Mj. Bonete et al., GLUCOSE-DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOFERAX-MEDITERRANEI - ENZYME-PURIFICATION, CHARACTERIZATION AND N-TERMINAL SEQUENCE, FEBS letters, 383(3), 1996, pp. 227-229
An NAD(P)-glucose dehydrogenase from the extremely halophilic Archaeon
, Haloferax mediterranei, has been purified to electrophoretic homogen
eity, The purified enzyme has been characterised with respect to its c
ofactor specificity, subunit composition and its salt and thermal stab
ility, The N-terminal amino acid sequence has been determined and N-te
rminus alignment with sequences of other glucose dehydrogenases shows
that the halophilic enzyme most closely resembles the NAD(P)-linked gl
ucose dehydrogenase from the thermophilic Archaeon Thermoplasma acidop
hilum. However, the halophilic glucose dehydrogenase appears to be a d
imeric protein, in contrast to the tetrameric enzyme from the thermoph
ile.