Über die Konfigurations-Spezifität der Leberesterase (des Menschen) gemäß kinetischer Behandlung der Einzelvorgänge. (VII.) Mitteilung: „Über asymmetrische Esterhydrolyse durch Enzyme“ in der von R. Willstätter, R. Kühn und E. Bamann begonnenen Untersuchungsreihe.)

Publisher Website
Google Scholar
Abstract
The ratio of the hydrolysis of the 2 optical antipodes of mandelic acid ester could not be deduced from the reaction courses of the isolated components. By determining the total hydrolysis of "racemates" by titration, and the % of both compounds which had been split by optical analysis, a set of "pS"-curves could be plotted, the mathematical and graphic analysis of which showed that the optimum in the pS-curve could be explained by assuming that the [long dash]ester forms at least 2 components: ES- and ES-2, the latter being rather slowly hydrolysed and of course only having been formed in sufficient quantities when the conc. of the ester was high. The splitting up of both compounds was inhibited in the presence of the + ester, but not to the same degree. The + ester was less inhibited by the presence of the [long dash]ester though this compound had a great affinity for the enzyme. This leads to the conclusion that the specific groups of the enzyme which split up the + ester are not identical with those which hydrolyse the [long dash]ester. The presence of 2 distinct enzymes is not postulated but the opinion is advanced that difference in position of the active groups on the colloidal bearer might be the cause of the phenomena.