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
Hauptverfasser: Hagan, Russell M., Raxworthy, Michael J., Gulliver, Peter A.
Format: Artikel
Sprache:eng
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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.
ISSN:0006-2952
1873-2968
DOI:10.1016/0006-2952(80)90574-2