Nicotinamide adenine dinucleotide metabolism in plants. II. Responses of nicotinamide nucleotides to chemical regulators in bean leaves

1974 ◽  
Vol 52 (4) ◽  
pp. 707-713 ◽  
Author(s):  
S. C. Chen ◽  
H. R. Godavari ◽  
E. R. Waygood
Keyword(s):  
Phaseolus Vulgaris ◽  
Nicotinic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Nicotinamide Adenine ◽  
Phaseolus Vulgaris L ◽  
Cyclic Pattern ◽  
Nad Metabolism ◽  
Detached Leaves ◽  
Time Periods ◽  
Bean Leaves

Incorporation of nicotinic acid-7-14C into nicotinamide adenine dinucleotide by the trifoliate leaves of the bean plant (Phaseolus vulgaris L. var. Brittle Wax) was studied for varying time periods from 5 min to 48 h. Nine radioactive compounds were isolated and identified as all the possible intermediates of NAD metabolism operating in a cyclic pattern. All the intermediates were labelled rapidly and N-methyl nicotinic acid (trigonelline) was detected within 5 min. About 80% of the nicotinic acid fed was accumulated in trigonelline. Senescence induced by floating detached leaves on water enhanced incorporation of the label into nucleotides, NAD > NADP. Treatment with growth regulators altered the NAD/NADP ratios. Benzimidazole and kinetin enhanced NADP synthesis while benzyladenine and ethionine reduced NADP synthesis. The regulator-mediated NADP synthesis is enhanced by light and appears to be inversely related to the synthesis of trigonelline.

Nicotinamide adenine dinucleotide metabolism in plants. I. Intermediates of biosynthesis in wheat leaves and the effect of benzimidazole

1970 ◽  
Vol 48 (12) ◽  
pp. 2267-2278 ◽  
Author(s):  
H. R. Godavari ◽  
E. R. Waygood
Keyword(s):  
Nicotinic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Triticum Aestivum L ◽  
Total Radioactivity ◽  
Significant Loss ◽  
Nicotinamide Adenine ◽  
Nad Metabolism ◽  
Nicotinamide Riboside ◽  
Nicotinamide Mononucleotide ◽  
Wheat Leaves

Leaves of wheat (Triticum aestivum L. var. Selkirk) were incubated with nicotinic acid-7-14C and nicotinamide-7-14C for varying time periods from 5 min to 12 h. Aliquots of alcoholic extracts of leaves were subjected to paper chromatography and radioautography to isolate the intermediates of the synthesis and breakdown of nicotinamide adenine dinucleotide. Nine compounds were isolated quantitatively and identified as intermediates in the pathway of NAD metabolism. All the intermediates were labeled rapidly and the rapidity of labeling became a problem in rigorously proving the sequential operation of the pathway. The results indicate that the Preiss-Handler pathway: nicotinic acid→nicotinic acid mononucleotide→nicotinic acid adenine dinucleotide→NAD operates in wheat leaves. The degradation of NAD proceeded from NAD→nicotinamide mononucleotide→nicotinamide riboside→nicotinamide. Deamidation of the nicotinamide to nicotinic acid initiated a fresh cycle of biosynthesis. The total radioactivity recovered in the intermediates indicates that no measurable amount was lost to other metabolic pathways. Nicotinamide is recovered without significant loss and recycled. The rapid appearance of labeled nicotinamide indicates a possible interconversion of nicotinic acid and nicotinamide. About 80% of the radioactivity accumulated was present in trigonelline which is considered, on the basis of other evidence, to be a non-toxic form of nicotinic acid. Benzimidazole treatment of the leaves increased the incorporation of 14C into NADP.

scholarly journals Pathogen induced subversion of NAD+ metabolism mediating host cell death: a target for development of chemotherapeutics

2021 ◽  
Vol 7 (1) ◽  
Author(s):  
Ayushi Chaurasiya ◽  
Swati Garg ◽  
Ashish Khanna ◽  
Chintam Narayana ◽  
Ved Prakash Dwivedi ◽  
...  
Keyword(s):  
Cell Death ◽  
Host Cell ◽  
Nicotinamide Adenine Dinucleotide ◽  
Malaria Parasite ◽  
Host Cells ◽  
Nicotinamide Adenine ◽  
Targeted Therapeutics ◽  
Nad Metabolism ◽  
Host Cell Death ◽  
Nanomolar Range

AbstractHijacking of host metabolic status by a pathogen for its regulated dissemination from the host is prerequisite for the propagation of infection. M. tuberculosis secretes an NAD+-glycohydrolase, TNT, to induce host necroptosis by hydrolyzing Nicotinamide adenine dinucleotide (NAD+). Herein, we expressed TNT in macrophages and erythrocytes; the host cells for M. tuberculosis and the malaria parasite respectively, and found that it reduced the NAD+ levels and thereby induced necroptosis and eryptosis resulting in premature dissemination of pathogen. Targeting TNT in M. tuberculosis or induced eryptosis in malaria parasite interferes with pathogen dissemination and reduction in the propagation of infection. Building upon our discovery that inhibition of pathogen-mediated host NAD+ modulation is a way forward for regulation of infection, we synthesized and screened some novel compounds that showed inhibition of NAD+-glycohydrolase activity and pathogen infection in the nanomolar range. Overall this study highlights the fundamental importance of pathogen-mediated modulation of host NAD+ homeostasis for its infection propagation and novel inhibitors as leads for host-targeted therapeutics.

scholarly journals Increased nicotinamide adenine dinucleotide content and synthesis in Plasmodium falciparum-infected human erythrocytes

Blood ◽  
1990 ◽  
Vol 75 (8) ◽  
pp. 1705-1710 ◽  
Author(s):  
CR Zerez ◽  
EF Jr Roth ◽  
S Schulman ◽  
KR Tanaka
Keyword(s):  
Plasmodium Falciparum ◽  
Nicotinic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Biosynthetic Pathway ◽  
Pentose Phosphate ◽  
Nicotinamide Adenine ◽  
Nicotinamide Phosphoribosyltransferase ◽  
Nad Synthesis ◽  
Infected Rbcs ◽  
Nicotinic Acid Phosphoribosyltransferase

Abstract Plasmodium falciparum-infected red blood cells (RBCs) are characterized by increases in the activity of glycolytic enzymes. Because nicotinamide adenine dinucleotide (NAD) and NAD phosphate (NADP) are cofactors in the reactions of glycolysis and pentose phosphate shunt, we have examined NAD and NADP content in P. falciparum-infected RBCs. Although NADP content was not significantly altered, NAD content was increased approximately 10-fold in infected RBCs (66% parasitemia) compared with uninfected control RBCs. To determine the mechanism for the increase in NAD content, we examined the activity of several NAD biosynthetic enzymes. It is known that normal human RBCs make NAD exclusively from nicotinic acid and lack the capacity to make NAD from nicotinamide. We demonstrate that infected RBCs have readily detectable nicotinamide phosphoribosyltransferase (NPRT), the first enzyme in the NAD biosynthetic pathway that uses nicotinamide, and abundant nicotinamide deamidase, the enzyme that converts nicotinamide to nicotinic acid, thereby indicating that infected RBCs can make NAD from nicotinamide. In addition, infected RBCs have a threefold increase in nicotinic acid phosphoribosyltransferase (NAPRT), the first enzyme in the NAD biosynthetic pathway that uses nicotinic acid. Thus, the increase in NAD content in P falciparum-infected RBCs appears to be mediated by increases in NAD synthesis from both nicotinic acid and nicotinamide.

A method for 13 C-labeling of metabolic carbohydrates within French bean leaves (Phaseolus vulgaris L.) for decomposition studies in soils

2009 ◽  
Vol 23 (12) ◽  
pp. 1792-1800 ◽  
Author(s):  
Cyril Girardin ◽  
Daniel P. Rasse ◽  
Philippe Biron ◽  
Jaleh Ghashghaie ◽  
Claire Chenu
Keyword(s):  
Phaseolus Vulgaris ◽  
French Bean ◽  
Phaseolus Vulgaris L ◽  
Bean Leaves

scholarly journals Nicotinate, quinolinate and nicotinamide as precursors in the biosynthesis of nicotinamide–adenine dinucleotide in barley

1969 ◽  
Vol 115 (4) ◽  
pp. 679-685 ◽  
Author(s):  
I. J. Ryrie ◽  
K. J. Scott
Keyword(s):  
Nicotinic Acid ◽  
Nicotinamide Adenine Dinucleotide ◽  
Erysiphe Graminis ◽  
Nicotinamide Adenine ◽  
Nad Biosynthesis ◽  
Barley Leaves

1. The relative efficiencies of nicotinate, quinolinate and nicotinamide as precursors of NAD+ were measured in the first leaf of barley seedlings. 2. In small amounts, both [14C]nicotinate and [14C]quinolinate were quickly and efficiently incorporated into NAD+ and some evidence is presented suggesting that NAD+ is formed from each via nicotinic acid mononucleotide and deamido-NAD. 3. [14C]Nicotinamide served equally well as a precursor of NAD+ and although significant amounts of [14C]NMN were detected, most of the [14C]NAD+ was derived from nicotinate intermediates formed by deamination of [14C]nicotinamide. 4. Radioactive NMN was also a product of the metabolism of [14C]nicotinate and [14C]quinolinate but most probably it arose from the breakdown of [14C]NAD+. 5. In barley leaves where the concentration of NAD+ is markedly increased by infection with Erysiphe graminis, the pathways of NAD+ biosynthesis did not appear to be altered after infection. A comparison of the rates of [14C]NAD+ formation in infected and non-infected leaves indicated that the increase in NAD+ content was not due to an increased rate of synthesis.

Acyl-CoA-binding domain containing 3 modulates NAD+ metabolism through activating poly(ADP-ribose) polymerase 1

2015 ◽  
Vol 469 (2) ◽  
pp. 189-198 ◽  
Author(s):  
Yong Chen ◽  
Sookhee Bang ◽  
Soohyun Park ◽  
Hanyuan Shi ◽  
Sangwon F. Kim
Keyword(s):  
Nicotinamide Adenine Dinucleotide ◽  
Cell Metabolism ◽  
Living Cells ◽  
Binding Domain ◽  
Nicotinamide Adenine ◽  
Cellular Functions ◽  
Nad Metabolism ◽  
Domain 3 ◽  
And Function

Nicotinamide adenine dinucleotide (NAD) is a coenzyme found in all living cells and plays a fundamental role is basic cellular functions. Our findings revealed that acyl-CoA binding domain 3 (ACBD3) has prominent impacts on the cellular NAD+ metabolism via regulating PARP1 activation-dependent automodification and thus cell metabolism and function.

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