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Volumn 49, Issue 13, 2006, Pages 3982-3989

S-alkylated homocysteine derivatives: New inhibitors of human betaine-homocysteine S-methyltransferase

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 4 (3 CARBOXYMETHYLSULFANYLETHYLSULFANYL)BUTYRIC ACID; 5 (3 AMINO 3 CARBOXYPROPYLSULFANYL)PENTANOIC ACID; 6 (3 AMINO 3 CARBOXYPROPYLSULFANYL)HEXANOIC ACID; AMINO ACID DERIVATIVE; BETAINE; BETAINE HOMOCYSTEINE METHYLTRANSFERASE; HOMOCYSTEINE DERIVATIVE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 33745662826     PISSN: 00222623     EISSN: None     Source Type: Journal    
DOI: 10.1021/jm050885v     Document Type: Article
Times cited : (26)

References (44)
  • 1
    • 0015427721 scopus 로고
    • Methionine metabolism in mammals: Kinetic study of betaine-homocysteine methyltransferase
    • Finkelstein, J. D.; Harris, B. J.; Kyle, W. E. Methionine metabolism in mammals: kinetic study of betaine-homocysteine methyltransferase. Arch. Biochem. Biophys. 1972, 153, 320-324.
    • (1972) Arch. Biochem. Biophys. , vol.153 , pp. 320-324
    • Finkelstein, J.D.1    Harris, B.J.2    Kyle, W.E.3
  • 2
    • 0032147170 scopus 로고    scopus 로고
    • Human betaine-homocysteine methyltransferase is a zinc metalloenzyme
    • Millian, N. S.; Garrow, T. A. Human betaine-homocysteine methyltransferase is a zinc metalloenzyme. Arch. Biochem. Biophys. 1998, 356, 93-98.
    • (1998) Arch. Biochem. Biophys. , vol.356 , pp. 93-98
    • Millian, N.S.1    Garrow, T.A.2
  • 3
    • 0345624497 scopus 로고    scopus 로고
    • Recombinant human liver betaine-homocysteine S-methyltransferase: Identification of three cysteine residues critical for zinc binding
    • Breksa, A. P., III; Garrow, T. A. Recombinant human liver betaine-homocysteine S-methyltransferase: identification of three cysteine residues critical for zinc binding. Biochemistry 1999, 38, 13991-13998.
    • (1999) Biochemistry , vol.38 , pp. 13991-13998
    • Breksa III, A.P.1    Garrow, T.A.2
  • 5
    • 1942457281 scopus 로고    scopus 로고
    • Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding
    • Gonzalez, B.; Pajares, M. A.; Martinez-Ripoll, M.; Blundell, T. L.; Sanz-Aparicio, J. Crystal structure of rat liver betaine homocysteine S-methyltransferase reveals new oligomerization features and conformational changes upon substrate binding. J. Mol. Biol. 2004, 338, 771-782.
    • (2004) J. Mol. Biol. , vol.338 , pp. 771-782
    • Gonzalez, B.1    Pajares, M.A.2    Martinez-Ripoll, M.3    Blundell, T.L.4    Sanz-Aparicio, J.5
  • 6
    • 0032569165 scopus 로고    scopus 로고
    • Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine
    • Peariso, K.; Goulding, C. W.; Huang, S.; Matthews, R. G.; Penner-Hahn, J. E. Characterization of the zinc binding site in methionine synthase enzymes of Escherichia coli: The role of zinc in the methylation of homocysteine. J. Am. Chem. Soc. 1998, 120, 8410-8416.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 8410-8416
    • Peariso, K.1    Goulding, C.W.2    Huang, S.3    Matthews, R.G.4    Penner-Hahn, J.E.5
  • 7
    • 0035969951 scopus 로고    scopus 로고
    • Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy
    • Peariso, K.; Zhou, Z. S.; Smith, A. E.; Matthews, R. G.; Penner-Hahn, J. E. Characterization of the zinc sites in cobalamin-independent and cobalamin-dependent methionine synthase using zinc and selenium X-ray absorption spectroscopy. Biochemistry 2001, 40, 987-993.
    • (2001) Biochemistry , vol.40 , pp. 987-993
    • Peariso, K.1    Zhou, Z.S.2    Smith, A.E.3    Matthews, R.G.4    Penner-Hahn, J.E.5
  • 8
    • 2342498275 scopus 로고    scopus 로고
    • Oligomerization is required for betaine-homocysteine S-methyltransferase function
    • Szegedi, S. S.; Garrow, T. A. Oligomerization is required for betaine-homocysteine S-methyltransferase function. Arch. Biochem. Biophys. 2004, 426, 32-42.
    • (2004) Arch. Biochem. Biophys. , vol.426 , pp. 32-42
    • Szegedi, S.S.1    Garrow, T.A.2
  • 9
    • 0026045338 scopus 로고
    • Betaine-homocysteine methyltransferase: Organ distribution in man, pig and rat and subcellular distribution in the rat
    • McKeever, M. P.; Weir, D. G.; Molloy, A.; Scott, J. M. Betaine-homocysteine methyltransferase: organ distribution in man, pig and rat and subcellular distribution in the rat. Clin. Sci. 1991, 81, 551-556.
    • (1991) Clin. Sci. , vol.81 , pp. 551-556
    • McKeever, M.P.1    Weir, D.G.2    Molloy, A.3    Scott, J.M.4
  • 10
    • 11244327723 scopus 로고    scopus 로고
    • Osmotic regulation of renal betaine transport: Transcription and beyond
    • Kempson, S. A.; Montrose, M. H. Osmotic regulation of renal betaine transport: transcription and beyond. Pfluegers Arch. 2004, 449, 227-234.
    • (2004) Pfluegers Arch. , vol.449 , pp. 227-234
    • Kempson, S.A.1    Montrose, M.H.2
  • 11
    • 0031938727 scopus 로고    scopus 로고
    • Betaine as an osmolyte in rat liver: Metabolism and cell-to-cell interactions
    • Wettstein, M.; Weik, C.; Holneicher, C.; Häussinger, D. Betaine as an osmolyte in rat liver: metabolism and cell-to-cell interactions. Hepatology 1998, 27, 787-793.
    • (1998) Hepatology , vol.27 , pp. 787-793
    • Wettstein, M.1    Weik, C.2    Holneicher, C.3    Häussinger, D.4
  • 12
    • 4944244022 scopus 로고    scopus 로고
    • Neural control of hepatic osmolytes and parenchymal cell hydration
    • Haussinger, D. Neural control of hepatic osmolytes and parenchymal cell hydration. Anat. Rec., Part A 2004, 280, 893-900.
    • (2004) Anat. Rec., Part A , vol.280 , pp. 893-900
    • Haussinger, D.1
  • 13
    • 11144344914 scopus 로고    scopus 로고
    • High sodium chloride intake decreases betaine-homocysteine methyltransferase expression in guinea pig liver and kidney
    • Delgado-Reyes, C. V.; Garrow, T. A. High sodium chloride intake decreases betaine-homocysteine methyltransferase expression in guinea pig liver and kidney. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2005, 288, R182-R187.
    • (2005) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.288
    • Delgado-Reyes, C.V.1    Garrow, T.A.2
  • 15
    • 0037164104 scopus 로고    scopus 로고
    • Homocysteine and risk of ischemic heart disease and stroke: A meta-analysis
    • Homocysteine Studies Collaboration. Homocysteine and risk of ischemic heart disease and stroke: a meta-analysis. JAMA, J. Am. Med. Assoc. 2002, 288, 2015-2022.
    • (2002) JAMA, J. Am. Med. Assoc. , vol.288 , pp. 2015-2022
  • 16
    • 0032569645 scopus 로고    scopus 로고
    • Meta-analysis of hyperhomocysteinemia as a risk factor for venous thromboembolic disease
    • Ray, J. G. Meta-analysis of hyperhomocysteinemia as a risk factor for venous thromboembolic disease. Arch. Intern. Med. 1998, 158, 2101-2106.
    • (1998) Arch. Intern. Med. , vol.158 , pp. 2101-2106
    • Ray, J.G.1
  • 18
    • 0032771090 scopus 로고    scopus 로고
    • Folic acid and homocyst(e)ine metabolic defects and the risk of placental abruption, pre-eclampsia and spontaneous pregnancy loss: A systematic review
    • Ray, J. G.; Laskin, C. A. Folic acid and homocyst(e)ine metabolic defects and the risk of placental abruption, pre-eclampsia and spontaneous pregnancy loss: A systematic review. Placenta 1999, 20, 519-529.
    • (1999) Placenta , vol.20 , pp. 519-529
    • Ray, J.G.1    Laskin, C.A.2
  • 19
    • 0030299046 scopus 로고    scopus 로고
    • Folate, vitamin B-12, and neuropsychiatric disorders
    • Bottiglieri, T. Folate, vitamin B-12, and neuropsychiatric disorders. Nutr. Rev. 1996, 54, 382-390.
    • (1996) Nutr. Rev. , vol.54 , pp. 382-390
    • Bottiglieri, T.1
  • 22
    • 0021220516 scopus 로고
    • Methionine metabolism in mammals. Distribution of homocysteine between competing pathways
    • Finkelstein, J. D.; Martin, J. J. Methionine metabolism in mammals. Distribution of homocysteine between competing pathways. J. Biol. Chem. 1984, 259, 9508-9513.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9508-9513
    • Finkelstein, J.D.1    Martin, J.J.2
  • 23
    • 0036136732 scopus 로고    scopus 로고
    • S-adenosylmethionine: A control switch that regulates liver function
    • Mato, J. M.; Corrales, F. J.; Lu, S. C.; Avila, M. A. S-adenosylmethionine: a control switch that regulates liver function. FASEB J. 2002, 16, 15-26.
    • (2002) FASEB J. , vol.16 , pp. 15-26
    • Mato, J.M.1    Corrales, F.J.2    Lu, S.C.3    Avila, M.A.4
  • 25
    • 32144460483 scopus 로고    scopus 로고
    • Methionine dependence of tumours: A biochemical strategy for optimizing paclitaxel chemosensitivity in vitro
    • Pavillard, V.; Nicolaou, A.; Double, J. A.; Phillips, R. M. Methionine dependence of tumours: A biochemical strategy for optimizing paclitaxel chemosensitivity in vitro. Biochem. Pharmacol. 2006, 71, 772-778.
    • (2006) Biochem. Pharmacol. , vol.71 , pp. 772-778
    • Pavillard, V.1    Nicolaou, A.2    Double, J.A.3    Phillips, R.M.4
  • 26
    • 0034711007 scopus 로고    scopus 로고
    • The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes
    • Mosharov, E.; Cranford, M. R.; Banerjee, R. The quantitatively important relationship between homocysteine metabolism and glutathione synthesis by the transsulfuration pathway and its regulation by redox changes. Biochemistry 2000, 39, 13005-13011.
    • (2000) Biochemistry , vol.39 , pp. 13005-13011
    • Mosharov, E.1    Cranford, M.R.2    Banerjee, R.3
  • 27
    • 0021100297 scopus 로고
    • Evidence for direct methyl transfer in betaine: Homocysteine S-methyl-transferase
    • Awad, W. M., Jr.; Whitney, P. L.; Skiba, W. E.; Mangum, J. H.; Wells, M. S. Evidence for direct methyl transfer in betaine: homocysteine S-methyl-transferase. J. Biol. Chem. 1983, 258, 12790-12792.
    • (1983) J. Biol. Chem. , vol.258 , pp. 12790-12792
    • Awad Jr., W.M.1    Whitney, P.L.2    Skiba, W.E.3    Mangum, J.H.4    Wells, M.S.5
  • 28
    • 2442603566 scopus 로고    scopus 로고
    • Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis
    • Castro, C.; Gratson, A. A.; Evans, J. C.; Jiracek, J.; Collinsova, M.; Ludwig, M. L.; Garrow, T. A. Dissecting the catalytic mechanism of betaine-homocysteine S-methyltransferase by use of intrinsic tryptophan fluorescence and site-directed mutagenesis. Biochemistry 2004, 43, 5341-5351.
    • (2004) Biochemistry , vol.43 , pp. 5341-5351
    • Castro, C.1    Gratson, A.A.2    Evans, J.C.3    Jiracek, J.4    Collinsova, M.5    Ludwig, M.L.6    Garrow, T.A.7
  • 29
    • 0026593201 scopus 로고
    • Betaine:homocysteine methyltransferase from rat liver: Purification and inhibition by a boronic acid substrate analogue
    • Lee, K. H.; Cava, M.; Amiri, P.; Ottoboni, T.; Lindquist, R. N. Betaine:homocysteine methyltransferase from rat liver: Purification and inhibition by a boronic acid substrate analogue. Arch. Biochem. Biophys. 1992, 292, 77-86.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 77-86
    • Lee, K.H.1    Cava, M.2    Amiri, P.3    Ottoboni, T.4    Lindquist, R.N.5
  • 30
    • 0037330285 scopus 로고    scopus 로고
    • Combining combinatorial chemistry and affinity chromatography: Highly selective inhibitors of human betaine:homocysteine S-methyltransferase
    • Collinsova, M.; Castro, C.; Garrow, T. A.; Yiotakis, A.; Dive, V.; Jiracek, J. Combining combinatorial chemistry and affinity chromatography: highly selective inhibitors of human betaine:homocysteine S-methyltransferase. Chem. Biol. 2003, 10, 113-122.
    • (2003) Chem. Biol. , vol.10 , pp. 113-122
    • Collinsova, M.1    Castro, C.2    Garrow, T.A.3    Yiotakis, A.4    Dive, V.5    Jiracek, J.6
  • 31
    • 0038084224 scopus 로고    scopus 로고
    • Separation of diastereomers of phosphinic pseudopeptides by capillary zone electrophoresis and reverse phase high-performance liquid chromatography
    • Koval, D.; Kasicka, V.; Jiracek, J.; Collinsova, M. Separation of diastereomers of phosphinic pseudopeptides by capillary zone electrophoresis and reverse phase high-performance liquid chromatography. J. Sep. Sci. 2003, 26, 653-660.
    • (2003) J. Sep. Sci. , vol.26 , pp. 653-660
    • Koval, D.1    Kasicka, V.2    Jiracek, J.3    Collinsova, M.4
  • 32
    • 0037348835 scopus 로고    scopus 로고
    • Physicochemical characterization of phosphinic pseudopeptides by capillary zone electrophoresis in highly acid background electrolytes
    • Koval, D.; Kasicka, V.; Jiracek, J.; Collinsova, M. Physicochemical characterization of phosphinic pseudopeptides by capillary zone electrophoresis in highly acid background electrolytes. Electrophoresis 2003, 24, 774-781.
    • (2003) Electrophoresis , vol.24 , pp. 774-781
    • Koval, D.1    Kasicka, V.2    Jiracek, J.3    Collinsova, M.4
  • 33
    • 0037171626 scopus 로고    scopus 로고
    • Determination of dissociation constant of phosphinate group in phosphinic pseudopeptides by capillary zone electrophoresis
    • Koval, D.; Kasicka, V.; Jiracek, J.; Collinsova, M.; Garrow, T. A. Determination of dissociation constant of phosphinate group in phosphinic pseudopeptides by capillary zone electrophoresis. J. Chromatogr., B 2002, 770, 145-154.
    • (2002) J. Chromatogr., B , vol.770 , pp. 145-154
    • Koval, D.1    Kasicka, V.2    Jiracek, J.3    Collinsova, M.4    Garrow, T.A.5
  • 34
    • 0036181682 scopus 로고    scopus 로고
    • Analysis and characterization of phosphinic pseudopeptides by capillary zone electrophoresis
    • Koval, D.; Kasicka, V.; Jiracek, J.; Collinsova, M.; Garrow, T. A. Analysis and characterization of phosphinic pseudopeptides by capillary zone electrophoresis. Electrophoresis 2002, 23, 215-222.
    • (2002) Electrophoresis , vol.23 , pp. 215-222
    • Koval, D.1    Kasicka, V.2    Jiracek, J.3    Collinsova, M.4    Garrow, T.A.5
  • 35
    • 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. 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0023571453 scopus 로고
    • Design and synthesis of phosphonate inhibitors of glutamine synthetase
    • Farrington, G. K.; Kumar, A.; Wedler, F. C. Design and synthesis of phosphonate inhibitors of glutamine synthetase. J. Med. Chem. 1987, 30, 2062-2067.
    • (1987) J. Med. Chem. , vol.30 , pp. 2062-2067
    • Farrington, G.K.1    Kumar, A.2    Wedler, F.C.3
  • 38
    • 0034741936 scopus 로고    scopus 로고
    • 2′-C-Alkoxy and 2′-C-aryloxy derivatives of N-(2-phosphonomethoxyethyl)purines and -pyrimidines: Synthesis and biological activity
    • Rejman, D.; Masojidkova, M.; De Clercq, E.; Rosenberg, I. 2′-C-Alkoxy and 2′-C-aryloxy derivatives of N-(2- phosphonomethoxyethyl)purines and -pyrimidines: Synthesis and biological activity. Nucleosides, Nucleotides Nucleic Acids 2001, 20, 1497-1522.
    • (2001) Nucleosides, Nucleotides Nucleic Acids , vol.20 , pp. 1497-1522
    • Rejman, D.1    Masojidkova, M.2    De Clercq, E.3    Rosenberg, I.4
  • 39
    • 33745654167 scopus 로고
    • Reaction of N-hydroxymethylchloroacetamide with triethyl phosphite and some dialkyl chlorophosphites
    • Arbuzov, B. A.; Vinogradova, V. S.; Novoselskaja, A. D. Reaction of N-hydroxymethylchloroacetamide with triethyl phosphite and some dialkyl chlorophosphites. J. Gen. Chem. USSR (Engl. Transl.) 1967, 37, 2061-2065.
    • (1967) J. Gen. Chem. USSR (Engl. Transl.) , vol.37 , pp. 2061-2065
    • Arbuzov, B.A.1    Vinogradova, V.S.2    Novoselskaja, A.D.3
  • 40
    • 0029787429 scopus 로고    scopus 로고
    • Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase
    • Garrow, T. A. Purification, kinetic properties, and cDNA cloning of mammalian betaine-homocysteine methyltransferase. J. Biol. Chem. 1996, 271, 22831-22838.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22831-22838
    • Garrow, T.A.1
  • 41
    • 0018678175 scopus 로고
    • Reversible enzyme inhibition
    • Purich, D. L., Ed.; Academic Press: New York
    • Todhunter, J. A. Reversible enzyme inhibition. In Enzyme Kinetics and Mechanism: Purich, D. L., Ed.; Academic Press: New York, 1979; pp 383-411.
    • (1979) Enzyme Kinetics and Mechanism , pp. 383-411
    • Todhunter, J.A.1
  • 42
    • 0030695481 scopus 로고    scopus 로고
    • N-Dibenzylhospho-N′-3-(2,6-dichlorophenyl)propyl-guanidine is a bisubstrate-analogue for creatine kinase
    • Min, K.-L.; Steghens, J.-P.; Henry, R.; Doutheau, A.; Collombel, C. N-Dibenzylhospho-N′-3-(2,6-dichlorophenyl)propyl-guanidine is a bisubstrate-analogue for creatine kinase. Biochim. Biophys. Acta 1997, 1342, 83-89.
    • (1997) Biochim. Biophys. Acta , vol.1342 , pp. 83-89
    • Min, K.-L.1    Steghens, J.-P.2    Henry, R.3    Doutheau, A.4    Collombel, C.5


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