Abstract
Monamines derived from the decarboxylation of aromatic L-amino acids are formed by every type of living organism from bacteria to plants and animals. These compounds and their derivatives are important regulatory substances. Although consensus has been difficult to reach, it appears that only two enzymes catalyze the decarboxylation of aromatic amino acids in mammals. first, histidine decarboxylase (EC 4.1.1.22), a very specific enzyme; and second, aromatic L-amino acid decarboxylase (EC 4.1.1.28) (AADC), a very nonspecific enzyme. The notable features of AADC are as follows. The enzyme is found in tissues where a functional role is obvious, such as catecholaminergic neurons, serotonergic neurons, the adrenal medulla, pineal gland, and enterochromaffin tissue. The highest levels of AADC, however, are found in tissues such as the kidney, liver, and gastrointestinal tract where its functional status is unclear. In those tissues in which AADC is clearly functional, it is assumed the enzyme is present in massive excess relative to the activity of other monoamine enzymes. Thus, the prevailing concept has been that AADC is not rate-limiting in monoamine synthesis. The enzyme does not appear to be under metabolic control. In fact, the Michaelis constant of the enzyme for even its best substrates is several orders of magnitude greater than the endogenous concentration of those amino acids.
Keywords
- Tyrosine Hydroxylase
- Aromatic Amino Acid
- Decarboxylase Activity
- Histidine Decarboxylase
- Dopa Decarboxylase
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
This is a preview of subscription content, log in via an institution.
Buying options
Tax calculation will be finalised at checkout
Purchases are for personal use only
Learn about institutional subscriptionsReferences
Aures D. and Hakanson R (1971) Histidine Decarboxylase, in Methods in Enzymology, Vol 18, pt B (Colowick S. P. and Kaplan N O., eds ), Academic, New York
Aures D, Fleming R, and Hakanson R (1968a). Separation and detection of biogenic amines by thin-layer chromatography J Chromatogr. 33, 480–493
Aures D, Hakanson R, and Clark W. G. (1970) Histidine Decarboxylase and Dopa Decarboxylase, in Handbook of Neurochemistry (Lajtha A., ed.), pp 165–196, Plenum, New York.
Aures D., Hakanson R, and Schauer A (1968b) Histidine decarboxylase and dopa decarboxylase in the rat stomach. Properties and cellular localization. Eur J. Pharmacol. 3, 217–234.
Awapara J. and Saine S (1975) Fluctuations in dopa decarboxylase activity with age. J Neurochem. 24, 817–818
Awapara J., Perry T. L, Hanly C, and Peck E. (1964) Substrate specificity of dopa decarboxylase Clin. Chim Acta 10, 286–289.
Awapara J, Sandman R P, and Hanly C (1962) Activation of dopa decarboxylase by pyridoxal phosphate. Arch Biochem Biophys 98, 520–525.
Axelrod J., Saavedra J. and Usdin E. (1976) Trace Amines in the Brain, in Psychopharmacology Vol 1 (Usdin E. and Sandler M., eds.), pp. 1–20. Marcel, New York
Barboni E, Born Voltattorni C, D’Erme M, Fiori A., Minelli A., and Rosei A (1982) Inhibitors binding to AADC Life Sci. 31, 1519–1524.
Bartholini J., Constantinidis J., Puig M, Tissot R, Pletscher A (1975) The stereoisomers of 3,4-dihydroxyphenylserine as precursors of norepinephrme. J. Pharmacol Exp Ther 193, 523–532.
Bartholini G., Constantinidis J., Tissot R., and Pletscher A (1971) Formation of monoamines from various amino acids m the brain after inhibition of extracerebral decarboxylase Biochem. Pharmacol 20, 1243–1247.
Beaven M. A, Sol1 A H., and Lewin K J. (1982) Histamine synthesis by intact mast cells from canine fundic mucosa and liver. Gastroenterology 82, 254–262.
Beaven M. A., Wilcox G., and Terpstra G. K. (1978) A microprocedure for the measurement of 14CO2 release from [14C]carboxy-labeled amino acids Anal Biochem 84, 638–641.
Bender D. A. and Coulson W. F. (1977) AADC: pH dependence of substrates and inhibitors. Biochem. Soc. Trans 5, 1353–1356.
Bender D. A. and Coulson W. F. (1972) Variations in AADC activity towards DOPA and 5HTP caused by pH changes and denaturation J. Neurochem. 19, 2801–2810
Bennett D. S and Giarman N J. (1965) Schedule of appearance of serotonin and associated enzyme in the developing rat brain. J Neurochem. 12, 911–918.
Bergmark J, Granerus G., and Henningsson S. (1976) Histamine metabolism of the guinea pig gastric mucosa. J. Physiol. (Lond.) 257, 419–431.
Bertler A. and Rosengren E. (1959a) On the distribution in brain monoamines and of enzymes responsible for their formation. Experientia 15, 382–384.
Bertler A. and Rosengren E (1959b) Occurrence and distribution of catecholamines in brain Acta Physiol. Scand. 47, 350–361
Bertler A., Falck B, and Rosengren E (1963) The direct demonstration of a barrier mechanism in brain capillaries. Acta Pharmacol Toxicol 20, 317–321.
Bey P., Jung M. J, Koch-Weser J, Palfreyman M G, Sjoerdsma A., Wagner J., and Zraika M. (1980) Further studies on the inhibition of monoamine synthesis by monofluoromethyldopa. Br J. Pharmacol 70, 571–576.
Bianchine J. R. (1980) Drugs For Parkinson’s Disease, in The Pharmacologic Basis of Therapeutics (Gilman A. G., Goodman L. S., Gilman A., eds.), 6th ed, pp. 482–483, Macmillan, New York
Blaschko H. (1939) The specific action of L-dopa decarboxylase J Physiol (Lond.) 96, 50P–51P.
Blaschko H. (1942) The activity of L-dopa decarboxylase. J Physiol (Lond.) 101, 337–349.
Blaschko H. (1945) The amino acid decarboxylases of mammalian tissues Adv. Enzymol. 5, 67–85.
Blaschko H. (1950) Substrate specificity of amino acid decarboxylases Biochim Biophys Acta 4, 130–137.
Blaschko H. and Holton P. (1950) Enzymic formation of ortho-tyramine. J Physiol. (Lond.) 110, 482–487
Blaschko H., Burn J H., and Langemann H. (1950) The formation of noradrenaline from dihydroxyphenylserine Br. J. Pharmacol 5, 431–437.
Blaschko H., Hagen P., and Welch A. D. (1955) Observations on the intracellular granules of the adrenal medulla. J. Physiol. (Lond.) 129, 27–49.
Blaschko H., Holton P, and Stanley G. H. S. (1949) Enzymic formation of pressor amines J. Physiol. (Lond ) 108, 427–439.
Borri Voltattorni C, Minelli A., and Borri P. (1977a) Interaction of L-α-methyl-α-hydrazino-3,4-dihydroxyphenylpropionic acid with dopa decarboxylase from pig kidney. FEBS Lett 75, 277–280.
Borri Voltattorni C., Minelli A., and Borri P. (1977b) Interaction of N-(d,l-seryl)N′-(2,3,4-trihydroxybenzyl)-hydrazine with dopa decarboxylase from pig kidney. Experientia 33, 158–160.
Borri Voltattorni C, Minelli A., and Borri P. (1981) The interaction of 2,3,4-trihydroxybenzylhydraine with dopa decarboxylase from pig kidney Life Sci 28, 103–108.
Borri Voltattorni C., Minelli A, Cirotto C., Barra D., and Turano C. (1982) Subunit structure of dopa decarboxylase from pig kidney. Arch Biochem. Biophys 217, 58–64.
Borri Voltattorni C, Minelli A., and Dominici P. (1983) Interaction of aromatic amino acids in D and L forms with DOPA decarboxylase from pig kidney. Biochemistry 22, 2249–2254.
Borri Voltattorni C, Minelli A., and Turano C. (1971) Spectral properties of the coenzyme bound to dopa decarboxylase from pig kidney. FEBS Lett. 17, 231–235.
Borri Voltattorni C, Minelli A., Vecchini P., Fiori A, and Turano C. (1979) Purification and characterization of dopa decarboxylase from pig kidney Eur J Biochem 93, 181–188.
Bosin T. R., Baldwin J. R., and Maickel R. P. (1978) Inhibition of dopa decarboxylation by analogues of tryptophan. Biochem Pharmacol. 27, 1289–1291
Bosin T. R, Buckpitt A. R, and Maickel R. P. (1974) Substrate specificity of AADC. Life Sci. 14, 899–908.
Bossa F., Martini F., Barra D., Borri Voltattorni C., Minelli A., and Turano C. (1977) The chymotryptic phosphopyridoxal peptide of dopa decarboxylase from pig kidney. Biochem. Biophys. Res Commun 78, 177–184.
Bouchard S. and Roberge A. G. (1979) Biochemical properties and kinetic parameters of DOPA-5HTP decarboxylase in brain, liver, and adrenals of cat. Can. J Biochem. 57, 1014–1018.
Boulton A A. (1978) The tyramines: Functionally significant biogenic amines or metabolic accidents? Life Sci 23, 659–672.
Bowsher R. R. and Henry D. P. (1983) Decarboxylation of p-tyrosine: A potential source of p-tyramine in mammalian tissues. J. Neurochem. 40, 992–1002.
Bowsher R. R., Verburg K. M., and Henry D. P. (1983) Rat histamine N-methyltransferase: Quantification, &sue distribution, purification, and immunologic properties J. Biol. Chem. 258, 12215–12220.
Bulbring E. and Gershon M. D. (1967) 5-Hydroxytryptamine participation in the vagal inhibitory innervation of the stomach. J Physiol (Lond.) 192, 823–846.
Buzard J. A. and Nytch P. D. (1957) Some characteristics of rat kidney 5HTP decarboxylase. J Biol. Chem 227, 225–230.
Calne D. B., Teychenne P. F., and Pfeiffer R F. (1977) Treatment of parkinsonism. Adv. Exp Med Biol. 90, 49–54
Carlsson A. and Lindquist M. (1962) In vivo decarboxylation of α-methyldopa and α-methyl-metatyrosine. Acta Physiol Scand 54, 87–94
Cavalli-Sforza L. L, Santachiara S. A, and Wang L. (1974) Electrophoretic study of 5HTP decarboxylase from brain and liver in several species. J Neurochem 23, 629–634
Charteris A. and John R. (1975) An investigation of the assay of dopamine using trinitrobenzenesulfonic acid Anal Biochem. 66, 365–371
Christenson J G., Dairman W., and Udenfriend S (1970) Preparation and properties of a homogeneous aromatic L-amino acid decarboxylase from hog kidney. Arch Biochem. Biophys 141, 356–367
Christenson J G., Dairman W., and Udenfriend S. (1972) On the identity of DOPA decarboxylase and 5HTP decarboxylase. Proc. Natl. Acad. Sci. USA 69, 343–374.
Clark W. G. (1959) Studies on inhibition of dopa decarboxylase in vitro and in vivo. Pharmacol. Rev. 11, 330–349.
Clark W. G. and Pogrund R. S (1961) Inhibition of dopa decarboxylase in vitro and in VIVO. Circ. Res 9, 721–732.
Clark C. T., Weissbach H., and Udenfriend S (1954) 5-Hydroxy-tryptophan decarboxylase. Preparation and properties. J Biol Chem 210, 139–148
Corgier M. and Pacheco H (1975) Purification and properties of aromatic L-amino acid decarboxylase of rat brain. Biochimie 57, 1005–1017.
Costa M. and Furness J. B (1979) On the possibility that an indoleamine is a neurotransmitter in the gastrointestinal tract. Biochem Pharmacol 28, 565–571.
Coulson W F., Henson G., and Jepson J B (1968) The specificity of rat liver aromatic amino acid decarboxylase. Biochem J. 107, 17P–18P
Culvenor A. J. and Jarrott B. (1979) Reduction of AADC protein in rats after chrome administration of alphamethyldopa Mol. Pharmacol. 15, 86–98.
Dairman W., Horst W D., Marchelle M E., and Bautz G. (1975) The proportionate loss of DOPA and 5HTP decarboxylating activity in rat central nervous system following intracisternal administration of 5,6-dihydroxytryptamine or 6-hydroxydopamine. J Neurochem 24, 619–623.
DaPrada M. (1977) Dopamine Content and Synthesis in Retina and N. Accumbens Septi. Pharmacological and Light-Induced Modifications in Advances in Biochemical Psychopharmacology, Vol. 16 (Costa E and Gessa G. L, eds ), pp. 311–319, Raven, New York.
David J C., Dairman W, and Udenfriend S. (1973) On the significance of the large amounts of non-neuronal AADC in kidney and liver. Pharmacologist 15, 246.
David J. C., Dairman W, and Udenfriend S. (1974) On the importance of decarboxylation in the metabolism of phenylalanine, tyrosine, and tryptophan. Arch. Biochem. Biophys 160, 561–568
Davis V E. and Awapara J. (1960) A method for the determination of some amino acid decarboxylases J Biol. Chem 235, 124–127
D’Erme M., Rosei M A, Fiori A., and DiStazio G. (1980) Assay of AADC by high performance liquid chromatography. Anal Biochem. 104, 59–61.
Dietrich L. S (1953) A rapid method for the determination of dopa decarboxylase in animal tissues. J. Biol Chem. 204, 587–591.
Dreyfus C. F., Bornstein M. B, and Gershon M. D. (1977) Synthesis of serotonin by neurons of the myenteric plexus in situ and in organotypic tissue culture Brain Res. 128, 125–139.
Dyck L E., Yang C. R, and Boulton A. A (1983) The biosynthesis of p-tyramine, m-tyramine, and β-phenylethylamine by rat striatal slices. J Neurosci Res 10, 211–220.
Eranko O. (1978) Small intensely fluorescent (SIF) cells and nervous transmission in sympathetic ganglia. Ann Rev Pharmacol. Toxicol 18, 417–430
Fellman J H. (1959) Purification and properties of adrenal L-dopa decarboxylase. Enzymologia 20, 366–376.
Ferrini R. and Glasser A (1964) In vitro decarboxylation of new phenylalanine derivatives Biochem. Pharmacol. 13, 798–800.
Florkin M. and Stotz E. H, eds. (1964) Comprehensive Biochemistry, Vol 13, Report of the Commission on Enzymes of the International Union of Biochemistry, pp. 122–123, Elsevier, New York
Florkin M. and Stotz E H., eds. (1973) Comprehensive Biochemistry, Vol. 13, Enzyme Nomenclature, pp. 272–273, Elsevier, New York.
Fozard J. R. (1982) Highly potent irreversible inhibitors of AADC. Trends Pharmacol. Sci. 3, 429
Fozard J. R., Spedding M, Palfreyman M. G., Wagner J, Mohring J., and Koch-Weser J, (1980) Depression of sympathetic nervous function by D,L-α-monofluoromethyl dopa, an enzyme-activated, irreversible inhibitor of AADC J. Cardiovasc. Pharmacol. 2, 229–245.
Frohlich E. D. (1980) Methyldopa: Mechanisms and treatment 25 years later. Arch. Intern. Med. 140, 954–959.
Fujita T. (1977) Concepts of paraneurons. Arch Histol. Jpn. 40, 1–12.
Fujita T. and Kobayashi S. (1979) Current views on the paraneurone concept. Trends in Neurosci. 2, 27–30.
Furness J. B., Costa M., and Howe P R. C. (1980) Intrinsic Amine-Handling Neurons in the Intestine, in Advances in Biochemical Psychopharmacology (Eranko O, Soinila S. and Paivarinta H., eds.), Vol 25, Raven, New York.
Gardner C. R. and Richards H. H (1981) Use of D,L-alpha-monofluoro-methyldopa to distinguish subcellular pools of AADC in mouse brain. Brain Res 216, 291–298
Gershon M. D. and Ross L. L. (1966a) Radioisotopic studies of the binding exchange and distribution of 5-hydroxytryptamine synthesized from its radioactive precursor. J. Physiol. (Lond ) 186, 451–476.
Gershon M. D. and Ross L. L (1966b) Location of sites of 5-hydroxytryptamine storage and metabolism by radioautography. J. Physiol. (Lond.) 186, 477–492.
Gershon M. D, Dreyfus C. F., Pickel V. M., Joh T. H., and Reis D. J. (1977) Serotonergic neurons in the peripheral nervous system: Identification in gut by histochemical localization of tryptophan hydroxylase. Proc. Natl Acad Set. USA 74, 3086–3089.
Gershon M. D., Robinson R G., and Ross L. L. (1976) Serotonin accumulation in the guinea-pig myenteric plexus. Ion dependence, structure-activity relationship and the effect of drugs. J Pharmacol Exp. Ther. 198, 548–561
Goldstein M., Anagnoste B., Battista A. F., Owen W. S, and Nakatani S. (1969) Studies of amines in the striatum in monkeys with nigral lesions. J. Neurochem. 16, 645–653.
Goldstein M., Fuxe K., and Hokfelt T. (1972) Characterization and tissue localization of catecholamine-synthesizing enzymes. Pharmacol Rev 24, 293–295.
Gonnard P. and Gamier M. (1966) Multiplicity of decarboxylases for cyclic amino acids. Bull. Soc. Chim Biol 48, 225–238.
Hagen P. (1962) Observations on the substrate specificity of dopa decarboxylase from ox adrenal medulla, human phaeochromocytoma and human argentaffinoma. Br. J. Pharmacol 18, 175–182
Hakanson R. and Owman C. (1966) Distribution and properties of amino acid decarboxylases in gastric mucosa. Biochem. Pharmacol 15, 489–499.
Hakanson R. and Owman C. (1967) Concomitant histochemical demonstration of histamine and catecholamines in enterochromaffin-like cells of gastric mucosa Life Sci. 6, 759–766
Hardebo J. E. and Owman C. (1980) Barrier mechanisms for neurotransmitter monoamines and their precursors at the blood-brain interface. Ann. Neural. 8, 1–11.
Hardebo J. E., Edvinsson L., Owman C h., and Rosengren E. (1977) Quantitative evaluation of the blood-brain barrier capacity to form dopamine from circulating L-dopa Acta Physiol. Scand. 99, 377–384.
Hardebo J. E., Emson P. C., Falck B., Owman C h., and Rosengren E (1980) Enzymes related to monoamine transmitter metabolism in brain microvessels. J. Neurochem 35, 1388–1393.
Hartman W. J., Akawie R. I., and Clark W G. (1955) Competitive inhibition of dopa decarboxylase in vttro J. Biol. Chem 216, 507–529
Henning M. (1975) Central Action of Alpha-Methyldopa, in Central Action of Drugs in Blood Pressure Regulation (Davies D. S and Reid J. L.,eds ), pp. 157–165, University Park, Baltimore.
Hofstee B. H J. (1975) Fractionation of protein mixtures through differential adsorption on a gradient of substituted agaroses of increasing hydrophobicrty Prep Biochem 5, 7–19.
Hokfelt T., Fuxe K., and Goldstein M. (1973a) Immunohistochemical localization of AADC in central dopamine and 5-hydroxytryptamine nerve cell bodies of the rat. Bran Res 53, 175–180.
Hokfelt T., Fuxe K, and Goldstein M. (197313) Immunohistochemical studies on monoamine-containing cell systems. Brain Res 62, 461–469.
Holtzin P (1959) Role of L-dopa decarboxylase in the biosynthesis of catecholamines in nervous tissue and the adrenal medulla. Pharmacol. Rev. 11, 317–329.
Holtz P., Heise R, and Luedtke K. (1938) Enzymic destruction of L-dopa by the kidney. Arch. Exp Path Pharmakol. 191, 87–118.
Inagaki C. and Tanaka C. (1978) Characteristics of enzymic decarboxylation of L-threo-3,4-dihydroxyphenylserine using hog renal AADC. Biochem. Pharmacol. 27, 1081–1086.
Iuvone P. M., Galli C. L., Garrison-Gund C. K., and Neff N H. (1978) Light stimulates tyrosine hydroxylase activity and dopamine synthesis in retinal amacrine neurons. Science 202, 901–902.
Jaeger C. B, Albert V R, Joh T H., and Reis D. J. (1983a) AADC in the rat brain: Coexistance with vasopressin in small neurons of the suprachiasmatic nucleus Brain Res. 276, 362–366.
Jaeger C. B., Ruggiero D. A, Albert V. R., Park D. H., Joh T. H., and Reis D. J. (1984) AADC in the rat brain Immunocytochemical localization in neurons of the brain stem. Neuroscience 11, 691–713.
Jaeger C. B., Teitelman G, Joh T H, Albert V. R., Park D. H., and Reis D. J. (1983b) Some neurons of the rat central nervous system contain AADC but not monoamines. Science 219, 1233–1235.
Johnston C. A., Spinedi E., and Negro-Vilar A (1984) AADC activity in the rat median eminence, neuromtermediate lobe and anterior lobe of the pituitary Neuroendocrinology 39, 54–59.
Jones R. S. G., Juorio A V, and Boulton A. A. (1983) Changes in levels of dopamine and tyramine in the rat caudate nucleus following alterations of impulse flow in the nigrostriatal pathway. J. Neurochem 40, 396–401.
Jung M. J., Hornsperger J-M., Gerhart F., and Wagner J. (1984) Inhibition of AADC and depletion of biogenic amines in brain of rats treated with a-monofluoromethyl-p-tyrosine Similitudes and differences with the effects of α-monofluoromethyldopa. Biochem. Pharmacol 33, 327–330.
Jung M. J., Palfreyman M. G, Wagner J., Bey P., Ribereau-Gayon G., Zraika M., and Koch-Weser J (1979) Inhibition of monoamine synthesis by irreversible blockage of AADC with α-monofluoromethyl-dopa. Life Sci 24, 1037–1042
Juorio A. V. (1979) Drug-induced changes in the formation, storage, and metabolism of tyramine in the mouse Br J. Pharmacol. 66, 377–384.
Juorio A. V. (1983) The effect of some decarboxylase inhibitors on striatal tyramines in the mouse. Neuropharmacology 22, 71–73.
Juorio A. V. and Jones R S G. (1981) The effect of mesencephalic lesions on tyramine and dopamine in the caudate nucleus of the rat J Neurochem 36, 1898–1903
Karoum F, Potkin S. G., and Wyatt R. J. (1980) Quantitation and Metabolism of Phenylethylamine and Tyramines Three Isomers in Humans, in Noncatecholic Phenylethylumines, (Mosnain A. D and Wolf M. E., eds.), Marcel Dekker, New York.
Kato S, Nakamura T., and Negishi K. (1980) Postnatal development of dopaminergic cells in the rat retina. J Comp Neural 191, 227–236.
Klingman G. I. (1965) Catecholamine levels and dopa-decarboxylase activity in peripheral organs and adrenergic tissues in the rat after ilmmunosympathectomy J Pharmacol. Exp Ther 148, 14–21
Knox W. E. (1951) The oxidation in liver of L-tyrosine to acetoacetate through p-hydroxyphenylpyruvate and homogentisic acid Biochem J. (Lond.) 49, 686–693
Kuntzman R., Shore P A, Bogdanski D., and Brodie B. B. (1961) Micro-analytical procedures for fluorometric assay of brain dopa-5HTP decarboxylase, norepinephrine and serotonin, and a detailed mapping of decarboxylase activity in brain J. Neurochem 6, 226–232
Laduron P and Belpaire F (1968) A rapid assay and partial purification of dopa decarboxylase Anal Biochem. 26, 210–218
Lamprecht F and Coyle J T (1972) Dopa decarboxylase in the developing rat brain. Brain Res 41, 503–506.
Lancaster G. A. and Sourkes T. L (1972) Purrflcation and properties of hog-kidney dopa decarboxylase Can J. Biochem. 50, 791–797
Landon M. (1977) A method for the direct detection of AADC in electrophoretic media. Anal Biochem 77, 293–297
Langelier P, Parent A., Poirier L J. (1972) Decarboxylase activity of the brain capillary walls and parenchyma in the rat, cat and monkey Brain Res 45, 622–629
Langemann H. (1958) 5-Hydroxytryptophan Decarboxylase, in 5-Hydroxytryptamine (Lewis G P, ed.), pp 153–157, Pergamon, Oxford.
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.
Libet B. (1977) The Role SIF Cells Play in Ganglionic Transmission, in Advances in Biochemical Psychopharmacology (Costa E. and Gessa G. L., eds.) Vol. 16, 541–546, Raven, New York.
Lloyd K. G. and Hornykiewicz O. (1970) Occurrence and distribution of dopa decarboxylase in the human brain. Brain Res. 22, 426–428.
Lloyd K. G. and Hornykiewicz O. (1972) Occurrence and distribution of AADC in the human brain. J. Neurochem. 19, 1549–1559
Lovenberg W., Barchas J., Weissbach H., and Udenfriend S. (1963) Characteristics of the inhibition of AADC by α-methylamino acids. Arch. Biochem. Biophys. 103, 9–14.
Lovenberg W., Weissbach H, and Udenfriend S. (1962) Aromatic L-amino acid decarboxylase J. Biol. Chem. 237, 89–93
MacKay A. V. P., Davies P., Dewar A. J., and Yates C M. (1978) Regional distribution of enzymes associated with neurotransmission by monoamines, acetylcholine and gaba in the human brain. J Neurochem. 30, 827–839
Mackowiak E. D., Hare T. A., and Vogel W. H. (1972) Measurement of AADC—a technical comment. Biochem. Med. 6, 562–567.
Maneckjee R. and Baylin S. B. (1983) Use of radiolabeled monofluoro-methyldopa to define the subunit structure of human L-DOPA decarboxylase. Biochemistry 22, 6058–6063.
Maycock A. L., Aster S D., and Patchett A. A. (1980) Inactivation of 3-(3,4-dihydroxyphenyl)alanine decarboxylase by 2-(fluoromethyl)-3-(3,4-dihydroxyphenyl)alanine. Biochemistry 19, 709–718.
McCaman M W., McCaman R E., and Lees G. J, (1972) Liquid cation exchange—a basis for sensitive radiometric assays for AADC. Anal. Biochem. 45, 242–252.
McCaman R. E., McCaman M. W., Hunt J. M., and Smith M. S (1965) Microdetermination of monoamine oxidase and 5HTP decarboxylase activities in nervous tissues. J Neurochem. 12, 15–23.
Melamed E., Hefti F, Pettibone D J., Liebman J., and Wurtman R. J. (1981) AADC in rat corpus striatum: Implications for action of L-dopa in Parkinsonism Neurology 31, 651–655.
Melamed E., Hefti F., and Wurtman R. J. (1980) DOPA and 5HTP decarboxylase activities in rat striatum: Effect of selective destruction of dopaminergic or serotoninergic input. J. Neurochem. 34, 1753–1756.
Minelli A., Charteris A. T., Borri Voltattorni C, and John R. A (1979) Reactions of dopa decarboxylase with dopa. Biochem J. 183, 361–368.
Morgan W. and Kamp C W. (1980) A GABAergic influence on the light-induced increase in dopamine turnover in the dark-adapted rat retina in vivo J. Neurochem 34, 1082–1086.
Morgan W.W. and Kamp C W (1982) Postnatal development of the light response of the dopaminergic neurons in the rat retina J Neurochem. 39, 283–285.
Muller B., Harris T., Borri Voltattorni C., and Bell C (1984) Distribution of neurons containing dopa decarboxylase and dopamine-β-hydroxylase in some sympathetic ganglia of the dog: A quantitative study Neuroscience 11, 733–740.
Nagatsu, T. (1973) Biochemistry of Catecholamines, pp. 50–60, University Park, Baltimore
Nagatsu T., Yamamoto T, and Kato T. (1979) A new and highly sensitive voltammetric assay for AADC activity by high-performance liquid chromatography. Anal Biochem. 100, 160–165.
Neff N. H., Karoum F., and Hadjiconstantinou N. (1983) Dopamine-containing small intensely fluorescent cells and sympathetic ganglion function. Fed Proc. 42, 3009–3011
Nomenclature Commission of the lnternational Union of Biochemistry (1979) Enzyme Nomenclature, 1978, pp. 920–923, Academic, New York.
Oie H. K., Gazdar A. F., Minna J. D., Weir G. C., and Baylin S. B. (1983) Clonal analysis of insulin and somatostatin secretion and dopa decarboxylase expression by a rat islet cell tumor Endocrinology 112, 1070–1075.
Okuno S. and Fujisawa H. (1983) Accurate assay of dopa decarboxylase by preventing nonenzymatic decarboxylation of dopa. Anal. Biochem. 129, 412–415.
O’Leary M. H. and Baughn R. L (1975) New pathway for metabolism of dopa. Nature 253, 52–53.
O’Leary M. H. and Baughn R. L. (1977) Decarboxylation-dependent transamination catalyzed by mammalian dopa decarboxylase. J. Biol Chem. 252, 7168–7173.
Pahlman S., Rosengren J., and Hjerten S (1977) Hydrophobic interaction chromatography on uncharged Sepharose derivatives J. Chromatogr. 131, 99–108.
Palfreyman M. G., Danzin C., Bey P., Jung M J., Ribereau-Gayon G., Aubry M, Vevert J. P., and Sjoerdsma A. (1978) α-Difluoromethyl dopa, a new enzyme-activated irreversible inhibitor of AADC. J Neurochem. 31, 922–932.
Pearse A. G. (1974) The apud cell concept and its implication in pathology. Pathol Ann. 9, 27–34.
Pearse A. G E (1969) The cytochemistry and ultrastructure of polypeptide hormone-producing cells of the apud series and the embryologic, physiologic and pathologic implications of the concept. J. Histochem. Cytochem. 17, 303–313
Porter C.C. (1973) Inhibitors of AADC-their biochemistry. Adv Neural 2, 37–58.
Radola B. J. (1973) Analytical and preparative isoelectric focusing in gel-stabilized layers Ann. NY Acad. Sci. 209, 127–143.
Rahman M. K. and Nagatsu T. (1982) Demonstration of AADC activity in human brain with L-DOPA and 5HTP as substrates by high-performance liquid chromatography with electrochemical detection. Neurochem. lnt. 4, 1–6.
Rahman M. K., Nagatsu T., and Kato T (1980) New and highly sensitive assay for 5HTP decarboxylase activity by high-performance liquid chromatography-voltammetry. J Chromatogr. 221, 265–270.
Rahman M. K., Nagatsu T., and Kato T. (1981) Aromatic L-amino acid decarboxylase activity in central and peripheral tissues and serum of rats with DOPA and 5HTP as substrates. Biochem. Pharmacol. 30, 645–649.
Rahman M K., Nagatsu T., Sakuri T, Hori S., Abe M., and Matsuda M. (1982) Effect of pyrldoxal phosphate deficiency on AADC activity with DOPA and 5HTP as substrates in rats. Jpn J Pharmacol 32, 803–811
Reichlin S. (1981) Neuroendocrinology, in Textbook of Endocrinology, 6th ed. (Williams R. H, ed.), pp. 625–628, Saunders, Philadelphia.
Reymond M J. and Porter J. C. (1982) Hypothalamic secretion of dopamine after inhibition of AADC activity. Endocrinology 111, 1051–1056.
Ribereau-Gayon G, Danzin C., Palfreyman M. G., Aubry M., Wagner J., Metcalf B. W, and Jung M. J. (1979) In vitro and in vivo effects of α-acetylenic dopa and α-vinyl dopa on AADC. Biochem Pharmacol 28, 1331–1335.
Ribereau-Gayon G, Palfreyman M. G., Zraika M., Wagner J., and Jung M. J. (1980) Irreversible inhibition of AADC by α-difluoromethyl-DOPA and metabolism of the inhibitor. Biochem. Pharmacol. 29, 2465–2469
Roberge A. G. and Poirier L. J (1973) Effect of chronically administered L-dopa on dopa/5HTP decarboxylase and tyrosine and tryptophan hydroxylases in cat brain. J Neural. Trans. 34, 171–185.
Robins E, Robins J. M., Croninger A. B., Moses S G., Spencer J., and Hudgens R. W. (1967) The low level of 5HTP decarboxylase in human brain. Biochem. Med. 1, 240–251.
Rosengren E. (1960) Are dopa decarboxylase and 5-hydroxytryptophan decarboxylase individual enzymes? Acta Physiol Scand. 49, 364–369.
Rudd E. A., Cunningham W. C., and Thanassi J W. (1979) Coenzyme-substrate adducts as inhibitors of mouse liver DOPA decarboxylase J Med. Chem. 22, 233–237.
Rudd E. A. and Thanassi J. W. (1981) Inhibition of AADC by coenzymeamino acid adducts. Biochemistry 20, 7469–7475.
Sacks W, Vogel W H, Nagatsu T, Lloyd K. G., and Sandler M. (1979) Round Table On Is There DOPA Decarboxylase in Human Brain?, in Catecholamines. Basic and Clinical Frontiers, Vol. 1 (Usdin E., Kopin I. J., and Barchas J, eds.), pp. 127–131, Pergamon, New York.
Schayer R. W (1957) Histidine decarboxylase of rat stomach and other mammalian tissues. Am J. Physiol. 189, 533–536.
Schott H. F. and Clark W. G. (1952) Dopa decarboxylase inhibition through the interaction of coenzyme and substrate. J. Biol. Chem 196, 449–462
Segel I. H. (1975) Enzyme Kinetics, pp 41–43, Wiley, New York
Sherald A F, Sparrow J. C, and Wright T R F (1973) A spectrophotometric assay for drosophilia dopa decarboxylase. Anal Biochem. 56, 300–305
Sims K. L and Bloom F E (1973) Rat brain DOPA and 5HTP decarboxylase activities. Differential effect of 6-hydroxydopamine Brain Res 49, 165–175.
Sims K. L, Davis G. A., and Bloom F E (1973) Activities of DOPA and 5HTP decarboxylases in rat brain Assay characteristics and distribution. J Neurochem. 20, 449–464
Snyder S. H. and Axelrod J. (1964) A sensitive assay for 5HTP decarboxylase. Biochem. Pharmacol 13, 805–806.
Soll A. H, Lewin K. J, and Beaven M A (1981) Isolation of histamine-containing cells from rat gastric mucosa. Biochemical and morphologic differences from mast cells. Gastroenterology 80, 717–727.
Somerville A. R (1964) The assay of AADC using radioactive substrates. Biochem. Pharmacol. 13, 1681–1683
Sourkes T. L. (1954) Inhibition of dopa decarboxylase by derivatives of phenylalanine. Arch Biochem Biophys 51, 444–456
Sourkes T. L. (1965) The action of α-methyldopa in the brain. Br. Med. Bull. 20–21, 66–69
Sourkes T. L (1966) Dopa decarboxylase: Substrates, coenzyme, inhibitors Pharmacol. Rev 18, 53–60.
Sourkes T. L (1972) Influence of specific nutrients on catecholamine synthesis and metabolism. Pharmacol. Rev 24, 349–352
Sourkes T L (1977) Enzymology of Aromatic Amino Acid Decarboxylases, in Structure and Function of Monoamine Enzymes (Usdin E, Weiner N, and Youdim M. B H, eds ), pp. 477–496, Dekker, New York.
Sourkes T. L and D’Iorio (1963) Inhibitors of Catecholamine Metabolism, in Metabolic Inhibitors (Hochster R M and Quastel J H, eds.), pp 79–87, Academic, New York.
Sourkes T., Heneage P., and Trano Y. (1952) Enzymatic decarboxylation of isomers and derivatives of dihydroxyphenylalanme. Arch. Biothem. Biophys, 40, 185–193
Srinivasan K. and Awapara J (1978) Substrate specificity and other properties of dopa decarboxylase from guinea pig kidneys. Biochim Biophys Acta 526, 597–604.
Suer C. T., McKendall G., and Itskovitz H. D. (1984) Serotonin formation in nonblood-perfused rat kidneys J Pharmacol. Exp Ther 228, 53–56
Streffer C. (1967) A method for determination of AADC activity. Biochim Biophys. Acta 139, 193–195
Szabo M., Nakawatase C., Kovathana N., and Frohman L. A. (1977) Effect of the dopa decarboxylase inhibitor MK486 on L-dopa-induced inhibition of prolactin secretion. Evidence for CNS participation in the L-dopa effects. Neuroendocrinology 24, 24–34.
Tabakoff B. and Black R F (1980) A high performance liquid chromatography method for measuring brain DOPA levels and dopamine synthesis rates. J Neurochem 34, 1707–1711.
Tanaka C. (1972) Low Activity of DOPA Decarboxylase in Cerebral Vessels of Spontaneously Hypertensive Rats, in Spontaneous Hypertenslon: Its Pathogenesis and Complications (Okamoto K., ed.), pp. 62–63, Springer-Verlag, Berlin.
Taylor K. M. and Snyder S H (1972) Isotopic microassay of histamine, histidine decarboxylase and histamine methyltransferase in brain tissue. J. Neurochem. 19, 1343–1358
Tran V T. and Snyder S. H. (1981) Histidine decarboxylase J. Biol. Chern 56, 680–686.
Udenfriend S., Clark C T., and Titus E. (1953) 5-Hydroxytryptophan decarboxylase. A new route of metabolism of tryptophan. J Amer Chem Soc. 75, 501–502
Van Huysse J. W., Bowsher R. R., Henry D. P., and Willis L. R. (1984b) In vivo renal synthesis of para-tyramine in the rabbit. Fed. Proc. 43, 452.
Van Huysse J W., Henry D. P., and Willis L. R. (1983a) Amine profile of rabbit and human urine. Fed. Proc. 42, 1132.
Van Huysse J. W, Henry D. P., and Willis L. R (1983b) In vrvo synthesis para-tyramine by the mammalian kidney. Clin. Res. 31, 752A.
Van Huysse J. W., Henry D. P., and Willis L. R. (1984a) Renal tubular secretions of para-tyramine and norepinephrine in the rabbit. Pharmacologist 26, 132
Vogel W. H., McFarland H., and Prince L. N. (1970) Decarboxylation of dopa in various human adult and fetal tissues Biochem. Pharmacol. 19, 618–620.
Wade L. A. and Katzman R (1975) Rat brain regional uptake and decarboxylation of L-dopa following carotid injection. Am J. Physiol. 228, 352–359
Wang F. and Perlman R. L. (1981) Activity of AADC in pheochromocytoma cells. Biochem Pharmacol. 30, 3355–3359.
Waton N. G. (1956a) The effect of organic solvents on mammalian histidine decarboxylase. Biochem J 64, 318–322.
Waton N. G. (1956b) Studies on mammalian histidine decarboxylase. Br. J. Pharmacol 11, 119–127.
Weiner R. I and Ganong W. F (1978) Role of monoamines and histamine in regulation of anterior pituitary secretion Physiol Rev. 58, 905–976.
Weissbach H., Lovenberg W., and Udenfriend S. (1960) Enzymatic decarboxylatron of α-methyl amino acids. Biochem. Biophys. Res. Commun. 3, 225–227.
Weissbach H., Lovenberg W., and Udenfriend S. (1961) Characteristics of mammalian histidine decarboxylating enzymes Biochim Biophys. Acta 50, 177–179.
Westermann E, Balzer H., and Knell J, (1958) Inhibition of serotonin synthesis by α-methyl-dopa. Arch. Exp. Path. Pharmakol. 234, 194–205.
Wood W. I. (1976) Tables for the preparation of ammonium sulfate solutions. Anal. Biochem. 73, 250–257.
Wooten G. F. and Horne M. K (1982) A new autoradiographic approach for imaging forebrain dopamine distribution. Ann. Neurol 12, 163–168.
Wurtman R. J. and Watkins C J. (1977) Suppression of noradrenaline synthesis in sympathetic nerves by carbidopa, an inhibitor of peripheral dopa decarboxylase Nature 265, 79–80
Yuwiler A., Geller E., and Eiduson S. (1959) Studies on 5-hydroxytryptophan decarboxylase I. In vitro inhibition and substrate interaction. Arch. Biochem. Biophys. 80, 162–173.
Yuwiler A., Geller E., and Eiduson S. (1960) Studies on 5-hydroxytryptophan decarboxylase. II. Additional inhibition studies and suggestions on the nature of the enzymic site. Arch. Biochem Biophys. 89, 143–147.
Zavisca F. G., Breau A. P., and Wurtman R. J. (1979) Mechanism of action of methyldopa in the rat: role of 3-O-methylated metabolites Circ Res. 45, 684–690.
Author information
Authors and Affiliations
Editor information
Rights and permissions
Copyright information
© 1986 The Humana Press Inc.
About this protocol
Cite this protocol
Bowsher, R.R., Henry, D.P. (1986). Aromatic L-Amino Acid Decarboxylase. In: Boulton, A.A., Baker, G.B., Yu, P.H. (eds) Neurotransmitter Enzymes. Neuromethods, vol 5. Humana Press. https://doi.org/10.1385/0-89603-079-2:33
Download citation
DOI: https://doi.org/10.1385/0-89603-079-2:33
Publisher Name: Humana Press
Print ISBN: 978-0-89603-079-4
Online ISBN: 978-1-59259-610-2
eBook Packages: Springer Protocols