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Volumn 53, Issue 28, 2014, Pages 4739-4753

Biosynthesis of a central intermediate in hydrogen sulfide metabolism by a novel human sulfurtransferase and its yeast ortholog

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; ENCODING (SYMBOLS); ENZYMES; GENES; MAMMALS; METABOLISM; PHYSIOLOGICAL MODELS; PHYSIOLOGY; SULFUR COMPOUNDS; YEAST;

EID: 84904668283     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi500650h     Document Type: Article
Times cited : (66)

References (64)
  • 3
    • 77954579286 scopus 로고    scopus 로고
    • Redox biochemistry of hydrogen sulfide
    • Kabil, O. and Banerjee, R. (2010) Redox biochemistry of hydrogen sulfide J. Biol. Chem. 285, 21903-21907
    • (2010) J. Biol. Chem. , vol.285 , pp. 21903-21907
    • Kabil, O.1    Banerjee, R.2
  • 5
    • 84860736030 scopus 로고    scopus 로고
    • Roles of hydrogen sulfide in the pathogenesis of diabetes mellitus and its complications
    • Szabo, C. (2012) Roles of hydrogen sulfide in the pathogenesis of diabetes mellitus and its complications Antioxid. Redox Signaling 17, 68-80
    • (2012) Antioxid. Redox Signaling , vol.17 , pp. 68-80
    • Szabo, C.1
  • 6
    • 84860117196 scopus 로고    scopus 로고
    • Physiological implications of hydrogen sulfide: A whiff exploration that blossomed
    • Wang, R. (2012) Physiological implications of hydrogen sulfide: A whiff exploration that blossomed Physiol. Rev. 92, 791-896
    • (2012) Physiol. Rev. , vol.92 , pp. 791-896
    • Wang, R.1
  • 7
    • 78650503537 scopus 로고    scopus 로고
    • Hydrogen sulfide in the endocrine and reproductive systems
    • Zhu, X. Y., Gu, H., and Ni, X. (2011) Hydrogen sulfide in the endocrine and reproductive systems Expert Rev. Clin. Pharmacol. 4, 75-82
    • (2011) Expert Rev. Clin. Pharmacol. , vol.4 , pp. 75-82
    • Zhu, X.Y.1    Gu, H.2    Ni, X.3
  • 8
    • 78650541124 scopus 로고    scopus 로고
    • Hydrogen sulfide-mediated myocardial pre- and post-conditioning
    • Predmore, B. L. and Lefer, D. J. (2011) Hydrogen sulfide-mediated myocardial pre- and post-conditioning Expert Rev. Clin. Pharmacol. 4, 83-96
    • (2011) Expert Rev. Clin. Pharmacol. , vol.4 , pp. 83-96
    • Predmore, B.L.1    Lefer, D.J.2
  • 11
    • 78650489682 scopus 로고    scopus 로고
    • Hydrogen sulfide in the pathogenesis of atherosclerosis and its therapeutic potential
    • Lynn, E. G. and Austin, R. C. (2011) Hydrogen sulfide in the pathogenesis of atherosclerosis and its therapeutic potential Expert Rev. Clin. Pharmacol. 4, 97-108
    • (2011) Expert Rev. Clin. Pharmacol. , vol.4 , pp. 97-108
    • Lynn, E.G.1    Austin, R.C.2
  • 12
    • 0036700930 scopus 로고    scopus 로고
    • Hydrogen sulfide as a neuromodulator
    • Kimura, H. (2002) Hydrogen sulfide as a neuromodulator Mol. Neurobiol. 26, 13-19
    • (2002) Mol. Neurobiol. , vol.26 , pp. 13-19
    • Kimura, H.1
  • 13
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura, Y. and Kimura, H. (2004) Hydrogen sulfide protects neurons from oxidative stress FASEB J. 18, 1165-1167
    • (2004) FASEB J. , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 14
    • 73449101844 scopus 로고    scopus 로고
    • Hydrogen sulfide-releasing NSAIDs attenuate neuroinflammation induced by microglial and astrocytic activation
    • Lee, M., Sparatore, A., Del Soldato, P., Mcgeer, E., and McGeer, P. L. (2010) Hydrogen sulfide-releasing NSAIDs attenuate neuroinflammation induced by microglial and astrocytic activation Glia 58, 103-113
    • (2010) Glia , vol.58 , pp. 103-113
    • Lee, M.1    Sparatore, A.2    Del Soldato, P.3    McGeer, E.4    McGeer, P.L.5
  • 18
    • 84862909327 scopus 로고    scopus 로고
    • Hydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actions
    • Sen, N., Paul, B. D., Gadalla, M. M., Mustafa, A. K., Sen, T., Xu, R., Kim, S., and Snyder, S. H. (2012) Hydrogen sulfide-linked sulfhydration of NF-κB mediates its antiapoptotic actions Mol. Cell 45, 13-24
    • (2012) Mol. Cell , vol.45 , pp. 13-24
    • Sen, N.1    Paul, B.D.2    Gadalla, M.M.3    Mustafa, A.K.4    Sen, T.5    Xu, R.6    Kim, S.7    Snyder, S.H.8
  • 20
    • 83655165310 scopus 로고    scopus 로고
    • 2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response
    • 2S-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response Sci. Signaling 4, ra86
    • (2011) Sci. Signaling , vol.4 , pp. 86
    • Krishnan, N.1    Fu, C.X.2    Pappin, D.J.3    Tonks, N.K.4
  • 22
  • 23
    • 84867522886 scopus 로고    scopus 로고
    • Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite
    • Jackson, M. R., Melideo, S. L., and Jorns, M. S. (2012) Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite Biochemistry 51, 6804-6815
    • (2012) Biochemistry , vol.51 , pp. 6804-6815
    • Jackson, M.R.1    Melideo, S.L.2    Jorns, M.S.3
  • 24
    • 44949214775 scopus 로고    scopus 로고
    • Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria
    • Hildebrandt, T. M., Grieshaber, M. K., and Westley, J. (2008) Three enzymatic activities catalyze the oxidation of sulfide to thiosulfate in mammalian and invertebrate mitochondria FEBS J. 275, 3352-3361
    • (2008) FEBS J. , vol.275 , pp. 3352-3361
    • Hildebrandt, T.M.1    Grieshaber, M.K.2    Westley, J.3
  • 25
    • 77951225834 scopus 로고    scopus 로고
    • A new structure-based classification of sulfide:quinone oxidoreductases
    • Marcia, M., Ermler, U., Peng, G., and Michel, H. (2010) A new structure-based classification of sulfide:quinone oxidoreductases Proteins 78, 1073-1083
    • (2010) Proteins , vol.78 , pp. 1073-1083
    • Marcia, M.1    Ermler, U.2    Peng, G.3    Michel, H.4
  • 26
    • 77955672171 scopus 로고    scopus 로고
    • Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes
    • Lagoutte, E., Mimoun, S., Andriamihaja, M., Chaumontet, C., Blachier, F., and Bouillaud, F. (2010) Oxidation of hydrogen sulfide remains a priority in mammalian cells and causes reverse electron transfer in colonocytes Biochim. Biophys. Acta 1797, 1500-1511
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1500-1511
    • Lagoutte, E.1    Mimoun, S.2    Andriamihaja, M.3    Chaumontet, C.4    Blachier, F.5    Bouillaud, F.6
  • 27
    • 0014098318 scopus 로고
    • 35S-Thiosulphate oxidation by rat liver mitochondria in the presence of glutathione
    • 35S]-Thiosulphate oxidation by rat liver mitochondria in the presence of glutathione Biochem. J. 103, 791
    • (1967) Biochem. J. , vol.103 , pp. 791
    • Koj, A.1    Frendo, J.2    Janik, Z.3
  • 28
    • 0344963392 scopus 로고
    • The metabolic state of thiosulfate
    • Szczepkowski, T. W., Skarzynski, B., and Weber, M. (1961) The metabolic state of thiosulfate Nature 189, 1007-1008
    • (1961) Nature , vol.189 , pp. 1007-1008
    • Szczepkowski, T.W.1    Skarzynski, B.2    Weber, M.3
  • 30
    • 0032718594 scopus 로고    scopus 로고
    • Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa
    • Levitt, M. D., Furne, J., Springfield, J., Suarez, F., and DeMaster, E. (1999) Detoxification of hydrogen sulfide and methanethiol in the cecal mucosa J. Clin. Invest. 104, 1107-1114
    • (1999) J. Clin. Invest. , vol.104 , pp. 1107-1114
    • Levitt, M.D.1    Furne, J.2    Springfield, J.3    Suarez, F.4    Demaster, E.5
  • 31
    • 0035879968 scopus 로고    scopus 로고
    • Oxidation of hydrogen sulfide and methanethiol to thiosulfate by rat tissues: A specialized function of the colonic mucosa
    • Furne, J., Springfield, J., Koenig, T., DeMaster, E., and Levitt, M. D. (2001) Oxidation of hydrogen sulfide and methanethiol to thiosulfate by rat tissues: A specialized function of the colonic mucosa Biochem. Pharmacol. 62, 255-259
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 255-259
    • Furne, J.1    Springfield, J.2    Koenig, T.3    Demaster, E.4    Levitt, M.D.5
  • 33
    • 76749087089 scopus 로고    scopus 로고
    • Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase
    • Johnson-Winters, K., Nordstrom, A. R., Emesh, S., Astashkin, A. V., Rajapakshe, A., Berry, R. E., Tollin, G., and Enemark, J. H. (2010) Effects of interdomain tether length and flexibility on the kinetics of intramolecular electron transfer in human sulfite oxidase Biochemistry 49, 1290-1296
    • (2010) Biochemistry , vol.49 , pp. 1290-1296
    • Johnson-Winters, K.1    Nordstrom, A.R.2    Emesh, S.3    Astashkin, A.V.4    Rajapakshe, A.5    Berry, R.E.6    Tollin, G.7    Enemark, J.H.8
  • 35
    • 0023196348 scopus 로고
    • Urinary thiosulphate as an indicator of exposure to hydrogen sulphide vapour
    • Kangas, J. and Savolainen, H. (1987) Urinary thiosulphate as an indicator of exposure to hydrogen sulphide vapour Clin. Chim. Acta 164, 7-10
    • (1987) Clin. Chim. Acta , vol.164 , pp. 7-10
    • Kangas, J.1    Savolainen, H.2
  • 36
    • 84885421757 scopus 로고    scopus 로고
    • Disturbance of brain energy and redox homeostasis provoked by sulfite and thiosulfate: Potential pathomechanisms involved in the neuropathology of sulfite oxidase deficiency
    • Grings, M., Moura, A. P., Parmeggiani, B., Marcowich, G. F., Amaral, A. U., Wyse, A. T. D., Wajner, M., and Leipnitz, G. (2013) Disturbance of brain energy and redox homeostasis provoked by sulfite and thiosulfate: Potential pathomechanisms involved in the neuropathology of sulfite oxidase deficiency Gene 531, 191-198
    • (2013) Gene , vol.531 , pp. 191-198
    • Grings, M.1    Moura, A.P.2    Parmeggiani, B.3    Marcowich, G.F.4    Amaral, A.U.5    Wyse, A.T.D.6    Wajner, M.7    Leipnitz, G.8
  • 37
    • 3042561729 scopus 로고    scopus 로고
    • Fatal hydrogen sulfide poisoning at a dye works
    • Kage, S., Ikeda, H., Ikeda, N., Tsujita, A., and Kudo, K. (2004) Fatal hydrogen sulfide poisoning at a dye works Leg. Med. 6, 182-186
    • (2004) Leg. Med. , vol.6 , pp. 182-186
    • Kage, S.1    Ikeda, H.2    Ikeda, N.3    Tsujita, A.4    Kudo, K.5
  • 38
    • 0021112852 scopus 로고
    • The catalytic mechanism of yeast thiosulfate reductase
    • Chauncey, T. R. and Westley, J. (1983) The catalytic mechanism of yeast thiosulfate reductase J. Biol. Chem. 258, 15037-15045
    • (1983) J. Biol. Chem. , vol.258 , pp. 15037-15045
    • Chauncey, T.R.1    Westley, J.2
  • 39
    • 0021107322 scopus 로고
    • Improved purification and sulfhydryl analysis of thiosulfate reductase
    • Chauncey, T. R. and Westley, J. (1983) Improved purification and sulfhydryl analysis of thiosulfate reductase Biochim. Biophys. Acta 744, 304-311
    • (1983) Biochim. Biophys. Acta , vol.744 , pp. 304-311
    • Chauncey, T.R.1    Westley, J.2
  • 40
    • 0018483519 scopus 로고
    • Purification and steady-state kinetic analysis of yeast thiosulfate reductase
    • Uhteg, L. C. and Westley, J. (1979) Purification and steady-state kinetic analysis of yeast thiosulfate reductase Arch. Biochem. Biophys. 195, 211-222
    • (1979) Arch. Biochem. Biophys. , vol.195 , pp. 211-222
    • Uhteg, L.C.1    Westley, J.2
  • 41
    • 0014178501 scopus 로고
    • Oxidation of thiosulphate to sulphate in animal tissues
    • Koj, A. and Frendo, J. (1967) Oxidation of thiosulphate to sulphate in animal tissues Folia Biol. (Krakow, Pol.) 15, 49-65
    • (1967) Folia Biol. (Krakow, Pol.) , vol.15 , pp. 49-65
    • Koj, A.1    Frendo, J.2
  • 42
    • 0014234438 scopus 로고
    • Enzymic reduction of thiosulphate in preparations from beef liver
    • Koj, A. (1968) Enzymic reduction of thiosulphate in preparations from beef liver Acta Biochim. Pol. 15, 161-169
    • (1968) Acta Biochim. Pol. , vol.15 , pp. 161-169
    • Koj, A.1
  • 44
    • 33847163530 scopus 로고    scopus 로고
    • Ligation independent cloning vectors for expression of SUMO fusions
    • Weeks, S. D., Drinker, M., and Loll, P. J. (2007) Ligation independent cloning vectors for expression of SUMO fusions Protein Expression Purif. 53, 40-50
    • (2007) Protein Expression Purif. , vol.53 , pp. 40-50
    • Weeks, S.D.1    Drinker, M.2    Loll, P.J.3
  • 45
    • 77957011016 scopus 로고
    • Rhodanese
    • Sorbo, B. (1955) Rhodanese Methods Enzymol. 2, 334-337
    • (1955) Methods Enzymol. , vol.2 , pp. 334-337
    • Sorbo, B.1
  • 46
    • 0023070121 scopus 로고
    • Sulfane sulfur
    • Wood, J. L. (1987) Sulfane sulfur Methods Enzymol. 143, 25-29
    • (1987) Methods Enzymol. , vol.143 , pp. 25-29
    • Wood, J.L.1
  • 48
    • 0014027818 scopus 로고
    • The rhodanese reaction mechanism of sulfur-sulfur bond cleavage
    • Mintel, R. and Westley, J. (1966) The rhodanese reaction mechanism of sulfur-sulfur bond cleavage J. Biol. Chem. 241, 3381-3385
    • (1966) J. Biol. Chem. , vol.241 , pp. 3381-3385
    • Mintel, R.1    Westley, J.2
  • 49
    • 84870390566 scopus 로고
    • On the acceptor specificity of rhodanese
    • Sorbo, B. (1962) On the acceptor specificity of rhodanese Acta Chem. Scand. 16, 243-245
    • (1962) Acta Chem. Scand. , vol.16 , pp. 243-245
    • Sorbo, B.1
  • 50
    • 34047225116 scopus 로고    scopus 로고
    • Common themes and variations in the rhodanese superfamily
    • Cipollone, R., Ascenzi, P., and Visca, P. (2007) Common themes and variations in the rhodanese superfamily UBMB Life 59, 51-59
    • (2007) UBMB Life , vol.59 , pp. 51-59
    • Cipollone, R.1    Ascenzi, P.2    Visca, P.3
  • 51
    • 0034084865 scopus 로고    scopus 로고
    • Whos your neighbor? New computational approaches for functional genomics
    • Galperin, M. Y. and Koonin, E. V. (2000) Whos your neighbor? New computational approaches for functional genomics Nat. Biotechnol. 18, 609-613
    • (2000) Nat. Biotechnol. , vol.18 , pp. 609-613
    • Galperin, M.Y.1    Koonin, E.V.2
  • 52
    • 84891612724 scopus 로고    scopus 로고
    • Characteristics and function of sulfur dioxygenase in echiuran worm Urechis unicinctus
    • Zhang, L. T., Liu, X. L., Liu, J. G., and Zhang, Z. F. (2013) Characteristics and function of sulfur dioxygenase in echiuran worm Urechis unicinctus PLoS One 8, e81885
    • (2013) PLoS One , vol.8 , pp. 81885
    • Zhang, L.T.1    Liu, X.L.2    Liu, J.G.3    Zhang, Z.F.4
  • 57
    • 0018790584 scopus 로고
    • The structure of bovine liver rhodanese: II. The active site in the sulfur-substituted and the sulfur-free enzyme
    • Ploegman, J. H., Drent, G. é., Kalk, K. H., and Hol, W. G. (1979) The structure of bovine liver rhodanese: II. The active site in the sulfur-substituted and the sulfur-free enzyme J. Mol. Biol. 127, 149-162
    • (1979) J. Mol. Biol. , vol.127 , pp. 149-162
    • Ploegman, J.H.1    Kalk, K.H.2    Hol, W.G.3
  • 58
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Griffith, O. W. (1999) Biologic and pharmacologic regulation of mammalian glutathione synthesis Free Radical Biol. Med. 27, 922-935
    • (1999) Free Radical Biol. Med. , vol.27 , pp. 922-935
    • Griffith, O.W.1
  • 63
    • 33746361541 scopus 로고    scopus 로고
    • PHY·FI: Fast and easy online creation and manipulation of phylogeny color figures
    • Fredslund, J. (2006) PHY·FI: Fast and easy online creation and manipulation of phylogeny color figures BMC Bioinf. 7, 315
    • (2006) BMC Bioinf. , vol.7 , pp. 315
    • Fredslund, J.1


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