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Characterization of a b 2δ Complex fromEscherichia coli ATP Synthase*
Results indicate the feasibility of the b 2δ complex reaching from the membrane to the membrane-distal portion of the F1 sector, as required if it is to serve as a second stalk.
Solution structure of the N-terminal domain of the δ subunit of the E. coli ATPsynthase
NMR studies of the δ subunit of the Escherichia coli F1F0-ATPsynthase reveal that it consists of an N-terminal six α-helix bundle and a less well ordered C terminus. Both domains are part of one of
Studies on the de novo biosynthesis of NAD in Escherichia coli. The separation of the nadB gene product from the nadA gene product and its purification.
The facile separation of the wild-type quinolinate synthetase A and B proteins out of a nadC mutant suggests that quinolinic acid does not exists as a tightly bound complex.
Chromosomal Location of the C Gene Involved in the Biosynthesis of Nicotinamide Adenine Dinucleotide in Escherichia coli K-12
A gene involved in the synthesis of nicotinamide adenine dinucleotide has been found to be cotransducible with the genes involved in the utilization of arabinose (ara) and the biosynthesis of leucine
De Novo Biosynthesis of Nicotinamide Adenine Dinucleotide in Escherichia coli: Excretion of Quinolinic Acid by Mutants Lacking Quinolinate Phosphoribosyl Transferase
Observations suggest that biosynthesis of NAD de novo is regulated by both repression and feedback inhibition, and that quinolinic acid excretion is controlled by the concentration of nicotinamide adenine dinucleotide precursors.