PROPERTIES AND SURFACE LOCATION OF A SULFHYDRYL OXIDIZING ENZYME IN FUNGUS SPORES

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Abstract
Spores of the fungus Myrothecium verrucaria contain a surface located enzyme which can effect the direct oxidation of both D-and L-cysteine, glutathione, homocysteine, and thiophenol to the respective disulfides. Thioacetate, thiosalicylate, and thioglycolate are not oxidized. As inferred from inhibitor studies, the enzyme does not require heavy metals for its activity. The enzyme in extracts of spores is not associated with particulate matter. Thioglycolate reversibly inhibits the enzyme, apparently in a competitive manner.