Ornithine decarboxylase: Inhibition by a-hydrazinoornithine

Sami I. Harik; Solomon H Snyder

doi:10.1016/0005-2744(73)90433-6

Ornithine decarboxylase: Inhibition by a-hydrazinoornithine

Sami I. Harik, Solomon H Snyder

School of Medicine

Research output: Contribution to journal › Article › peer-review

Abstract

a-Hydrazinoornithine is a potent inhibitor of ornithine decarboxylase (EC 4.1.1.17, l-ornithine carboxy-lyase) with K_i values for the enzyme from Escherichia coli and rat ventral prostate of 5 · 10^-7 and 2·10^-6 M, respectively. Inhibition of ornithine decarboxylase by a-hydrazinoornithine is relatively selective, since the drug is 1-2 orders of magnitude less potent in inhibiting other pyridoxal phosphate-dependent amino acid decarboxylases. Other hydrazino compounds examined are much less potent inhibitors of ornithine deacrboxylase than a-hydrazinoornithine. Inhibition by a-hydrazinoornithine is reversible and competitive with respect to substrate.

Original language	English (US)
Pages (from-to)	501-509
Number of pages	9
Journal	BBA - Enzymology
Volume	327
Issue number	2
DOIs	https://doi.org/10.1016/0005-2744(73)90433-6
State	Published - Dec 19 1973

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title = "Ornithine decarboxylase: Inhibition by a-hydrazinoornithine",

abstract = "a-Hydrazinoornithine is a potent inhibitor of ornithine decarboxylase (EC 4.1.1.17, l-ornithine carboxy-lyase) with Ki values for the enzyme from Escherichia coli and rat ventral prostate of 5 · 10-7 and 2·10-6 M, respectively. Inhibition of ornithine decarboxylase by a-hydrazinoornithine is relatively selective, since the drug is 1-2 orders of magnitude less potent in inhibiting other pyridoxal phosphate-dependent amino acid decarboxylases. Other hydrazino compounds examined are much less potent inhibitors of ornithine deacrboxylase than a-hydrazinoornithine. Inhibition by a-hydrazinoornithine is reversible and competitive with respect to substrate.",

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AU - Harik, Sami I.

AU - Snyder, Solomon H

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N2 - a-Hydrazinoornithine is a potent inhibitor of ornithine decarboxylase (EC 4.1.1.17, l-ornithine carboxy-lyase) with Ki values for the enzyme from Escherichia coli and rat ventral prostate of 5 · 10-7 and 2·10-6 M, respectively. Inhibition of ornithine decarboxylase by a-hydrazinoornithine is relatively selective, since the drug is 1-2 orders of magnitude less potent in inhibiting other pyridoxal phosphate-dependent amino acid decarboxylases. Other hydrazino compounds examined are much less potent inhibitors of ornithine deacrboxylase than a-hydrazinoornithine. Inhibition by a-hydrazinoornithine is reversible and competitive with respect to substrate.

AB - a-Hydrazinoornithine is a potent inhibitor of ornithine decarboxylase (EC 4.1.1.17, l-ornithine carboxy-lyase) with Ki values for the enzyme from Escherichia coli and rat ventral prostate of 5 · 10-7 and 2·10-6 M, respectively. Inhibition of ornithine decarboxylase by a-hydrazinoornithine is relatively selective, since the drug is 1-2 orders of magnitude less potent in inhibiting other pyridoxal phosphate-dependent amino acid decarboxylases. Other hydrazino compounds examined are much less potent inhibitors of ornithine deacrboxylase than a-hydrazinoornithine. Inhibition by a-hydrazinoornithine is reversible and competitive with respect to substrate.

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Ornithine decarboxylase: Inhibition by a-hydrazinoornithine

Abstract

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