Rhythmic changes in the activities of NAD kinase and NADP phosphatase in the achlorophyllous ZC mutant of Euglena gracilis klebs (strain Z)

Laval-Martin, Danielle; Carré, Isabelle A.; Barbera, S; Edmunds, Lowell

doi:10.1016/0003-9861(90)90742-h

Cited by 20 publications

(10 citation statements)

References 19 publications

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“…Their activity was observed in rat liver Golgi apparatus and mitochondria [162,163], in dormant seeds of Avena sativa L. [164] and to be necessary for NADP utilization in Haemophilus influenzae [165]. NADPase activity of the phytoflagellate Euglena gracilis ZC mutant shows circadian oscillation similar to NADK activity, suggesting that both enzymes represent clock 'gears' [166,167]. Two NADPase isozymes were purified from the Arthrobacter sp.…”

Section: Nadp Degradationmentioning

confidence: 99%

The power to reduce: pyridine nucleotides – small molecules with a multitude of functions

Pollak

Dölle

Ziegler

2007

Biochemical Journal

630

550

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The pyridine nucleotides NAD and NADP play vital roles in metabolic conversions as signal transducers and in cellular defence systems. Both coenzymes participate as electron carriers in energy transduction and biosynthetic processes. Their oxidized forms, NAD + and NADP + , have been identified as important elements of regulatory pathways. In particular, NAD + serves as a substrate for ADP-ribosylation reactions and for the Sir2 family of NAD + -dependent protein deacetylases as well as a precursor of the calcium mobilizing molecule cADPr (cyclic ADP-ribose). The conversions of NADP + into the 2 -phosphorylated form of cADPr or to its nicotinic acid derivative, NAADP, also result in the formation of potent intracellular calcium-signalling agents. Perhaps, the most critical function of NADP is in the maintenance of a pool of reducing equivalents which is essential to counteract oxidative damage and for other detoxifying reactions. It is well known that the NADPH/NADP + ratio is usually kept high, in favour of the reduced form. Research within the past few years has revealed important insights into how the NADPH pool is generated and maintained in different subcellular compartments. Moreover, tremendous progress in the molecular characterization of NAD kinases has established these enzymes as vital factors for cell survival. In the present review, we summarize recent advances in the understanding of the biosynthesis and signalling functions of NAD(P) and highlight the new insights into the molecular mechanisms of NADPH generation and their roles in cell physiology.

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Section: Nadp Degradationmentioning

confidence: 99%

The power to reduce: pyridine nucleotides – small molecules with a multitude of functions

Pollak

Dölle

Ziegler

2007

Biochemical Journal

630

550

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“…However, little information is available regarding NADPase because the enzyme has not yet been identified. NADPase activity has been detected in rat liver mitochondria (4) and in bacteria (5), and it was also found to correlate with the circadian rhythm of Euglena (6) and with seed dormancy in Avena sativa L. (7). Although NADPase activity has been detected in an outer membrane-associated acid phosphatase found in Hemophilus influenzae, this enzyme physiologically functions in the uptake and utilization of exogenous NADP ϩ (8).…”

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confidence: 99%

MJ0917 in Archaeon Methanococcus jannaschii Is a Novel NADP Phosphatase/NAD Kinase

Kawai

Fukuda

Mukai

et al. 2005

Journal of Biological Chemistry

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Among the NAD kinase homologs found in the Kyoto Encyclopedia of Genes and Genomes, the primary structures of only two archaeal proteins (MJ0917 of Methanococcus jannaschii and MMP1489 of Methanococcus maripaludis) are characteristic and consist of two clearly distinguishable regions, viz. a C-terminal NAD kinase region and an N-terminal inositol-1-phosphatase (Ins-1-Pase) region (see Fig. 1A). M. jannaschii and M. maripaludis are hydrogenotrophic methanogenic Archaea whose entire genomic sequences have been determined (17, 18); they are thermophilic and mesophilic Archaea growing preferably at 85 and 37°C, respectively (17, 19). Ins-1-Pase (EC 3.1.3.25) is known to dephosphorylate D-myo-inositol 1-phosphate, yielding myo-inositol, which is necessary for the synthesis of phosphatidylinositol (20).A homolog (MJ0109) of the N-terminal region of MJ0917 (MJ0917-N) exists in M. jannaschii, but not in M. maripaludis. MJ0109 comprises 252 residues and has been shown to be a bifunctional Ins-1-Pase/fructose-1,6-bisphosphatase (Fru-1,6-Pase) (21,22). Other archaeal MJ0917-N homologs (AF2372 of Archaeoglobus fulgidus and TK0787 of Thermococcus kodakaraensis) and a hyperthermophilic bacterial homolog (TM1415 of Thermotoga maritima) have also been shown to be bifunctional Ins-1-Pases/Fru-1,6-Pases (22-25). The crystal structures of MJ0109 and AF2372 have been solved (22,23).The characteristic primary structures of MJ0917 and MMP1489, as well as the presence of Ins-1-Pase (MJ0109) in M. jannaschii, raised questions about the function of both MJ0917 and MMP1489. We hypothesized that MJ0917 and MMP1489 may be novel bifunctional NADPases/NAD kinases with the potential to generate intracellular NADP ϩ and to maintain a suitable balance of NAD ϩ /NADP ϩ . To confirm this hypothesis, we chose MJ0917 and analyzed its biochemical properties.* This work was supported in part by Grant-in-aid 15780212 from the Ministry of Education, Culture, Sports, Science, and Technology of Japan and by the Program for Promotion of Basic Research Activities for Innovative Biosciences. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact. □ S The on-line version of this article (available at http://www.jbc.org) contains supplemental TABLES 1S and 2S. 1 To whom correspondence should be addressed. Tel.: 3767; E-mail: kmurata@kais.kyoto-u.ac.jp. 2 The abbreviations used are: NAADP ϩ , nicotinic acid-adenine dinucleotide phosphate; NADPase, NADP phosphatase; Ins-1-Pase, inositol-1-phosphatase; Fru-1,6-Pase, fructose-1,6-bisphosphatase; poly(P), inorganic polyphosphate; pNPPase, p-nitrophenylphosphatase; Fru-1,6-P 2 , fructose 1,6-bisphosphate; NMN ϩ , nicotinamide mononucleotide; NADPHase, NADPH phosphatase.

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“…NADK and NAD + phosphatase activities have both been detected in the soluble and membrane-bound fractions of the achlorophyllous ZC mutant of E. gracilis Z. The levels and affinities of these activities change depending on circadian rhythms and cell division cycles suggesting a relationship between NAD + /NADP + metabolism and the circadian oscillating loop (Laval-Martin et al 1990a, 1990b Stephan et al (2000) demonstrated that E. gracilis Z has two soluble NADK isoenzymes (isoenzymes 1 and 2), which display similar molecular weights (68 kDa), but differ in their substrate specificities toward triphosphate nucleotides and their catalytic mechanisms. Similar to the enzyme previously described in bacteria, isoenzyme 1 was found to be as active in the presence of ATP as GTP, functioned using a ping-pong mechanism with K m values of 0.26 mM for NAD + and 0.03 mM for ATP.…”

Section: Niacinmentioning

confidence: 97%

Biochemistry and Physiology of Vitamins in Euglena

Watanabe

Yoshimura

Shigeoka

2017

Advances in Experimental Medicine and Biology

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Euglena gracilis Z requires vitamins B1 and B12 for growth. It takes up and accumulates large amounts of these exogenous vitamins through energy-dependent active transport systems. Except for these essential vitamins, E. gracilis Z has the ability to synthesize all human vitamins. Euglena synthesizes high levels of antioxidant vitamins such as vitamins C and E, and, thus, are used as nutritional supplements for humans and domestic animals. Methods to effectively produce vitamins in Euglena have been investigated.Previous biochemical studies indicated that E. gracilis Z contains several vitamin-related novel synthetic enzymes and metabolic pathways which suggests that it is a highly suitable organism for elucidating the physiological functions of vitamins in comparative biochemistry and biological evolution. E. gracilis Z has an unusual biosynthetic pathway for vitamin C, a hybrid of the pathways found in animals and plants. This chapter presents up-to-date information on the biochemistry and physiological functions of vitamins in this organism.

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Rhythmic changes in the activities of NAD kinase and NADP phosphatase in the achlorophyllous ZC mutant of Euglena gracilis klebs (strain Z)

Cited by 20 publications

References 19 publications

The power to reduce: pyridine nucleotides – small molecules with a multitude of functions

The power to reduce: pyridine nucleotides – small molecules with a multitude of functions

MJ0917 in Archaeon Methanococcus jannaschii Is a Novel NADP Phosphatase/NAD Kinase

Biochemistry and Physiology of Vitamins in Euglena

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