메뉴 건너뛰기




Volumn 290, Issue 11, 2015, Pages 6705-6713

Quantitative analysis of purine nucleotides indicates that purinosomes increase de Novo purine biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CYTOLOGY; ENZYMES; MOBILE SECURITY; NUCLEOTIDES;

EID: 84924943411     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.628701     Document Type: Article
Times cited : (92)

References (37)
  • 1
    • 0018265594 scopus 로고
    • De novo purine synthesis in avian liver: Co-purification of the enzymes and properties of the pathway
    • Rowe, P. B., McCairns, E., Madsen, G., Sauer, D., and Elliott, H. (1978) De novo purine synthesis in avian liver: co-purification of the enzymes and properties of the pathway. J. Biol. Chem. 253, 7711-7721
    • (1978) J. Biol. Chem. , vol.253 , pp. 7711-7721
    • Rowe, P.B.1    McCairns, E.2    Madsen, G.3    Sauer, D.4    Elliott, H.5
  • 2
    • 0014430403 scopus 로고
    • Glutamine phosphoribosylpyrophosphate amidotransferase: Purification, substructure, amino acid composition, and absorption spectra
    • Rowe, P. B., and Wyngaarden, J. B. (1968) Glutamine phosphoribosylpyrophosphate amidotransferase: purification, substructure, amino acid composition, and absorption spectra. J. Biol. Chem. 243, 6373-6383
    • (1968) J. Biol. Chem. , vol.243 , pp. 6373-6383
    • Rowe, P.B.1    Wyngaarden, J.B.2
  • 3
    • 0019315396 scopus 로고
    • Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis
    • Smith, G. K., Mueller, W. T., Wasserman, G. F., Taylor, W. D., and Benkovic, S. J. (1980) Characterization of the enzyme complex involving the folate-requiring enzymes of de novo purine biosynthesis. Biochemistry 19, 4313-4321
    • (1980) Biochemistry , vol.19 , pp. 4313-4321
    • Smith, G.K.1    Mueller, W.T.2    Wasserman, G.F.3    Taylor, W.D.4    Benkovic, S.J.5
  • 4
    • 0020983052 scopus 로고
    • Molecular compartmentation by enzyme cluster formation: A view over current investigations
    • Wombacher, H. (1983) Molecular compartmentation by enzyme cluster formation: a view over current investigations. Mol. Cell. Biochem. 56, 155-164
    • (1983) Mol. Cell. Biochem. , vol.56 , pp. 155-164
    • Wombacher, H.1
  • 5
    • 0023061429 scopus 로고
    • Complexes of sequential metabolic enzymes
    • Srere, P. A. (1987) Complexes of sequential metabolic enzymes. Annu. Rev. Biochem. 56, 89-124
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 89-124
    • Srere, P.A.1
  • 6
    • 0025895417 scopus 로고
    • Physiological significance of metabolic channelling
    • Ovádi, J. (1991) Physiological significance of metabolic channelling. J. Theor. Biol. 152, 1-22
    • (1991) J. Theor. Biol. , vol.152 , pp. 1-22
    • Ovádi, J.1
  • 7
    • 0027366579 scopus 로고
    • The cell: Bag of enzymes or network of channels?
    • Mathews, C. K. (1993) The cell: bag of enzymes or network of channels? J. Bacteriol. 175, 6377-6381
    • (1993) J. Bacteriol. , vol.175 , pp. 6377-6381
    • Mathews, C.K.1
  • 8
    • 0347330758 scopus 로고
    • An immobilized three-enzyme system: A model for microenvironmental compartmentation in mitochondria
    • Srere, P. A., Mattiasson, B., and Mosbach, K. (1973) An immobilized three-enzyme system: a model for microenvironmental compartmentation in mitochondria. Proc. Natl. Acad. Sci. U.S.A. 70, 2534-2538
    • (1973) Proc. Natl. Acad. Sci. U.S.A. , vol.70 , pp. 2534-2538
    • Srere, P.A.1    Mattiasson, B.2    Mosbach, K.3
  • 9
    • 0020842547 scopus 로고
    • Coimmobilized multienzymes: An in vitro model for cellular processes
    • De Luca, M., and Kricka, L. J. (1983) Coimmobilized multienzymes: an in vitro model for cellular processes. Arch. Biochem. Biophys. 226, 285-291
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 285-291
    • De Luca, M.1    Kricka, L.J.2
  • 10
    • 0019196211 scopus 로고
    • Evidence for a membrane-bound multienzyme sequence degrading cyclic adenosine 3′:5′-monophosphate
    • Wombacher, H. (1980) Evidence for a membrane-bound multienzyme sequence degrading cyclic adenosine 3′:5′-monophosphate. Arch. Biochem. Biophys. 201, 8-19
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 8-19
    • Wombacher, H.1
  • 11
    • 41749092312 scopus 로고    scopus 로고
    • Reversible compartmentalization of de novo purine biosynthetic complexes in living cells
    • An, S., Kumar, R., Sheets, E. D., and Benkovic, S. J. (2008) Reversible compartmentalization of de novo purine biosynthetic complexes in living cells. Science 320, 103-106
    • (2008) Science , vol.320 , pp. 103-106
    • An, S.1    Kumar, R.2    Sheets, E.D.3    Benkovic, S.J.4
  • 12
    • 77951236102 scopus 로고    scopus 로고
    • Dynamic regulation of a metabolic multi-enzyme complex by protein kinase CK2
    • An, S., Kyoung, M., Allen, J. J., Shokat, K. M., and Benkovic, S. J. (2010) Dynamic regulation of a metabolic multi-enzyme complex by protein kinase CK2. J. Biol. Chem. 285, 11093-11099
    • (2010) J. Biol. Chem. , vol.285 , pp. 11093-11099
    • An, S.1    Kyoung, M.2    Allen, J.J.3    Shokat, K.M.4    Benkovic, S.J.5
  • 13
    • 77955593994 scopus 로고    scopus 로고
    • Microtubule-assisted mechanism for functional metabolic macromolecular complex formation
    • An, S., Deng, Y., Tomsho, J. W., Kyoung, M., and Benkovic, S. J. (2010) Microtubule-assisted mechanism for functional metabolic macromolecular complex formation. Proc. Natl. Acad. Sci. U.S.A. 107, 12872-12876
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 12872-12876
    • An, S.1    Deng, Y.2    Tomsho, J.W.3    Kyoung, M.4    Benkovic, S.J.5
  • 17
    • 48049092827 scopus 로고    scopus 로고
    • Quantitative profiling of nucleotides and related phosphate-containing metabolites in cultured mammalian cells by liquid chromatography tandem electrospray mass spectrometry
    • Cordell, R. L., Hill, S. J., Ortori, C. A., and Barrett, D. A. (2008) Quantitative profiling of nucleotides and related phosphate-containing metabolites in cultured mammalian cells by liquid chromatography tandem electrospray mass spectrometry. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 871, 115-124
    • (2008) J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. , vol.871 , pp. 115-124
    • Cordell, R.L.1    Hill, S.J.2    Ortori, C.A.3    Barrett, D.A.4
  • 18
    • 0030859943 scopus 로고    scopus 로고
    • Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis
    • Yamaoka, T., Kondo, M., Honda, S., Iwahana, H., Moritani, M., Ii, S., Yoshimoto, K., and Itakura, M. (1997) Amidophosphoribosyltransferase limits the rate of cell growth-linked de novo purine biosynthesis in the presence of constant capacity of salvage purine biosynthesis. J. Biol. Chem. 272, 17719-17725
    • (1997) J. Biol. Chem. , vol.272 , pp. 17719-17725
    • Yamaoka, T.1    Kondo, M.2    Honda, S.3    Iwahana, H.4    Moritani, M.5    Ii, S.6    Yoshimoto, K.7    Itakura, M.8
  • 19
    • 0035877810 scopus 로고    scopus 로고
    • Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses
    • Yamaoka, T., Yano, M., Kondo, M., Sasaki, H., Hino, S., Katashima, R., Moritani, M., and Itakura, M. (2001) Feedback inhibition of amidophosphoribosyltransferase regulates the rate of cell growth via purine nucleotide, DNA, and protein syntheses. J. Biol. Chem. 276, 21285-21291
    • (2001) J. Biol. Chem. , vol.276 , pp. 21285-21291
    • Yamaoka, T.1    Yano, M.2    Kondo, M.3    Sasaki, H.4    Hino, S.5    Katashima, R.6    Moritani, M.7    Itakura, M.8
  • 20
    • 77954086132 scopus 로고    scopus 로고
    • Development and optimization of a metabolomic method for analysis of adherent cell cultures
    • Danielsson, A. P., Moritz, T., Mulder, H., and Spégel, P. (2010) Development and optimization of a metabolomic method for analysis of adherent cell cultures. Anal. Biochem. 404, 30-39
    • (2010) Anal. Biochem. , vol.404 , pp. 30-39
    • Danielsson, A.P.1    Moritz, T.2    Mulder, H.3    Spégel, P.4
  • 21
    • 79251624872 scopus 로고    scopus 로고
    • Metabolite extraction from adherently growing mammalian cells for metabolomics studies: Optimization of harvesting and extraction protocols
    • Dettmer, K., Nürnberger, N., Kaspar, H., Gruber, M. A., Almstetter, M. F., and Oefner, P. J. (2011) Metabolite extraction from adherently growing mammalian cells for metabolomics studies: optimization of harvesting and extraction protocols. Anal. Bioanal. Chem. 399, 1127-1139
    • (2011) Anal. Bioanal. Chem. , vol.399 , pp. 1127-1139
    • Dettmer, K.1    Nürnberger, N.2    Kaspar, H.3    Gruber, M.A.4    Almstetter, M.F.5    Oefner, P.J.6
  • 22
    • 77951072181 scopus 로고    scopus 로고
    • Metabolomic analysis via reversed-phase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer
    • Lu, W., Clasquin, M. F., Melamud, E., Amador-Noguez, D., Caudy, A. A., and Rabinowitz, J. D. (2010) Metabolomic analysis via reversed-phase ion-pairing liquid chromatography coupled to a stand alone orbitrap mass spectrometer. Anal. Chem. 82, 3212-3221
    • (2010) Anal. Chem. , vol.82 , pp. 3212-3221
    • Lu, W.1    Clasquin, M.F.2    Melamud, E.3    Amador-Noguez, D.4    Caudy, A.A.5    Rabinowitz, J.D.6
  • 23
    • 0028143584 scopus 로고
    • Physiological concentrations of purines and pyrimidines
    • Traut, T. W. (1994) Physiological concentrations of purines and pyrimidines. Mol. Cell. Biochem. 140, 1-22
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 1-22
    • Traut, T.W.1
  • 24
    • 78649708170 scopus 로고    scopus 로고
    • Nucleotide and nucleotide sugar analysis by liquid chromatography-electrospray ionization-mass spectrometry on surface-conditioned porous graphitic carbon
    • Pabst, M., Grass, J., Fischl, R., Léonard, R., Jin, C., Hinterkörner, G., Borth, N., and Altmann, F. (2010) Nucleotide and nucleotide sugar analysis by liquid chromatography-electrospray ionization-mass spectrometry on surface-conditioned porous graphitic carbon. Anal. Chem. 82, 9782-9788
    • (2010) Anal. Chem. , vol.82 , pp. 9782-9788
    • Pabst, M.1    Grass, J.2    Fischl, R.3    Léonard, R.4    Jin, C.5    Hinterkörner, G.6    Borth, N.7    Altmann, F.8
  • 25
    • 84875391007 scopus 로고    scopus 로고
    • Inosine triphosphate pyrophosphohydrolase (ITPA) polymorphic sequence variants in adult hematological malignancy patients and possible association with mitochondrial DNA defects
    • Zamzami, M. A., Duley, J. A., Price, G. R., Venter, D. J., Yarham, J. W., Taylor, R. W., Catley, L. P., Florin, T. H., Marinaki, A. M., and Bowling, F. (2013) Inosine triphosphate pyrophosphohydrolase (ITPA) polymorphic sequence variants in adult hematological malignancy patients and possible association with mitochondrial DNA defects. J. Hematol. Oncol. 6, 24
    • (2013) J. Hematol. Oncol. , vol.6 , pp. 24
    • Zamzami, M.A.1    Duley, J.A.2    Price, G.R.3    Venter, D.J.4    Yarham, J.W.5    Taylor, R.W.6    Catley, L.P.7    Florin, T.H.8    Marinaki, A.M.9    Bowling, F.10
  • 26
    • 70449546957 scopus 로고
    • The high permeability of human red cells to adenine and hypoxanthine and their ribosides
    • Whittam, R. (1960) The high permeability of human red cells to adenine and hypoxanthine and their ribosides. J. Physiol. 154, 614-623
    • (1960) J. Physiol. , vol.154 , pp. 614-623
    • Whittam, R.1
  • 28
    • 84870949744 scopus 로고    scopus 로고
    • Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms
    • Thomas, E. C., Gunter, J. H., Webster, J. A., Schieber, N. L., Oorschot, V., Parton, R. G., and Whitehead, J. P. (2012) Different characteristics and nucleotide binding properties of inosine monophosphate dehydrogenase (IMPDH) isoforms. PLoS One 7, e51096
    • (2012) PLoS One , vol.7 , pp. e51096
    • Thomas, E.C.1    Gunter, J.H.2    Webster, J.A.3    Schieber, N.L.4    Oorschot, V.5    Parton, R.G.6    Whitehead, J.P.7
  • 29
    • 0022396333 scopus 로고
    • Z-nucleotide accumulation in erythrocytes from Lesch-Nyhan patients
    • Sidi, Y., and Mitchell, B. S. (1985) Z-nucleotide accumulation in erythrocytes from Lesch-Nyhan patients. J. Clin. Invest. 76, 2416-2419
    • (1985) J. Clin. Invest. , vol.76 , pp. 2416-2419
    • Sidi, Y.1    Mitchell, B.S.2
  • 32
    • 14244258689 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells
    • Sun, H., Li, N., Wang, X., Chen, T., Shi, L., Zhang, L., Wang, J., Wan, T., and Cao, X. (2005) Molecular cloning and characterization of a novel muscle adenylosuccinate synthetase, AdSSL1, from human bone marrow stromal cells. Mol. Cell. Biochem. 269, 85-94
    • (2005) Mol. Cell. Biochem. , vol.269 , pp. 85-94
    • Sun, H.1    Li, N.2    Wang, X.3    Chen, T.4    Shi, L.5    Zhang, L.6    Wang, J.7    Wan, T.8    Cao, X.9
  • 33
    • 0016289678 scopus 로고
    • Human adenylosuccinate synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta
    • Van der Weyden, M. B., and Kelly, W. N. (1974) Human adenylosuccinate synthetase. Partial purification, kinetic and regulatory properties of the enzyme from placenta. J. Biol. Chem. 249, 7282-7289
    • (1974) J. Biol. Chem. , vol.249 , pp. 7282-7289
    • Van Der Weyden, M.B.1    Kelly, W.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.