Vangnai Alisa S, Toyama Hirohide, De-Eknamkul Wanchai, Yoshihara Nozomi, Adachi Osao, Matsushita Kazunobu
Department of Biochemistry, Faculty of Science, Chulalongkorn University, Bangkok 10330, Thailand.
FEMS Microbiol Lett. 2004 Dec 15;241(2):157-62. doi: 10.1016/j.femsle.2004.10.014.
Quinoprotein quinate dehydrogenase (QDH) is a membrane-bound enzyme containing pyrroloquinoline quinone (PQQ) as the prosthetic group. QDH in Gluconobacter oxydans IFO3244 was found to be inducible by quinate and it is not constitutively expressed in the absence of quinate. The purification of holo-form of QDH to nearly homogeneity was achieved. The purified QDH appears to have two subunits of approximately 65 and 21 kDa, which could be the result of proteolysis of single polypeptide. Kinetic analysis indicated that the purified enzyme is much more specific to quinate than QDH from Acinetobacter calcoaceticus. The efficiency of the artificial electron acceptor was also determined.
喹啉蛋白奎尼酸脱氢酶(QDH)是一种膜结合酶,以吡咯喹啉醌(PQQ)作为辅基。已发现氧化葡萄糖酸杆菌IFO3244中的QDH可被奎尼酸诱导,在没有奎尼酸的情况下它不是组成型表达的。已实现将全酶形式的QDH纯化至几乎均一。纯化的QDH似乎有两个亚基,分子量约为65 kDa和21 kDa,这可能是单条多肽链蛋白水解的结果。动力学分析表明,纯化的酶对奎尼酸的特异性比乙酸钙不动杆菌的QDH高得多。还测定了人工电子受体的效率。