Unknown

Dataset Information

0

MtdC, a novel class of methylene tetrahydromethanopterin dehydrogenases.


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.

SUBMITTER: Vorholt JA 

PROVIDER: S-EPMC1196156 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

MtdC, a novel class of methylene tetrahydromethanopterin dehydrogenases.

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]

Similar Datasets

| S-EPMC3234859 | biostudies-literature
| S-EPMC2373965 | biostudies-literature
| S-EPMC8520639 | biostudies-literature
| S-EPMC10502027 | biostudies-literature
| S-EPMC3409193 | biostudies-literature
| S-EPMC5971449 | biostudies-literature
| S-EPMC4372733 | biostudies-literature
| S-EPMC4342496 | biostudies-literature
| S-EPMC6286250 | biostudies-literature
| S-EPMC5554190 | biostudies-other