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Evidence is limited that ALA may inhibit specific cytochrome P450 enzymes, potentially altering the metabolism of drugs that are substrates for these enzymes

10.34172/mj.2021.022 38

Moreover, characterization studies help establish a foundation for future laboratory investigations

The inability of 5-cholesten-3-one to serve as substrate for the bacterial ketosteroid isomerase was noted in the original publication ( Investigations of the Pseudomonas ketosteroid isomerase based on deuterium and tritium labeling of reactants provided evidence for direct and stereospecific diaxial proton transfer from the 4 to the 6 position ( The role of glutathione in the mammalian GSTs catalyzing the ketosteroid isomerization was not evident, since the bacterial isomerase did not require a cofactor ( a value of the thiol of glutathione is lowered by 2.5 units from 9.2 in solution to 6.7 when bound to GST A1-1 ( a value from 6.7 to 7.2 when Tyr9 was mutated into Phe ( a of Tyr9 is 8.1 in the free GST A1-1, but the value increases to 9.2 when glutathione is bound ( a appears dependent on the ionized thiolate, since S-methylglutathione is without effect on the ionization of Tyr9

, Turkovic, B