NADP-glutamate dehydrogenase from the halophilic archaeon Haloferax mediterranei: enzyme purification, N-terminal sequence and stability.
An NADP(H)-specific glutamate dehydrogenase of Haloferax mediterranei has been purified to apparent homogeneity and characterised. The purified enzyme was stabilized by glycerol in absence of salt. Glutamate dehydrogenase from Hf. mediterranei is a hexameric enzyme with a native molecular mass of 320 kDa composed of monomers each with a molecular mass of 55 kDa. At pH 8.5 the enzyme has Kms of 0.018, 0.34 and 4.2 mM for NADP+, 2-oxoglutarate and ammonium, respectively. Amino acid composition and sequence of the first 16 residues of the N-terminus have been determined.
Ferrer
J
J
División de Bioquímica, Facultad de Ciencias, Universidad de Alicante, Spain.
Pérez-Pomares
F
F
Bonete
M J
MJ
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D003470:Culture Media; D004795:Enzyme Stability; D018086:Glutamate Dehydrogenase (NADP+) / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D006216:Halobacteriaceae / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007656:Ketoglutaric Acids / Q000378:metabolism; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009249:NADP / Q000378:metabolism; D000644:Quaternary Ammonium Compounds / Q000378:metabolism; D013696:Temperature
D000596:Amino Acids; D003470:Culture Media; D007656:Ketoglutaric Acids; D000644:Quaternary Ammonium Compounds; D009249:NADP; D018086:Glutamate Dehydrogenase (NADP+)