메뉴 건너뛰기




Volumn 50, Issue 3, 2011, Pages 419-425

Pre-steady-state kinetic analysis of enzyme-monitored turnover during cystathionine β-synthase-catalyzed H2S generation

Author keywords

[No Author keywords available]

Indexed keywords

ABSORPTION MAXIMA; AMINOACRYLATES; BIMOLECULAR RATE CONSTANTS; HEME COFACTOR; HOMOCYSTEINES; PRE-STEADY-STATE KINETIC ANALYSIS; STEADY-STATE KINETICS; SYNTHASES;

EID: 78751546668     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi1010893     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0036845556 scopus 로고    scopus 로고
    • Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter?
    • Wang, R. (2002) Two's company, three's a crowd: Can H2S be the third endogenous gaseous transmitter? FASEB J. 16, 1792-1798
    • (2002) FASEB J. , vol.16 , pp. 1792-1798
    • Wang, R.1
  • 2
    • 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
  • 3
    • 77954579286 scopus 로고    scopus 로고
    • The redox biochemistry of hydrogen sulfide
    • Kabil, O. and Banerjee, R. (2010) The 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
  • 7
    • 0035970010 scopus 로고    scopus 로고
    • Ultradian metabolic oscillation of Saccharomyces cerevisiae during aerobic continuous culture: Hydrogen sulphide, a population synchronizer, is produced by sulphite reductase
    • Sohn, H. and Kuriyama, H. (2001) Ultradian metabolic oscillation of Saccharomyces cerevisiae during aerobic continuous culture: Hydrogen sulphide, a population synchronizer, is produced by sulphite reductase Yeast 18, 125-135
    • (2001) Yeast , vol.18 , pp. 125-135
    • Sohn, H.1    Kuriyama, H.2
  • 8
    • 0020483746 scopus 로고
    • Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat
    • Stipanuk, M. H. and Beck, P. W. (1982) Characterization of the enzymic capacity for cysteine desulphhydration in liver and kidney of the rat Biochem. J. 206, 267-277
    • (1982) Biochem. J. , vol.206 , pp. 267-277
    • Stipanuk, M.H.1    Beck, P.W.2
  • 10
    • 77956194462 scopus 로고    scopus 로고
    • Cystathionine γ-lyase-deficient mice require dietary cysteine to protect against acute lethal myopathy and oxidative injury
    • Ishii, I., Akahoshi, N., Yamada, H., Nakano, S., Izumi, T., and Suematsu, M. (2010) Cystathionine γ-lyase-deficient mice require dietary cysteine to protect against acute lethal myopathy and oxidative injury J. Biol. Chem. 285, 26358-26368
    • (2010) J. Biol. Chem. , vol.285 , pp. 26358-26368
    • Ishii, I.1    Akahoshi, N.2    Yamada, H.3    Nakano, S.4    Izumi, T.5    Suematsu, M.6
  • 11
    • 66449109703 scopus 로고    scopus 로고
    • H2S biogenesis by cystathionine γ-lyase leads to the novel sulfur metabolites, lanthionine and homolanthionine, and is responsive to the grade of hyperhomocysteinemia
    • Chiku, T., Padovani, D., Zhu, W., Singh, S., Vitvitsky, V., and Banerjee, R. (2009) H2S biogenesis by cystathionine γ-lyase leads to the novel sulfur metabolites, lanthionine and homolanthionine, and is responsive to the grade of hyperhomocysteinemia J. Biol. Chem. 284, 11601-11612
    • (2009) J. Biol. Chem. , vol.284 , pp. 11601-11612
    • Chiku, T.1    Padovani, D.2    Zhu, W.3    Singh, S.4    Vitvitsky, V.5    Banerjee, R.6
  • 12
    • 69249100078 scopus 로고    scopus 로고
    • Relative contributions of cystathionine β-synthase and γ-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions
    • Singh, S., Padovani, D., Leslie, R. A., Chiku, T., and Banerjee, R. (2009) Relative contributions of cystathionine β-synthase and γ-cystathionase to H2S biogenesis via alternative trans-sulfuration reactions J. Biol. Chem. 284, 22457-22466
    • (2009) J. Biol. Chem. , vol.284 , pp. 22457-22466
    • Singh, S.1    Padovani, D.2    Leslie, R.A.3    Chiku, T.4    Banerjee, R.5
  • 13
    • 78650504604 scopus 로고    scopus 로고
    • Structural basis for substrate activation and regulation by cystathionine β-synthase (CBS) domains in cystathionine β-synthase
    • Koutmos, M., Kabil, O., Smith, J. L., and Banerjee, R. (2010) Structural basis for substrate activation and regulation by cystathionine β-synthase (CBS) domains in cystathionine β-synthase Proc. Natl. Acad. Sci. U.S.A. 107, 20958-20963
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 20958-20963
    • Koutmos, M.1    Kabil, O.2    Smith, J.L.3    Banerjee, R.4
  • 15
    • 3142749051 scopus 로고    scopus 로고
    • Cystathionine β-synthase: Structure, Function, Regulation, and Location of Homocystinuria-causing Mutations
    • Miles, E. W. and Kraus, J. P. (2004) Cystathionine β-synthase: Structure, Function, Regulation, and Location of Homocystinuria-causing Mutations J. Biol. Chem. 279, 29871-29874
    • (2004) J. Biol. Chem. , vol.279 , pp. 29871-29874
    • Miles, E.W.1    Kraus, J.P.2
  • 17
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine β-synthase: A unique pyridoxal 5′-phosphate-dependent heme protein
    • Meier, M., Janosik, M., Kery, V., Kraus, J. P., and Burkhard, P. (2001) Structure of human cystathionine β-synthase: A unique pyridoxal 5′-phosphate-dependent heme protein EMBO J. 20, 3910-3916
    • (2001) EMBO J. , vol.20 , pp. 3910-3916
    • Meier, M.1    Janosik, M.2    Kery, V.3    Kraus, J.P.4    Burkhard, P.5
  • 18
    • 3943113663 scopus 로고    scopus 로고
    • Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations
    • Eliot, A. C. and Kirsch, J. F. (2004) Pyridoxal phosphate enzymes: Mechanistic, structural, and evolutionary considerations Annu. Rev. Biochem. 73, 383-415
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 383-415
    • Eliot, A.C.1    Kirsch, J.F.2
  • 19
    • 0022344850 scopus 로고
    • Detection and identification of intermediates in the reaction of l -serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy
    • Drewe, W. F., Jr. and Dunn, M. F. (1985) Detection and identification of intermediates in the reaction of l -serine with Escherichia coli tryptophan synthase via rapid-scanning ultraviolet-visible spectroscopy Biochemistry 24, 3977-3987
    • (1985) Biochemistry , vol.24 , pp. 3977-3987
    • Drewe Jr., W.F.1    Dunn, M.F.2
  • 20
    • 0029865896 scopus 로고    scopus 로고
    • Formation of the α-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase
    • Woehl, E. U., Tai, C. H., Dunn, M. F., and Cook, P. F. (1996) Formation of the α-aminoacrylate immediate limits the overall reaction catalyzed by O-acetylserine sulfhydrylase Biochemistry 35, 4776-4783
    • (1996) Biochemistry , vol.35 , pp. 4776-4783
    • Woehl, E.U.1    Tai, C.H.2    Dunn, M.F.3    Cook, P.F.4
  • 21
    • 0033515107 scopus 로고    scopus 로고
    • Characterization of the heme and pyridoxal phosphate cofactors of human cystathionine β-synthase reveals nonequivalent active sites
    • Taoka, S., West, M., and Banerjee, R. (1999) Characterization of the heme and pyridoxal phosphate cofactors of human cystathionine β-synthase reveals nonequivalent active sites Biochemistry 38, 2738-2744
    • (1999) Biochemistry , vol.38 , pp. 2738-2744
    • Taoka, S.1    West, M.2    Banerjee, R.3
  • 22
    • 2942542787 scopus 로고    scopus 로고
    • Visualization of PLP-bound intermediates in hemeless variants of human cystathionine β-synthase: Evidence that lysine 119 is a general base
    • Evande, R., Ojha, S., and Banerjee, R. (2004) Visualization of PLP-bound intermediates in hemeless variants of human cystathionine β-synthase: Evidence that lysine 119 is a general base Arch. Biochem. Biophys. 427, 188-196
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 188-196
    • Evande, R.1    Ojha, S.2    Banerjee, R.3
  • 23
    • 0037151019 scopus 로고    scopus 로고
    • Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine β-synthase
    • Taoka, S. and Banerjee, R. (2002) Stopped-flow kinetic analysis of the reaction catalyzed by the full-length yeast cystathionine β-synthase J. Biol. Chem. 277, 22421-22425
    • (2002) J. Biol. Chem. , vol.277 , pp. 22421-22425
    • Taoka, S.1    Banerjee, R.2
  • 24
    • 0035845648 scopus 로고    scopus 로고
    • The reaction of yeast cystathionine β-synthase is rate-limited by the conversion of aminoacrylate to cystathionine
    • Jhee, K. H., Niks, D., McPhie, P., Dunn, M. F., and Miles, E. W. (2001) The reaction of yeast cystathionine β-synthase is rate-limited by the conversion of aminoacrylate to cystathionine Biochemistry 40, 10873-10880
    • (2001) Biochemistry , vol.40 , pp. 10873-10880
    • Jhee, K.H.1    Niks, D.2    McPhie, P.3    Dunn, M.F.4    Miles, E.W.5
  • 25
    • 0034697356 scopus 로고    scopus 로고
    • Yeast cystathionine β-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein
    • Jhee, K. H., McPhie, P., and Miles, E. W. (2000) Yeast cystathionine β-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein J. Biol. Chem. 275, 11541-11544
    • (2000) J. Biol. Chem. , vol.275 , pp. 11541-11544
    • Jhee, K.H.1    McPhie, P.2    Miles, E.W.3
  • 26
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabo, C. (2007) Hydrogen sulphide and its therapeutic potential Nat. Rev. Drug Discovery 6, 917-935
    • (2007) Nat. Rev. Drug Discovery , vol.6 , pp. 917-935
    • Szabo, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.