Archives of Microbiology

, Volume 175, Issue 5, pp 376–383

Isolation and characterization of a veratrol:corrinoid protein methyl transferase from Acetobacterium dehalogenans

Authors

  • Tina Engelmann
    • Institut für Mikrobiologie, FSU Jena, Philosophenweg 12, 07743 Jena, Germany
  • Franz Kaufmann
    • Dept. of Microbiology, University of Massachussetts, Amherst, MA 01003, USA
  • Gabriele Diekert
    • Institut für Mikrobiologie, FSU Jena, Philosophenweg 12, 07743 Jena, Germany
Original Paper

DOI: 10.1007/s002030100275

Cite this article as:
Engelmann, T., Kaufmann, F. & Diekert, G. Arch Microbiol (2001) 175: 376. doi:10.1007/s002030100275

Abstract.

From 3-methoxyphenol-grown cells of Acetobacterium dehalogenans, an inducible enzyme was purified that mediated the transfer of the methyl groups of veratrol (1,2-dimethoxybenzene) to a corrinoid protein enriched from the same cells. In this reaction, veratrol was converted via 2-methoxyphenol to 1,2-dihydroxybenzene. The veratrol:corrinoid protein methyl transferase, designated MTIver, had an apparent molecular mass of about 32 kDa. With respect to the N-terminal amino acid sequence and other characteristics, MTIver is different from the vanillate:corrinoid protein methyl transferase (MTIvan) isolated earlier from the same bacterium. For the methyl transfer from veratrol to tetrahydrofolate, two additional protein fractions were required, one of which contained a corrinoid protein. This protein was not identical with the corrinoid protein of the vanillate O-demethylase system. However, the latter corrinoid protein could also serve as methyl acceptor for the veratrol:corrinoid protein methyl transferase. MTIver catalyzed the demethylation of veratrol, 3,4-dimethoxybenzoate, 2-methoxyphenol, and 3-methoxyphenol. Vanillate (3-methoxy-4-hydroxybenzoate), 2-methoxybenzoate, or 4-methoxybenzoate could not serve as substrates.

Acetobacterium dehalogenans Corrinoid protein Ether cleavage Methyl transferase O-demethylase Vanillate demethylation Veratrol demethylation

Copyright information

© Springer-Verlag 2001