Henriksson G, Sild V, Szabó I J, Pettersson G, Johansson G
Department of Biochemistry, University of Uppsala, Sweden.
Biochim Biophys Acta. 1998 Mar 3;1383(1):48-54. doi: 10.1016/s0167-4838(97)00180-5.
Substrate structural mapping suggests that the catalytic site of cellobiose dehydrogenase from Phanerochaete chrysosporium forms a narrow cave with two hexose binding subsites. Kinetic data also show that beta-di or oligosaccharides are favored electron donors with respect to both KM and kcat. Surprisingly, thiocellobiose showed an even higher kcat than cellobiose, although the KM value was somewhat higher. The CDH was purified using an updated protocol.
底物结构图谱表明,黄孢原毛平革菌纤维二糖脱氢酶的催化位点形成了一个带有两个己糖结合亚位点的狭窄洞穴。动力学数据还表明,就米氏常数(KM)和催化常数(kcat)而言,β-二糖或寡糖是更有利的电子供体。令人惊讶的是,硫代纤维二糖的kcat甚至比纤维二糖更高,尽管其KM值略高。使用改进的方案纯化了该纤维二糖脱氢酶。