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MtdC, a Novel Class of Methylene Tetrahydromethanopterin Dehydrogenases

By Julia A. Vorholt, Marina G. Kalyuzhnaya, Christoph H. Hagemeier, Mary E. Lidstrom and Ludmila Chistoserdova


Novel methylene tetrahydromethanopterin (H(4)MPT) 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-H(4)MPT 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-H(4)MPT 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 H(4)MPT-linked pathway for formaldehyde oxidation/detoxification

Topics: Enzymes and Proteins
Publisher: American Society for Microbiology
Year: 2005
DOI identifier: 10.1128/JB.187.17.6069-6074.2005
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Provided by: PubMed Central
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