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

FEMS Microbiol Lett. 2004 Dec 15;241(2):157-62. doi: 10.1016/j.femsle.2004.10.014.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alcohol Oxidoreductases / chemistry
  • Alcohol Oxidoreductases / isolation & purification*
  • Alcohol Oxidoreductases / metabolism*
  • Amino Acid Sequence
  • Gluconobacter oxydans / enzymology*
  • Gluconobacter oxydans / growth & development
  • Molecular Sequence Data
  • Oxidation-Reduction
  • PQQ Cofactor / metabolism
  • Quinic Acid / metabolism*
  • Substrate Specificity

Substances

  • Quinic Acid
  • PQQ Cofactor
  • Alcohol Oxidoreductases
  • quinate dehydrogenase