scholarly journals Pyridine nucleotide cycle of Salmonella typhimurium: in vivo recycling of nicotinamide adenine dinucleotide.

1980 ◽  
Vol 142 (3) ◽  
pp. 1032-1035 ◽  
Author(s):  
J W Foster ◽  
A M Baskowsky-Foster
Keyword(s):  
Salmonella Typhimurium ◽  
Nicotinamide Adenine Dinucleotide ◽  
Pyridine Nucleotide ◽  
Nicotinamide Adenine ◽  
Pyridine Nucleotide Cycle

Characterization of the nadR locus in Escherichia coli

1974 ◽  
Vol 20 (2) ◽  
pp. 205-209 ◽  
Author(s):  
Gerald J. Tritz
Keyword(s):  
Escherichia Coli ◽  
Genetic Control ◽  
Quinolinic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Pyridine Nucleotide ◽  
Nicotinamide Adenine ◽  
Positive Type ◽  
Pyridine Nucleotide Cycle

The biosynthesis of nicotinamide adenine dinucleotide (NAD) is under the genetic control of the nadR+ locus. The nadR+ allele is dominant to the nadR allele in transheterogenotes, indicating that the regulation is of the positive type. Mutants of the nadR type are unable to synthesize quinolinic acid; however, they do retain the ability to convert quinolinic acid into NAD and to recycle this NAD through the pyridine nucleotide cycle. Thus, the nadR+ locus regulates only genes involved in the biosynthesis of quinolinic acid.

Decreased erythrocyte nicotinamide adenine dinucleotide redox potential and abnormal pyridine nucleotide content in sickle cell disease

Blood ◽  
1988 ◽  
Vol 71 (2) ◽  
pp. 512-515 ◽  
Author(s):  
CR Zerez ◽  
NA Lachant ◽  
SJ Lee ◽  
KR Tanaka
Keyword(s):  
Sickle Cell Disease ◽  
Redox Potential ◽  
Sickle Cell ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Pyridine Nucleotide ◽  
Nicotinamide Adenine ◽  
Pyridine Nucleotides ◽  
Cell Disease ◽  
Sickle Erythrocyte

Abstract RBCs from individuals with sickle cell disease are more susceptible to oxidant damage. Because key antioxidant defense reactions are linked to the pyridine nucleotides nicotinamide adenine dinucleotide (NAD) and nicotinamide adenine dinucleotide phosphate (NADP), we tested the hypothesis that the RBC redox potential as manifested by the NADH/[NAD+ + NADH] and NADPH/[NADP+ + NADPH] ratios is decreased in sickle erythrocytes. Our data demonstrate that sickle RBCs have a significant decrease in the NADH/[NAD+ + NADH] ratio compared with normal RBCs (P less than .00005). Interestingly, sickle RBCs also had a significant increase in total NAD content compared with normal RBCs (P less than .00005). In contrast, although sickle RBCs had a significant increase in the total NADP content compared with normal RBCs (P less than .00005), sickle RBCs had no significant alteration in the NADPH/[NADP+ + NADPH] ratio. High reticulocyte controls demonstrated that these changes were not related to cell age. Thus, sickle RBCs have a decrease in NAD redox potential that may be a reflection of their increased oxidant sensitivity. The changes in these pyridine nucleotides may have further metabolic consequences for the sickle erythrocyte.

scholarly journals New Chemical Probe Targeting Bacterial NAD Kinase

Molecules ◽  
2020 ◽  
Vol 25 (21) ◽  
pp. 4893
Author(s):  
David A. Clément ◽  
Clarisse Leseigneur ◽  
Muriel Gelin ◽  
Dylan Coelho ◽  
Valérie Huteau ◽  
...  
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Kinase Inhibitors ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Infection Model ◽  
Detailed Knowledge ◽  
Nad Kinase ◽  
Chemical Probe ◽  
Covalent Coupling

Nicotinamide adenine dinucleotide (NAD) kinases are essential and ubiquitous enzymes involved in the tight regulation of NAD/nicotinamide adenine dinucleotide phosphate (NADP) levels in many metabolic pathways. Consequently, they represent promising therapeutic targets in cancer and antibacterial treatments. We previously reported diadenosine derivatives as NAD kinase inhibitors with bactericidal activities on Staphylococcus aureus. Among them, one compound (namely NKI1) was found effective in vivo in a mouse infection model. With the aim to gain detailed knowledge about the selectivity and mechanism of action of this lead compound, we planned to develop a chemical probe that could be used in affinity-based chemoproteomic approaches. Here, we describe the first functionalized chemical probe targeting a bacterial NAD kinase. Aminoalkyl functional groups were introduced on NKI1 for further covalent coupling to an activated SepharoseTM matrix. Inhibitory properties of functionalized NKI1 derivatives together with X-ray characterization of their complexes with the NAD kinase led to identify candidate compounds that are amenable to covalent coupling to a matrix.

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