scholarly journals Preparation and properties of nylon-tube-supported nicotinamide--adenine dinucleotide kinase

1977 ◽  
Vol 161 (2) ◽  
pp. 441-443 ◽  
Author(s):  
P V Sundaram ◽  
D K Apps
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Ph Dependence ◽  
Nicotinamide Adenine ◽  
Nad Kinase ◽  
Nylon Tube ◽  
Pigeon Liver

Pigeon liver NAD kinase was covalently coupled to the inside surfaces of nylon tubes, both directly to the nylon and via polyamine specers Km values and the inactivation energy of the reaction changed upon immobilization, but the pH-dependence remained unaltered. The activities and stabilities of different preparations are compared.

Kinetics of the oxidation of reduced nicotinamide adenine dinucleotide by horseradish peroxidase compounds I and II

1986 ◽  
Vol 64 (4) ◽  
pp. 323-327 ◽  
Author(s):  
Mohammed A. Kashem ◽  
H. Brian Dunford
Keyword(s):  
Horseradish Peroxidase ◽  
Active Site ◽  
Nicotinamide Adenine Dinucleotide ◽  
Ph Dependence ◽  
Transient State ◽  
Nicotinamide Adenine ◽  
Compound I ◽  
Single Ionization ◽  
Reduced Nicotinamide Adenine Dinucleotide ◽  
Kinetics Of

The transient state kinetics of the oxidation of reduced nicotinamide adenine dinucleotide (NADH) by horseradish peroxidase compound I and II (HRP-I and HRP-II) was investigated as a function of pH at 25.0 °C in aqueous solutions of ionic strength 0.11 using both a stopped-flow apparatus and a conventional spectrophotometer. In agreement with studies using many other substrates, the pH dependence of the HRP-I–NADH reaction can be explained in terms of a single ionization of pKa = 4.7 ± 0.5 at the active site of HRP-I. Contrary to studies with other substrates, the pH dependence of the HRP-H–NADH reaction can be interpreted in terms of a single ionization with pKa of 4.2 ± 1.4 at the active site of HRP-II. An apparent reversibility of the HRP-II–NADH reaction was observed. Over the pH range of 4–10 the rate constant for the reaction of HRP-I with NADH varied from 2.6 × 105 to5.6 × 102 M−1 s−1 and of HRP-II with NADH varied from 4.4 × 104 to 4.1 M−1 s−1. These rate constants must be taken into consideration to explain quantitatively the oxidase reaction of horseradish peroxidase with NADH.

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.

scholarly journals Interactions of nicotinamide-adenine dinucleotide phosphate analogues and fragments with pigeon liver malic enzyme. Synergistic effect between the nicotinamide and adenine moieties

1987 ◽  
Vol 245 (2) ◽  
pp. 407-414 ◽  
Author(s):  
H J Lee ◽  
G G Chang
Keyword(s):  
Synergistic Effect ◽  
Nicotinamide Adenine Dinucleotide ◽  
Malic Enzyme ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nucleotide Binding ◽  
Phosphate Group ◽  
Nicotinamide Adenine ◽  
Oxidative Decarboxylation ◽  
Wide Range ◽  
Pigeon Liver

The structural requirements of the NADP+ molecule as a coenzyme in the oxidative decarboxylation reaction catalysed by pigeon liver malic enzyme were studied by kinetic and fluorimetric analyses with various NADP+ analogues and fragments. The substrate L-malate had little effect on the nucleotide binding. Etheno-NADP+, 3-acetylpyridine-adenine dinucleotide phosphate, and nicotinamide-hypoxanthine dinucleotide phosphate act as alternative coenzymes for the enzyme. Their kinetic parameters were similar to that of NADP+. Thionicotinamide-adenine dinucleotide phosphate, 3-aminopyridine-adenine dinucleotide phosphate, 5′-adenylyl imidodiphosphate, nicotinamide-adenine dinucleotide 3′-phosphate and NAD+ act as inhibitors for the enzyme. The first two were competitive with respect to NADP+ and non-competitive with respect to L-malate; the other inhibitors were non-competitive with NADP+. All NADP+ fragments were inhibitory to the enzyme, with a wide range of affinity, depending on the presence or absence of a 2′-phosphate group. Compounds with this group bind to the enzyme 2-3 orders of magnitude more tightly than those without this group. Only compounds with this group were competitive inhibitors with respect to NADP+. We conclude that the 2′-phosphate group is crucial for the nucleotide binding of this enzyme, whereas the carboxyamide carbonyl group of the nicotinamide moiety is important for the coenzyme activity. There is a strong synergistic effect between the binding of the nicotinamide and adenosine moieties of the nucleotide molecule.

scholarly journals NAD kinase controls antibiotic susceptibility and pathogenic potential in Staphylococcus aureus

2021 ◽  
Author(s):  
Clarisse Leseigneur ◽  
Laurent Boucontet ◽  
Olivier Gorgette ◽  
Catherine Thouvenot ◽  
Emma Colucci-Guyon ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Nicotinamide Adenine Dinucleotide ◽  
Defense Mechanisms ◽  
Antioxidant Properties ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Primary Electron ◽  
Nicotinamide Adenine ◽  
Nad Kinase ◽  
Pathogenic Potential

Nicotinamide adenine dinucleotide phosphate (NADPH) is the primary electron donor for reductive reactions that are essential for the biosynthesis of major cell components in all organisms. Nicotinamide adenine dinucleotide kinase (NADK) is the only enzyme that catalyzes synthesis of NADP(H) from NAD(H). While the enzymatic properties and physiological functions of NADK have been thoroughly studied, the role of NADK in bacterial pathogenesis remains unknown. Here, we used CRISPR interference to knockdown NADK gene expression in order to address the role of NADK in Staphylococcus aureus pathogenic potential. We find that NADK protects bacteria from antimicrobial defense mechanisms encountered in the host during infection such as oxidative and envelope stresses. Furthermore, we show that antioxidant properties of NADK promote S. aureus survival in infected macrophages. Remarkably, NADK inhibition drastically decreases mortality of zebrafish infected with S. aureus. These findings support a key role for NADK in bacteria interactions with innate immune cells and during infection. Last, we reveal that decreasing NADK expression increases S. aureus susceptibility to antibiotics, opening the way to development of synergistic treatments based on NADK inhibitors and current antibiotics.

scholarly journals Effect of pH on the inhibition of the nicotinamide–adenine dinucleotide-specific isocitrate dehydrogenase from baker's yeast by anions

1968 ◽  
Vol 109 (3) ◽  
pp. 361-368 ◽  
Author(s):  
C. Cennamo ◽  
G. Montecuccoli ◽  
G. Bonaretti ◽  
L. Razzoli
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Nicotinamide Adenine Dinucleotide ◽  
Substrate Concentration ◽  
Ph Dependence ◽  
Chloride Concentration ◽  
Enzymic Activity ◽  
Baker’S Yeast ◽  
Nicotinamide Adenine ◽  
Baker's Yeast ◽  
Effect Of Ph

1. The sensitivity of the NAD+-specific isocitrate dehydrogenase from baker's yeast towards inhibition by anions decreases with decrease in pH. The patterns of the pH-dependence of the enzymic activity can be explained by this effect. 2. In the presence of a high isocitrate concentration, citrate, unlike AMP, has no antagonizing effect on the inhibition of the enzyme by anions. In the presence of AMP, citrate inhibits the enzyme at high isocitrate concentration and activates at low isocitrate concentration. 3. The effects on the enzymic activity of the previous incubation of the enzyme were studied in relation to the substrate concentration, the chloride concentration and the presence of citrate and AMP.

scholarly journals Interaction of pigeon-liver nicotinamide-adenine dinucleotide kinase with cibacron blue F3GA

1976 ◽  
Vol 159 (2) ◽  
pp. 441-443 ◽  
Author(s):  
D K Apps ◽  
C D Gleed
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Spectrophotometric Titration ◽  
Nad Kinase ◽  
Binding Region ◽  
Cibacron Blue ◽  
Steady State Rate ◽  
State Rate ◽  
A Site ◽  
Cibacron Blue F3ga ◽  
Pigeon Liver

The interaction of pigeon liver NAD kinase with Cibacron Blue F3GA was investigated. By using steady-state rate measurements, spectrophotometric titration and chromatography of the enzyme on immobilized dye, it was shown that binding occurs at two nucleotide sites with different affinities, and also at a site distinct from the substrate-binding region.

Effect of Niacin on Mitochondria of Allium Cepa Root Cells

1967 ◽  
Vol 25 ◽  
pp. 78-79
Author(s):  
M. Arif Hayat
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Hydrogen Transfer ◽  
Nicotinamide Adenine Dinucleotide Phosphate ◽  
Nicotinamide Adenine ◽  
Root Tips ◽  
Root Cells ◽  
Transfer Processes ◽  
Standard Procedures ◽  
A Cell ◽  
Critical Interest

Although it is recognized that niacin (pyridine-3-carboxylic acid), incorporated as the amide in nicotinamide adenine dinucleotide (NAD) or in nicotinamide adenine dinucleotide phosphate (NADP), is a cofactor in hydrogen transfer in numerous enzyme reactions in all organisms studied, virtually no information is available on the effect of this vitamin on a cell at the submicroscopic level. Since mitochondria act as sites for many hydrogen transfer processes, the possible response of mitochondria to niacin treatment is, therefore, of critical interest.Onion bulbs were placed on vials filled with double distilled water in the dark at 25°C. After two days the bulbs and newly developed root system were transferred to vials containing 0.1% niacin. Root tips were collected at ¼, ½, 1, 2, 4, and 8 hr. intervals after treatment. The tissues were fixed in glutaraldehyde-OsO4 as well as in 2% KMnO4 according to standard procedures. In both cases, the tissues were dehydrated in an acetone series and embedded in Reynolds' lead citrate for 3-10 minutes.

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