GLUCOSE-DEHYDROGENASE FROM ACINETOBACTER-CALCOACETICUS - QUINOPROTEIN
GLUCOSE-DEHYDROGENASE FROM ACINETOBACTER-CALCOACETICUS - QUINOPROTEIN
复制标题
DOI：
10.1016/0014-5793(79)80584-0
复制
发表时间：
1979-01-01
期刊：
影响因子：
3.5
通讯作者：
VANZEELAND, JK
中科院分区：
文献类型：
--
作者：
DUINE, JA;FRANK, J;VANZEELAND, JK
Many~ seudoinonas and Acetubacter species are capable of oxidizing aldoses to the corresponding lactone, by NAD (P)-independent dehydrogenases [11. One of these enzymes, glucose dehydrogenase (glucose:(acceptor) oxidoreductase, EC 1.1. 99.-), has been purified from Acinetobucter ca~ coaceticus and it appeared to contain a novel prosthetic group of unknown structure [2].Here, the properties of the prosthetic groups bf glucose dehydrogenase and methanol dehydrogenase (EC 1. 1.99. X, an enzyme which is present in methylatrophic bacteria, grown on methane or methanol) are compared. Furthermore, a procedure for testing the activity of the prosthetic groups and similar compounds, using the apoenzyme of a glucose dehydrogenase, is described.
