N.2    Omata, S.3    Yamauchi, T.4    Isobe, T.5    Ichimura, T.6
  • 72
    • 0032479302 scopus 로고    scopus 로고
    • Structure of tetrametic human phenylalanine hydroxylase and its implications for phenylketonuria
    • Fusetti F, Erlandsen H, Flatmark T, Stevens RC (1998): Structure of tetrametic human phenylalanine hydroxylase and its implications for phenylketonuria. J Biol Chem 273: 16962-16967.
    • (1998) J Biol Chem , vol.273 , pp. 16962-16967
    • Fusetti, F.1    Erlandsen, H.2    Flatmark, T.3    Stevens, R.C.4
  • 73
    • 0025743436 scopus 로고
    • Affinity labeling of the active site and the reactive sulfhydryl associated with activation of rat liver phenylalanine hydroxylase
    • Gibbs BS, Benkovic SJ (1991): Affinity labeling of the active site and the reactive sulfhydryl associated with activation of rat liver phenylalanine hydroxylase. Biochemistry 30: 6795-3802.
    • (1991) Biochemistry , vol.30 , pp. 6795-13802
    • Gibbs, B.S.1    Benkovic, S.J.2
  • 74
    • 0027483322 scopus 로고
    • Expression of rat liver phenylalanine hydroxylase in insect cells and site-directed mutagenesis of putative non-heme iron-binding sites
    • Gibbs BS, Wojchowski D, Benkovic SJ (1993): Expression of rat liver phenylalanine hydroxylase in insect cells and site-directed mutagenesis of putative non-heme iron-binding sites. J Biol Chem 268: 8046-8052.
    • (1993) J Biol Chem , vol.268 , pp. 8046-8052
    • Gibbs, B.S.1    Wojchowski, D.2    Benkovic, S.J.3
  • 76
    • 0032578427 scopus 로고    scopus 로고
    • Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: Self-hydroxylation of phe300 and the pterin-binding site
    • Goodwill KE, Sabatier C, Stevens RC (1998): Crystal structure of tyrosine hydroxylase with bound cofactor analogue and iron at 2.3 Å resolution: self-hydroxylation of phe300 and the pterin-binding site. Biochemistry 37: 13437-13445.
    • (1998) Biochemistry , vol.37 , pp. 13437-13445
    • Goodwill, K.E.1    Sabatier, C.2    Stevens, R.C.3
  • 77
    • 0039084143 scopus 로고
    • An overview of serotonin and psychiatry
    • Stahl SM (ed): New York: Raven Press, Ltd.
    • Grahame-Smith DG (1992): An overview of serotonin and psychiatry. In Stahl SM (ed): "Serotonin 1A Receptors in Depression and Anxiety." New York: Raven Press, Ltd., pp. 1-21.
    • (1992) Serotonin 1A Receptors in Depression and Anxiety , pp. 1-21
    • Grahame-Smith, D.G.1
  • 78
    • 0023393590 scopus 로고
    • Full-length cDNA for rabbit tryptophan hydroxylase: Functional domains and evolution of aromatic amino acid hydroxylases
    • Grenett HE, Ledley FD, Reed LL, Woo SLC (1987): Full-length cDNA for rabbit tryptophan hydroxylase: functional domains and evolution of aromatic amino acid hydroxylases. Proc Natl Acad Sxi U S A 84: 5530-5534.
    • (1987) Proc Natl Acad Sxi U S A , vol.84 , pp. 5530-5534
    • Grenett, H.E.1    Ledley, F.D.2    Reed, L.L.3    Woo, S.L.C.4
  • 79
    • 0023819354 scopus 로고
    • 2+-dependent phosphorylation of tyrosine hydroxylase
    • 2+-dependent phosphorylation of tyrosine hydroxylase. J Biol Chem 263: 9542-9549.
    • (1988) J Biol Chem , vol.263 , pp. 9542-9549
    • Griffith, L.C.1    Schulman, H.2
  • 81
    • 0023265418 scopus 로고
    • A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics
    • Grima B, Lamouroux A, Boni C, Julien J-F, Javoy-Agid F, Mallet J (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
  • 82
    • 33845469510 scopus 로고
    • Chemical mechanisms of catalysis by cytochromes P-450: A unified view
    • Guengerich FP, MacDonald TL (1984): Chemical mechanisms of catalysis by cytochromes P-450: a unified view. Acc Chem Res 17: 9-16.
    • (1984) Acc Chem Res , vol.17 , pp. 9-16
    • Guengerich, F.P.1    MacDonald, T.L.2
  • 83
    • 0014023432 scopus 로고
    • The production of meta-tritiotyrosine from p-tritio-phenylalanine by phenylalanine hydroxylase
    • Guroff G, Levitt M, Daly J, Udenfriend S (1966): The production of meta-tritiotyrosine from p-tritio-phenylalanine by phenylalanine hydroxylase. Biochem Biophys Res Commun 25: 253-259.
    • (1966) Biochem Biophys Res Commun , vol.25 , pp. 253-259
    • Guroff, G.1    Levitt, M.2    Daly, J.3    Udenfriend, S.4
  • 85
    • 0023430333 scopus 로고
    • Isolation and characterization of tetrahydropterin oxidation products generated in the tyrosine 3-monooxygenase (tyrosine hydroxylase) reaction
    • Haavik J, Flatmark T (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
  • 86
    • 0023837249 scopus 로고
    • Soluble tyrosine hydroxylase (tyrosine 3-monooxygenase) from bovine adrenal medulla: Large-scale purification and physicochemical properties
    • Haavik J, Andersson KK, Petersson L, Flatmark T (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
  • 87
    • 0025212130 scopus 로고
    • pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40
    • Haavik J, Martinez A, Flatmark T (1990): pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of Ser-40. FEBS Lett 262: 363-365.
    • (1990) FEBS Lett , vol.262 , pp. 363-365
    • Haavik, J.1    Martinez, A.2    Flatmark, T.3
  • 88
    • 0027988151 scopus 로고
    • Microtubule-associated protein kinase-2 phosphorylates and activates tyrosine hydroxylase following depolarization of bovine adrenal chromaffin cells
    • Halloran SM, Vulliet PR (1994): Microtubule-associated protein kinase-2 phosphorylates and activates tyrosine hydroxylase following depolarization of bovine adrenal chromaffin cells. J Biol Chem 269: 30960-30965.
    • (1994) J Biol Chem , vol.269 , pp. 30960-30965
    • Halloran, S.M.1    Vulliet, P.R.2
  • 89
    • 0002450846 scopus 로고
    • The proton in biological redox reactions
    • Kaiser ET, Kezdy FJ (eds): New York: John Wiley & Sons, Inc.
    • Hamilton GA (1971): The proton in biological redox reactions. In Kaiser ET, Kezdy FJ (eds): "Progress in Biorganic Chemistry, Vol. 1." New York: John Wiley & Sons, Inc., pp. 83-157.
    • (1971) Progress in Biorganic Chemistry, Vol. 1 , vol.1 , pp. 83-157
    • Hamilton, G.A.1
  • 90
    • 0030035292 scopus 로고    scopus 로고
    • Regulation of L-DOPA biosynthesis by site-specific phosphorylation of tyrosine hydroxylase in AtT-20 cells expressing wild-type and serine 40-substituted enzyme
    • Harada K, Wu J, Haycock JW, Goldstein M (1996): Regulation of L-DOPA biosynthesis by site-specific phosphorylation of tyrosine hydroxylase in AtT-20 cells expressing wild-type and serine 40-substituted enzyme. J Neurochem 67: 629-635.
    • (1996) J Neurochem , vol.67 , pp. 629-635
    • Harada, K.1    Wu, J.2    Haycock, J.W.3    Goldstein, M.4
  • 91
    • 0021327555 scopus 로고
    • Kinetic isotope effects on cytochrome P-450-catalyzed oxidation reactions
    • Harada N, Miwa GT, Walsh JS, Lu AYH (1984): Kinetic isotope effects on cytochrome P-450-catalyzed oxidation reactions. J Biol Chem 259: 3005-3010.
    • (1984) J Biol Chem , vol.259 , pp. 3005-3010
    • Harada, N.1    Miwa, G.T.2    Walsh, J.S.3    Lu, A.Y.H.4
  • 92
    • 0025353854 scopus 로고
    • Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40
    • Haycock JW (1990): Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. J Biol Chem 265: 11682-11691.
    • (1990) J Biol Chem , vol.265 , pp. 11682-11691
    • Haycock, J.W.1
  • 94
    • 0020364148 scopus 로고
    • Multiple site phosphorylation of tyrosine hydroxylase. Differential regulation in situ by 8-bromo-cAMP and acetylcholine
    • Haycock JW, Bennett WF, George RJ, Waymire JC (1982a): Multiple site phosphorylation of tyrosine hydroxylase. Differential regulation in situ by 8-bromo-cAMP and acetylcholine. J Biol Chem 257: 13699-13703.
    • (1982) J Biol Chem , vol.257 , pp. 13699-13703
    • Haycock, J.W.1    Bennett, W.F.2    George, R.J.3    Waymire, J.C.4
  • 95
    • 0020364621 scopus 로고
    • Phosphorylation and activation of tyrosine hydroxylase mediate the acetylcholine-induced increase in catecholamine biosynthesis in adrenal chromaffin cells
    • Haycock JW, Meligeni JA, Bennett WF, Waymire JC (1982b): Phosphorylation and activation of tyrosine hydroxylase mediate the acetylcholine-induced increase in catecholamine biosynthesis in adrenal chromaffin cells. J Biol Chem 257: 12641-12648.
    • (1982) J Biol Chem , vol.257 , pp. 12641-12648
    • Haycock, J.W.1    Meligeni, J.A.2    Bennett, W.F.3    Waymire, J.C.4
  • 96
    • 0026568161 scopus 로고
    • ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ
    • Haycock JW, Ahn NG, Cobb MH, Krebs EG (1992): ERK1 and ERK2, two microtubule-associated protein 2 kinases, mediate the phosphorylation of tyrosine hydroxylase at serine-31 in situ. Proc Natl Acad Sci U S A 89: 2365-2369.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 2365-2369
    • Haycock, J.W.1    Ahn, N.G.2    Cobb, M.H.3    Krebs, E.G.4
  • 97
    • 0031712749 scopus 로고    scopus 로고
    • Role of serine-19 phosphorylation in regulating tyrosine hydroxylase studied with site- And phosphospecific antibodies and site-directed mutagenesis
    • Haycock JW, Lew JY, Garcia-Espana A, Lee KY, Harada K, Meller E, Goldstein M (1998): Role of serine-19 phosphorylation in regulating tyrosine hydroxylase studied with site- and phosphospecific antibodies and site-directed mutagenesis. J Neurochem 71: 1670-1675.
    • (1998) J Neurochem , vol.71 , pp. 1670-1675
    • Haycock, J.W.1    Lew, J.Y.2    Garcia-Espana, A.3    Lee, K.Y.4    Harada, K.5    Meller, E.6    Goldstein, M.7
  • 98
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes
    • Hegg EL, Que L Jr (1997): The 2-His-1-carboxylate facial triad. An emerging structural motif in mononuclear non-heme iron(II) enzymes. Eur J Biochem 250: 625-629.
    • (1997) Eur J Biochem , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que Jr., L.2
  • 99
    • 3643061399 scopus 로고    scopus 로고
    • A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines
    • Hillas PJ, Fitzpatrick PF (1996): A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry 35: 6969-6975.
    • (1996) Biochemistry , vol.35 , pp. 6969-6975
    • Hillas, P.J.1    Fitzpatrick, P.F.2
  • 101
    • 0018170647 scopus 로고
    • Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: Mechanism of enzyme activation
    • Job TH, Park DH, Reis DJ (1978): Direct phosphorylation of brain tyrosine hydroxylase by cyclic AMP-dependent protein kinase: mechanism of enzyme activation. Proc Natl Acad Sci U S A 75: 4744-4748.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 4744-4748
    • Job, T.H.1    Park, D.H.2    Reis, D.J.3
  • 102
  • 103
    • 0000783838 scopus 로고    scopus 로고
    • Pterin-dependent amino acid hydroxylases
    • Kappock TJ, Caradonna JP (1996): Pterin-dependent amino acid hydroxylases. Chem Rev 96: 2659-2756.
    • (1996) Chem Rev , vol.96 , pp. 2659-2756
    • Kappock, T.J.1    Caradonna, J.P.2
  • 104
    • 0029587741 scopus 로고
    • Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coll. Comparison of resting and activated states
    • Kappock TJ, Harkins PC, Friedenberg S, Caradonna JP (1995): Spectroscopic and kinetic properties of unphosphorylated rat hepatic phenylalanine hydroxylase expressed in Escherichia coll. Comparison of resting and activated states. J Biol Chem 270: 30532-30544.
    • (1995) J Biol Chem , vol.270 , pp. 30532-30544
    • Kappock, T.J.1    Harkins, P.C.2    Friedenberg, S.3    Caradonna, J.P.4
  • 105
    • 78651125086 scopus 로고
    • The structure of the phenylalanine-hydroxylation cofactor
    • Kaufman S (1963): The structure of the phenylalanine-hydroxylation cofactor. Biochemistry 50: 1085-1093.
    • (1963) Biochemistry , vol.50 , pp. 1085-1093
    • Kaufman, S.1
  • 106
    • 0018801071 scopus 로고
    • The activity of 2,4,5-triamino-6-hydroxypyrimidine in the phenylalanine hydroxylase system
    • Kaufman S (1979): The activity of 2,4,5-triamino-6-hydroxypyrimidine in the phenylalanine hydroxylase system. J Biol Chem 254: 5150-5154.
    • (1979) J Biol Chem , vol.254 , pp. 5150-5154
    • Kaufman, S.1
  • 107
    • 0021925072 scopus 로고
    • Aromatic amino acid hydroxylases
    • Kaufman S (1985): Aromatic amino acid hydroxylases. Biochem Soc Trans 13: 433-436.
    • (1985) Biochem Soc Trans , vol.13 , pp. 433-436
    • Kaufman, S.1
  • 109
    • 0020491525 scopus 로고
    • Specificity of amino acids as activators and substrates for phenylalanine hydroxylase
    • Kaufman S, Mason K (1982): Specificity of amino acids as activators and substrates for phenylalanine hydroxylase. J Biol Chem 257: 14667-14678.
    • (1982) J Biol Chem , vol.257 , pp. 14667-14678
    • Kaufman, S.1    Mason, K.2
  • 110
    • 0001100973 scopus 로고
    • The source of oxygen in the phenylalanine hydroxylase and the dopamine-β-hydroxylase catalyzed reactions
    • Kaufman S, Bridgers WF, Eisenberg F, Friedman S (1962): The source of oxygen in the phenylalanine hydroxylase and the dopamine-β-hydroxylase catalyzed reactions. Biochem Biophys Res Commun 9: 497-502.
    • (1962) Biochem Biophys Res Commun , vol.9 , pp. 497-502
    • Kaufman, S.1    Bridgers, W.F.2    Eisenberg, F.3    Friedman, S.4
  • 111
    • 0033599363 scopus 로고    scopus 로고
    • Circular dichroism and magnetic circular dichroism spectroscopy of the catalytically competent ferrous active site of phenylalanine hydroxylase and its interaction with pterin cofactor
    • Kemsley JN, Mitic N, Zaleski KL, Caradonna JP, Solomon El (1999): Circular dichroism and magnetic circular dichroism spectroscopy of the catalytically competent ferrous active site of phenylalanine hydroxylase and its interaction with pterin cofactor. J Am Chem Soc 121: 1528-1536.
    • (1999) J Am Chem Soc , vol.121 , pp. 1528-1536
    • Kemsley, J.N.1    Mitic, N.2    Zaleski, K.L.3    Caradonna, J.P.4    Solomon, E.5
  • 112
    • 7744231498 scopus 로고    scopus 로고
    • Mechanisms whereby mononuclear copper proteins functionalize organic substrates
    • Klinman JP (1996): Mechanisms whereby mononuclear copper proteins functionalize organic substrates. Chem Rev 96: 2541-2562.
    • (1996) Chem Rev , vol.96 , pp. 2541-2562
    • Klinman, J.P.1
  • 113
    • 0029049876 scopus 로고
    • Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene
    • Knappskog PM, Flatmark T, Mallet J, Ludecke B, Bartholome K (1995): Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene. Hum Mol Genet 4: 1209-1212.
    • (1995) Hum Mol Genet , vol.4 , pp. 1209-1212
    • Knappskog, P.M.1    Flatmark, T.2    Mallet, J.3    Ludecke, B.4    Bartholome, K.5
  • 114
    • 0030437749 scopus 로고    scopus 로고
    • Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme
    • Knappskog PM, Flatmark T, Aarden JM, Haavik J, Martinez A (1996): Structure/function relationships in human phenylalanine hydroxylase. Effect of terminal deletions on the oligomerization, activation and cooperativity of substrate binding to the enzyme. Eur J Biochem 242: 813-821.
    • (1996) Eur J Biochem , vol.242 , pp. 813-821
    • Knappskog, P.M.1    Flatmark, T.2    Aarden, J.M.3    Haavik, J.4    Martinez, A.5
  • 118
    • 0029862429 scopus 로고    scopus 로고
    • Location of the active site and proposed catalytic mechanism of pterin-4a-carbinolamine dehydratase
    • Köster S, Stier G, Ficner R, Hölzer M, Curtius H-C, Suck D, Ghisla S (1996): Location of the active site and proposed catalytic mechanism of pterin-4a-carbinolamine dehydratase. Eur J Biochem 241: 858-864.
    • (1996) Eur J Biochem , vol.241 , pp. 858-864
    • Köster, S.1    Stier, G.2    Ficner, R.3    Hölzer, M.4    Curtius, H.-C.5    Suck, D.6    Ghisla, S.7
  • 119
    • 0030898129 scopus 로고    scopus 로고
    • Phosphorylation and activation of brain tryptophan hydroxylase: Identification of serine-58 as a substrate site for protein kinase A
    • Kuhn DM, Arthur R,Jr., States JC (1997): Phosphorylation and activation of brain tryptophan hydroxylase: identification of serine-58 as a substrate site for protein kinase A. J Neurochem 68: 2220-2223.
    • (1997) J Neurochem , vol.68 , pp. 2220-2223
    • Kuhn, D.M.1    Arthur Jr., R.2    States, J.C.3
  • 120
    • 0030924507 scopus 로고    scopus 로고
    • Amino-terminal analysis of tryptophan hydroxylase: Protein kinase phosphorylation occurs at serine-58
    • Kumer SC, Mockus SM, Rucker PJ, Vrana KE (1997): Amino-terminal analysis of tryptophan hydroxylase: protein kinase phosphorylation occurs at serine-58. J Neurochem 69: 1738-1745.
    • (1997) J Neurochem , vol.69 , pp. 1738-1745
    • Kumer, S.C.1    Mockus, S.M.2    Rucker, P.J.3    Vrana, K.E.4
  • 121
    • 0019932176 scopus 로고
    • Tyrosine hydroxylase from bovine striatum: Catalytic properties of the phosphorylated and nonphosphorylated forms of the purified enzyme
    • Lazar MA, Lockfeld AJ, Truscott RJW, Barchas JD (1982): Tyrosine hydroxylase from bovine striatum: catalytic properties of the phosphorylated and nonphosphorylated forms of the purified enzyme. J Neurochem 39: 409-422.
    • (1982) J Neurochem , vol.39 , pp. 409-422
    • Lazar, M.A.1    Lockfeld, A.J.2    Truscott, R.J.W.3    Barchas, J.D.4
  • 124
    • 0025991739 scopus 로고
    • Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: An additional phosphorylated residue in isoform 2, generated through alternative splicing
    • Le Bourdellès B, Horellou P, Le Caer J-P, Denèfle P, Latta M, Haavik J, Guibert B, Mayaux J-F, Mallet J (1991): Phosphorylation of human recombinant tyrosine hydroxylase isoforms 1 and 2: an additional phosphorylated residue in isoform 2, generated through alternative splicing. J Biol Chem 266: 17124-17130.
    • (1991) J Biol Chem , vol.266 , pp. 17124-17130
    • Le Bourdellès, B.1    Horellou, P.2    Le Caer, J.-P.3    Denèfle, P.4    Latta, M.5    Haavik, J.6    Guibert, B.7    Mayaux, J.-F.8    Mallet, J.9
  • 125
    • 0022417659 scopus 로고
    • Homology between phenylalanine and tyrosine hydroxylases reveals common structural and functional domains
    • Ledley FD, DiLella AG, Kwok SCM, Woo SLC (1985): Homology between phenylalanine and tyrosine hydroxylases reveals common structural and functional domains. Biochemistry 24: 3389-3394.
    • (1985) Biochemistry , vol.24 , pp. 3389-3394
    • Ledley, F.D.1    DiLella, A.G.2    Kwok, S.C.M.3    Woo, S.L.C.4
  • 126
    • 0016280129 scopus 로고
    • The tryptophan hydroxylase of Chromobacterium violaceum
    • Letendre CH, Dickens G, Guroff G (1974): The tryptophan hydroxylase of Chromobacterium violaceum. J Biol Chem 249: 7186-7191.
    • (1974) J Biol Chem , vol.249 , pp. 7186-7191
    • Letendre, C.H.1    Dickens, G.2    Guroff, G.3
  • 127
    • 0030932624 scopus 로고    scopus 로고
    • Spectroscopic characterization of the catalytically competent ferrous site of the resting, activated, and substrate-bound forms of phenylalanine hydroxylase
    • Loev KE, Westre TE, Kappock TJ, Mitic N, Glasfeld E, Caradonna JP, Hedman B, Hodgson KO, Solomon EI (1997): Spectroscopic characterization of the catalytically competent ferrous site of the resting, activated, and substrate-bound forms of phenylalanine hydroxylase. J Am Chem Soc 119: 1901-1915.
    • (1997) J Am Chem Soc , vol.119 , pp. 1901-1915
    • Loev, K.E.1    Westre, T.E.2    Kappock, T.J.3    Mitic, N.4    Glasfeld, E.5    Caradonna, J.P.6    Hedman, B.7    Hodgson, K.O.8    Solomon, E.I.9
  • 128
    • 0027715957 scopus 로고
    • Identification of the intersubunit binding region in rat tyrosine hydroxylase
    • Lohse DL, Fitzpatrick PF (1993): Identification of the intersubunit binding region in rat tyrosine hydroxylase. Biochem Biophys Res Commun 197: 1543-1548.
    • (1993) Biochem Biophys Res Commun , vol.197 , pp. 1543-1548
    • Lohse, D.L.1    Fitzpatrick, P.F.2
  • 129
    • 0014201305 scopus 로고
    • Tryptophan hydroxylation: Measurement in pineal gland, brainstem, and carcinoid tumor
    • Lovenberg W, Jequier E, Sjoerdsma A (1967): Tryptophan hydroxylation: measurement in pineal gland, brainstem, and carcinoid tumor. Science 155: 217-219.
    • (1967) Science , vol.155 , pp. 217-219
    • Lovenberg, W.1    Jequier, E.2    Sjoerdsma, A.3
  • 130
    • 0028816765 scopus 로고
    • A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome
    • Ludecke B, Dworniczak B, Bartholome K (1995): A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome. Hum Genet 95: 123-125.
    • (1995) Hum Genet , vol.95 , pp. 123-125
    • Ludecke, B.1    Dworniczak, B.2    Bartholome, K.3
  • 132
    • 0025302550 scopus 로고
    • Involvement of activator protein in the activation of tryptophan hydroxylase by cAMP-dependent protein kinase
    • Makita Y, Okuno S, Fujisawa H (1990): Involvement of activator protein in the activation of tryptophan hydroxylase by cAMP-dependent protein kinase. FEBS Lett 268: 185-188.
    • (1990) FEBS Lett , vol.268 , pp. 185-188
    • Makita, Y.1    Okuno, S.2    Fujisawa, H.3
  • 133
    • 0018840628 scopus 로고
    • Purification and characterization of tyrosine hydroxylase from a clonal pheochromocytoma cell line
    • Markey KA, Kondo S, Shenkman L, Goldstein M (1980): Purification and characterization of tyrosine hydroxylase from a clonal pheochromocytoma cell line. Molec Pharmacol 17: 79-85.
    • (1980) Molec Pharmacol , vol.17 , pp. 79-85
    • Markey, K.A.1    Kondo, S.2    Shenkman, L.3    Goldstein, M.4
  • 134
    • 0021761508 scopus 로고
    • Stoichiometric reduction of phenylalanine hydroxylase by its cofactor a requirement for enzymatic activity
    • Marota JJA, Shiman R (1984): Stoichiometric reduction of phenylalanine hydroxylase by its cofactor a requirement for enzymatic activity. Biochemistry 23: 1303-1311.
    • (1984) Biochemistry , vol.23 , pp. 1303-1311
    • Marota, J.J.A.1    Shiman, R.2
  • 135
    • 0028108347 scopus 로고
    • Activation of molecular oxygen by flavins and flavoproteins
    • Massey V (1994): Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 269: 22459-22462.
    • (1994) J Biol Chem , vol.269 , pp. 22459-22462
    • Massey, V.1
  • 136
    • 0022381620 scopus 로고
    • Stereochemistry of biopterin cofactor and facile methods for the determination of the stereochemistry of a biologically active 5,6,7,8-tetrahydropterin
    • Matsuura S, Sugimoto T, Murata S, Sugawara Y, Iwasaki H (1985): Stereochemistry of biopterin cofactor and facile methods for the determination of the stereochemistry of a biologically active 5,6,7,8-tetrahydropterin. J.Biochem. 98: 1341-1348.
    • (1985) J.Biochem. , vol.98 , pp. 1341-1348
    • Matsuura, S.1    Sugimoto, T.2    Murata, S.3    Sugawara, Y.4    Iwasaki, H.5
  • 137
    • 0033167087 scopus 로고    scopus 로고
    • Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conforniationally sensitive to phosphorylation state and dopamine binding
    • McCulloch RI, Fitzpatrick PF (1999): Limited proteolysis of tyrosine hydroxylase identifies residues 33-50 as conforniationally sensitive to phosphorylation state and dopamine binding. Arch Biochem Biophys 367: 143-145.
    • (1999) Arch Biochem Biophys , vol.367 , pp. 143-145
    • McCulloch, R.I.1    Fitzpatrick, P.F.2
  • 138
    • 0021848582 scopus 로고
    • Nerve growth factor and other agents mediate phosphorylation and activation of tyrosine hydroxylase. A convergence of multiple kinase activities
    • McTigue M, Cremins J, Halegoua S (1985): Nerve growth factor and other agents mediate phosphorylation and activation of tyrosine hydroxylase. A convergence of multiple kinase activities. J Biol Chem 260: 9047-9056.
    • (1985) J Biol Chem , vol.260 , pp. 9047-9056
    • McTigue, M.1    Cremins, J.2    Halegoua, S.3
  • 139
    • 0020445353 scopus 로고
    • Phosphorylation and activation of tyrosine hydroxylase mediate the cAMP-induced increase in catecholamine biosynthesis in adrenal chromaffin cells
    • Meligeni JA, Haycock JW, Bennett WF, Waymire JC (1982): Phosphorylation and activation of tyrosine hydroxylase mediate the cAMP-induced increase in catecholamine biosynthesis in adrenal chromaffin cells. J Biol Chem 257: 12632-12640.
    • (1982) J Biol Chem , vol.257 , pp. 12632-12640
    • Meligeni, J.A.1    Haycock, J.W.2    Bennett, W.F.3    Waymire, J.C.4
  • 140
    • 0029658895 scopus 로고    scopus 로고
    • Mössbauer, electron-paramagnetic-resonance and X-ray-absorption fine-structure studies of the iron environment in recombinant human tyrosine hydroxylase
    • Meyer-Klaucke W, Winkler H, Schünemann V, Trautwein AX, Nolting H-F, Haavik J (1996): Mössbauer, 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    Schünemann, V.3    Trautwein, A.X.4    Nolting, H.-F.5    Haavik, J.6
  • 141
    • 0029054416 scopus 로고
    • Resonance Raman studies of catecholate and phenolate complexes of recombinant human tyrosine hydroxylase
    • Michaud-Soret I, Andersson KK, Que L Jr, Haavik J (1995): Resonance Raman studies of catecholate and phenolate complexes of recombinant human tyrosine hydroxylase. Biochemistry 34: 5504-5510.
    • (1995) Biochemistry , vol.34 , pp. 5504-5510
    • Michaud-Soret, I.1    Andersson, K.K.2    Que Jr., L.3    Haavik, J.4
  • 142
    • 0022256073 scopus 로고
    • The use of the natural cofactor (6R)-L-erythrotetrahydrobiopterin in the analysis of nonphosphorylated and phosphorylated rat striatal tyrosine hydroxylase atpH 7.0
    • Miller LP, Lovenberg W (1985): The use of the natural cofactor (6R)-L-erythrotetrahydrobiopterin in the analysis of nonphosphorylated and phosphorylated rat striatal tyrosine hydroxylase atpH 7.0. Biochem Int 7: 689-697.
    • (1985) Biochem Int , vol.7 , pp. 689-697
    • Miller, L.P.1    Lovenberg, W.2
  • 143
    • 0024290401 scopus 로고
    • 2]Phenylalanine, an alternate substrate for rat liver phenylalanine hydroxylase
    • 2]Phenylalanine, an alternate substrate for rat liver phenylalanine hydroxylase. Biochemistry 27: 3658-3663.
    • (1988) Biochemistry , vol.27 , pp. 3658-3663
    • Miller, R.J.1    Benkovic, S.J.2
  • 144
    • 0025687385 scopus 로고    scopus 로고
    • Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells
    • Mitchell JP, Hardie DG, Vulliet PR (1998): Site-specific phosphorylation of tyrosine hydroxylase after KCl depolarization and nerve growth factor treatment of PC12 cells. J Biol Chem 265: 22358-22364.
    • (1998) J Biol Chem , vol.265 , pp. 22358-22364
    • Mitchell, J.P.1    Hardie, D.G.2    Vulliet, P.R.3
  • 145
    • 0000726987 scopus 로고
    • Studies on 6-methyl-5-deazatetrahydropterin and its 4a adducts
    • Moad G, Luthy CL, Benkovic PA, Benkovic SJ (1979): Studies on 6-methyl-5-deazatetrahydropterin and its 4a adducts. J Am Chem Soc 101: 6068-6076.
    • (1979) J Am Chem Soc , vol.101 , pp. 6068-6076
    • Moad, G.1    Luthy, C.L.2    Benkovic, P.A.3    Benkovic, S.J.4
  • 148
    • 0032524864 scopus 로고    scopus 로고
    • Expression and characterization of the catalytic core of tryptophan hydroxylase
    • Moran GR, Daubner SC, Fitzpatrick PF (1998): Expression and characterization of the catalytic core of tryptophan hydroxylase. J Biol Chem 273: 12259-12266.
    • (1998) J Biol Chem , vol.273 , pp. 12259-12266
    • Moran, G.R.1    Daubner, S.C.2    Fitzpatrick, P.F.3
  • 149
    • 0033534158 scopus 로고    scopus 로고
    • The influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: Characterization of melhyltryptophans and azatryptophans as substrates
    • Moran GR, Phillips RMI, Fitzpatrick PF (1999): The influence of steric bulk and electrostatics on the hydroxylation regiospecificity of tryptophan hydroxylase: characterization of melhyltryptophans and azatryptophans as substrates. Biochemistry 38: 16283-16289.
    • (1999) Biochemistry , vol.38 , pp. 16283-16289
    • Moran, G.R.1    Phillips, R.M.I.2    Fitzpatrick, P.F.3
  • 150
    • 9044252959 scopus 로고
    • Tyrosine hydroxylase the initial step in norepinephrine biosynthesis
    • NagatsuT, Levin M, Udenfriend S (1964): Tyrosine hydroxylase the initial step in norepinephrine biosynthesis. J Biol Chem 239: 2910-2917.
    • (1964) J Biol Chem , vol.239 , pp. 2910-2917
    • Nagatsu, T.1    Levin, M.2    Udenfriend, S.3
  • 151
    • 0020149383 scopus 로고
    • Tryptophan 5-monooxygenase from mouse mastocytoma P815 a simple purification and general properties
    • Nakata H, Fujisawa H (1982): Tryptophan 5-monooxygenase from mouse mastocytoma P815 a simple purification and general properties. Eur J Biochem 124: 595-601.
    • (1982) Eur J Biochem , vol.124 , pp. 595-601
    • Nakata, H.1    Fujisawa, H.2
  • 152
    • 0018800373 scopus 로고
    • Phenylalanine hydroxylase from Chromobacterium violacetim purification and characterization
    • Nakata H, Yamauchi T, Fujisawa H (1979): Phenylalanine hydroxylase from Chromobacterium violacetim purification and characterization. J Biol Chem 254: 1829-1833.
    • (1979) J Biol Chem , vol.254 , pp. 1829-1833
    • Nakata, H.1    Yamauchi, T.2    Fujisawa, H.3
  • 153
    • 0023655749 scopus 로고
    • Interaction of tyrosine hydroxylase with ribonucleic acid and purification with DNA-cellulose or poly(A)-sepharose affinity chromatography
    • Nelson TJ, Kaufman S (1987): Interaction of tyrosine hydroxylase with ribonucleic acid and purification with DNA-cellulose or poly(A)-sepharose affinity chromatography. Arch Biochem Biophys 257: 69-84.
    • (1987) Arch Biochem Biophys , vol.257 , pp. 69-84
    • Nelson, T.J.1    Kaufman, S.2
  • 154
    • 0028117344 scopus 로고
    • Suicidality and 5-hydroxyindoleacetic acid concentration associated with a tryptophan hydoxylase polymorphism
    • Nielsen DA, Goldman D, Virkkunen M, Tokola R, Rawlings R, Linnoila M (1994): Suicidality and 5-hydroxyindoleacetic acid concentration associated with a tryptophan hydoxylase polymorphism. Arch Gen Psychiatry 51: 34-38.
    • (1994) Arch Gen Psychiatry , vol.51 , pp. 34-38
    • Nielsen, D.A.1    Goldman, D.2    Virkkunen, M.3    Tokola, R.4    Rawlings, R.5    Linnoila, M.6
  • 155
    • 0020092368 scopus 로고
    • Purification and some properties of tyrosine 3-monooxygenase from rat adrenal
    • Okuno S, Fujisawa H (1982): Purification and some properties of tyrosine 3-monooxygenase from rat adrenal. Eur J Biochem 122: 49-55.
    • (1982) Eur J Biochem , vol.122 , pp. 49-55
    • Okuno, S.1    Fujisawa, H.2
  • 156
    • 0023490535 scopus 로고
    • Isolation and characterization of the human tyrosine hydroxylase gene: Identification of 5′ alternative splice sites responsible for multiple mRNAs
    • O'Malley KL, Anhalt MJ, Martin BM, Kelsoe JR, Winfield SL, Ginns EI (1987): Isolation and characterization of the human tyrosine hydroxylase gene: Identification of 5′ alternative splice sites responsible for multiple mRNAs. Biochemistry 26: 6910-6914.
    • (1987) Biochemistry , vol.26 , pp. 6910-6914
    • O'Malley, K.L.1    Anhalt, M.J.2    Martin, B.M.3    Kelsoe, J.R.4    Winfield, S.L.5    Ginns, E.I.6
  • 157
    • 0019877113 scopus 로고
    • Rat liver phenylalanine hydroxylase. Activation by sulfhydryl modification
    • Parniak MA, Kaufman S (1981): Rat liver phenylalanine hydroxylase. Activation by sulfhydryl modification. J Biol Chem 256: 6876-6882.
    • (1981) J Biol Chem , vol.256 , pp. 6876-6882
    • Parniak, M.A.1    Kaufman, S.2
  • 158
    • 0023038339 scopus 로고
    • Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme
    • Pember SO, Villafranca JJ, Benkovic SJ (1986): Phenylalanine hydroxylase from Chromobacterium violaceum is a copper-containing monooxygenase. Kinetics of the reductive activation of the enzyme. Biochemistry 25: 6611-6619.
    • (1986) Biochemistry , vol.25 , pp. 6611-6619
    • Pember, S.O.1    Villafranca, J.J.2    Benkovic, S.J.3
  • 159
    • 0024963678 scopus 로고
    • Mechanistic studies on phenylalanine hydroxylase from Chromobacterium violaceum. Evidence for the formation of an enzyme-oxygen complex
    • Pember SO, Johnson KA, Villafranca JJ, Benkovic SJ (1989): Mechanistic studies on phenylalanine hydroxylase from Chromobacterium violaceum. Evidence for the formation of an enzyme-oxygen complex. Biochemistry 28: 2124-2130.
    • (1989) Biochemistry , vol.28 , pp. 2124-2130
    • Pember, S.O.1    Johnson, K.A.2    Villafranca, J.J.3    Benkovic, S.J.4
  • 160
    • 0019835638 scopus 로고
    • Effect of cyclic AMP-dependent protein phosphorylating conditions on the pH-dependent activity of tyrosine hydroxylase from beef and rat striata
    • Pollock RJ, Kapatos G, Kaufman S (1981): Effect of cyclic AMP-dependent protein phosphorylating conditions on the pH-dependent activity of tyrosine hydroxylase from beef and rat striata. J Neurochem 37: 855-860.
    • (1981) J Neurochem , vol.37 , pp. 855-860
    • Pollock, R.J.1    Kapatos, G.2    Kaufman, S.3
  • 161
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que L Jr, Ho RYN (1996): Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96: 2607-2524.
    • (1996) Chem Rev , vol.96 , pp. 2607-12524
    • Que Jr., L.1    Ho, R.Y.N.2
  • 162
    • 0031784349 scopus 로고    scopus 로고
    • Mutational analysis of substrate inhibition in tyrosine hydroxylase
    • Quinscy NS, Luong AQ, Dickson PW (1998): Mutational analysis of substrate inhibition in tyrosine hydroxylase. J Neurochem 71: 2132-2138.
    • (1998) J Neurochem , vol.71 , pp. 2132-2138
    • Quinscy, N.S.1    Luong, A.Q.2    Dickson, P.W.3
  • 163
    • 0032560609 scopus 로고    scopus 로고
    • Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: Evidence for a novel regulatory mechanism
    • Ramsey AJ, Fitzpatrick PF (1998): Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism. Biochemistry 37: 8980-8986.
    • (1998) Biochemistry , vol.37 , pp. 8980-8986
    • Ramsey, A.J.1    Fitzpatrick, P.F.2
  • 164
    • 0028826732 scopus 로고    scopus 로고
    • Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues
    • l995
    • Ramsey AJ, Daubner SC, Ehrlich JI, Fitzpatrick PF (l995): Identification of iron ligands in tyrosine hydroxylase by mutagenesis of conserved histidinyl residues. Prot Sci 4: 2082-2086.
    • Prot Sci , vol.4 , pp. 2082-2086
    • Ramsey, A.J.1    Daubner, S.C.2    Ehrlich, J.I.3    Fitzpatrick, P.F.4
  • 165
    • 0030568905 scopus 로고    scopus 로고
    • Characterization of the active site iron in tyrosine hydroxylase: Redox states of the iron
    • Ramsey AJ, Hillas PJ, Fitzpatrick PF (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
  • 167
    • 0027613060 scopus 로고
    • Deletion mutagenesis of rat PC12 tyrosine hydroxylase regulatory and catalytic domains
    • Ribeiro P, Wang Y, Citron BA, Kaufman S (1993): Deletion mutagenesis of rat PC12 tyrosine hydroxylase regulatory and catalytic domains. J Molec Neurosci 4: 125-139.
    • (1993) J Molec Neurosci , vol.4 , pp. 125-139
    • Ribeiro, P.1    Wang, Y.2    Citron, B.A.3    Kaufman, S.4
  • 168
    • 0021827585 scopus 로고
    • Purification and characterization of rat striatal tyrosine hydroxylase. Comparison of the activation by cyclic AMP-dependent phosphorylation and by other effectors
    • Richtand NM, Inagami T, Misono K, Kuczenski R (1985): Purification and characterization of rat striatal tyrosine hydroxylase. Comparison of the activation by cyclic AMP-dependent phosphorylation and by other effectors. J Biol Chem 260: 8465-8473.
    • (1985) J Biol Chem , vol.260 , pp. 8465-8473
    • Richtand, N.M.1    Inagami, T.2    Misono, K.3    Kuczenski, R.4
  • 169
    • 0026032616 scopus 로고
    • Phosphorylation of rat tyrosine hydroxylase and its model peptides in vitro by cyclic AMP-dependent protein kinase
    • Roskoski R Jr, Ritchie P (1991): Phosphorylation of rat tyrosine hydroxylase and its model peptides in vitro by cyclic AMP-dependent protein kinase. J Neurochem 56: 1019-1023.
    • (1991) J Neurochem , vol.56 , pp. 1019-1023
    • Roskoski Jr., R.1    Ritchie, P.2
  • 170
    • 0024356448 scopus 로고
    • Cerebrospinal fluid monoamine metabolites and suicidal behavior in depressed patients
    • Roy A, DeJong J, Linnoila M (1989): Cerebrospinal fluid monoamine metabolites and suicidal behavior in depressed patients. Arch Gen Psychiatry 46: 609-612.
    • (1989) Arch Gen Psychiatry , vol.46 , pp. 609-612
    • Roy, A.1    DeJong, J.2    Linnoila, M.3
  • 171
    • 0018690805 scopus 로고
    • Plotting methods for analyzing enzyme rate data
    • Rudolph FB, Fromm HJ (1979): Plotting methods for analyzing enzyme rate data. Methods Enzymol 63: 138-159.
    • (1979) Methods Enzymol , vol.63 , pp. 138-159
    • Rudolph, F.B.1    Fromm, H.J.2
  • 173
  • 174
    • 0001357567 scopus 로고
    • Phenylalanine hydroxylase and dihydropterin reductase
    • Blakley RL, Benkovic SJ (eds): New York: John Wiley & Sons
    • Shiman R (1985): Phenylalanine hydroxylase and dihydropterin reductase. In Blakley RL, Benkovic SJ (eds): "Folates and Pterins, Vol. 2." New York: John Wiley & Sons, pp. 179-249.
    • (1985) Folates and Pterins, Vol. 2 , vol.2 , pp. 179-249
    • Shiman, R.1
  • 175
    • 0019332540 scopus 로고
    • Substrate activation of phenylalanine hydroxylase. A kinetic characterizaion
    • Shiman R, Gray DW (1980): Substrate activation of phenylalanine hydroxylase. A kinetic characterizaion. J Biol Chem 255: 4793-4800.
    • (1980) J Biol Chem , vol.255 , pp. 4793-4800
    • Shiman, R.1    Gray, D.W.2
  • 176
    • 0018801561 scopus 로고
    • A simple purification of phenylalanine hydroxylase by substrate-induced hydrophobic chromatography
    • Shiman R, Gray DW, Pater A (1979): A simple purification of phenylalanine hydroxylase by substrate-induced hydrophobic chromatography. J Biol Chem 254: 11300-11306.
    • (1979) J Biol Chem , vol.254 , pp. 11300-11306
    • Shiman, R.1    Gray, D.W.2    Pater, A.3
  • 177
    • 0025336708 scopus 로고
    • Mechanism of phenylalanine regulation of phenylalanine hydroxylase
    • Shiman R, Jones SH, Gray DW (1990): Mechanism of phenylalanine regulation of phenylalanine hydroxylase. J Biol Chem 265: 11633-11642.
    • (1990) J Biol Chem , vol.265 , pp. 11633-11642
    • Shiman, R.1    Jones, S.H.2    Gray, D.W.3
  • 178
    • 0028124992 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site
    • Shiman R, Gray DW, Hill MA (1994a): Regulation of rat liver phenylalanine hydroxylase. I. Kinetic properties of the enzyme's iron and enzyme reduction site. J Biol Chem 269: 24637-24646.
    • (1994) J Biol Chem , vol.269 , pp. 24637-24646
    • Shiman, R.1    Gray, D.W.2    Hill, M.A.3
  • 179
    • 0027937757 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. H. Substrate binding and the role of activation in the control of enzymatic activity
    • Shiman R, Xia T, Hill MA, Gray DW (1994b): Regulation of rat liver phenylalanine hydroxylase. H. Substrate binding and the role of activation in the control of enzymatic activity. J Biol Chem 269: 24647-24656.
    • (1994) J Biol Chem , vol.269 , pp. 24647-24656
    • Shiman, R.1    Xia, T.2    Hill, M.A.3    Gray, D.W.4
  • 181
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER (1993): Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Ann Rev Biochem 62: 797-821.
    • (1993) Ann Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 182
    • 0027508290 scopus 로고
    • Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2
    • Sutherland C, Alterio J, Campbell DG, Le Bourdelles B, Mallet J, Haavik J, Cohen P (1993): Phosphorylation and activation of human tyrosine hydroxylase in vitro by mitogen-activated protein (MAP) kinase and MAP-kinase-activated kinases 1 and 2. Eur J Biochem 217: 715-722.
    • (1993) Eur J Biochem , vol.217 , pp. 715-722
    • Sutherland, C.1    Alterio, J.2    Campbell, D.G.3    Le Bourdelles, B.4    Mallet, J.5    Haavik, J.6    Cohen, P.7
  • 183
    • 0022929951 scopus 로고
    • +: Determination of the sites on tyrosine hydroxylase phosphorylated by cyclic AMP-dependent and calcium/calmodulin-dependent protein kinases
    • +: Determination of the sites on tyrosine hydroxylase phosphorylated by cyclic AMP-dependent and calcium/calmodulin-dependent protein kinases. Molec Pharmacol 30: 476-485.
    • (1986) Molec Pharmacol , vol.30 , pp. 476-485
    • Tachikawa, E.1    Tank, A.W.2    Yanagihara, N.3    Mosimann, W.4    Weiner, N.5
  • 184
    • 12044251740 scopus 로고
    • 18O in oxygen binding to the reversible oxygen carriers hemoglobin, myoglobin, hemerythrin, and hemocyanin: A new probe for oxygen binding and reductive activation by proteins
    • 18O in oxygen binding to the reversible oxygen carriers hemoglobin, myoglobin, hemerythrin, and hemocyanin: a new probe for oxygen binding and reductive activation by proteins. J Am Chem Soc 115: 8891-8897.
    • (1993) J Am Chem Soc , vol.115 , pp. 8891-8897
    • Tian, G.1    Klinman, J.P.2
  • 185
    • 76949113825 scopus 로고
    • The enzymatic conversion of phenylalanine to tyrosine
    • Udenfriend S, Cooper JR (1952): The enzymatic conversion of phenylalanine to tyrosine. J Biol Chem 194: 503-511.
    • (1952) J Biol Chem , vol.194 , pp. 503-511
    • Udenfriend, S.1    Cooper, J.R.2
  • 186
    • 0019313835 scopus 로고
    • Tyrosine 3-monooxygenase regulates catecholamine synthesis in pheochromocytoma cells
    • Vaccaro KK, Liang BT, Perelle BA, Perlman RL (1980): Tyrosine 3-monooxygenase regulates catecholamine synthesis in pheochromocytoma cells. J Biol Chem 255: 6539-6541.
    • (1980) J Biol Chem , vol.255 , pp. 6539-6541
    • Vaccaro, K.K.1    Liang, B.T.2    Perelle, B.A.3    Perlman, R.L.4
  • 188
    • 0018903550 scopus 로고
    • Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase
    • Vulliet PR, Langan TA, Weiner N (1980): Tyrosine hydroxylase: a substrate of cyclic AMP-dependent protein kinase. Proc Natl Acad Sci U S A 77: 92-96.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 92-96
    • Vulliet, P.R.1    Langan, T.A.2    Weiner, N.3
  • 189
    • 0021714437 scopus 로고
    • Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase
    • Vulliet PR, Woodgett JR, Cohen P (1984): Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. J Biol Chem 259: 13680-13683.
    • (1984) J Biol Chem , vol.259 , pp. 13680-13683
    • Vulliet, P.R.1    Woodgett, J.R.2    Cohen, P.3
  • 190
    • 0021761501 scopus 로고
    • Reductive activation of phenylalanine hydroxylase and its effect on the redox state of the non-heme iron
    • Wallick DE, Bloom LM, Gaffney BJ, Benkovic SJ (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
  • 191
    • 0024260075 scopus 로고
    • Phosphorylation of bovine adrenal chromaffin cell tyrosine hydroxylase. Temporal correlation of acetylcholine's effect on site phosphorylation, enzyme activation, and catecholamine synthesis
    • Waymire JC, Johnston JP, Hummer-Lickteig K, Lloyd A, Vigny A, Craviso GL (1988): Phosphorylation of bovine adrenal chromaffin cell tyrosine hydroxylase. Temporal correlation of acetylcholine's effect on site phosphorylation, enzyme activation, and catecholamine synthesis. J Biol Chem 263: 12439-12447.
    • (1988) J Biol Chem , vol.263 , pp. 12439-12447
    • Waymire, J.C.1    Johnston, J.P.2    Hummer-Lickteig, K.3    Lloyd, A.4    Vigny, A.5    Craviso, G.L.6
  • 192
    • 0027092320 scopus 로고
    • Site-directed mutagenesis of tyrosine hydroxylase role of serine 40 in catalysis
    • Wu J, Filer D, Friedhoff AJ, Goldstein M (1992): Site-directed mutagenesis of tyrosine hydroxylase role of serine 40 in catalysis. J Biol Chem 267: 25754-25758.
    • (1992) J Biol Chem , vol.267 , pp. 25754-25758
    • Wu, J.1    Filer, D.2    Friedhoff, A.J.3    Goldstein, M.4
  • 193
    • 0028033734 scopus 로고
    • Regulation of rat liver phenylalanine hydroxylase. III. Control of catalysis by (6A)-tetrahydrobiopterin and phenylalanine
    • Xia T, Gray DW, Shiman R (1994): Regulation of rat liver phenylalanine hydroxylase. III. Control of catalysis by (6A)-tetrahydrobiopterin and phenylalanine. J Biol Chem 269: 24657-24665.
    • (1994) J Biol Chem , vol.269 , pp. 24657-24665
    • Xia, T.1    Gray, D.W.2    Shiman, R.3
  • 194
    • 0018371869 scopus 로고
    • In vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3′: 5′-monophosphate-dependent protein kinase
    • Yamauchi T, Fujisawa H (1979): In vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3′: 5′-monophosphate-dependent protein kinase. J Biol Chem 254: 503-507.
    • (1979) J Biol Chem , vol.254 , pp. 503-507
    • Yamauchi, T.1    Fujisawa, H.2
  • 195
    • 0019510125 scopus 로고
    • 2+-, calmodulin-dependent protein kinase. Purification and characterization
    • 2+-, calmodulin-dependent protein kinase. Purification and characterization. J Biol Chem 256: 5404-5409.
    • (1981) J Biol Chem , vol.256 , pp. 5404-5409
    • Yamauchi, T.1    Nakata, H.2    Fujisawa, H.3
  • 196
    • 0028049314 scopus 로고
    • Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4a-carbinolamine dehydratase/DCoH as part of a three-component gene cluster
    • Zhao G, Xia T, Song J, Jensen RA (1994): Pseudomonas aeruginosa possesses homologues of mammalian phenylalanine hydroxylase and 4a-carbinolamine dehydratase/DCoH as part of a three-component gene cluster. Proc Natl Acad Sci U S A 91: 1366-1370.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 1366-1370
    • Zhao, G.1    Xia, T.2    Song, J.3    Jensen, R.A.4
  • 197
    • 0028912476 scopus 로고
    • Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development
    • Zhou Q-Y, Quaife CJ, Palmiter RD (1995): Targeted disruption of the tyrosine hydroxylase gene reveals that catecholamines are required for mouse fetal development. Nature 374: 640-643.
    • (1995) Nature , vol.374 , pp. 640-643
    • Zhou, Q.-Y.1    Quaife, C.J.2    Palmiter, R.D.3
  • 198
    • 0024582213 scopus 로고
    • Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation
    • Zigmond RE, Schwarzschild MA, Rittenhouse AR (1989): Acute regulation of tyrosine hydroxylase by nerve activity and by neurotransmitters via phosphorylation. Ann Rev Neurosci 12: 415-461.
    • (1989) Ann Rev Neurosci , vol.12 , pp. 415-461
    • Zigmond, R.E.1    Schwarzschild, M.A.2    Rittenhouse, A.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.