Two malate dehydrogenases in Methanobacterium thermoautotrophicum View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1998-06

AUTHORS

Heather Thompson, Adrian Tersteegen, Rudolf K. Thauer, R. Hedderich

ABSTRACT

Methanobacterium thermoautotrophicum (strain Marburg) was found to contain two malate dehydrogenases, which were partially purified and characterized. One was specific for NAD+ and catalyzed the dehydrogenation of malate at approximately one-third of the rate of oxalacetate reduction, and the other could equally well use NAD+ and NADP+ as coenzyme and catalyzed essentially only the reduction of oxalacetate. Via the N-terminal amino acid sequences, the encoding genes were identified in the genome of M. thermoautotrophicum (strain DeltaH). Comparison of the deduced amino acid sequences revealed that the two malate dehydrogenases are phylogenetically only distantly related. The NAD+-specific malate dehydrogenase showed high sequence similarity to L-malate dehydrogenase from Methanothermus fervidus, and the NAD(P)+-using malate dehyrogenase showed high sequence similarity to L-lactate dehydrogenase from Thermotoga maritima and L-malate dehydrogenase from Bacillus subtilis. A function of the two malate dehydrogenases in NADPH:NAD+ transhydrogenation is discussed. More... »

PAGES

38-42

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s002030050612

DOI

http://dx.doi.org/10.1007/s002030050612

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1042731588

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/9639601


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