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6. Quinate oxidation in Gluconobacter oxydans IFO3244: purification and characterization of quinoprotein quinate dehydrogenase

Author

Vangnai, Alisa S., Toyama, Hirohide, De-eknamkul, Wanchai, Yoshihara, Nozomi, Adachi, Osao, and Matsushita, Kazunobu

Subjects
DEHYDROGENASES, ENZYME analysis, IMP dehydrogenase, CHEMICAL purification
Abstract

Abstract: 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. [Copyright &y& Elsevier]

Published
2004
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