Structural snapshot of the enzyme reaction in the human enzyme orotidine 5’-phosphate decarboxylase. The two negative charges of the substrate and enzyme do not repel each other, but form an attractive interaction. Photo: Kai Tittmann
Structural snapshot of the enzyme reaction in the human enzyme orotidine 5'-phosphate decarboxylase. The two negative charges of the substrate and enzyme do not repel each other, but form an attractive interaction. Photo: Kai Tittmann Research team led by Göttingen University describes fundamental principle of enzyme catalysis It is well known in physics and chemistry that equal charges repel each other, while opposite charges attract. It was long assumed that this principle also applies when enzymes - the biological catalysts in all living organisms - form or break chemical bonds. It was thought that enzymes place charges in their -active centres-, where the chemical reactions actually take place, in such a way that they repel similar charges from the other molecules around them. This concept is known as "electrostatic stress". For example, if the substrate (the substance upon which the enzyme acts) carries a negative charge, the enzyme could use a negative charge to "stress" the substrate and thus facilitate the reaction.
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