Purification and subunit structure of nicotinamide adenine dinucleotide specific isocitrate dehydrogenase from Neurospora crassa

Biochemistry ◽  
1979 ◽  
Vol 18 (16) ◽  
pp. 3616-3622 ◽  
Author(s):  
Daniel A. Nealon ◽  
Robert A. Cook
Keyword(s):  
Neurospora Crassa ◽  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Subunit Structure

Catabolite-controlled regulation of glutamate dehydrogenases of Neurospora crassa

1970 ◽  
Vol 16 (1) ◽  
pp. 33-40 ◽  
Author(s):  
M. Kapoor ◽  
A. K. Grover
Keyword(s):  
Neurospora Crassa ◽  
Glutamate Dehydrogenase ◽  
Growth Medium ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Reciprocal Relationship ◽  
The Other ◽  
Nicotinamide Adenine ◽  
Specific Enzyme ◽  
Other Hand

The effect of the presence of catabolites in the growth medium on the synthesis of the two glutamate dehydrogenases of Neurospora crassa is reported. It has been demonstrated that the nicotinamide adenine dinucleotide (NAD) specific glutamate dehydrogenase is subject to repression by sucrose and glucose. Nicotinamide adenine dinucleotide phosphate (NADP) specific glutamate dehydrogenase, on the other hand, is induced by increasing concentrations of the catabolite. These data suggest that a reciprocal relationship exists between these two enzymes during synthesis in the presence of catabolites. Growth in higher concentrations of sucrose led to the formation of two isoenzymes of the NADP-specific enzyme; the second or the minor isozyme is not produced at very low catabolite concentrations. The catabolite effects produced by sucrose are overcome by glutamate, if the latter is incorporated into the growth medium. Glutamate represses both the isozymes of NADP-specific enzyme.

scholarly journals The effect of pH on the characteristics of the binding of nicotinamide–adenine dinucleotide by nicotinamide–adenine dinucleotide specific isocitrate dehydrogenase from pea mitochondria

1970 ◽  
Vol 116 (5) ◽  
pp. 819-824 ◽  
Author(s):  
G. F. Cox ◽  
D. D. Davies
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Maximum Velocity ◽  
Nicotinamide Adenine ◽  
Half Maximum ◽  
Ph Optimum ◽  
Effect Of Ph ◽  
Ph Values ◽  
Metabolic Significance

1. The effect of pH on the Vmax. and concentration of NAD+ at half-maximum velocity at a constant isocitrate concentration was examined, and the results were related to the requirements for binding of H+ ions to the enzyme. 2. The effect of varying the NAD+ concentration on the pH optimum with constant isocitrate concentration was studied. 3. A comparison has been made between the effect of isocitrate concentration on the characteristics of binding of NAD+ and the effect of NAD+ concentration on the characteristics of isocitrate binding at three different pH values. 4. The mechanistic and metabolic significance of these studies is considered.

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