Carlberg I, Sahlman L, Mannervik B
FEBS Lett. 1985 Jan 21;180(1):102-6. doi: 10.1016/0014-5793(85)80240-4.
Among the three closely related enzymes, lipoamide dehydrogenase, mercuric reductase, and glutathione reductase only the latter is inhibited by 2,4,6-trinitrobenzenesulfonate (TNBS). On the other hand, all three enzymes exhibit high rates of TNBS-dependent NADPH oxidation. In the case of glutathione reductase and mercuric reductase this TNBS-dependent activity displays substrate inhibition by excess of NADPH and is strongly stimulated by NADP+. The stimulation is especially pronounced with mercuric reductase, 25-fold under some conditions. Neither substrate inhibition nor stimulation by NAD+ is observed with lipoamide dehydrogenase.
在三种密切相关的酶——硫辛酰胺脱氢酶、汞还原酶和谷胱甘肽还原酶中，只有后者会受到2,4,6-三硝基苯磺酸盐（TNBS）的抑制。另一方面，这三种酶都表现出较高的TNBS依赖型NADPH氧化速率。就谷胱甘肽还原酶和汞还原酶而言，这种TNBS依赖型活性会因过量的NADPH而表现出底物抑制作用，并受到NADP+的强烈刺激。汞还原酶的这种刺激作用尤为明显，在某些条件下可达25倍。硫辛酰胺脱氢酶既未观察到底物抑制作用，也未观察到NAD+的刺激作用。
