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Journal of Bacteriology, September 2005, p. 6069-6074, Vol. 187, No. 17
0021-9193/05/$08.00+0 doi:10.1128/JB.187.17.6069-6074.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Marina G. Kalyuzhnaya,2,
Christoph H. Hagemeier,3
Mary E. Lidstrom,2,4 and
Ludmila Chistoserdova2*
Laboratorie des Interactions Plantes-Microorganismes, 31326 Castanet-Tolosan, France,1 Department of Chemical Engineering, University of Washington, Seattle, Washington 98195,2 Max-Planck-Institut für terrestrische Mikrobiologie, D-35043 Marburg, Germany,3 Department of Microbiology, University of Washington, Seattle, Washington 981954
Received 5 April 2005/ Accepted 16 June 2005
Novel methylene tetrahydromethanopterin (H4MPT) dehydrogenase enzymes, named MtdC, were purified after expressing in Escherichia coli genes from, respectively, Gemmata sp. strain Wa1-1 and environmental DNA originating from unidentified microbial species. The MtdC enzymes were shown to possess high affinities for methylene-H4MPT and NADP but low affinities for methylene tetrahydrofolate or NAD. The substrate range and the kinetic properties revealed by MtdC enzymes distinguish them from the previously characterized bacterial methylene-H4MPT dehydrogenases, MtdA and MtdB. While revealing higher sequence similarity to MtdA enzymes, MtdC enzymes appear to fulfill a function homologous to the function of MtdB, as part of the H4MPT-linked pathway for formaldehyde oxidation/detoxification.
J.A.V. and M.G.K. contributed equally to this work.
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