Journal
NEUROSCIENCE LETTERS
Volume 401, Issue 3, Pages 261-265Publisher
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2006.03.031
Keywords
tryptophan hydroxylase-2; tyrosine hydroxylase; manganese; phenylalanine; hyperphenylalaninemia; Parkinsonism
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We cloned the human tryptophan hydroxylase-2 (hTPH2) gene by RT-PCR, and expressed and purified its product as a maltose-binding protein (MBP)-fusion protein. We investigated the effects of essential divalent cations and L-phenylalanine (L-Phe) on the hTPH2 activity for the first time, and compared them with those on human tyrosine hydroxylase (hTH1) activity. We found that cobaltous and manganous ions inhibited the activities of both enzymes but that hTH1 was affected at lower concentrations than hTPH2. From kinetic analyses, we found that phenylalanine acted as an inhibitor more strongly against hTPH2 than against hTH1 These data are important for elucidating the molecular mechanism underlying the alterations in the contents of serotonin and catecholamines in the brain under pathological and physiological conditions, such as hyperphenylalaninemia and chronic manganese toxicity. (c) 2006 Elsevier Ireland Ltd. All rights reserved.
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