Glucose dehydrogenase from the halophilic Archaeon Haloferax mediterranei: enzyme purification, characterisation and N-terminal sequence.
An NAD(P)-glucose dehydrogenase from the extremely halophilic Archaeon, Haloferax mediterranei, has been purified to electrophoretic homogeneity. The purified enzyme has been characterised with respect to its cofactor specificity, subunit composition and its salt and thermal stability. The N-terminal amino acid sequence has been determined and N-terminus alignment with sequences of other glucose dehydrogenases shows that the halophilic enzyme most closely resembles the NAD(P)-linked glucose dehydrogenase from the thermophilic Archaeon Thermoplasma acidophilum. However, the halophilic glucose dehydrogenase appears to be a dimeric protein, in contrast to the tetrameric enzyme from the thermophile.
Bonete
M J
MJ
Divisíon de Bioquimica, Facultad de Ciencias, Universidad de Alicante, Spain. mjbonete@ua.es
Pire
C
C
LLorca
F I
FI
Camacho
M L
ML
D000595:Amino Acid Sequence; D001105:Archaea / Q000201:enzymology*; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D042843:Glucose 1-Dehydrogenase; D005948:Glucose Dehydrogenases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism*; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry / Q000302:isolation & purification; D017386:Sequence Homology, Amino Acid; D013379:Substrate Specificity; D013822:Thermoplasma / Q000201:enzymology
D010446:Peptide Fragments; D005948:Glucose Dehydrogenases; D042843:Glucose 1-Dehydrogenase