Thiols as peroxidase substrates.

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Svensson BE, Graslund A, Strom G, Moldeus P

Thiols as peroxidase substrates.

Free Radic Biol Med. 1993 Feb;14(2):167-75.

PubMed ID

8381104 [ View in PubMed

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Abstract

The abilities of haem peroxidases to catalyse the oxidation of various thiols were studied using the spin-trapping electron spin resonance (ESR) technique. Myeloperoxidase, a neutrophil and monocyte enzyme, catalysed the oxidation of cysteamine, cysteine methyl, and ethyl ester and to some extent 2-mercaptoethanol and thioglycollic acid. This peroxidase poorly catalysed the oxidation of cysteine, N-acetylcysteine, penicillamine, and glutathione under the same conditions. The dependence on pH of peroxidase-catalysed thiol oxidation may indicate that the thiolate anion form is the actual peroxidase substrate. Another leucocyte peroxidase, eosinophil peroxidase, had similar catalytic properties toward thiols as myeloperoxidase. Lactoperoxidase (found in milk, saliva, and tears) and the plant horseradish peroxidase were, however, different from the aforementioned leucocyte peroxidases in their abilities to catalyse the oxidation of thiols.

DrugBank Data that Cites this Article

Drug Enzymes

Drug	Enzyme	Kind	Organism	Pharmacological Action	Actions
Cysteamine	Myeloperoxidase	Protein	Humans	Unknown	Substrate	Details