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Volumn 64, Issue 2, 2009, Pages 139-145

Kinetic characterization of recombinant human cystathionine β-synthase purified from E. coli

Author keywords

6 His tag; Continuous assay; Cystathionine; Heme; Kinetic characterization; Pyridoxal 5 phosphate; Transsulfuration

Indexed keywords

CYSTATHIONINE BETA SYNTHASE; HEME; HISTIDINE; PYRIDOXAL 5 PHOSPHATE; RECOMBINANT PROTEIN;

EID: 58749087051     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.10.012     Document Type: Article
Times cited : (10)

References (35)
  • 1
    • 0028127106 scopus 로고
    • Transsulfuration depends on heme in addition to pyridoxal 5′-phosphate. Cystathionine beta-synthase is a heme protein
    • Kery V., Bukovska G., and Kraus J.P. Transsulfuration depends on heme in addition to pyridoxal 5′-phosphate. Cystathionine beta-synthase is a heme protein. J. Biol. Chem. 269 (1994) 25283-25288
    • (1994) J. Biol. Chem. , vol.269 , pp. 25283-25288
    • Kery, V.1    Bukovska, G.2    Kraus, J.P.3
  • 2
    • 0035421273 scopus 로고    scopus 로고
    • Structure of human cystathionine beta-synthase: a unique pyridoxal 5′-phosphate-dependent heme protein
    • Meier M., Janosik M., Kery V., Kraus J.P., and Burkhard P. Structure of human cystathionine beta-synthase: a unique pyridoxal 5′-phosphate-dependent heme protein. EMBO J. 20 (2001) 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
  • 3
    • 0037143565 scopus 로고    scopus 로고
    • Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme
    • Taoka S., Lepore B.W., Kabil O., Ojha S., Ringe D., and Banerjee R. Human cystathionine beta-synthase is a heme sensor protein. Evidence that the redox sensor is heme and not the vicinal cysteines in the CXXC motif seen in the crystal structure of the truncated enzyme. Biochemistry 41 (2002) 10454-10461
    • (2002) Biochemistry , vol.41 , pp. 10454-10461
    • Taoka, S.1    Lepore, B.W.2    Kabil, O.3    Ojha, S.4    Ringe, D.5    Banerjee, R.6
  • 4
    • 0034697356 scopus 로고    scopus 로고
    • Yeast cystathionine beta-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. Yeast cystathionine beta-synthase is a pyridoxal phosphate enzyme but, unlike the human enzyme, is not a heme protein. J. Biol. Chem. 275 (2000) 11541-11544
    • (2000) J. Biol. Chem. , vol.275 , pp. 11541-11544
    • Jhee, K.H.1    McPhie, P.2    Miles, E.W.3
  • 5
    • 17344382635 scopus 로고    scopus 로고
    • Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: purification and characterization of recombinant yeast cystathionine beta-synthase
    • Maclean K.N., Janosik M., Oliveriusova J., Kery V., and Kraus J.P. Transsulfuration in Saccharomyces cerevisiae is not dependent on heme: purification and characterization of recombinant yeast cystathionine beta-synthase. J. Inorg. Biochem. 81 (2000) 161-171
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 161-171
    • Maclean, K.N.1    Janosik, M.2    Oliveriusova, J.3    Kery, V.4    Kraus, J.P.5
  • 6
    • 0023939665 scopus 로고
    • The gene for cystathionine beta-synthase (CBS) maps to the subtelomeric region on human chromosome 21q and to proximal mouse chromosome 17
    • Munke M., Kraus J.P., Ohura T., and Francke U. The gene for cystathionine beta-synthase (CBS) maps to the subtelomeric region on human chromosome 21q and to proximal mouse chromosome 17. Am. J. Hum. Genet. 42 (1988) 550-559
    • (1988) Am. J. Hum. Genet. , vol.42 , pp. 550-559
    • Munke, M.1    Kraus, J.P.2    Ohura, T.3    Francke, U.4
  • 8
    • 0034830612 scopus 로고    scopus 로고
    • Mental retardation in Down syndrome: a hydrogen sulfide hypothesis
    • Kamoun P. Mental retardation in Down syndrome: a hydrogen sulfide hypothesis. Med. Hypotheses 57 (2001) 389-392
    • (2001) Med. Hypotheses , vol.57 , pp. 389-392
    • Kamoun, P.1
  • 9
    • 27744450418 scopus 로고    scopus 로고
    • Hyperhomocysteinemia and arteriosclerosis: historical perspectives
    • McCully K.S. Hyperhomocysteinemia and arteriosclerosis: historical perspectives. Clin. Chem. Lab. Med. 43 (2005) 980-986
    • (2005) Clin. Chem. Lab. Med. , vol.43 , pp. 980-986
    • McCully, K.S.1
  • 10
    • 0026533906 scopus 로고
    • The pathogenesis of homocysteinemia: interruption of the coordinate regulation by S-adenosylmethionine of the remethylation and transsulfuration of homocysteine
    • Selhub J., and Miller J.W. The pathogenesis of homocysteinemia: interruption of the coordinate regulation by S-adenosylmethionine of the remethylation and transsulfuration of homocysteine. Am. J. Clin. Nutr. 55 (1992) 131-138
    • (1992) Am. J. Clin. Nutr. , vol.55 , pp. 131-138
    • Selhub, J.1    Miller, J.W.2
  • 12
    • 0035807013 scopus 로고    scopus 로고
    • Regulation of human cystathionine beta-synthase by S-adenosyl-l-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region
    • Janosik M., Kery V., Gaustadnes M., Maclean K.N., and Kraus J.P. Regulation of human cystathionine beta-synthase by S-adenosyl-l-methionine: evidence for two catalytically active conformations involving an autoinhibitory domain in the C-terminal region. Biochemistry 40 (2001) 10625-10633
    • (2001) Biochemistry , vol.40 , pp. 10625-10633
    • Janosik, M.1    Kery, V.2    Gaustadnes, M.3    Maclean, K.N.4    Kraus, J.P.5
  • 14
    • 9744276776 scopus 로고    scopus 로고
    • Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent heme sensor protein
    • Banerjee R., and Zou C.G. Redox regulation and reaction mechanism of human cystathionine-beta-synthase: a PLP-dependent heme sensor protein. Arch. Biochem. Biophys. 433 (2005) 144-156
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 144-156
    • Banerjee, R.1    Zou, C.G.2
  • 17
    • 36049049474 scopus 로고    scopus 로고
    • Ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process
    • Cherney M.M., Pazicni S., Frank N., Marvin K.A., Kraus J.P., and Burstyn J.N. Ferrous human cystathionine beta-synthase loses activity during enzyme assay due to a ligand switch process. Biochemistry 46 (2007) 13199-13210
    • (2007) Biochemistry , vol.46 , pp. 13199-13210
    • Cherney, M.M.1    Pazicni, S.2    Frank, N.3    Marvin, K.A.4    Kraus, J.P.5    Burstyn, J.N.6
  • 18
    • 0018073909 scopus 로고
    • Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits
    • Kraus J., Packman S., Fowler B., and Rosenberg L.E. Purification and properties of cystathionine beta-synthase from human liver. Evidence for identical subunits. J. Biol. Chem. 253 (1978) 6523-6528
    • (1978) J. Biol. Chem. , vol.253 , pp. 6523-6528
    • Kraus, J.1    Packman, S.2    Fowler, B.3    Rosenberg, L.E.4
  • 19
    • 0020577306 scopus 로고
    • Cystathionine beta-synthase from human liver: improved purification scheme and additional characterization of the enzyme in crude and pure form
    • Kraus J.P., and Rosenberg L.E. Cystathionine beta-synthase from human liver: improved purification scheme and additional characterization of the enzyme in crude and pure form. Arch. Biochem. Biophys. 222 (1983) 44-52
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 44-52
    • Kraus, J.P.1    Rosenberg, L.E.2
  • 20
    • 0028519108 scopus 로고
    • Expression of human cystathionine beta-synthase in Escherichia coli: purification and characterization
    • Bukovska G., Kery V., and Kraus J.P. Expression of human cystathionine beta-synthase in Escherichia coli: purification and characterization. Protein Expr. Purif. 5 (1994) 442-448
    • (1994) Protein Expr. Purif. , vol.5 , pp. 442-448
    • Bukovska, G.1    Kery, V.2    Kraus, J.P.3
  • 21
    • 0031798556 scopus 로고    scopus 로고
    • Correction of disease-causing CBS mutations in yeast
    • Shan X., and Kruger W.D. Correction of disease-causing CBS mutations in yeast. Nat. Genet. 19 (1998) 91-93
    • (1998) Nat. Genet. , vol.19 , pp. 91-93
    • Shan, X.1    Kruger, W.D.2
  • 22
    • 0035124772 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease
    • Janosik M., Meier M., Kery V., Oliveriusova J., Burkhard P., and Kraus J.P. Crystallization and preliminary X-ray diffraction analysis of the active core of human recombinant cystathionine beta-synthase: an enzyme involved in vascular disease. Acta Crystallogr. D Biol. Crystallogr. 57 (2001) 289-291
    • (2001) Acta Crystallogr. D Biol. Crystallogr. , vol.57 , pp. 289-291
    • Janosik, M.1    Meier, M.2    Kery, V.3    Oliveriusova, J.4    Burkhard, P.5    Kraus, J.P.6
  • 23
    • 38349053999 scopus 로고    scopus 로고
    • Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli
    • Frank N., Kent J.O., Meier M., and Kraus J.P. Purification and characterization of the wild type and truncated human cystathionine beta-synthase enzymes expressed in E. coli. Arch. Biochem. Biophys. 470 (2008) 64-72
    • (2008) Arch. Biochem. Biophys. , vol.470 , pp. 64-72
    • Frank, N.1    Kent, J.O.2    Meier, M.3    Kraus, J.P.4
  • 24
    • 0032566713 scopus 로고    scopus 로고
    • Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity
    • Taoka S., Ohja S., Shan X., Kruger W.D., and Banerjee R. Evidence for heme-mediated redox regulation of human cystathionine beta-synthase activity. J. Biol. Chem. 273 (1998) 25179-25184
    • (1998) J. Biol. Chem. , vol.273 , pp. 25179-25184
    • Taoka, S.1    Ohja, S.2    Shan, X.3    Kruger, W.D.4    Banerjee, R.5
  • 25
    • 1242285467 scopus 로고    scopus 로고
    • Role of active-site residues Thr81, Ser82, Thr85, Gln157, and Tyr158 in yeast cystathionine beta-synthase catalysis and reaction specificity
    • Aitken S.M., and Kirsch J.F. Role of active-site residues Thr81, Ser82, Thr85, Gln157, and Tyr158 in yeast cystathionine beta-synthase catalysis and reaction specificity. Biochemistry 43 (2004) 1963-1971
    • (2004) Biochemistry , vol.43 , pp. 1963-1971
    • Aitken, S.M.1    Kirsch, J.F.2
  • 26
    • 0014951927 scopus 로고
    • Studies on cystathionine synthase of rat liver. Properties of the highly purified enzyme
    • Kashiwamata S., and Greenberg D.M. Studies on cystathionine synthase of rat liver. Properties of the highly purified enzyme. Biochim Biophys Acta 212 (1970) 488-500
    • (1970) Biochim Biophys Acta , vol.212 , pp. 488-500
    • Kashiwamata, S.1    Greenberg, D.M.2
  • 27
    • 0028566384 scopus 로고
    • Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction
    • Weiner M.P., Costa G.L., Schoettlin W., Cline J., Mathur E., and Bauer J.C. Site-directed mutagenesis of double-stranded DNA by the polymerase chain reaction. Gene 151 (1994) 119-123
    • (1994) Gene , vol.151 , pp. 119-123
    • Weiner, M.P.1    Costa, G.L.2    Schoettlin, W.3    Cline, J.4    Mathur, E.5    Bauer, J.C.6
  • 28
    • 0343471377 scopus 로고    scopus 로고
    • Modification of a PCR-based site-directed mutagenesis method
    • Fisher C.L., and Pei G.K. Modification of a PCR-based site-directed mutagenesis method. Biotechniques 23 (1997) 570-574
    • (1997) Biotechniques , vol.23 , pp. 570-574
    • Fisher, C.L.1    Pei, G.K.2
  • 29
    • 0028984985 scopus 로고
    • Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli
    • Kery V., Elleder D., and Kraus J.P. Delta-aminolevulinate increases heme saturation and yield of human cystathionine beta-synthase expressed in Escherichia coli. Arch. Biochem. Biophys. 316 (1995) 24-29
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 24-29
    • Kery, V.1    Elleder, D.2    Kraus, J.P.3
  • 30
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0013790866 scopus 로고
    • Determination of heme a concentration in cytochrome preparations by hemochromogen method
    • Morrison M., and Horie S. Determination of heme a concentration in cytochrome preparations by hemochromogen method. Anal. Biochem. 12 (1965) 77-82
    • (1965) Anal. Biochem. , vol.12 , pp. 77-82
    • Morrison, M.1    Horie, S.2
  • 32
    • 0037457908 scopus 로고    scopus 로고
    • Kinetics of the yeast cystathionine beta-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction
    • Aitken S.M., and Kirsch J.F. Kinetics of the yeast cystathionine beta-synthase forward and reverse reactions: continuous assays and the equilibrium constant for the reaction. Biochemistry 42 (2003) 571-578
    • (2003) Biochemistry , vol.42 , pp. 571-578
    • Aitken, S.M.1    Kirsch, J.F.2
  • 33
    • 0034730104 scopus 로고    scopus 로고
    • Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation
    • Jhee K.H., McPhie P., and Miles E.W. Domain architecture of the heme-independent yeast cystathionine beta-synthase provides insights into mechanisms of catalysis and regulation. Biochemistry 39 (2000) 10548-10556
    • (2000) Biochemistry , vol.39 , pp. 10548-10556
    • Jhee, K.H.1    McPhie, P.2    Miles, E.W.3
  • 34
    • 33644549065 scopus 로고    scopus 로고
    • X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site
    • Rufer A.C., Thiebach L., Baer K., Klein H.W., and Hennig M. X-ray structure of glutathione S-transferase from Schistosoma japonicum in a new crystal form reveals flexibility of the substrate-binding site. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 (2005) 263-265
    • (2005) Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. , vol.61 , pp. 263-265
    • Rufer, A.C.1    Thiebach, L.2    Baer, K.3    Klein, H.W.4    Hennig, M.5
  • 35
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang F., Moss L.G., and Phillips Jr. G.N. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14 (1996) 1246-1251
    • (1996) Nat. Biotechnol. , vol.14 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3


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