Cheron G, Noat G, Ricard J
Centre de Biochimie et de Biologie Moléculaire du Centre National de la Recherche Scientifique, Marseille, France.
Biochem J. 1990 Jul 15;269(2):389-92. doi: 10.1042/bj2690389.
A transient-kinetic study of beta-glucosidase from soyabean cell walls was performed with the use of a stopped-flow apparatus. The progress curve of the reaction exhibits a 'slow' burst of about 1 s before the steady state is reached. In the time scale investigated this burst may be accounted for by only one exponential, whose time constant varies with the substrate concentration. As this concentration is increased the value of the time constant increases at first, then decreases. Premixing the enzyme with glucose, the last product of the reaction sequence, reverses the 'slow' burst into a 'slow' lag. Taken together, these results are only compatible with a model that involves the existence of a 'slow' conformational transition of the enzyme.
利用停流装置对来自大豆细胞壁的β-葡萄糖苷酶进行了瞬态动力学研究。反应的进程曲线在达到稳态之前呈现出约1秒的“缓慢”爆发。在所研究的时间尺度上,这种爆发仅由一个指数来解释,其时间常数随底物浓度而变化。随着该浓度的增加,时间常数的值起初增加,然后减小。将酶与反应序列的最后产物葡萄糖预混合,会将“缓慢”爆发转变为“缓慢”滞后。综上所述,这些结果仅与一个涉及酶存在“缓慢”构象转变的模型相符。