Two malate dehydrogenases in Methanobacterium thermoautotrophicum

Arch Microbiol. 1998 Jul;170(1):38-42. doi: 10.1007/s002030050612.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates / metabolism
  • Amino Acid Sequence
  • Archaeal Proteins / classification
  • Archaeal Proteins / genetics*
  • Archaeal Proteins / isolation & purification
  • Archaeal Proteins / metabolism
  • Bacillus subtilis / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Euryarchaeota / enzymology*
  • Euryarchaeota / genetics
  • Malate Dehydrogenase / classification
  • Malate Dehydrogenase / genetics*
  • Malate Dehydrogenase / isolation & purification
  • Malate Dehydrogenase / metabolism
  • Malates / metabolism
  • Molecular Sequence Data
  • NAD / metabolism
  • NADP / metabolism
  • Phylogeny
  • Sequence Alignment


  • Acetates
  • Archaeal Proteins
  • Malates
  • NAD
  • NADP
  • Malate Dehydrogenase