Ml. Camacho et al., ISOCITRATE DEHYDROGENASES FROM HALOFERAX-VOLCANII AND SULFOLOBUS-SOLFATARICUS - ENZYME-PURIFICATION, CHARACTERIZATION AND N-TERMINAL SEQUENCE, FEMS microbiology letters, 134(1), 1995, pp. 85-90
The isocitrate dehydroyenases from the extremely halophilic Archaeon,
Haloferax volcanii, and from the hyperthermophilic Archaeon, Sulfolobu
s solfataricus, have been purified to electrophoretic homogeneity. The
purified enzymes have been characterised with respect to their cofact
or specificities, subunit compositions and their salt and thermal stab
ilities. N-terminal amino acid sequences have been determined for both
enzymes, and multiple alignments with sequences of bacterial and euka
ryotic isocitrate dehydrogenases show that the archaeal enzymes most c
losely resemble the NADP-linked dimeric isocitrate dehydrogenases from
the Bacteria.