Disease relevance of triphosphopyridine nucleotide

• Elevated NAD(P) glycohydrolase activity: a possible enzymatic marker for malignancy in Burkitt's lymphoma cells [1].
• Chimeric structure of the NAD(P)+- and NADP+-dependent malic enzymes of Rhizobium (Sinorhizobium) meliloti [2].
• Kinetics and regulation of hepatoma mitochondrial NAD(P) malic enzyme [3].
• Chronic administration of pyrazole in the diet of rats does not cause toxicity and prevents the chronic effects of ethanol on: (1) the redox states of the hepatic NAD(P) couples; (2) liver tryptophan pyrrolase activity; (3) brain tryptophan and 5-hydroxytryptamine metabolism [4].
• The gene (ybeN) coding for nicotinate mononucleotide adenylyltransferase, an NAD(P) biosynthetic enzyme, has been identified and overexpressed in Escherichia coli [5].

High impact information on triphosphopyridine nucleotide

• The primary amino acid sequence of CsgA exhibits homology with members of the short-chain alcohol dehydrogenase (SCAD) family and several lines of evidence suggest that NAD(P)+ binding is essential for biological activity [6].
• Second, strains with csgA alleles encoding amino acid substitutions T6A and R10A in the NAD(P)+ binding pocket failed to develop [6].
• Phorbol myristate acetate activated in normal human neutrophils a single enzymatic entity that was dormant in unstimulated cells, optimally active at pH 7.0, and capable of oxidizing either NADH or NADPH, producing NAD(P)+ and superoxide (O27) [7].
• Ferredoxin-NAD(P)(+) oxidoreductase catalyses the final electron transfer of oxygenic photosynthesis from ferredoxin to NAD(P) [8].
• Activity changes in enzymes that require NAD(P) as coenzymes were also noted in rice cells ectopically expressing YK1, where the cell death caused by hydrogen peroxide and bacterial disease was down-regulated [9].

Chemical compound and disease context of triphosphopyridine nucleotide

• This fact was used to determine the stereospecificity at C4 of NAD(P) for the NADP-dependent alcohol dehydrogenase from Methanogenium organophilum and for the NAD-dependent (R)-2-hydroxyglutarate dehydrogenase from Acidaminococcus fermentans [10].
• An assay for the determination of NAD(P)+ and NAD(P)H in extracts from the obligate anaerobe bacterium Thermoanaerobacter finnii is developed and the strategy for this development is described [11].
• We have isolated several cDNA clones encoding delta 1-pyrroline-5-carboxylate reductase (P5CR, L-proline: NAD(P)+ 5-oxidoreductase, EC 1.5.1.2) which catalyzes the terminal step in proline biosynthesis, by direct complementation of a proC mutation in Escherichia coli with an expression library of soybean root nodule cDNA [12].
• L-Glutamate dehydrogenase (GLDH) independent of NAD(P) and oxygen was first obtained from the psychrotrophic bacterium Aeromonas sp. L101, originally isolated from the organs of salmon (Oncorhynchus keta) [13].
• Role of 2-amino-3-carboxy-1,4-naphthoquinone, a strong growth stimulator for bifidobacteria, as an electron transfer mediator for NAD(P)(+) regeneration in Bifidobacterium longum [14].

Biological context of triphosphopyridine nucleotide

• The extent of the hydrolysis of NAD(P)+ is dependent on the amount of both hydroperoxide and Ca2+ [15].
• This reaction is accompanied by a diminution of the NAD(P)H/NAD(P) ratio and a decrease of the internal negative membrane potential [16].
• ROS production at complex I is critically dependent upon a highly reduced state of the mitochondrial NAD(P)(+) pool and is achieved upon nearly complete inhibition of the respiratory chain [17].
• The most likely explanation for a change in the mechanism for oxidative decarboxylation from stepwise with NAD(P) to concerted with alternative dinucleotide substrates such as 3-APAD and PAAD is a difference in the configuration of bound malate when the different dinucleotide substrates are used [18].
• A detailed reconstruction of the NAD(P) metabolic subsystem using the SEED genomic platform (http://theseed.uchicago.edu/FIG/index.cgi) helped us accurately annotate respective genes in the entire set of 13 cyanobacterial species with completely sequenced genomes available at the time [19].

Anatomical context of triphosphopyridine nucleotide

• A NAD(P)-linked 3 alpha-hydroxysteroid dehydrogenase [3 alpha-hydroxysteroid: NAD(P) oxidoreductase, EC 1.1.1.50], purified to homogeneity from male rat liver cytosol, accounts for most of the oxidative activity for 3 alpha-hydroxysteroids and for benzenedihydrodiol (trans-1,2-dihydroxy-3,5-cyclohexadiene) of this tissue [20].
• In INS-1 mitochondria citrate oscillations are in phase with NAD(P) oscillations, and in intact INS-1 cells citrate oscillations parallel oscillations in ATP, suggesting that these processes are co-regulated [21].
• The imprinted membranes, associated with pH-sensitive field-effect transistors (ISFETs) or Au-quartz piezoelectric crystals, enable the potentiometric or microgravimetric analysis of the oxidized NAD(P)+ cofactors and the reduced NAD(P)H cofactors, respectively [22].
• Redox [NAD(P)H / NAD(P)(+)] fluctuations in isolated mitochondria and intact liver cells were found to display nonrandom, long-range correlations [23].
• Microfluorimetric techniques were used to measure [Ca2+]i, mitochondrial membrane potential [delta psi m, Rhodamine 123 (Rh 123) fluorescence], NAD(P)H/NAD(P)+ autofluorescence and flavoprotein autofluorescence combined with whole-cell voltage-clamp techniques [24].

Associations of triphosphopyridine nucleotide with other chemical compounds

• The single site mutation therefore altered GFOR, which in the wild-type situation contains NADP as nondissociable redox cofactor reacting in a ping-pong type mechanism, to a dehydrogenase with dissociable NAD(P) as cosubstrate and a sequential reaction type [25].
• In livers of 24-h-fasted animals perfused under conditions which would decrease cellular NAD(P)H/NAD(P)+ ratio (pyruvate (2.0 mM) or acetoacetate (10.0 mM], glucagon (1 X 10(-9) M) did not stimulate 45Ca2+ efflux [26].
• A similar defect in Complex I activity and Gly oxidation was found in the NMS1 nuclear mutant, defective in the processing of the nad4 transcript, but alternative NAD(P) H dehydrogenases were less activated [27].
• Betaine aldehyde dehydrogenase (BADH) catalyses the irreversible oxidation of betaine aldehyde to glycine betaine with the concomitant reduction of NAD(P)(+) to NADP(H) [28].
• 1. The reduction of mitochondrial NAD(P) by 2-oxoglutarate was monitored as a measure of 2-oxoglutarate dehydrogenase activity in its intramitochondrial locale [29].

Gene context of triphosphopyridine nucleotide

• The bovine enzyme, which is the first 'classical' NAD(P)(+) glycohydrolase whose structure has been established, presents a particularly high sequence identity with CD38, including the presence of 10 strictly conserved cysteine residues in the ectodomain and putative catalytic residues [30].
• A proposed mechanism of cell death is via activation of a futile cycling of the drug by the cytoplasmic two-electron reductase NAD(P) H: quinone oxidoreductase, also known as NQO1, DT-diaphorase and Xip3 [31].
• Homogeneous 3 alpha-hydroxysteroid dehydrogenase (3 alpha-HSD; EC 1.1.1.50) of rat liver cytosol is a monomeric (Mr 34000) NAD(P)+ dependent oxidoreductase which displays 9-, 11- & 15-hydroxyprostaglandin dehydrogenase activity [32].
• It is distinct from the cytosolic enzyme, glucose-6-phosphate dehydrogenase (G6PDH), using a separate pool of NAD(P)+ and capable of oxidizing several phosphorylated hexoses [33].
• Human CD38 is an authentic NAD(P)+ glycohydrolase [34].

Analytical, diagnostic and therapeutic context of triphosphopyridine nucleotide

• This paper describes the development of a novel optically interrogated enzyme electrode with generic applicability for NAD(P) dependent enzymes [35].
• Recycling of NAD(P) by multienzyme systems immobilized by microencapsulation in artificial cells [36].
• After microinjection of glucose-6-P leading to reduction of NAD(P), a sequence of difference spectra (after substrate minus before) is recorded [37].
• No shift of pI values was observed, when isoelectric focusing was performed with the F4 enzyme species in the presence of NAD(P)+ or NAD(P)H [38].
• 2. Substrate specificity and starch gel electrophoresis experiments indicated an absence of the NAD(P) glutamate dehydrogenase (E.C. 1.4.1.3) [39].

References