J. Ferrer et al., NADP-GLUTAMATE DEHYDROGENASE FROM THE HALOPHILIC ARCHAEON HALOFERAX-MEDITERRANEI - ENZYME-PURIFICATION, N-TERMINAL SEQUENCE AND STABILITY, FEMS microbiology letters, 141(1), 1996, pp. 59-63
An NADP(H)-specific glutamate dehydrogenase of Haloferax mediterranei
has been purified to apparent homogeneity and characterised. The purif
ied enzyme was stabilized by glycerol in absence of salt. Glutamate de
hydrogenase from Hf. mediterranei is a hexameric enzyme with a native
molecular mass of 320 kDa composed of monomers each with a molecular m
ass of 55 kDa. At pH 8.5 the enzyme has K-ms of 0.018, 0.34 and 4.2 mM
for NADP(+), 2-oxoglutarate and ammonium, respectively. Amino acid co
mposition and sequence of the first 16 residues of the N-terminus have
been determined.