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ABSTRACT:
SUBMITTER: Vorholt JA
PROVIDER: S-EPMC1196156 | biostudies-literature | 2005 Sep
REPOSITORIES: biostudies-literature
Vorholt Julia A JA Kalyuzhnaya Marina G MG Hagemeier Christoph H CH Lidstrom Mary E ME Chistoserdova Ludmila L
Journal of bacteriology 20050901 17
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 prev ...[more]