Soulié J M, Riviere M, Buc J, Gontero B, Ricard J
Eur J Biochem. 1987 Jan 15;162(2):271-4. doi: 10.1111/j.1432-1033.1987.tb10595.x.
The inactivation of reduced chloroplast fructose-bisphosphatase by oxidized thioredoxin fb has been studied during the enzyme reaction along the principle of Tian and Tsou [Biochemistry (1982) 21, 1028-1032]. A minimum model for this process is presented and its kinetic and equilibrium parameters have been determined. Thioredoxin fb binding to the enzyme is fast relative to catalysis and product desorption. Under quasi-equilibrium conditions oxidized thioredoxin is a non-competitive inhibitor of the enzyme reaction and must bind to a regulatory 'thioredoxin site'. The slow deactivation is thermodynamically favoured, and as expected from binding data, slowed down by the presence of substrate, fructose bisphosphate. The desorption of thioredoxin fb from the enzyme is extremely slow and this small protein may be regarded as a 'regulatory' subunit of fructose-bisphosphatase.
根据田和邹的原理[《生物化学》（1982年）21卷，1028 - 1032页]，在酶反应过程中研究了氧化型硫氧还蛋白fb对还原型叶绿体果糖二磷酸酶的失活作用。提出了该过程的最小模型，并确定了其动力学和平衡参数。相对于催化作用和产物解吸，硫氧还蛋白fb与酶的结合很快。在准平衡条件下，氧化型硫氧还蛋白是酶反应的非竞争性抑制剂，且必须结合到一个调节性“硫氧还蛋白位点”。缓慢失活在热力学上是有利的，并且正如结合数据所预期的那样，底物果糖二磷酸的存在会使其减慢。硫氧还蛋白fb从酶上的解吸极其缓慢，这种小蛋白可被视为果糖二磷酸酶的一个“调节性”亚基。
