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Despite several discoveries in recent years, the physiology of acidophilic Micrarchaeota, such as “ Candidatus  Micrarchaeum harzensis A_DKE”, remains largely enigmatic, as they highly express numerous genes encoding hypothetical proteins. Due to a lacking genetic system, it is difficult to elucidate the biological function of the corresponding proteins and heterologous expression is required. In order to prove the viability of this approach, A_DKE’s isocitrate dehydrogenase ( Mh IDH) was recombinantly produced in  Escherichia coli  and purified to electrophoretic homogeneity for biochemical characterization.  Mh IDH showed optimal activity around pH 8 and appeared to be specific for NADP +  yet promiscuous regarding divalent cations as cofactors. Kinetic studies showed  K M  -values of 53.03 ± 5.63 µM and 1.94 ± 0.12 mM and  k cat  -values of 38.48 ± 1.62 and 43.99 ± 1.46 s −1  resulting in  k cat  / K M  -values of 725 ± 107.62 and 22.69 ± 2.15 mM −1  s −1  for DL-isocitrate and NADP + , respectively.  Mh IDH’s exceptionally low affinity for NADP + , potentially limiting its reaction rate, can likely be attributed to the presence of a proline residue in the NADP +  binding pocket, which might cause a decrease in hydrogen bonding of the cofactor and a distortion of local secondary structure.

Biochemical Characterization of Recombinant Isocitrate Dehydrogenase and Its Putative Role in the Physiology of an Acidophilic Micrarchaeon