Abstract
Tyrosine hydroxylase activity is stimulated in vitro by a variety of seemingly unrelated compounds. These compounds include: 1) anions and polyanions such as heparin, polyglutamic acid and melanin (Kuczenski and Mandell, 1972; Katz et al., 1976; Nagatsu et al., 1978); 2) phospholipids (Lloyd and Kaufman, 1974; Raese et al., 1976; Lloyd, 1979); 3) ATP, Mg++ and cyclic AMP dependent protein kinase (Harris et al., 1974; Lovenberg et al., 1975); and 4) limited proteolysis (Kuczenski, 1973). The activation exhibited by these modulators is suprisingly similar, suggesting that a common mechanism might be involved (Katz et al., 1976; Weiner et al., 1978). For example, phospholipid activation and exposure to phosphorylating conditions result in a form of tyrosine hydroxylase that has a decreased Km for pterin cofactor with no change in the Vmax. Under conditions of maximal activation, the pH optimum of the enzyme is shifted from 6.2 to 6.4–6.8 (Lloyd and Kaufman, 1975; Weiner et al., 1978). The similarity of the kinetic changes may be explained by the ability of these agents to cause the tyrosine hydroxylase molecule to assume a common conformation.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
Similar content being viewed by others
References
Andrews, P. (1964). The gel filtration behaviour of proteins related to their molecular weights over a wide range. Biochem. J. 96, 595–606.
Gosting, L. (1956). Solution of boundary spreading equations for electrophoresis and the velocity ultracentrifuge. Advan. Protein Chem. 11, 429–485.
Harris, J., Morgenroth, V., III, Roth, R. and Baldessarini, R. (1974). Regulation of catecholamine synthesis in the rat brain in vitro by cyclic AMP. Nature 252, 156–158.
Hoeldtke, R. and Kaufman, S. (1977). Bovine adrenal tyrosine hydroxylase: Purification and properties. J. Biol. Chem. 252, 3160–3169.
Katz, I., Yamauchi, T. and Kaufman, S. (1976). Activation of tyrosine hydroxylase by polyanions and salts. Biochem. Biophys. Acta. 444, 567–578.
Kuczenski, R., and Mandell, A. (1972). Allosteric activation of hypothalamic tyrosine hydroxylase by ions and sulphated mucopolysaccarides. J. Neurochem. 19, 131–137.
Kuczenski, R. (1973). Rat brain tyrosine hydroxylase: Activation by limited tryptic proteolysis. J. Biol. Chem. 248, 2261–2265.
Laemmli, U. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227, 680–685.
Laurent, T. and Killander, J. (1964). A theory of gel filtration and its experimental verification. J. Chromatog. 14, 317–330.
Lloyd, T. and Kaufman, S. (1974). The stimulation of partially purified bovine caudate tyrosine hydroxylase by phosphatidyl-L-serine. Biochem. Biophys. Res. Comm. 59, 1262–1269.
Lloyd, T. (1979). The effects of phosphatidylinositol on tyrosine hydroxylase. J. Biol. Chem. 254, 7247–7254.
Lovenberg, W., Bruckwick, E. and Hanbauer, I. (1975). ATP, cyclic AMP and magnesium increase the affinity of rat striatal tyrosine hydroxylase for its cofactor. Proc. Nat. Acad. Sci. USA. 72, 2955–2958.
Markey, K., Kondo, S., Schenkman, L. and Goldstein, M. (1980). Purification and characterization of tyrosine hydroxylase from a clonal pheochromocytoma cell line. Molec. Pharm. 17, 79–85.
Martin, R. and Ames, B. (1961). A method for determining the sedimentation behavior of enzymes: Application to protein mixtures. J. Biol. Chem. 236, 1372–1379.
Masserano, J. and Weiner, N. (1979). The rapid activation of adrenal tyrosine hydroxylase by decapitation and its relationship to a cyclic AMP-dependent phosphorylating system. Molec. Pharmacol. 16, 513–528.
Meligeni, J. and Weiner, N. (1981). Isoelectric focusing of tyrosine hydroxylase. This volume.
Nagatsu, T., Numata (Sudo), Y., Kato, T., Sugiyama, K. and Akino, M. (1978). Effects of melanin on tyrosine hydroxylase and phenylalanine hydroxylase. Biochem. Biophys. Acta. 523, 47–52.
Raese, J., Patrick, R. and Barchas, J. (1976). Phospholipid-induced activation of tyrosine hydroxylase from rat brain striatal synaptosomes. Biochem. Pharmacol. 25, 2245–2250.
Raese, J., Edelman, A., Lazar, M. and Barchas, J. (1977). Bovine striatal tyrosine hydroxylase: Multiple forms and evidence for phosphorylation by cyclic AMP-dependent protein kinase. In Structure and Function of Monoamine Enzymes (eds. E. Usdin, N. Weiner and M.B.H. Youdim) Marcel Decker, Inc., New York, pp. 383–421.
Siegel, L. and Monty, K. (1966). Determination of the molecular weights and frictional ratios of proteins in impure systems by use of gel filtration centrifugation. Applications to crude preparations of sulfite and hydroxylamine reductases. Biochim. Biophys. Acta. 112, 346–362.
Vulliet, P., Langan, T. and Weiner, N. (1980a). Tyrosine hydroxylase: A substrate of cyclic AMP-dependent protein kinase in vitro. Proc Nat. Acad. Sci. USA. 77, 92–96.
Vulliet, P., Meligeni, J. and Weiner, N. (1980b). Physical properties rat pheochromocytoma tyrosine hydroxylase. Pharmacologist 22, 237.
Vulliet, P. and Weiner, N. (1978). Purification and characterization of tyrosine hydroxylase from rat pheochromocytoma. Fed. Proc. 37, 825.
Waymire, J., Bjur, R. and Weiner, N. (1971). Assay of tyrosine hydroxylase by coupled decarboxylation of dopa formed from l-14C-L-tyrosine. Anal. Biochem. 43, 588–600.
Weiner, N., Lee, F.-L., Dryer, E. and Barnes, E. (1978). The activation of tyrosine hydroxylase during acute nerve stimulation. Life Sci. 22, 1197–1216.
Yamauchi, T. and Fujisawa, H. (1979a). In Vitro phosphorylation of bovine adrenal tyrosine hydroxylase by adenosine 3’:5’-monophosphate dependent protein kinase. J. Biol. Chem. 254, 503–507.
Yamauchi, T. and Fujisawa, H. (1979b). Regulation of bovine adrenal tyrosine 3-monooxygenase by phosphorylation-dephosphorylation reaction, catalyzed by adenosine 3’:5’-monophosphate dependent protein kinase and phosphoprotein phosphatase. J. Biol. Chem. 254, 6408–6413.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Copyright information
© 1981 The Contributors
About this chapter
Cite this chapter
Vulliet, P.R., Weiner, N. (1981). A schematic model for the allosteric activation of tyrosine hydroxylase. In: Usdin, E., Weiner, N., Youdim, M.B.H. (eds) Function and Regulation of Monoamine Enzymes: Basic and Clinical Aspects. Palgrave Macmillan, London. https://doi.org/10.1007/978-1-349-06276-8_2
Download citation
DOI: https://doi.org/10.1007/978-1-349-06276-8_2
Publisher Name: Palgrave Macmillan, London
Print ISBN: 978-1-349-06278-2
Online ISBN: 978-1-349-06276-8
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)