Benserazide and carbidopa as substrates of catechol- O-methyltransferase: New mechanism of action in Parkinson's disease
The DOPA-decarboxylase (aromatic- l-amino acid decarboxylase) inhibitors benserazide, its active metabolite 2,3,4-trihydroxybenzylhydrazine and carbidopa are substrates of highly purified catechol- O-methyltransferase. The affinity and maximal velocity of both benserazide and trihydroxy-benzyl hydra...
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Veröffentlicht in: | Biochemical pharmacology 1980-12, Vol.29 (23), p.3123-3126 |
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Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
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Online-Zugang: | Volltext |
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Zusammenfassung: | The DOPA-decarboxylase (aromatic-
l-amino acid decarboxylase) inhibitors benserazide, its active metabolite 2,3,4-trihydroxybenzylhydrazine and carbidopa are substrates of highly purified catechol-
O-methyltransferase. The affinity and maximal velocity of both benserazide and trihydroxy-benzyl hydrazine are extremely favourable implying that these compounds may compete as substrates for catechol-
O-methyltransferase with
l-DOPA. These results are discussed in the light of the ability of benserazide to cause further elevation of plasma
l-DOPA than carbidopa and the use of these compounds in Parkinson's disease. |
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ISSN: | 0006-2952 1873-2968 |
DOI: | 10.1016/0006-2952(80)90574-2 |