Abstract

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.

摘要

酶的共同特征是催化作用在不同底物上的反应的能力，称为“广泛特异性”或“多特异性”，并能在同一活性位点催化不同的反应（“混杂”）。这些性质似乎违背了酶催化作用的极端特异性的概念，并已根据进化和代谢适应性进行了重新评估。本文研究了在抑制作用于不同底物的多特异性或混杂酶的敏感性研究中，不同抑制作用的潜在用途。醛糖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，在此用作处理差异抑制方法的具体案例。