Studies on fumarase. 4. The effects of inhibitors on fumarase activity

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Abstract
Compounds found to be competitive inhibitors and non-inhibitors of fumarase are discussed. All competitive inhibition was temp.-dependent. At low temps. the combination of fumarase and inhibitors was exothermic, while at higher temps. the combination was endothermic. All competitive inhibition was pH-dependent. Variation of Ki and of Kn values with pH are discussed with reference to Dixon''s theory (1953). A tentative hypothesis of the structure of the active center and reaction sequence accompanying the reversible hydration of fumarate to L-malate is suggested.

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