MtdC, a Novel Class of Methylene Tetrahydromethanopterin Dehydrogenases

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2005 Aug 20

PMID 16109948

Citations 6

Authors

Julia A Vorholt

Marina G Kalyuzhnaya

Christoph H Hagemeier

Mary E Lidstrom

Ludmila Chistoserdova

Affiliations

Soon will be listed here.

Abstract

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.

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