Evidence for an intermediate in quinolinate biosynthesis in Escherichia coli

  title={Evidence for an intermediate in quinolinate biosynthesis in Escherichia coli},
  author={Floyd Wicks and Shigeki Sakakibara and R. K. Gholson},
  journal={Journal of Bacteriology},
  pages={136 - 141}
Evidence for the formation of an unstable intermediate in the synthesis of quinolinate from aspartate and dihydroxyacetone phosphate by Escherichia coli was obtained using toluenized cells of nadA and nadB mutants of this organism and partially purified A and B proteins in dialysis and membrane cone experiments. The results of these experiments indicate that the nadB gene product forms an unstable compound from aspartate in the presence of flavine adenine dinucleotide, and that this compound is… 
Isolation of a catabolic product of 2-butynedioic acid that acts as a precursor of nicotinamide adenine dinucleotide
The de novo nicotinamide adenine dinucleotide biosynthetic pathway of Escherichia coli was investigated and a precursor of quinolinic acid, a key intermediate in the pathway, was synthesized from14C-aspartic acid.
Active-site models for complexes of quinolinate synthase with substrates and intermediates.
The structure of QS from Pyrococcus furiosus has been determined at 2.8 Å resolution and is a homodimer consisting of three domains per protomer, suggesting that the domains are the result of gene triplication.
Incorporation of 13 C glucose into nicotinamide in E. coli and in S. cerevisiae
The mode of incorporation into nicotinamide of label from 13C-labeled samples of D-glucose, in Escherichia coli and Saccharomyces cerevisiae, was determined by means of 13C NMR spectroscopy. The
Quinolinate Synthase: An Example of the Roles of the Second and Outer Coordination Spheres in Enzyme Catalysis.
This work has chosen the [4Fe-4S] cluster-dependent enzyme quinolinate synthase, which shows low in vitro substrate binding specificity, atypical reactivity that produces dead-end products, and a unique modulation of its active site volume.
Properties of NadV / NatV Proteins in a Pyridine Nucleotide (NAD+) Scavenging System Encoded by Vibriophage KVP40
Comparison with proteins of known function indicates that NadV possesses a nicotinamide phosphoribosyl-transferase domain (NAmPRTase) that can convert nicotin ammonia mononucleotide (NMN), indicated NadV of KVP40 also possesses an ATPase function, and ATP might affect the kinetics of the reactions catalyzed by NAm PRTase of NadV.


Isolation of a metabolite capable of differentially supporting the growth of nicotinamide adenine dinucleotide auxotrophs of Escherichia coli
A compound, isolated from the culture fluid of a nadC auxotroph of Escherichia coli grown in a minimal medium, supports the growth of both a nnA and a ndB mutant, which may be the precursor of quinolinic acid, an intermediate in the biosynthesis of nicotinamide adenosine dinucleotide.
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.
Cross-Feeding of Escherichia coli Mutants Defective in the Biosynthesis of Nicotinamide Adenine Dinucleotide
Mutants of Escherichia coli defective in the biosynthesis of nicotinamide adenine dinucleotide are able to grow in a Casamino Acids medium lacking NAD and its immediate precursors, nicotinic acid and Nicotinamide, providing a means of isolating the intermediate, prequinolinic acid, as well as a biological assay for the compound.
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
Detection of precursors of quinolinic acid in Escherichia coli.
A technique is described which allows the detection of precursors of quinolinic acid produced by Escherichia coli, independent of a bioassay. This is based on a double autoradiogram utilizing
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.
The work of Nishizuka and Hayaishi clearly establishes a possible enzymatic basis for t,he conversion of tryptophan t,o niacin, but leaves unanswered several basic questions concerning this conversion.
Mapping of the nadB Locus Adjacent to a Previously Undescribed Purine Locus in Escherichia coli K-12
It is proposed that all mutants blocked in the de novo pathway of nicotinamide adenine dinucleotide biosynthesis be designated nad rather than nic and mutants blocking in the pyridine nucleotide cycle be designated pnc.