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Volumn 41, Issue 5, 2009, Pages 352-361

Molecular properties, functions, and potential applications of NAD kinases

Author keywords

Coenzyme metabolism; NAD kinase; NAD+ NADH; NADP+ NADPH

Indexed keywords

ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE KINASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHOTRANSFERASE;

EID: 66449104358     PISSN: 16729145     EISSN: 17457270     Source Type: Journal    
DOI: 10.1093/abbs/gmp029     Document Type: Review
Times cited : (47)

References (73)
  • 1
    • 0345701347 scopus 로고    scopus 로고
    • Genes required for mycobacterial growth defined by high density mutagenesis
    • DOI 10.1046/j.1365-2958.2003.03425.x
    • Sassetti CM, Boyd DH and Rubin EJ. Genes required for mycobacterial growth defined by high-density mutagenesis. Mol Microbiol 2003, 48: 77-84. (Pubitemid 36411469)
    • (2003) Molecular Microbiology , vol.48 , Issue.1 , pp. 77-84
    • Sassetti, C.M.1    Boyd, D.H.2    Rubin, E.J.3
  • 3
    • 0036334571 scopus 로고    scopus 로고
    • From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways
    • Gerdes SY, Scholle MD, D'souza M, Bernal A, Baev MV, Farrell M and Kurnasov OV, et al. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J Bacteriol 2002, 184: 4555-4572.
    • (2002) J Bacteriol , vol.184 , pp. 4555-4572
    • Gerdes, S.Y.1    Scholle, M.D.2    D'souza, M.3    Bernal, A.4    Baev, M.V.5    Farrell, M.6    Kurnasov, O.V.7
  • 5
    • 0028341061 scopus 로고
    • Evidence for two NAD kinases in Salmonella typhimurium
    • Cheng W and Roth JR. Evidence for two NAD kinases in Salmonella typhimurium. J Bacteriol 1994, 176: 4260-4268. (Pubitemid 24226462)
    • (1994) Journal of Bacteriology , vol.176 , Issue.14 , pp. 4260-4268
    • Cheng, W.1    Roth, J.R.2
  • 7
    • 33747347559 scopus 로고    scopus 로고
    • Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions
    • DOI 10.1074/jbc.M513919200
    • Bieganowski P, Seidle HF, Wojcik M and Brenner C. Synthetic lethal and biochemical analyses of NAD and NADH kinases in Saccharomyces cerevisiae establish separation of cellular functions. J Biol Chem 2006, 281: 22439-22445. (Pubitemid 44242272)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.32 , pp. 22439-22445
    • Bieganowski, P.1    Seidle, H.F.2    Wojcik, M.3    Brenner, C.4
  • 8
    • 22144434877 scopus 로고    scopus 로고
    • Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae
    • DOI 10.1111/j.1742-4658.2005.04749.x
    • Shi F, Kawai S, Mori S, Kono E and Murata K. Identification of ATP-NADH kinase isozymes and their contribution to supply of NADP(H) in Saccharomyces cerevisiae. FEBS J 2005, 272: 3337-3349. (Pubitemid 40979306)
    • (2005) FEBS Journal , vol.272 , Issue.13 , pp. 3337-3349
    • Shi, F.1    Kawai, S.2    Mori, S.3    Kono, E.4    Murata, K.5
  • 9
    • 33646723659 scopus 로고    scopus 로고
    • Partial rescue of pos5 mutants by YEF1 and UTR1 genes in Saccharomyces cerevisiae
    • DOI 10.1111/j.1745-7270.2006.00162.x
    • Li YF and Shi F. Partial rescue of pos5 mutants by YEF1 and UTR1 genes in Saccharomyces cerevisiae. Acta Biochim Biophys Sin 2006, 38: 293-298. (Pubitemid 43752320)
    • (2006) Acta Biochimica et Biophysica Sinica , vol.38 , Issue.5 , pp. 293-298
    • Li, Y.-F.1    Shi, F.2
  • 10
    • 3543001681 scopus 로고    scopus 로고
    • Cloning and characterization of two NAD kinases from arabidopsis. Identification of a calmodulin binding isoform
    • DOI 10.1104/pp.104.040428
    • Turner WL, Waller JC, Vanderbeld B and Snedden WA. Cloning and characterization of two NAD kinases from Arabidopsis. Identification of a calmodulin binding isoform. Plant Physiol 2004, 135: 1243-1255. (Pubitemid 39009374)
    • (2004) Plant Physiology , vol.135 , Issue.3 , pp. 1243-1255
    • Turner, W.L.1    Waller, J.C.2    Vanderbeld, B.3    Snedden, W.A.4
  • 11
    • 27144540627 scopus 로고    scopus 로고
    • NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection
    • DOI 10.1007/s11103-005-6802-y
    • Chai MF, Chen QJ, An R, Chen YM, Chen J and Wang XC. NADK2, an Arabidopsis chloroplastic NAD kinase, plays a vital role in both chlorophyll synthesis and chloroplast protection. Plant Mol Biol 2005, 59: 553-564. (Pubitemid 41487108)
    • (2005) Plant Molecular Biology , vol.59 , Issue.4 , pp. 553-564
    • Chai, M.-F.1    Chen, Q.-J.2    An, R.3    Chen, Y.-M.4    Chen, J.5    Wang, X.-C.6
  • 12
    • 43549127287 scopus 로고    scopus 로고
    • Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H)
    • Kawai S and Murata K. Structure and function of NAD kinase and NADP phosphatase: key enzymes that regulate the intracellular balance of NAD(H) and NADP(H). Biosci Biotechnol Biochem 2008, 72: 919-930.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 919-930
    • Kawai, S.1    Murata, K.2
  • 13
    • 0039314162 scopus 로고
    • Enzymatic synthesis of triphosphopyridine nucleotide
    • Kornberg A. Enzymatic synthesis of triphosphopyridine nucleotide. J Biol Chem 1950, 182: 805-813.
    • (1950) J Biol Chem , vol.182 , pp. 805-813
    • Kornberg, A.1
  • 15
    • 33745854833 scopus 로고    scopus 로고
    • Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis
    • DOI 10.2174/138955706777698688
    • Magni G, Orsomando G and Raffaelli N. Structural and functional properties of NAD kinase, a key enzyme in NADP biosynthesis. Mini Rev Med Chem 2006, 6: 739-746. (Pubitemid 44027726)
    • (2006) Mini-Reviews in Medicinal Chemistry , vol.6 , Issue.7 , pp. 739-746
    • Magni, G.1    Orsomando, G.2    Raffaelli, N.3
  • 16
    • 0001877450 scopus 로고
    • Metaphosphate: a new phosphoryl donor for NAD phosphorylation
    • Murata K, Uchida T, Tani K, Kato J and Chibata I. Metaphosphate: a new phosphoryl donor for NAD phosphorylation. Agric Biol Chem 1980, 44: 61-68.
    • (1980) Agric Biol Chem , vol.44 , pp. 61-68
    • Murata, K.1    Uchida, T.2    Tani, K.3    Kato, J.4    Chibata, I.5
  • 17
    • 0042060978 scopus 로고    scopus 로고
    • Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid
    • DOI 10.1128/JB.185.16.4844-4850.2003
    • Garavaglia S, Galizzi A and Rizzi M. Allosteric regulation of Bacillus subtilis NAD kinase by quinolinic acid. J Bacteriol 2003, 185: 4844-4850. (Pubitemid 36962292)
    • (2003) Journal of Bacteriology , vol.185 , Issue.16 , pp. 4844-4850
    • Garavaglia, S.1    Galizzi, A.2    Rizzi, M.3
  • 18
    • 28244443305 scopus 로고    scopus 로고
    • MJ0917 in archaeon Methanococcus jannaschii is a novel NADP phosphatase/NAD kinase
    • DOI 10.1074/jbc.M506426200
    • Kawai S, Fukada C, Mukai T and Murata K. MJ0917 in archaeon Methanococcus jannaschii is a novel NADP phosphatase/NAD kinase. J Biol Chem 2005, 280: 39200-39207. (Pubitemid 41713872)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39200-39207
    • Kawai, S.1    Fukuda, C.2    Mukai, T.3    Murata, K.4
  • 19
    • 23744455573 scopus 로고    scopus 로고
    • First archaeal inorganic polyphosphate/ATP-dependent NAD kinase, from hyperthermophilic archaeon Pyrococcus horikoshii: Cloning, expression, and characterization
    • DOI 10.1128/AEM.71.8.4352-4358.2005
    • Sakuraba H, Kawakami R and Ohshima T. First archaeal inorganic polyphosphate/ ATP-dependent NAD kinase, from hyperthermophilic archaeon Pyrococcus horikoshii: cloning, expression, and characterization. Appl Environ Microbiol 2005, 71: 4352-4358. (Pubitemid 41129487)
    • (2005) Applied and Environmental Microbiology , vol.71 , Issue.8 , pp. 4352-4358
    • Sakuraba, H.1    Kawakami, R.2    Ohshima, T.3
  • 20
  • 21
    • 3042646688 scopus 로고    scopus 로고
    • Overexpression, purification, and characterization of ATP-NAD kinase of Sphingomonas sp. A1
    • DOI 10.1016/j.pep.2004.03.012, PII S1046592804001111
    • Ochiai A, Mori S, Kawai S and Murata K. Overexpression, purification, and characterization of ATP-NAD kinase of Sphingomonas sp. A1. Protein Expr Purif 2004, 36: 124-130. (Pubitemid 38836772)
    • (2004) Protein Expression and Purification , vol.36 , Issue.1 , pp. 124-130
    • Ochiai, A.1    Mori, S.2    Kawai, S.3    Murata, K.4
  • 22
    • 0035948228 scopus 로고    scopus 로고
    • Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase
    • DOI 10.1016/S0378-1097(01)00215-4, PII S0378109701002154
    • Kawai S, Mori S, Suzuki S and Murata K. Molecular cloning and identification of UTR1 of a yeast Saccharomyces cerevisiae as a gene encoding an NAD kinase. FEMS Microbiol Lett 2001, 200: 181-184. (Pubitemid 32566359)
    • (2001) FEMS Microbiology Letters , vol.200 , Issue.2 , pp. 181-184
    • Kawai, S.1    Suzuki, S.2    Mori, S.3    Murata, K.4
  • 23
    • 0037881908 scopus 로고    scopus 로고
    • A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae
    • DOI 10.1093/emboj/cdg211
    • Outten CE and Culotta VC. A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae. EMBO J 2003, 22: 2015-2024. (Pubitemid 36565527)
    • (2003) EMBO Journal , vol.22 , Issue.9 , pp. 2015-2024
    • Outten, C.E.1    Culotta, V.C.2
  • 25
    • 0032836258 scopus 로고    scopus 로고
    • Inorganic polyphosphate: A molecule of many functions
    • DOI 10.1146/annurev.biochem.68.1.89
    • Kornberg A, Rao NN and Ault-Riche D. Inorganic polyphosphate: molecule ofmany functions. Annu Rev Biochem 1999, 68: 89-125. (Pubitemid 29449188)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 89-125
    • Kornberg, A.1    Rao, N.N.2    Ault-Riche, D.3
  • 26
    • 0035667482 scopus 로고    scopus 로고
    • Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase
    • DOI 10.1016/S1389-1723(01)80294-2
    • Kawai S, Mori S, Mukai T, Matsukawa H, Matuo Y and Murata K. Establishment of a mass-production system for NADP using bacterial inorganic polyphosphate/ATP-NAD kinase. J Biosci Bioeng 2001, 92: 447-452. (Pubitemid 34016989)
    • (2001) Journal of Bioscience and Bioengineering , vol.92 , Issue.5 , pp. 447-452
    • Kawai, S.1    Mori, S.2    Mukai, T.3    Matsukawa, H.4    Matuo, Y.5    Murata, K.6
  • 27
    • 21244467584 scopus 로고    scopus 로고
    • Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution
    • DOI 10.1074/jbc.M502518200
    • Mori S, Kawai S, Shi F, Mikami B and Murata K. Molecular conversion of NAD kinase to NADH kinase through single amino acid residue substitution. J Biol Chem 2005, 280: 24104-24112. (Pubitemid 40884898)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 24104-24112
    • Mori, S.1    Kawai, S.2    Shi, F.3    Mikami, B.4    Murata, K.5
  • 28
    • 0023129316 scopus 로고
    • Negative modulation of Escherichia coli NAD kinase by NADPH and NADH
    • Zerez CR, Moul DE, Gomez EG, Lopez VM and Andreoli AJ. Negative modulation of Escherichia coli NAD kinase by NADPH and NADH. J Bacteriol 1987, 169: 184-188. (Pubitemid 17228706)
    • (1987) Journal of Bacteriology , vol.169 , Issue.1 , pp. 184-188
    • Zerez, C.R.1    Moul, D.E.2    Gomez, E.G.3
  • 29
    • 0022511813 scopus 로고
    • NAD kinase from Bacillus licheniformis: Inhibition by NADP and other properties
    • Zerez CR, Moul DE and Andreoli AJ. NAD kinase from Bacillus liche- niformis: inhibition by NADP and other properties. Arch Microbiol 1986, 144: 313-316. (Pubitemid 16074942)
    • (1986) Archives of Microbiology , vol.144 , Issue.4 , pp. 313-316
    • Zerez, C.R.1    Moul, D.E.2    Andreoli, A.J.3
  • 30
    • 2942563978 scopus 로고    scopus 로고
    • Characterization of Mycobacterium tuberculosis NAD kinase: Functional analysis of the full-length enzyme by site-directed mutagenesis
    • DOI 10.1021/bi049650w
    • Raffaelli N, Finaurini L, Mazzola F, Pucci L, Sorci L, Amici A and Magni G. Characterization of Mycobacterium tuberculosis NAD kinase: functional analysis of the full-length enzyme by site-directed mutagen- esis. Biochemistry 2004, 43: 7610-7617. (Pubitemid 38745777)
    • (2004) Biochemistry , vol.43 , Issue.23 , pp. 7610-7617
    • Raffaelli, N.1    Finaurini, L.2    Mazzola, F.3    Pucci, L.4    Sorci, L.5    Amici, A.6    Magni, G.7
  • 31
    • 4644277321 scopus 로고    scopus 로고
    • A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allosteric enzyme in NADP biosynthesis
    • DOI 10.1074/jbc.M406586200
    • Garavaglia S, Raffaelli N, Finaurini L, Magni G and Rizzi M. A novel fold revealed by Mycobacterium tuberculosis NAD kinase, a key allo- steric enzyme in NADP biosynthesis. J Biol Chem 2004, 279: 40980-40986. (Pubitemid 39287698)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.39 , pp. 40980-40986
    • Garavaglia, S.1    Raffaelli, N.2    Finaurini, L.3    Magni, G.4    Rizzi, M.5
  • 32
    • 0020469659 scopus 로고
    • + kinase: Purification, properties and affinity gel studies
    • DOI 10.1016/0020-711X(82)90106-9
    • Bulter JR and McGuinness ET. Candida utilis NAD+ kinase: purification, properties and affinity gel studies. Int J Biochem 1982, 14: 839-844. (Pubitemid 13232870)
    • (1982) International Journal of Biochemistry , vol.14 , Issue.9 , pp. 839-844
    • Butler, J.R.1    McGuinness, E.T.2
  • 33
    • 0016788478 scopus 로고
    • Pigeon-liver NAD kinase. The structural and kinetic basis of regulation of NADPH
    • Apps DK. Pigeon-liver NAD kinase. The structural and kinetic basis of regulation of NADPH. Eur J Biochem 1975, 55: 475-483.
    • (1975) Eur J Biochem , vol.55 , pp. 475-483
    • Apps, D.K.1
  • 34
    • 2442588994 scopus 로고    scopus 로고
    • Primary structure of inorganic polyphosphate/ATP-NAD kinase from Micrococcus flavus, and occurrence of substrate inorganic polyphosphate for the enzyme
    • Kawai S, Mori S and Murata K. Primary structure of inorganic poly- phosphate/ATP-NAD kinase from Micrococcus flavus, and occurrence of substrate inorganic polyphosphate for the enzyme. Biosci Biotechnol Biochem 2003, 67: 1751-1760. (Pubitemid 39251758)
    • (2003) Bioscience, Biotechnology and Biochemistry , vol.67 , Issue.8 , pp. 1751-1760
    • Kawai, S.1    Mori, S.2    Murata, K.3
  • 35
    • 0036607768 scopus 로고    scopus 로고
    • Diacylglyceride kinases, sphingosine kinases and NAD kinases: Distant relatives of 6-phosphofructokinases
    • DOI 10.1016/S0968-0004(02)02093-5, PII S0968000402020935
    • Labesse G, Douguet D, Assairi L and Gilles AM. Diacylglyceride kinases, sphingosine kinases and NAD kinases: distant relatives of 6- phosphofructokinases. Trends Biochem Sci 2002, 27: 273-275. (Pubitemid 34628662)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.6 , pp. 273-275
    • Labesse, G.1    Douguet, D.2    Assairi, L.3    Gilles, A.-M.4
  • 36
    • 36349024511 scopus 로고    scopus 로고
    • NAD kinases use substrate-assisted catalysis for specific recognition of NAD
    • DOI 10.1074/jbc.M701394200
    • Poncet-Montange G, Assairi L, Arold S, Pochet S and Labesse G. NAD kinases use substrate-assisted catalysis for specific recognition of NAD. J Biol Chem 2007, 282: 33925-33934. (Pubitemid 350159448)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.47 , pp. 33925-33934
    • Poncet-Montange, G.1    Assairi, L.2    Arold, S.3    Pochet, S.4    Labesse, G.5
  • 37
    • 11144251556 scopus 로고    scopus 로고
    • NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex
    • DOI 10.1016/j.bbrc.2004.11.163, PII S0006291X04027263
    • Mori S, Yamasaki M, Maruyama Y, Momma K, Kawai S, Hashimoto W and Mikami B, et al. NAD-binding mode and the significance of intersubunit contact revealed by the crystal structure of Mycobacterium tuberculosis NAD kinase-NAD complex. Biochem Biophys Res Commun 2005, 327: 500-508. (Pubitemid 40040503)
    • (2005) Biochemical and Biophysical Research Communications , vol.327 , Issue.2 , pp. 500-508
    • Mori, S.1    Yamasaki, M.2    Maruyama, Y.3    Momma, K.4    Kawai, S.5    Hashimoto, W.6    Mikami, B.7    Murata, K.8
  • 39
    • 27644457115 scopus 로고    scopus 로고
    • Crystal structures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP
    • DOI 10.1016/j.jmb.2005.09.026, PII S0022283605010910
    • Liu J, Lou Y, Yokota H, Adams PD, Kim R and Kim SH. Crystalstructures of an NAD kinase from Archaeoglobus fulgidus in complex with ATP, NAD, or NADP. J Mol Biol 2005, 354: 289-303. (Pubitemid 41579847)
    • (2005) Journal of Molecular Biology , vol.354 , Issue.2 , pp. 289-303
    • Liu, J.1    Lou, Y.2    Yokota, H.3    Adams, P.D.4    Kim, R.5    Kim, S.-H.6
  • 40
    • 0018851537 scopus 로고
    • Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems
    • Foster JW and Moat AG. Nicotinamide adenine dinucleotide biosynthesis and pyridine nucleotide cycle metabolism in microbial systems. Microbiol Rev 1980, 44: 83-105. (Pubitemid 10087652)
    • (1980) Microbiological Reviews , vol.44 , Issue.1 , pp. 83-105
    • Foster, J.W.1    Moat, A.G.2
  • 41
    • 0034023238 scopus 로고    scopus 로고
    • New functions of a long-known molecule: Emerging roles of NAD in cellular signaling
    • DOI 10.1046/j.1432-1327.2000.01187.x
    • Ziegler M. New functions of a long-known molecule. Emerging roles of NAD in cellular signaling. Eur J Biochem 2000, 267: 1550-1564. (Pubitemid 30165506)
    • (2000) European Journal of Biochemistry , vol.267 , Issue.6 , pp. 1550-1564
    • Ziegler, M.1
  • 42
    • 0038028647 scopus 로고    scopus 로고
    • 12 biosynthesis in Salmonella typhimurium
    • DOI 10.1099/mic.0.26040-0
    • Maggio-Hall LA and Escalante-Semerena JC. Alpha-5,6- dimethylbenzimidazole adenine dinucleotide (alpha-DAD), a putative new intermediate of coenzyme B12 biosynthesis in Salmonella typhi- murium. Microbiology 2003, 149: 983-990. (Pubitemid 36553367)
    • (2003) Microbiology , vol.149 , Issue.4 , pp. 983-990
    • Maggio-Hall, L.A.1    Escalante-Semerena, J.C.2
  • 43
    • 0347457075 scopus 로고    scopus 로고
    • Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine
    • DOI 10.1126/science.1077650
    • Starai VJ, Celic I, Cole RN, Boeke JD and Escalante-Semerena JC. Sir2-dependent activation of acetyl-CoA synthetase by deacetylation of active lysine. Science 2002, 298, 2390-2392. (Pubitemid 36014212)
    • (2002) Science , vol.298 , Issue.5602 , pp. 2390-2392
    • Starai, V.J.1    Celic, I.2    Cole, R.N.3    Boeke, J.D.4    Escalante-Semerena, J.C.5
  • 44
    • 27744558510 scopus 로고    scopus 로고
    • Sources of NADPH in yeast vary with carbon source
    • DOI 10.1074/jbc.M509461200
    • Minard KI and McAlister-Henn L. Sources of NADPH in yeast vary with carbon source. J Biol Chem 2005, 280: 39890-39896. (Pubitemid 41779123)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.48 , pp. 39890-39896
    • Minard, K.I.1    McAlister-Henn, L.2
  • 46
    • 33847711060 scopus 로고    scopus 로고
    • The power to reduce: Pyridine nucleotides - Small molecules with a multitude of functions
    • DOI 10.1042/BJ20061638
    • Pollak N, Dolle C and Ziegler M. The power to reduce: pyridine nucleotides -small molecules with a multitude of functions. Biochem J 2007, 402, 205-218. (Pubitemid 46383418)
    • (2007) Biochemical Journal , vol.402 , Issue.2 , pp. 205-218
    • Pollak, N.1    Dolle, C.2    Ziegler, M.3
  • 47
    • 1342325419 scopus 로고    scopus 로고
    • The Soluble and Membrane-bound Transhydrogenases UdhA and PntAB Have Divergent Functions in NADPH Metabolism of Escherichia coli
    • DOI 10.1074/jbc.M311657200
    • Sauer U, Canonaco F, Heri S, Perrenoud A and Fischer E. The soluble and membrane-bound transhydrogenases UdhA and PntAB have divergent functions in NADPH metabolism of Escherichia coli. J Biol Chem 2004, 279: 6613-6619. (Pubitemid 38248798)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.8 , pp. 6613-6619
    • Sauer, U.1    Canonaco, F.2    Heri, S.3    Perrenoud, A.4    Fischer, E.5
  • 48
    • 37549068090 scopus 로고    scopus 로고
    • +/ NADPH in cellular functions and cell death: regulation and biological consequences
    • Ying W. NAD+/NADH and NADP+/NADPH in cellular functions and cell death: regulation and biological consequences. Antioxid Redox Signal 2008, 10: 179-206.
    • (2008) Antioxid Redox Signal , vol.10 , pp. 179-206
    • Ying, W.1
  • 50
    • 49949085210 scopus 로고    scopus 로고
    • A novel strategy involved anti-oxidative defense: the conversion of NADH into NADPH by a metabolic network
    • Singh R, Lemire J, Mailloux RJ and Appanna VD. A novel strategy involved anti-oxidative defense: the conversion of NADH into NADPH by a metabolic network. PLoS ONE 2008, 3: e2682: 1-7.
    • (2008) PLoS ONE , vol.3 , pp. 1-7
    • Singh, R.1    Lemire, J.2    Mailloux, R.J.3    Appanna, V.D.4
  • 51
    • 34548563918 scopus 로고    scopus 로고
    • Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens
    • DOI 10.1128/JB.00555-07
    • Singh R, Mailloux RJ, Puiseux-Dao S and Appanna VD. Oxidative stress evokes a metabolic adaptation that favors increased NADPH synthesis and decreased NADH production in Pseudomonas fluorescens. J Bacteriol 2007, 189: 6665-6675. (Pubitemid 47397373)
    • (2007) Journal of Bacteriology , vol.189 , Issue.18 , pp. 6665-6675
    • Singh, R.1    Mailloux, R.J.2    Puiseux-Dao, S.3    Appanna, V.D.4
  • 52
    • 54049133332 scopus 로고    scopus 로고
    • Metabolic adaptation and oxaloacetate homeostasis in P. fluorescens exposed to aluminum toxicity
    • Lemire J, Kumar P, Mailloux RJ, Cossar K and Appanna VD. Metabolic adaptation and oxaloacetate homeostasis in P. fluorescens exposed to aluminum toxicity. J Basic Microbiol 2008, 48: 252-259.
    • (2008) J Basic Microbiol , vol.48 , pp. 252-259
    • Lemire, J.1    Kumar, P.2    Mailloux, R.J.3    Cossar, K.4    Appanna, V.D.5
  • 53
    • 34548485039 scopus 로고    scopus 로고
    • NADP(H) phosphatase activities of archaeal inositol monophosphatase and eubacterial 3′-phosphoadenosine 5′-phosphate phosphatase
    • DOI 10.1128/AEM.02703-06
    • Fukuda C, Kawai S and Murata K. NADP(H) phosphatase activities of archaeal inositol monophosphatase and eubacterial 3′-phosphoadenosine 5′-phosphate phosphatase. Appl Environ Microbiol 2007, 73: 5447-5452. (Pubitemid 47378747)
    • (2007) Applied and Environmental Microbiology , vol.73 , Issue.17 , pp. 5447-5452
    • Fukuda, C.1    Kawai, S.2    Murata, K.3
  • 54
    • 0031877248 scopus 로고    scopus 로고
    • Cofactor engineering: A novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase
    • De Felipe FL, Kleerebezem M, De Vos WM and Hugenholtz J. Cofactor engineering: a novel approach to metabolic engineering in Lactococcus lactis by controlled expression of NADH oxidase. J Bacteriol 1998, 180: 3804-3808. (Pubitemid 28361574)
    • (1998) Journal of Bacteriology , vol.180 , Issue.15 , pp. 3804-3808
    • De Felipe, F.L.1    Kleerebezem, M.2    De Vos, W.M.3    Hugenholtz, J.4
  • 55
    • 0043234233 scopus 로고    scopus 로고
    • POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA
    • DOI 10.1128/EC.2.4.809-820.2003
    • Strand MK, Stuart GR, Longley MJ, Graziewicz MA, Dominick OC and Copeland WC. POS5 gene of Saccharomyces cerevisiae encodes a mitochondrial NADH kinase required for stability of mitochondrial DNA. Eukaryot Cell 2003, 2: 809-820. (Pubitemid 36996726)
    • (2003) Eukaryotic Cell , vol.2 , Issue.4 , pp. 809-820
    • Strand, M.K.1    Stuart, G.R.2    Longley, M.J.3    Graziewicz, M.A.4    Dominick, O.C.5    Copeland, W.C.6
  • 56
    • 36348971843 scopus 로고    scopus 로고
    • NAD kinase levels control the NADPH concentration in human cells
    • DOI 10.1074/jbc.M704442200
    • Pollak N, Niere M and Ziegler M. NAD kinase levels control the NADPH concentration in human cells. J Biol Chem 2007, 282:33562-33571. (Pubitemid 350159523)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33562-33571
    • Pollak, N.1    Niere, M.2    Ziegler, M.3
  • 57
    • 0035862752 scopus 로고    scopus 로고
    • + kinase in the rat conceptus
    • DOI 10.1006/taap.2000.9093
    • Akella SS and Harris C. Developmental ontogeny of NAD kinase in the rat conceptus. Toxicol Appl Pharmacol 2001, 170: 124-129. (Pubitemid 32108687)
    • (2001) Toxicology and Applied Pharmacology , vol.170 , Issue.2 , pp. 124-129
    • Akella, S.S.1    Harris, C.2
  • 58
    • 1542319976 scopus 로고    scopus 로고
    • Alternative Start Sites in the Saccharomyces cerevisiae GLR1 Gene Are Responsible for Mitochondrial and Cytosolic Isoforms of Glutathione Reductase
    • DOI 10.1074/jbc.M312421200
    • Outten CE and Culotta VC. Alternative start sites in the Saccharomyces cerevisiae GLR1 gene are responsible for mitochondrial and cytosolic isoforms of glutathione reductase. J Biol Chem 2004, 279: 7785-7791. (Pubitemid 38294662)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7785-7791
    • Outten, C.E.1    Culotta, V.C.2
  • 59
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the fenton reaction in vivo and in vitro
    • Imlay JA and Linn S. Toxic DNA damage by hydrogen peroxide through Fenton reaction in vivo and in vitro. Science 1988, 240: 640-642. (Pubitemid 18123978)
    • (1988) Science , vol.240 , Issue.4852 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 60
    • 37549005208 scopus 로고    scopus 로고
    • Detection of reactive oxygen species via endogenous oxi- dative pentose phosphate cycle activity in response to oxygen concentration: implications for the mechanism of HIF-1alpha stabilization under moderate hypoxia
    • Tuttle SW, Maity A, Oprysko PR, Kachur AV, Ayene IS, Biaglow JE and Koch CJ. Detection of reactive oxygen species via endogenous oxi- dative pentose phosphate cycle activity in response to oxygen concentration: implications for the mechanism of HIF-1alpha stabilization under moderate hypoxia. J Biol Chem 2007, 282: 36790-36796.
    • (2007) J Biol Chem , vol.282 , pp. 36790-36796
    • Tuttle, S.W.1    Maity, A.2    Oprysko, P.R.3    Kachur, A.V.4    Ayene, I.S.5    Biaglow, J.E.6    Koch, C.J.7
  • 61
    • 0019433376 scopus 로고
    • Calmodulin activates NAD kinase of sea urchin eggs: An early event of fertilization
    • Epel D, Patton C, Wallace RW and Cheung WY. Calmodulin activates NAD kinase of sea urchin eggs: an early event of fertilization. Cell 1981, 23: 543-549. (Pubitemid 11096348)
    • (1981) Cell , vol.23 , Issue.2 , pp. 543-549
    • Epel, D.1    Patton, C.2    Wallace, R.W.3    Cheung, W.Y.4
  • 62
    • 0021987751 scopus 로고
    • Calmodulin-dependent NAD kinase of human neutrophils
    • DOI 10.1016/0003-9861(85)90256-5
    • Williams MB and Jones HP. Calmodulin-dependent NAD kinase of human neutrophils. Arch Biochem Biophys 1985, 237: 80-87. (Pubitemid 15111999)
    • (1985) Archives of Biochemistry and Biophysics , vol.237 , Issue.1 , pp. 80-87
    • Williams, M.B.1    Jones, J.P.2
  • 65
    • 0030907241 scopus 로고    scopus 로고
    • Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species
    • DOI 10.1093/emboj/16.6.1137
    • Harding SA, Oh SH and Roberts DM. Transgenic tobacco expressing a foreign calmodulin gene shows an enhanced production of active oxygen species. EMBO J 1997, 16: 1137-1144. (Pubitemid 27136080)
    • (1997) EMBO Journal , vol.16 , Issue.6 , pp. 1137-1144
    • Harding, S.A.1    Oh, S.-H.2    Roberts, D.M.3
  • 67
    • 0037017447 scopus 로고    scopus 로고
    • Proline metabolism and NAD kinase activity in greenbean plants subjected to cold-shock
    • DOI 10.1016/S0031-9422(01)00481-2, PII S0031942201004812
    • Ruiz JM, Sanchez E, Garcia PC, Lcipez-Lefebre LR, Rivero RM and Romero L. Proline metabolism and NAD kinase activity in green bean plants subjected to cold-shock. Phytochemistry 2002, 59: 473-478. (Pubitemid 34205245)
    • (2002) Phytochemistry , vol.59 , Issue.5 , pp. 473-478
    • Kanchanapoom, T.1    Kasai, R.2    Yamasaki, K.3
  • 70
    • 0037100683 scopus 로고    scopus 로고
    • Identification of 113 conserved essential genes using a high- throughput gene disruption system in streptococcus pneumoniae
    • Thanassi JA, Hartman-Neumann SL, Dougherty TJ, Dougherty BA and Pucci MJ. Identification of 113 conserved essential genes using a high- throughput gene disruption system in Streptococcus pneumoniae. Nucleic Acids Res 2002, 30: 3152-3162.
    • (2002) Nucleic Acids Res , vol.30 , pp. 3152-3162
    • Thanassi, J.A.1    Hartman-Neumann, S.L.2    Dougherty, T.J.3    Dougherty, B.A.4    Pucci, M.J.5
  • 72
    • 0036334571 scopus 로고    scopus 로고
    • From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways
    • Gerdes SY, Scholle MD, D'souza M, Bernal A, Baev MV, Farrell M and Kurnasov OV, et al. From genetic footprinting to antimicrobial drug targets: examples in cofactor biosynthetic pathways. J Bacteriol 2002, 184: 4555-4572.
    • (2002) J Bacteriol , vol.184 , pp. 4555-4572
    • Gerdes, S.Y.1    Scholle, M.D.2    D'souza, M.3    Bernal, A.4    Baev, M.V.5    Farrell, M.6    Kurnasov, O.V.7


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