Multidimensional energy analysis of pyridoxal-enzyme and quinoenzyme reactions

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Multidimensional free energy analysis of the reactions of the catalytic reactions of two pyridoxal enzymes(serine palmitoyltransferase and threonine synthase) and a quinoenzyme cupper amine oxidase were carried out to elucidate the energetic mechanism of these enzymes. The mechanisms by which the versatile catalyst pyridoxal phosphate is organized to catalyze only one type of reaction, i. e., a stereochemical mechanism and the product-assisted catalysis, were clarified. Analysis of the reaction of cupper amine oxidase, together with the ultra-high-resolution structure of the enzyme, revealed that the dynamic motion of the enzyme provides the basis for the quantum tunneling effect that promotes its catalysis.