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MtdC, a Novel Class of Methylene Tetrahydromethanopterin Dehydrogenases

Julia A. Vorholt,^1, Marina G. Kalyuzhnaya,^2, Christoph H. Hagemeier,³ Mary E. Lidstrom,^2,4 and Ludmila Chistoserdova^2*

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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