Dopamine inhibition of human tyrosine hydroxylase type 1 is controlled by the specific portion in the N-terminus of the enzyme

Journal of Neurochemistry

Volumn 72, Issue 5, 1999, Pages 2145-2153

  Nakashima, Akira ^a   Mori, Keiji ^a   Suzuki, Takahiro ^b   Kurita, Hideki ^a   Otani, Motohiko ^a   Nagatsu, Toshiaru ^b   Ota, Akira ^a  

^a FUJITA HEALTH UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b FUJITA HEALTH UNIVERSITY   (Japan)

Author keywords

Dopamine inhibition; Iron; Maltose binding protein; N Terminus deleted mutant; Tetrahydrobiopterin; Tyrosine hydroxylase

Indexed keywords

(LEVO ERYTHRO 1',2' DIHYDROXYPROPYL) 2 AMINO 4 HYDROXY 5,6,7,8 TETRAHYDROPTERIDINE; DOPAMINE; HYBRID PROTEIN; IRON; LEVODOPA; MALTOSE BINDING PROTEIN; PTERIDINE DERIVATIVE; TYROSINE; TYROSINE 3 MONOOXYGENASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; CATALYSIS; CONTROLLED STUDY; DELETION MUTANT; ENZYME ACTIVITY; ENZYME INHIBITION; ESCHERICHIA COLI; MICHAELIS CONSTANT; NONHUMAN; PRIORITY JOURNAL;

CATALYSIS; DOPAMINE; ESCHERICHIA COLI; HUMANS; IRON; ISOENZYMES; KINETICS; MUTATION; PEPTIDE FRAGMENTS; RECOMBINANT PROTEINS; TYROSINE 3-MONOOXYGENASE;

ESCHERICHIA COLI;

EID: 0033005087     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.1999.0722145.x     Document Type: Article

References (43)

1. Abate C. and Job T. H. (1991) Limited proteolysis of rat brain tyrosine hydroxylase defines as N-terminal region required for regulation of cofactor binding and directing substrate specificity. J. Mol. Neurosci. 2, 203-215.
2. Abate C., Smith J. A., and Joh T. H. (1988) Characterization of the catalytic domain of bovine adrenal tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 151, 1446-1453.
3. Alterio J., Ravassard P., Haavik J., Le Caer J.-P., Faucon-Biguet N., Waksman G., and Mallet J. (1998) Human tyrosine hydroxylase isoforms: inhibition by excess tetrahydropterin and unusual behavior of isoform 3 after cAMP-dependent protein kinase phosphorylation. J. Biol. Chem. 273, 10196-10201.
4. Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
5. Brenneman A. R. and Kaufman S. (1964) The role of tetrahydropteridines in the enzymatic conversion of tyrosine to 3,4-dihydroxyphenylalanine. Biochem. Biophys. Res. Commun. 17, 177-183.
6. Daubner S. C., Lauriano C., Haycock J. W., and Fitzpatrick P. F. (1992) Site-directed mutagenesis of serine 40 of rat tyrosine hydroxylase. J. Biol. Chem. 267, 12639-12646.
7. Daubner S. C., Hillas P. J., and Fitzpatrick P. F. (1997) Characterization of chimeric pterin-dependent hydroxylases: contributions of the regulatory domains of tyrosine and phenylalanine hydroxylase to substrate specificity. Biochemistry 36, 11574-11582.
8. Døskeland A. P., Martínez A., Knappskog P. M., and Flatmark T. (1996) Phosphorylation of recombinant human phenylalanine hydroxylase: effect on catalytic activity, substrate activation and protection against non-specific cleavage of the fusion protein by restriction protease. Biochem. J. 313, 409-414.
9. Fujisawa H. and Okuno S. (1987) Tyrosine 3-monooxygenase from rat adrenals. Methods Enzymol. 142, 63-71.
10. Goodwill K. E., Sabatier C., Marks C., Raag R., Fitzpatrick P. F., and Stevens R. C. (1997) Crystal structure of tyrosine hydroxylase at 2.3 Å and its implications for inherited neurodegenerative diseases. Nat. Struct. Biol. 4, 578-585.
11. Grima B., Lamouroux A., Boni C., Julien J.-F., Javoy-Agid F., and Mallet J. (1987) A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics. Nature 326, 707-711.
12. Guan C. D., Li P., Riggs P. D., and Inouye H. (1988) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67, 21-30.
13. Haavik J., Martínez A., and Flatmark T. (1990) pH-dependent release of catecholamines from tyrosine hydroxylase and the effect of phosphorylation of ser-40. FEBS Lett. 262, 363-365.
14. Hoeldtke R. and Kaufman S. (1977) Bovine adrenal tyrosine hydroxylase, J. Biol. Chem. 252, 3160-3169.
15. Ichinose H., Ohye T., Fujita K., Pantucek F., Lange K., Riederer P., and Nagatsu T. (1994) Quantification of mRNA of tyrosine hydroxylase and aromatic L-amino acid decarboxylase in the substantia nigra in Parkinson's disease and schizophrenia. J. Neural Transm. 8, 149-158.
16. Ikeda M., Fahien A., and Udenfriend S. (1966) A kinetic study of bovine adrenal tyrosine hydroxylase. J. Biol. Chem. 241, 4452-4456.
17. Kaneda N., Kobayashi K., Ichinose H., Kishi F., Nakazawa A., Kurosawa Y., Fujita K., and Nagatsu T. (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. 146, 971-975.
18. Katz I., Lloyd T., and Kaufman S. (1976) Studies on phenylalanine and tyrosine hydroxylation by rat brain tyrosine hydroxylase. Biochim. Biophys. Acta 445, 567-578.
19. Kaufman S. (1963) The structure of the phenylalanine hydroxylation cofactor. Proc. Natl. Acad. Sci. USA 50, 1085-1093.
20. Le Bourdellès B., Horellou P., Le Caer J.-P., Denefle P., Latta M., Haavik J., Guibert B., Mayaux, J.-F., and 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.
21. Levitt M., Spector S., Sjoerdsma A., and Udenfriend S. (1965) Elucidation of the rate-limiting step in norepinephrine biosynthesis in the perfused guinea pig heart. J. Pharmacol. Exp. Ther. 148, 1-8.
22. Lohse D. L. and Fitzpatrick P. F. (1993) Identification of the intersubunit binding region in rat tyrosine hydroxylase. Biochem. Biophys. Res. Commun. 197, 1543-1548.
23. Martínez A., Knappskog P. M., Olafsdottir S., Døskeland A., Eiken H. G., Svebak R. M., Bozzini M., Apold J., and Flatmark T. (1995) Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Biochem. J. 306, 589-597.
24. Martínez A., Haavik J., Flatmark T., Arrondo J. L. R., and Muga A. (1996) Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy: effect of iron/catecholamine binding and phosphorylation. J. Biol. Chem. 271, 19737-19742.
25. Matsuura S., Sugimoto T., Murata S., Sugawara Y., and 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.
26. Meyer-Klaucke W., Winkler H., Schünemann V., Trautwein A. X., Nolting H.-F., and 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.
27. Michaud-Soret I., Andersson K. K., Que L. Jr., and Haavik J. (1995) Resonance Raman studies of catecholate and phenolate complexes of recombinant human tyrosine hydroxylase. Biochemistry 34, 5504-5510.
28. Nagatsu T., Levitt M., and Udenfriend S. (1964) Tyrosine hydroxylase. The initial step in norepinephrine biosynthesis. J. Biol. Chem. 239, 2910-2917.
29. Nagatsu T., Yamamoto T., and Nagatsu I. (1970) Partial separation and properties of tyrosine hydroxylase from the human pheochromocytoma: effect of norepinephrine. Biochim. Biophys. Acta 198, 210-218.
30. Nagatsu T., Oka K., and Kato T. (1979) Highly sensitive assay for tyrosine hydroxylase activity by high-performance liquid chromatography. J. Chromatogr. 163, 247-252.
31. Nasrin S., Ichinose H., Hidaka H., and Nagatsu T. (1994) Recombinant human tyrosine hydroxylase types 1-4 show regulatory kinetic properties for the natural (6R)-tetrahydrobiopterin cofactor. J. Biochem. 116, 393-398.
32. Oka K., Ashiba G., Sugimoto T., Matsuura S., and Nagatsu T. (1982) Kinetic properties of tyrosine hydroxylase purified from bovine adrenal medulla and bovine caudate nucleus. Biochem. Biophys. Acta 706, 188-196.
33. Okuno S. and Fujisawa H. (1991) Conversion of tyrosine hydroxylase to stable and inactive form by the end products. J. Neurochem. 57, 53-60.
34. Ota A., Yoshida S., and Nagatsu T. (1996) Regulation of N-terminus-deleted human tyrosine hydroxylase type 1 by end products of catecholamine biosynthetic pathway. J. Neural Transm. 103, 1415-1428.
35. Ota A., Nakashima A., Mori K., and Nagatsu T. (1997) Effects of dopamine on N-terminus-deleted human tyrosine hydroxylase type 1 expressed in Escherichia coli. Neurosci. Lett. 229, 57-60.
36. 327 as residues critical for substrate inhibition in tyrosine hydroxylase. J. Neurochem. 66, 908-914.
37. Ramsey A. J. and Fitzpatrick P. F. (1998) Effects of phosphorylation of serine 40 of tyrosine hydroxylase on binding of catecholamines: evidence for a novel regulatory mechanism. Biochemistry 37, 8980-8986.
38. Ramsey A. J., Hillas P. J., and Fitzpatrick P. F. (1996) Characterization of the active site iron in tyrosine hydroxylase: redox states of the iron. J. Biol. Chem. 271, 24395-24400.
39. Ribeiro P., Wang Y., Citron B. A., and Kaufman S. (1992) Regulation of recombinant rat tyrosine hydroxylase by dopamine. Proc. Natl. Acad. Sci. USA 89, 9593-9597.
40. Sambrook J., Fritsch E. F., and Maniatis T. (1989) Molecular Cloning: A Laboratory Manual, 2nd ed., pp. 182-184. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
41. Shiman R., Akino M., and Kaufman S. (1971) Solubilization and partial purification of tyrosine hydroxylase from bovine adrenal medulla. J. Biol. Chem. 246, 1330-1340.
42. Udenfriend S., Zaltzman-Nirenberg P., and Nagatsu T. (1965) Inhibitors of purified beef adrenal tyrosine hydroxylase. Biochem. Pharmacol. 14, 837-845.
43. Wang Y., Citron B. A., Ribeiro P., and Kaufman S. (1991) High-level expression of rat PC12 tyrosine hydroxylase cDNA in Escherichia coli: purification and characterization of the cloned enzyme. Proc. Natl. Acad. Sci. USA 88, 8779-8783.