• Publications
  • Influence
The control of pyruvate kinases of Escherichia coli. I. Physicochemical and regulatory properties of the enzyme activated by fructose 1,6-diphosphate.
TLDR
The pyruvate kinase of Escherichia coli activated by fructose 1,6-diphosphate has been purified to homogeneity and is inhibited by GTP at concentrations much lower than any other nucleoside triphosphate, especially when GDP is used as the substrate. Expand
The control of pyruvate kinases of Escherichia coli. II. Effectors and regulatory properties of the enzyme activated by ribose 5-phosphate.
TLDR
The pyruvate kinases of Escherichia coli activated by ribose 5-phosphate (RP) has been partially purified and RP is the most powerful activator, with apparent activation constants as low as 1 Mu. Expand
Genetic and physiological characterization of Escherichia coli mutants deficient in phosphoenolpyruvate carboxykinase activity
TLDR
Enzyme levels increased in stationary-phase cultures by a mechanism independent of cyclic adenosine monophosphate or the product of the relA gene, and therefore, the mutations probably represented mutations in the structural gene for this enzyme. Expand
Malic enzyme of Escherichia coli. Diversity of the effectors controlling enzyme activity.
TLDR
It has been concluded that the complex activity controls of malic enzyme are necessitated in bacteria because of the absence of rigid compartmentation controls available to higher organisms. Expand
Regulatory characteristics of the diphosphopyridine nucleotide-specific malic enzyme of Escherichia coli.
  • B. Sanwal
  • Medicine, Biology
  • The Journal of biological chemistry
  • 10 March 1970
TLDR
It is suggested that the DPN+-specific malic enzyme does not function in vivo unless specific deinhibition is brought about by excess aspartate, because quite low levels of CoA are effective in inhibiting the enzyme. Expand
The control of pyruvate kinase of Escherichia coli. Binding of substrate and allosteric effectors to the enzyme activated by fructose 1,6-bisphosphate.
TLDR
The binding of various regulatory ligands and substrates to the fructose bisphosphate activated pyruvate kinase from Escherichia coli has been studied at equilibrium on the basis of a two-site model, where the substrate and fructose bisPhosphate bind to one conformation and the inhibitors to the other. Expand
Allosteric regulation of the activity of citrate synthetase of Escherichiacoli by α-ketoglutarate
TLDR
It is shown in the present communication that α-ketoglutarate also serves as an allosteric inhibitor of this enzyme. Expand
Regulatory mechanisms involving nicotinamide adenine nucleotides as allosteric effectors. I. Control characteristics of malate dehydrogenase.
  • B. Sanwal
  • Medicine, Chemistry
  • The Journal of biological chemistry
  • 10 April 1969
TLDR
The physiological importance of inhibition of malate dehydrogenase by DPNH is considered and the conclusion is reached that this inhibition is necessitated in bacteria because of the absence of rigid, compartmentation controls and the desirability of preventing gluconeogenetic channels from functioning when growth is occurring on glucose. Expand
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