Kawaminami S, Ozaki K, Ito S
Biological Science Laboratories, Kao Corporation, Tochigi, Japan.
Biochem Biophys Res Commun. 1995 Jul 17;212(2):539-43. doi: 10.1006/bbrc.1995.2003.
An endoglucanase in family D, purified from a strain of Bacillus, was found to catalyze the hydrolysis of p-nitrophenyl beta-D-cellotrioside to generate alpha-cellobiose, as determined by 1H-NMR spectroscopy. The hydrolysis of the beta-1,4 glucosidic bond by the enzyme proceeds, therefore, by an inversion mechanism. Furthermore, the interconversion of the alpha- and beta-anomeric protons in the products of hydrolysis, after equilibrium had been reached by mutarotation, was directly characterized by magnetization transfer NMR experiment that exploited the truncated driven nuclear Overhauser effect.
从一种芽孢杆菌菌株中纯化得到的D家族内切葡聚糖酶，经1H-NMR光谱测定，发现它能催化对硝基苯基β-D-纤维三糖苷水解生成α-纤维二糖。因此，该酶对β-1,4糖苷键的水解是通过一种转化机制进行的。此外，在变旋达到平衡后，水解产物中α-和β-异头质子的相互转化通过利用截短驱动核Overhauser效应的磁化转移NMR实验直接进行了表征。
