메뉴 건너뛰기




Volumn 5, Issue , 2014, Pages

Non-enzymatic chemistry enables 2-hydroxyglutarate-mediated activation of 2-oxoglutarate oxygenases

Author keywords

[No Author keywords available]

Indexed keywords

2 HYDROXYGLUTARIC ACID; 2 OXOGLUTARIC ACID; ASCORBIC ACID; FERRIC ION; FERROUS GLUCONATE; FERROUS ION; ISOENZYME; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; SUCCINIC ACID; SUCCINIC SEMIALDEHYDE; 4 AMINOBUTYRIC ACID; ALCOHOL DEHYDROGENASE; ALPHA-HYDROXYGLUTARATE; GLUTARIC ACID DERIVATIVE; OXYGENASE;

EID: 84896753329     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms4423     Document Type: Article
Times cited : (66)

References (58)
  • 2
    • 84863324422 scopus 로고    scopus 로고
    • IDH1 and IDH2 have critical roles in 2-hydroxyglutarate production in D-2-hydroxyglutarate dehydrogenase depleted cells
    • Matsunaga, H. et al. IDH1 and IDH2 have critical roles in 2-hydroxyglutarate production in D-2-hydroxyglutarate dehydrogenase depleted cells. Biochem. Biophys. Res. Commun. 423, 553-556 (2012).
    • (2012) Biochem. Biophys. Res. Commun , vol.423 , pp. 553-556
    • Matsunaga, H.1
  • 3
    • 77953702324 scopus 로고    scopus 로고
    • Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
    • Dang, L. et al. Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature 465, 966-966 (2010).
    • (2010) Nature , vol.465 , pp. 966-966
    • Dang, L.1
  • 4
    • 84867562009 scopus 로고    scopus 로고
    • IDH1 and IDH2 mutations in tumorigenesis: Mechanistic insights and clinical perspectives
    • Yang, H., Ye, D., Guan, K.-L. & Xiong, Y. IDH1 and IDH2 mutations in tumorigenesis: mechanistic insights and clinical perspectives. Clin. Cancer Res. 18, 5562-5571 (2012).
    • (2012) Clin. Cancer Res , vol.18 , pp. 5562-5571
    • Yang, H.1    Ye, D.2    Guan, K.-L.3    Xiong, Y.4
  • 5
    • 84865218876 scopus 로고    scopus 로고
    • Molecular pathogenesis of IDH1/2 mutations in gliomas
    • Ichimura, K. Molecular pathogenesis of IDH1/2 mutations in gliomas. Brain Tumor Pathol. 29, 131-139 (2012).
    • (2012) Brain Tumor Pathol , vol.29 , pp. 131-139
    • Ichimura, K.1
  • 6
    • 84875496294 scopus 로고    scopus 로고
    • (R)-2-hydroxyglutarate is sufficient to promote leukemogenesis and its effects are reversible
    • Losman, J.-A. et al. (R)-2-hydroxyglutarate is sufficient to promote leukemogenesis and its effects are reversible. Science 339, 1621-1625 (2013).
    • (2013) Science , vol.339 , pp. 1621-1625
    • Losman, J.-A.1
  • 8
    • 0035313697 scopus 로고    scopus 로고
    • HIF-1 and mechanisms of hypoxia sensing
    • DOI 10.1016/S0955-0674(00)00194-0
    • Semenza, G. L. HIF-1 and mechanisms of hypoxia sensing. Curr. Opin. Cell Biol. 13, 167-171 (2001). (Pubitemid 32209217)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.2 , pp. 167-171
    • Semenza, G.L.1
  • 11
    • 64849098267 scopus 로고    scopus 로고
    • Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1a
    • Zhao, S. et al. Glioma-derived mutations in IDH1 dominantly inhibit IDH1 catalytic activity and induce HIF-1a. Science 324, 261-265 (2009).
    • (2009) Science , vol.324 , pp. 261-265
    • Zhao, S.1
  • 12
    • 84866480031 scopus 로고    scopus 로고
    • D-2-hydroxyglutarate produced by mutant IDH1 perturbs collagen maturation and basement membrane function
    • Sasaki, M. et al. D-2-hydroxyglutarate produced by mutant IDH1 perturbs collagen maturation and basement membrane function. Genes Dev. 26, 2038-2049 (2012).
    • (2012) Genes Dev , vol.26 , pp. 2038-2049
    • Sasaki, M.1
  • 13
    • 79451471184 scopus 로고    scopus 로고
    • R132H-mutation of isocitrate dehydrogenase-1 is not sufficient for HIF-1a upregulation in adult glioma
    • Williams, S. et al. R132H-mutation of isocitrate dehydrogenase-1 is not sufficient for HIF-1a upregulation in adult glioma. Acta Neuropathol. (Berl.) 121, 279-281 (2011).
    • (2011) Acta Neuropathol. (Berl.) , vol.121 , pp. 279-281
    • Williams, S.1
  • 14
    • 79955547561 scopus 로고    scopus 로고
    • The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
    • Chowdhury, R. et al. The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases. EMBO Rep. 12, 463-469 (2011).
    • (2011) EMBO Rep , vol.12 , pp. 463-469
    • Chowdhury, R.1
  • 15
    • 78651463452 scopus 로고    scopus 로고
    • Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of a-ketoglutarate-dependent dioxygenases
    • Xu, W. et al. Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of a-ketoglutarate-dependent dioxygenases. Cancer Cell 19, 17-30 (2011).
    • (2011) Cancer Cell , vol.19 , pp. 17-30
    • Xu, W.1
  • 16
    • 84858796262 scopus 로고    scopus 로고
    • IDH mutation impairs histone demethylation and results in a block to cell differentiation
    • Lu, C. et al. IDH mutation impairs histone demethylation and results in a block to cell differentiation. Nature 483, 474-478 (2012).
    • (2012) Nature , vol.483 , pp. 474-478
    • Lu, C.1
  • 18
    • 0038383678 scopus 로고    scopus 로고
    • Loss of pVHL is sufficient to cause HIF dysregulation in primary cells but does not promote tumor growth
    • Mack, F. A. et al. Loss of pVHL is sufficient to cause HIF dysregulation in primary cells but does not promote tumor growth. Cancer Cell 3, 75-88 (2003).
    • (2003) Cancer Cell , vol.3 , pp. 75-88
    • MacK, F.A.1
  • 19
    • 38349000624 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1a-induced differentiation of myeloid leukemic cells is its transcriptional activity independent
    • Song, L. P. et al. Hypoxia-inducible factor-1a-induced differentiation of myeloid leukemic cells is its transcriptional activity independent. Oncogene 27, 519-527 (2007).
    • (2007) Oncogene , vol.27 , pp. 519-527
    • Song, L.P.1
  • 21
    • 84862776918 scopus 로고    scopus 로고
    • Transformation by the (R)-enantiomer of 2- hydroxyglutarate linked to EGLN activation
    • Koivunen, P. et al. Transformation by the (R)-enantiomer of 2- hydroxyglutarate linked to EGLN activation. Nature 483, 484-488 (2012).
    • (2012) Nature , vol.483 , pp. 484-488
    • Koivunen, P.1
  • 22
    • 0038747011 scopus 로고    scopus 로고
    • The first direct characterization of a high-valent iron intermediate in the reaction of an α-ketoglutarate-dependent dioxygenase: A high-spin Fe(IV) complex in taurine/α-ketoglutarate dioxygenase (TauD) from Escherichia coli
    • DOI 10.1021/bi030011f
    • Price, J. C., Barr, E. W., Tirupati, B., Bollinger, J. M. & Krebs, C. The first direct characterization of a high-valent iron intermediate in the reaction of an a-ketoglutarate-dependent dioxygenase: a high-spin Fe(IV) complex in taurine/a-ketoglutarate dioxygenase (TauD) from Escherichia coli. Biochemistry 42, 7497-7508 (2003). (Pubitemid 36740493)
    • (2003) Biochemistry , vol.42 , Issue.24 , pp. 7497-7508
    • Price, J.C.1    Barr, E.W.2    Tirupati, B.3    Bollinger Jr., J.M.4    Krebs, C.5
  • 23
    • 33645891676 scopus 로고    scopus 로고
    • Structural studies on 2-oxoglutarate oxygenases and related double-stranded b-helix fold proteins
    • Clifton, I. J. et al. Structural studies on 2-oxoglutarate oxygenases and related double-stranded b-helix fold proteins. J. Inorg. Biochem. 100, 644-669 (2006).
    • (2006) J. Inorg. Biochem , vol.100 , pp. 644-669
    • Clifton, I.J.1
  • 25
    • 77956631879 scopus 로고    scopus 로고
    • Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen
    • Flashman, E. et al. Evidence for the slow reaction of hypoxia-inducible factor prolyl hydroxylase 2 with oxygen. FEBS J. 277, 4089-4099 (2010).
    • (2010) FEBS J. , vol.277 , pp. 4089-4099
    • Flashman, E.1
  • 26
    • 0021329173 scopus 로고
    • Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase
    • Myllylä, R., Majamaa, K., Günzler, V., Hanauske-Abel, H. M. & Kivirikko, K. I. Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl-4-hydroxylase and lysyl hydroxylase. J. Biol. Chem. 259, 5403-5405 (1984). (Pubitemid 14144988)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.9 , pp. 5403-5405
    • Myllyla, R.1    Majamaa, K.2    Gunzler, V.3
  • 27
    • 2442628211 scopus 로고    scopus 로고
    • Fe(II)/a-ketoglutarate-dependent hydroxylases and related enzymes
    • Hausinger, R. P. Fe(II)/a-ketoglutarate-dependent hydroxylases and related enzymes. Crit. Rev. Biochem. Mol. Biol. 39, 21-68 (2004).
    • (2004) Crit. Rev. Biochem. Mol. Biol , vol.39 , pp. 21-68
    • Hausinger, R.P.1
  • 28
    • 77950906905 scopus 로고    scopus 로고
    • Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents
    • Flashman, E., Davies, S. L., Yeoh, K. K. & Schofield, C. J. Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents. Biochem. J. 427, 135-142 (2010).
    • (2010) Biochem. J. , vol.427 , pp. 135-142
    • Flashman, E.1    Davies, S.L.2    Yeoh, K.K.3    Schofield, C.J.4
  • 29
    • 33749410367 scopus 로고    scopus 로고
    • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    • DOI 10.1074/jbc.M604628200
    • Koivunen, P., Hirsilä, M., Kivirikko, K. I. & Myllyharju, J. The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases. J. Biol. Chem. 281, 28712-28720 (2006). (Pubitemid 44507013)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28712-28720
    • Koivunen, P.1    Hirsila, M.2    Kivirikko, K.I.3    Myllyharju, J.4
  • 30
    • 84866613772 scopus 로고    scopus 로고
    • Ascorbic acid: Chemistry, biology and the treatment of cancer
    • Du, J., Cullen, J. J. & Buettner, G. R. Ascorbic acid: chemistry, biology and the treatment of cancer. Biochim. Biophys. Acta Rev. Cancer 1826, 443-457 (2012).
    • (2012) Biochim. Biophys. Acta Rev. Cancer , vol.1826 , pp. 443-457
    • Du, J.1    Cullen, J.J.2    Buettner, G.R.3
  • 31
    • 0037733975 scopus 로고    scopus 로고
    • The importance of glutathione in human disease
    • DOI 10.1016/S0753-3322(03)00043-X
    • Townsend, D. M., Tew, K. D. & Tapiero, H. The importance of glutathione in human disease. Biomed. Pharmacother. 57, 145-155 (2003). (Pubitemid 36740460)
    • (2003) Biomedicine and Pharmacotherapy , vol.57 , Issue.3 , pp. 145-155
    • Townsend, D.M.1    Tew, K.D.2    Tapiero, H.3
  • 32
    • 84872782667 scopus 로고    scopus 로고
    • Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors
    • Leung, I. K. H. et al. Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors. J. Med. Chem. 56, 547-555 (2013).
    • (2013) J. Med. Chem , vol.56 , pp. 547-555
    • Leung, I.K.H.1
  • 33
    • 77249083153 scopus 로고    scopus 로고
    • Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions
    • Leung, I. K. H., Flashman, E., Yeoh, K. K., Schofield, C. J. & Claridge, T. D. W. Using NMR solvent water relaxation to investigate metalloenzyme-ligand binding interactions. J. Med. Chem. 53, 867-875 (2010).
    • (2010) J. Med. Chem , vol.53 , pp. 867-875
    • Leung, I.K.H.1    Flashman, E.2    Yeoh, K.K.3    Schofield, C.J.4    Claridge, T.D.W.5
  • 35
    • 84872090623 scopus 로고    scopus 로고
    • Dual-action inhibitors of HIF prolyl hydroxylases that induce binding of a second iron ion
    • Yeoh, K. K. et al. Dual-action inhibitors of HIF prolyl hydroxylases that induce binding of a second iron ion. Org. Biomol. Chem. 11, 732-745 (2013).
    • (2013) Org. Biomol. Chem , vol.11 , pp. 732-745
    • Yeoh, K.K.1
  • 36
    • 84873672891 scopus 로고    scopus 로고
    • Iron speciation in the cytosol: An overview
    • Hider, R. C. & Kong, X. Iron speciation in the cytosol: an overview. Dalton. Trans. 42, 3220-3229 (2013).
    • (2013) Dalton. Trans , vol.42 , pp. 3220-3229
    • Hider, R.C.1    Kong, X.2
  • 37
    • 33845555056 scopus 로고
    • Oxidation of mandelic acid by Fenton's reagent
    • Walling, C. & Amarnath, K. Oxidation of mandelic acid by Fenton's reagent. J. Am. Chem. Soc. 104, 1185-1189 (1982).
    • (1982) J. Am. Chem. Soc , vol.104 , pp. 1185-1189
    • Walling, C.1    Amarnath, K.2
  • 38
    • 0343447278 scopus 로고
    • Spectrophotometric investigation of iron (III) hydrolysis in light and heavy water at 25 °C
    • Knight, R. J. & Sylva, R. N. Spectrophotometric investigation of iron(III) hydrolysis in light and heavy water at 25 °C. J. Inorg. Nucl. Chem. 37, 779-783 (1975).
    • (1975) J. Inorg. Nucl. Chem , vol.37 , pp. 779-783
    • Knight, R.J.1    Sylva, R.N.2
  • 39
    • 84857789085 scopus 로고    scopus 로고
    • The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity
    • Masson, N. et al. The FIH hydroxylase is a cellular peroxide sensor that modulates HIF transcriptional activity. EMBO Rep. 13, 251-257 (2012).
    • (2012) EMBO Rep , vol.13 , pp. 251-257
    • Masson, N.1
  • 40
    • 0029939394 scopus 로고    scopus 로고
    • Catalytic metals, ascorbate and free radicals: Combinations to avoid
    • DOI 10.2307/3579271
    • Buettner, G. R. & Jurkiewicz, B. A. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 145, 532-541 (1996). (Pubitemid 26127160)
    • (1996) Radiation Research , vol.145 , Issue.5 , pp. 532-541
    • Buettner, G.R.1    Jurkiewicz, B.A.2
  • 41
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman, E. R. Oxidation of free amino-acids and amino-acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu. Rev. Biochem. 62, 797-821 (1993). (Pubitemid 23237888)
    • (1993) Annual Review of Biochemistry , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 42
    • 70349918112 scopus 로고    scopus 로고
    • Iron-mediated cleavage of C-C bonds in vicinal tricarbonyl compounds in water
    • Mecinović, J., Hamed, R. B. & Schofield, C. J. Iron-mediated cleavage of C-C bonds in vicinal tricarbonyl compounds in water. Angew Chem. Int. Ed. 48, 2796-2800 (2009).
    • (2009) Angew Chem. Int. Ed , vol.48 , pp. 2796-2800
    • Mecinović, J.1    Hamed, R.B.2    Schofield, C.J.3
  • 43
    • 84867169460 scopus 로고    scopus 로고
    • Oxidative modification of proteins: An emerging mechanism of cell signaling
    • Wall, S. B., Oh, J.-Y., Diers, A. R. & Landar, A. Oxidative modification of proteins: An emerging mechanism of cell signaling. Front. Physiol. 3, 369 (2012).
    • (2012) Front. Physiol , vol.3 , pp. 369
    • Wall, S.B.1    Oh, J.-Y.2    Diers, A.R.3    Landar, A.4
  • 44
    • 57649221592 scopus 로고    scopus 로고
    • Hypoxic reactive oxygen species regulate the integrated stress response and cell survival
    • Liu, L., Wise, D. R., Diehl, J. A. & Simon, M. C. Hypoxic reactive oxygen species regulate the integrated stress response and cell survival. J. Biol. Chem. 283, 31153-31162 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 31153-31162
    • Liu, L.1    Wise, D.R.2    Diehl, J.A.3    Simon, M.C.4
  • 47
    • 24144447915 scopus 로고    scopus 로고
    • Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-α activation
    • DOI 10.1016/j.cmet.2005.05.003, PII S1550413105001415
    • Mansfield, K. D. et al. Mitochondrial dysfunction resulting from loss of cytochrome c impairs cellular oxygen sensing and hypoxic HIF-a activation. Cell Metab. 1, 393-399 (2005). (Pubitemid 43960625)
    • (2005) Cell Metabolism , vol.1 , Issue.6 , pp. 393-399
    • Mansfield, K.D.1    Guzy, R.D.2    Pan, Y.3    Young, R.M.4    Cash, T.P.5    Schumacker, P.T.6    Simon, M.C.7
  • 48
    • 78650019179 scopus 로고    scopus 로고
    • Leukemic IDH1 and IDH2 mutations result in a hypermethylation phenotype, disrupt TET2 function, and impair hematopoietic differentiation
    • Figueroa, M. E. et al. Leukemic IDH1 and IDH2 mutations result in a hypermethylation phenotype, disrupt TET2 function, and impair hematopoietic differentiation. Cancer Cell 18, 553-567 (2010).
    • (2010) Cancer Cell , vol.18 , pp. 553-567
    • Figueroa, M.E.1
  • 49
    • 79959964863 scopus 로고    scopus 로고
    • Succinic semialdehyde dehydrogenase: Biochemical-molecularclinical disease mechanisms redox regulation and functional significance
    • Kim, K. J. et al. Succinic semialdehyde dehydrogenase: biochemical-molecularclinical disease mechanisms, redox regulation, and functional significance. Antioxid. Redox Signaling 15, 691-718 (2011).
    • (2011) Antioxid. Redox Signaling , vol.15 , pp. 691-718
    • Kim, K.J.1
  • 50
    • 0041365682 scopus 로고    scopus 로고
    • Succinic semialdehyde dehydrogenase deficiency in children and adults
    • DOI 10.1002/ana.10629
    • Pearl, P. L., Novotny, E. J., Acosta, M. T., Jakobs, C. & Gibson, K. M. Succinic semialdehyde dehydrogenase deficiency in children and adults. Ann. Neurol. 54, S73-S80 (2003). (Pubitemid 36903857)
    • (2003) Annals of Neurology , vol.54 , Issue.SUPPL. 6
    • Pearl, P.L.1    Novomy, E.J.2    Acosta, M.T.3    Jakobs, C.4    Gibson, K.M.5
  • 51
    • 77149164783 scopus 로고    scopus 로고
    • Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: Direct observation of formaldehyde
    • Hopkinson, R. J., Hamed, R. B., Rose, N. R., Claridge, T. D. W. & Schofield, C. J. Monitoring the activity of 2-oxoglutarate dependent histone demethylases by NMR spectroscopy: direct observation of formaldehyde. Chembiochem. 11, 506-510 (2010).
    • (2010) Chembiochem , vol.11 , pp. 506-510
    • Hopkinson, R.J.1    Hamed, R.B.2    Rose, N.R.3    Claridge, T.D.W.4    Schofield, C.J.5
  • 52
    • 67649980040 scopus 로고    scopus 로고
    • Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases
    • Chowdhury, R. et al. Structural basis for binding of hypoxia-inducible factor to the oxygen-sensing prolyl hydroxylases. Structure 17, 981-989 (2009).
    • (2009) Structure , vol.17 , pp. 981-989
    • Chowdhury, R.1
  • 55
    • 78650425625 scopus 로고    scopus 로고
    • Structural and mechanistic studies on g-butyrobetaine hydroxylase
    • Leung, I. K. H. et al. Structural and Mechanistic Studies on g-Butyrobetaine Hydroxylase. Chem. Biol. 17, 1316-1324 (2010).
    • (2010) Chem. Biol , vol.17 , pp. 1316-1324
    • Leung, I.K.H.1
  • 57
    • 68349133481 scopus 로고    scopus 로고
    • Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2
    • Mecinović, J., Chowdhury, R., Flashman, E. & Schofield, C. J. Use of mass spectrometry to probe the nucleophilicity of cysteinyl residues of prolyl hydroxylase domain 2. Anal. Biochem. 393, 215-221 (2009).
    • (2009) Anal. Biochem , vol.393 , pp. 215-221
    • Mecinović, J.1    Chowdhury, R.2    Flashman, E.3    Schofield, C.J.4
  • 58
    • 84873333801 scopus 로고    scopus 로고
    • Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor
    • Yang, M. et al. Substrate selectivity analyses of factor inhibiting hypoxia-inducible factor. Angew Chem. Int. Ed. 52, 1700-1704 (2013).
    • (2013) Angew Chem. Int. Ed , vol.52 , pp. 1700-1704
    • Yang, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.