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The interaction of 2,3,4-trihydroxybenzylhydrazine with dopa decarboxylase from pig kidney

Authors
Journal
Life Sciences
0024-3205
Publisher
Elsevier
Publication Date
Volume
28
Issue
1
Identifiers
DOI: 10.1016/0024-3205(81)90372-6
Disciplines
  • Biology

Abstract

Abstract The spectral modifications induced by addition of 2,3,4,-trihydroxybenzylhydrazine (Ro 4-5127) to Dopa decarboxylase indicate the binding of this compound to the coenzyme binding site and allow the titration of the enzyme: 1.07 moles of Ro 4-5127 bind 1 mole of enzyme. Inhibition data indicate that Ro 4-5127 behaves as a pseudoirreversible inhibitor of Dopa decarboxylase and that 100% inhibition is not reached at a 1:1 inhibitor/ enzyme molar ratio, as expected from spectral data, but at a molar ratio of about 6. On this basis it would be possible to suggest, beside the coenzyme binding site, the existence on the enzyme molecule of other sites where the compound could bind without affecting its spectral feature. The interaction of Ro 4-5127 with Dopa decarboxylase shows that “in vivo” Ro 4-5127 behaves as a more powerful inhibitor of Dopa decarboxylase than its precursor trihydroxybenzylhydrazine seryl derivative (Ro 4-4602) indicating that the strong “in vivo” inhibition exerted by Ro 4-4602 might reflect the effective interaction of Dopa decarboxylase with Ro 4-5127.

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