The aromatic amino acid hydroxylases

Advances in Enzymology and Related Areas of Molecular Biology

Volumn 74, Issue , 2000, Pages 235-294

  Fitzpatrick, Paul F ^a  

^a TEXAS A AND M UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

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

BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENE EXPRESSION REGULATION; HYDROXYLATION; METABOLISM; REVIEW;

AMINO ACIDS, CYCLIC; BINDING SITES; GENE EXPRESSION REGULATION, ENZYMOLOGIC; HYDROXYLATION; MODELS, MOLECULAR; NONHEME IRON PROTEINS; PHENYLALANINE HYDROXYLASE; TRYPTOPHAN HYDROXYLASE; TYROSINE 3-MONOOXYGENASE;

EID: 0033660818     PISSN: 0065258X     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Article

References (198)

1. 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.
2. 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.
3. 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.
4. Aitken A (1996): 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol 6: 341-347.
5. Albert KA, Helmer-Matyjek E, Nairn AC, Muller TH, Haycock JW, Greene LA, Goldstein M, Greengard P (1984): Calcium/phospholipid-dependent protein kinase (protein kinase C) phosphorylates and activates tyrosine hydroxylase. Proc Natl Acad Sci U S A 81: 7713-7717.
6. 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.
7. Alterio J, Ravassard P, Haavik J, Le Caer J, Biguet N, Waksman G, Mallet J (1998): Human tyrosine hydroxylase isoforms. J Biol Chem 273: 10196-10201.
8. Ames MM, Lerner P, Lovenberg W (1978): Tyrosine hydroxylase. Activation by protein phosphorylation and end product inhibition. J Biol Chem 253: 27-31.
9. 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.
10. 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.
11. 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.
12. Archer MC, Scrimgeour KG (1970): Rearrangement of quinonoid dihydropteridines to 7,8-dihydropteridines. Can J Biochem 48: 278-287.
13. 2+calmodulin-dependent protein kinase II: effect of an activator protein. J Neurochem 49: 1241-1249.
14. Bailey SW, Ayling JE (1978): Pyrimidines as cofactors for phenylalanine hydroxylase. Biochem Biophys Res Commun 85: 1614-1621.
15. Bailey SW, Ayling JE (1980): Cleavage of the 5-amino substituent of pyrimidine cofactors by phenylalanine hydroxylase. J Biol Chem 255: 7774-7781.
16. 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.
17. 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.
18. 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.
19. 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.
20. Benkovic S, Wallick D, Bloom L, Gaffney BJ, Domanico P, Dix T, Pember S (1985a): On the mechanism of action of phenylalanine hydroxylase. Biochem Soc Trans 13: 436-438.
21. 15N NMR study. J Am Chem Soc 107: 3706-3712.
22. 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.
23. 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.
24. Bloom LM, Benkovic SJ, Gaffney BJ (1986): Characterization of phenylalanine hydroxylase. Biochemistry 25: 4204-4210.
25. Boadle-Biber MC (1993): Regulation of serotonin synthesis. Prog Biophys Molec Biol 60: 1-15.
26. Bruice TC, Bruice PY (1976): Solution chemistry of arene oxides. Acc Chem Res 9: 378-384.
27. 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.
28. 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.
29. Byerley W, Plaetke R, Hoff M, Jensen S, Holik J, Reimherr F, Mellon C, Wender P, O'Connell P, Leppert M (1992): Tyrosine hydroxylase gene not linked to manic-depression in seven of eight pedigrees. Hum Hered 42: 259-263.
30. 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.
31. Carr RT, Benkovic SJ (1993): An examination of the copper requirement of phenylalanine hydroxylase from Chromobacterium violaceum. Biochemistry 32: 14132-14138.
32. Carr RT, Balasubramanian S, Hawkins PCD, Benkovic SJ (1995): Mechanism of metal-independent hydroxylation by Chromobacterium violaceum phenylalanine hydroxylase. Biochemistry 34: 7525-7532.
33. 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.
34. Cox DD, Benkovic SJ, Bloom LM, Bradley FC, Nelson MJ, Que L Jr, Wallick DE (1988): Catecholate LMCT bands as probes for the active sites of nonheme iron oxygenases. J Am Chem Soc 110: 2026-2032.
35. Daly J, Guroff G (1968): Production of m-methyltyrosine and p-hydroxymethylphenylalanine from p-methylphenylalanine by phenylalanine hydroxylase. Arch Biochem Biophys 125: 136-141.
36. 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.
37. 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.
38. Daubner SC, Fitzpatrick PF (1998): Mutation to phenylalanine of tyrosine 371 in tyrosine hydroxylase increases the affinity for phenylalanine. Biochemistry 37: 16440-16444.
39. Daubner SC, Fitzpatrick PF (1999): Site-directed mutants of charged residues in the active site of tyrosine hydroxylase. Biochemistry 38: 4448-4454.
40. 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.
41. 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.
42. Daubner SC, Hillas PJ, Fitzpatrick PF (1997b): Expression and characterization of the catalytic domain of human phenylalanine hydroxylase. Arch Biochem Biophys 348: 295-302.
43. 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.
44. Davis MD, Kaufman S (1991): Studies on the partially uncoupled oxidation of tetrahydropterins by phenylalanine hydroxylase. Neurochem Res 16: 813-819.
45. 4 dopamine receptor genes on chromosome 11. Am J Psychiatry 151: 102-106.
46. 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.
47. Dix TA, Benkovic SJ (1985): Mechanism of "uncoupled" tetrahydropterin oxidation by phenylalanine hydroxylase. Biochemistry 24: 5839-5846.
48. 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.
49. Dix TA, Kuhn DM, Benkovic SJ (1987): Mechanism of oxygen activation by tyrosine hydroxylase. Biochemistry 26: 3354-3361.
50. 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.
51. Doskeland AP, Schworer CM, Doskeland SO, Chrisman TD, Soderling TR, Corbin JD, Flatmark T (1984b): Some aspects of the phosphorylation of phenylalanine 4-monooxygenase by a calcium-dependent and calmodulin-dependent protein kinase. Eur J Biochem 145: 31-37.
52. 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.
53. 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.
54. 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.
55. 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.
56. Ellis HR, Daubner SC, Fitzpatrick PF: Mutation of serine 395 of tyrosine hydroxylase decouples oxygen-oxygen bond cleavage and tyrosine hydroxylation. (Submitted for publication).
57. 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.
58. Entsch B, Ballou DP, Massey V (1976): Flavin-oxygen derivatives involved in hydroxylation by p-hydroxybenzoate hydroxylase. J Biol Chem 251: 2550-2563.
59. 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.
60. 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.
61. Erny RE, Berezo MW, Perlman RL (1981): Activation of tyrosine 3-monooxygenase in pheochromocytoma cells by adenosine. J Biol Chem 256: 1335-1339.
62. Fisher DB, Kaufman S (1973a): The stimulation of rat liver phenylalanine hydroxylase by lysolecithin and α-chymotrypsin. J Biol Chem 248: 4345-4353.
63. Fisher DB, Kaufman S (1973b): Tetrahydropterin oxidation without hydroxylation catalyzed by rat liver phenylalanine hydroxylase. J Biol Chem 248: 4300-4304.
64. Fitzpatrick PF (1989): The metal requirement of rat tyrosine hydroxylase. Biochem Biophys Res Commun 161: 211-215.
65. Fitzpatrick PF (1991a): The steady state kinetic mechanism of rat tyrosine hydroxylase. Biochemistry 30: 3658-3662.
66. 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.
67. 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.
68. 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.
69. Fukami MH, Haavik J, Flatmark T (1990): Phenylalanine as substrate for tyrosine hydroxylase in bovine adrenal chromaffin cells. Biochem J 268: 525-528.
70. 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.
71. 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.
72. 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.
73. 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.
74. 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.
75. Goodwill KE, Sabatier C, Marks C, Raag R, Fitzpatrick PF, Stevens RC (1997): Crystal structure of tyrosine hydroxylase at 2.3 E̊ and its implications for inherited diseases. Nat Struct Biol 4: 578-585.
76. 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.
77. 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.
78. 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.
79. 2+-dependent phosphorylation of tyrosine hydroxylase. J Biol Chem 263: 9542-9549.
80. Grima B, Lamouroux A, Blanot F, Biguet NF, Mallet J (1985): Complete coding sequence of rat tyrosine hydroxylase mRNA. Proc Natl Acad Sci U S A 82: 617-621.
81. 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.
82. Guengerich FP, MacDonald TL (1984): Chemical mechanisms of catalysis by cytochromes P-450: a unified view. Acc Chem Res 17: 9-16.
83. 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.
84. Guroff G, Daly JW, Jerina DM, Renson J, Witkop B, Udenfriend S (1967): Hydroxylationinduced migration: the NIH shift. Science 157: 1524-1530.
85. 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.
86. 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.
87. 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.
88. 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.
89. 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.
90. 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.
91. 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.
92. Haycock JW (1990): Phosphorylation of tyrosine hydroxylase in situ at serine 8, 19, 31, and 40. J Biol Chem 265: 11682-11691.
93. 40. Neurochem Res 18: 15-26.
94. 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.
95. 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.
96. 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.
97. 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.
98. 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.
99. Hillas PJ, Fitzpatrick PF (1996): A mechanism for hydroxylation by tyrosine hydroxylase based on partitioning of substituted phenylalanines. Biochemistry 35: 6969-6975.
100. 2+, calmodulin-dependent protein kinase II. FEBS Letts. 219: 79-82.
101. 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.
102. Kaneda N, Kobayashi K, Ichinose H, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, NagatsuT (1987): Isolation of a novel cDNA clone for human tyrosine hydroxylase: Alternative RNA splicing produces four kinds of mRNA from a single gene. Biochem Biophys Res Commun 147: 971-975.
103. Kappock TJ, Caradonna JP (1996): Pterin-dependent amino acid hydroxylases. Chem Rev 96: 2659-2756.
104. 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.
105. Kaufman S (1963): The structure of the phenylalanine-hydroxylation cofactor. Biochemistry 50: 1085-1093.
106. Kaufman S (1979): The activity of 2,4,5-triamino-6-hydroxypyrimidine in the phenylalanine hydroxylase system. J Biol Chem 254: 5150-5154.
107. Kaufman S (1985): Aromatic amino acid hydroxylases. Biochem Soc Trans 13: 433-436.
108. Kaufman S (1995): Tyrosine hydroxylase. In Meister A (ed): "Advances in Enzymology and Related Areas of Molecular Biology." Vol. 70. John Wiley & Sons, Inc., pp. 103-220.
109. Kaufman S, Mason K (1982): Specificity of amino acids as activators and substrates for phenylalanine hydroxylase. J Biol Chem 257: 14667-14678.
110. 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.
111. 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.
112. Klinman JP (1996): Mechanisms whereby mononuclear copper proteins functionalize organic substrates. Chem Rev 96: 2541-2562.
113. 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.
114. 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.
115. Kobayashi K, Morita S, Sawada H, Mizuguchi T, Yamada K, Nagatsu I, Hata T, Watanabe Y, Fujita K, Nagatsu T (1995): Targeted disruption of the tyrosine hydroxylase locus results in severe catecholamine depletion and perinatal lethality in mice. J Biol Chem 270: 27235-27243.
116. Kobe B, Jennings IG, House CM, Michell BJ, Goodwill KE, Santarsiero BD, Stevens RC, Cotton RGH, Kemp BE (1999): Structural basis of intrasteric and allosteric controls of phenylalanine hydroxylase. Nat Struct Biol 6: 442-448.
117. Kobe G, Jennings IG, House CM, Feil SC, Michell BJ, Tiganis T, Parker MW, Cotton RGH, Kemp BE (1997): Regulation and crystallization of phosphorylated and dephosphorylated forms of truncated dimeric phenylalanine hydroxylase. Prot Sci 6: 1352-1357.
118. 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.
119. 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.
120. 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.
121. 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.
122. Lazarus RA, Dietrich RF, Wallick DE, Benkovic SJ (1981): On the mechanism of action of phenylalanine hydroxylase. Biochemistry 20: 6834-6841.
123. 13C NMR spectroscopy. J Am Chem Soc 104: 6869-6871.
124. 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.
125. 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.
126. Letendre CH, Dickens G, Guroff G (1974): The tryptophan hydroxylase of Chromobacterium violaceum. J Biol Chem 249: 7186-7191.
127. 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.
128. Lohse DL, Fitzpatrick PF (1993): Identification of the intersubunit binding region in rat tyrosine hydroxylase. Biochem Biophys Res Commun 197: 1543-1548.
129. Lovenberg W, Jequier E, Sjoerdsma A (1967): Tryptophan hydroxylation: measurement in pineal gland, brainstem, and carcinoid tumor. Science 155: 217-219.
130. 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.
131. Ludecke B, Knappskog PM, Clayton PT, Surtees RAH, Clelland JD, Heales SJR, Brand MP, Bartholome K, Flatmark T (1996): Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205) in the tyrosine hydroxylase gene. Hum Mol Genet 5: 1023-1028.
132. 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.
133. 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.
134. Marota JJA, Shiman R (1984): Stoichiometric reduction of phenylalanine hydroxylase by its cofactor a requirement for enzymatic activity. Biochemistry 23: 1303-1311.
135. Massey V (1994): Activation of molecular oxygen by flavins and flavoproteins. J Biol Chem 269: 22459-22462.
136. 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.
137. 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.
138. 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.
139. 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.
140. 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.
141. 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.
142. 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.
143. 2]Phenylalanine, an alternate substrate for rat liver phenylalanine hydroxylase. Biochemistry 27: 3658-3663.
144. 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.
145. 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.
146. Moran CR, Derecskei-Kovacs, Fitzpatrick PF (2000): On the catalytic mechanism of tryptophan hydroxylase. (Submitted for publication).
147. Moran GR, Fitzpatrick PF (2000): Investigations of the kinetic mechanism of tryptophan hydroxylase. (Unpublished manuscript).
148. Moran GR, Daubner SC, Fitzpatrick PF (1998): Expression and characterization of the catalytic core of tryptophan hydroxylase. J Biol Chem 273: 12259-12266.
149. 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.
150. NagatsuT, Levin M, Udenfriend S (1964): Tyrosine hydroxylase the initial step in norepinephrine biosynthesis. J Biol Chem 239: 2910-2917.
151. Nakata H, Fujisawa H (1982): Tryptophan 5-monooxygenase from mouse mastocytoma P815 a simple purification and general properties. Eur J Biochem 124: 595-601.
152. Nakata H, Yamauchi T, Fujisawa H (1979): Phenylalanine hydroxylase from Chromobacterium violacetim purification and characterization. J Biol Chem 254: 1829-1833.
153. 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.
154. 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.
155. Okuno S, Fujisawa H (1982): Purification and some properties of tyrosine 3-monooxygenase from rat adrenal. Eur J Biochem 122: 49-55.
156. 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.
157. Parniak MA, Kaufman S (1981): Rat liver phenylalanine hydroxylase. Activation by sulfhydryl modification. J Biol Chem 256: 6876-6882.
158. 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.
159. 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.
160. 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.
161. Que L Jr, Ho RYN (1996): Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96: 2607-2524.
162. Quinscy NS, Luong AQ, Dickson PW (1998): Mutational analysis of substrate inhibition in tyrosine hydroxylase. J Neurochem 71: 2132-2138.
163. 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.
164. 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.
165. 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.
166. Renson JD, Daly J, Weissbach H, Witkop B, Udenfriend S (1966): Enzymatic conversion of 5-tritiotryptophan to 4-tritio-5-hydroxytryptophan. Biochera Biophys Res Commun 25: 504-513.
167. 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.
168. 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.
169. 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.
170. Roy A, DeJong J, Linnoila M (1989): Cerebrospinal fluid monoamine metabolites and suicidal behavior in depressed patients. Arch Gen Psychiatry 46: 609-612.
171. Rudolph FB, Fromm HJ (1979): Plotting methods for analyzing enzyme rate data. Methods Enzymol 63: 138-159.
172. max-type cooperative enzyme phosphoglycerate dehydrogenase. Nat Struct Biol 2: 69-76.
173. Shamoo Y, Ghosaini LR, Keating KM, Williams KR, Sturtevant JM, Konigsberg WH (1989): Site-specific mutagenesis of T4 gene 32: the role of tyrosine residues in protein-nucleic acid interactions. Biochemistry 28: 7409-7417.
174. 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.
175. Shiman R, Gray DW (1980): Substrate activation of phenylalanine hydroxylase. A kinetic characterizaion. J Biol Chem 255: 4793-4800.
176. Shiman R, Gray DW, Pater A (1979): A simple purification of phenylalanine hydroxylase by substrate-induced hydrophobic chromatography. J Biol Chem 254: 11300-11306.
177. Shiman R, Jones SH, Gray DW (1990): Mechanism of phenylalanine regulation of phenylalanine hydroxylase. J Biol Chem 265: 11633-11642.
178. 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.
179. 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.
180. Sono M, Roach MP, Coulter ED, Dawson JH (1996): Heme-containing oxygenases. Chem Rev 96: 2841-2888.
181. 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.
182. 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.
183. +: Determination of the sites on tyrosine hydroxylase phosphorylated by cyclic AMP-dependent and calcium/calmodulin-dependent protein kinases. Molec Pharmacol 30: 476-485.
184. 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.
185. Udenfriend S, Cooper JR (1952): The enzymatic conversion of phenylalanine to tyrosine. J Biol Chem 194: 503-511.
186. Vaccaro KK, Liang BT, Perelle BA, Perlman RL (1980): Tyrosine 3-monooxygenase regulates catecholamine synthesis in pheochromocytoma cells. J Biol Chem 255: 6539-6541.
187. van den Heuvel LPWJ, Luiten B, Smeitink JAM, deRijk-van Andel JF, Hyland K, Steenbergen-Spanjers GCH, Janssen RJT, Wevers RA (1998): A common point mutation in the tyrosine hydroxylase gene in autosomal recessive L-DOPA-responsive dystonia in the Dutch population. Hum Genet 102: 644-646.
188. 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.
189. Vulliet PR, Woodgett JR, Cohen P (1984): Phosphorylation of tyrosine hydroxylase by calmodulin-dependent multiprotein kinase. J Biol Chem 259: 13680-13683.
190. 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.
191. 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.
192. 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.
193. 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.
194. 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.
195. 2+-, calmodulin-dependent protein kinase. Purification and characterization. J Biol Chem 256: 5404-5409.
196. 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.
197. 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.
198. 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.