Department of Biology, Biochemistry Unit, University of Pisa, Pisa, Italy.
Interdepartmental Research Center Nutrafood "Nutraceuticals and Food for Health", University of Pisa, Pisa, Italy.
J Enzyme Inhib Med Chem. 2020 Dec;35(1):840-846. doi: 10.1080/14756366.2020.1743988.
The ability to catalyse a reaction acting on different substrates, known as "broad-specificity" or "multi-specificity", and to catalyse different reactions at the same active site ("promiscuity") are common features among the enzymes. These properties appear to go against the concept of extreme specificity of the catalytic action of enzymes and have been re-evaluated in terms of evolution and metabolic adaptation. This paper examines the potential usefulness of a differential inhibitory action in the study of the susceptibility to inhibition of multi-specific or promiscuous enzymes acting on different substrates. Aldose reductase is a multi-specific enzyme that catalyses the reduction of both aldoses and hydrophobic cytotoxic aldehydes and is used here as a concrete case to deal with the differential inhibition approach.
酶的常见特征是能够催化作用于不同底物的反应，即“广谱特异性”或“多特异性”，并在同一活性部位催化不同的反应（“混杂性”）。这些特性似乎与酶催化作用的极端特异性概念相悖，并在进化和代谢适应方面进行了重新评估。本文探讨了在研究作用于不同底物的多特异性或混杂性酶的抑制敏感性时，差异抑制作用的潜在用途。醛还原酶是一种多特异性酶，可催化醛糖和疏水性细胞毒性醛的还原，本文将其用作具体案例来处理差异抑制方法。
