Some properties of the dehydrogenating enzymes of bacteria

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Abstract
The enzyme (or active center) of B. coli, which activates lactic acid as a H donator, has the property of specifically adsorbing compounds characterized by the possession of a particular structure which seems to be[long dash]CO[long dash]COH[long dash]or[long dash]CHOH[long dash]COH* where H* is mobile, the compound having acidic properties. The enzyme which activates succinic acid has also the property of adsorbing compounds characterized by the possession of a particular structure ([long dash]C[long dash]CH[long dash]COOH or[long dash]C[long dash]CH2[long dash]COOH). The formic acid enzyme is independent of the lower fatty acids (other than formic acid itself) and of all the substances so far investigated. The activity of glucose as a H donator is not perceptibly inhibited by presence of oxalic acid or hydroxymalonic acid. The reduction of methylene blue by glucose in the presence of bacteria is independent, therefore, of the intermediate production of lactic acid. Toluene on B. coli brings about an elimination of the activity of the organism to many substances, which can still be adsorbed at an active center. Toluene appears also to affect the adsorption coefficient of the active center towards substrates. The effect of toluene is interpretable on the basis of the active center hypothesis, but difficult to understand on other views. A "soluble" preparation of lactic acid enzyme has precisely the same specific adsorbing power on a particular type of compound as the lactic acid enzyme of B. coli, and the activations of the "soluble" preparation are the same after treatment with toluene. These observations support the active center hypothesis of enzyme action.

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