Aldridge W N
Robens Institute of Health and Safety, University of Surrey, Guildford, UK.
Chem Biol Interact. 1993 Jun;87(1-3):5-13. doi: 10.1016/0009-2797(93)90019-u.
Many proteins capable of hydrolysing esters are present in biological material of all kinds (microorganisms, plants, invertebrates and vertebrates). Some serve, as indicated by their substrate specificity and distribution within organisms, a defined biological function. However for most esterases a rather general substrate specificity is found indicating that they may have a broad biological function. Their properties will be briefly reviewed with particular emphasis on inhibitors. The mechanism of hydrolysis of esters by many carboxylesterases (B-esterases) is well established largely due to the reaction of OP compounds with their catalytic centre. For others, such as enzymes hydrolysing (i) OP compounds and/or (ii) carboxyl esters which are not inhibited by a time and temperature dependent reaction by OP compounds, reaction mechanisms are still conjecture. The purpose of this presentation is to explore similarities and differences between the esterases and to discuss possible routes for progress in the A-esterase group.
许多能够水解酯类的蛋白质存在于各类生物材料中(微生物、植物、无脊椎动物和脊椎动物)。正如它们的底物特异性和在生物体内的分布所表明的那样,一些蛋白质具有特定的生物学功能。然而,对于大多数酯酶而言,发现它们具有相当普遍的底物特异性,这表明它们可能具有广泛的生物学功能。将简要回顾它们的特性,尤其着重于抑制剂。许多羧酸酯酶(B酯酶)水解酯类的机制已得到充分确立,这主要归功于有机磷化合物与其催化中心的反应。对于其他酯酶,例如水解(i)有机磷化合物和/或(ii)不受有机磷化合物时间和温度依赖性反应抑制的羧酸酯的酶,其反应机制仍然只是推测。本报告的目的是探索酯酶之间的异同,并讨论A酯酶组可能的进展途径。