TY - JOUR
T1 - Glutamate synthase
T2 - properties of the reduced nicotinamide adenine dinucleotide dependent enzyme from Saccharomyces cerevisiae
AU - Roon, R. J.
AU - Even, H. L.
AU - Larimore, F.
PY - 1974
Y1 - 1974
N2 - A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.
AB - A reduced nicotinamide adenine dinucleotide (NADH) dependent glutamate synthase has been detected and partially purified from crude extracts of Saccharomyces cerevisiae. The enzyme is specific for NADH, glutamine, and α ketoglutarate (Km values of 2.6 μM, 1.0 mM, and 140 μM, respectively) and has a pH optimum between 7.1 and 7.7. The stoichiometry of the reaction has been determined as 2 mol of glutamate synthesized per mol of glutamine consumed. Glutamate synthase can be distinguished from either of the glutamate dehydrogenases of yeast on the basis of its substrate requirements and behavior during agarose gel and ion exchange chromatography. Variations in the specific activity of glutamate synthase, which occur in response to changes in the growth medium, are similar in character to those observed with the nicotinamide adenine dinucleotide phosphate dependent (anabolic) glutamate dehydrogenase.
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M3 - Article
C2 - 4362465
AN - SCOPUS:0016365925
SN - 0021-9193
VL - 118
SP - 89
EP - 95
JO - Journal of bacteriology
JF - Journal of bacteriology
IS - 1
ER -