메뉴 건너뛰기




Volumn 92, Issue 7, 2010, Pages 858-868

A structure-activity study to identify novel and efficient substrates of the human semicarbazide-sensitive amine oxidase/VAP-1 enzyme

Author keywords

Computational docking; PH dependence; Semicarbazide sensitive amine oxidases; SSAO VAP 1 substrates; Structure function relationships

Indexed keywords

1,12 DODECANEDIAMINE; AMINE OXIDASE (COPPER CONTAINING); AMINE OXIDASE (FLAVIN CONTAINING); BENZYLAMINE; DODECANE; UNCLASSIFIED DRUG; VASCULAR ADHESION PROTEIN 1; AMINE; AOC3 PROTEIN, HUMAN; BUTANE; CELL ADHESION MOLECULE; PROTEIN BINDING; RECOMBINANT PROTEIN; SEMICARBAZIDE DERIVATIVE;

EID: 77953540713     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2010.03.006     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 0035422806 scopus 로고    scopus 로고
    • Cell surface monoamine oxidases: enzymes in search of a function
    • Jalkanen S., Salmi M. Cell surface monoamine oxidases: enzymes in search of a function. EMBO J. 2001, 20:3893-3901.
    • (2001) EMBO J. , vol.20 , pp. 3893-3901
    • Jalkanen, S.1    Salmi, M.2
  • 2
    • 0037199441 scopus 로고    scopus 로고
    • Catalytic mechanism of the topa quinone containing copper amine oxidases
    • Mure M., Mills S.A., Klinman J.P. Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry 2002, 41:9269-9278.
    • (2002) Biochemistry , vol.41 , pp. 9269-9278
    • Mure, M.1    Mills, S.A.2    Klinman, J.P.3
  • 3
    • 0029869337 scopus 로고    scopus 로고
    • Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects
    • Lyles G.A. Mammalian plasma and tissue-bound semicarbazide-sensitive amine oxidases: biochemical, pharmacological and toxicological aspects. Int. J. Cell Biol. 1996, 28:259-274.
    • (1996) Int. J. Cell Biol. , vol.28 , pp. 259-274
    • Lyles, G.A.1
  • 4
    • 38749138925 scopus 로고    scopus 로고
    • Multiple binding sites for substrates and modulators of semicarbazide-sensitive amine oxidase:kinetic consequences
    • Holt A., Smith D.J., Cendron L., Zanotti G., Rigo A., Di Paolo M.L. Multiple binding sites for substrates and modulators of semicarbazide-sensitive amine oxidase:kinetic consequences. Mol. Pharmacol. 2008, 73:525-538.
    • (2008) Mol. Pharmacol. , vol.73 , pp. 525-538
    • Holt, A.1    Smith, D.J.2    Cendron, L.3    Zanotti, G.4    Rigo, A.5    Di Paolo, M.L.6
  • 6
    • 37549031262 scopus 로고    scopus 로고
    • VAP-1 and CD73, endothelial cell surface enzymes in leukocyte extravasation
    • Jalkanen S., Salmi M. VAP-1 and CD73, endothelial cell surface enzymes in leukocyte extravasation. Arterioscler Thromb. Vasc. Biol. 2008, 28:18-26.
    • (2008) Arterioscler Thromb. Vasc. Biol. , vol.28 , pp. 18-26
    • Jalkanen, S.1    Salmi, M.2
  • 7
    • 0030909369 scopus 로고    scopus 로고
    • Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane
    • Morris N.J., Ducret A., Aebersold R., Ross S.A., Keller S.R., Lienhard G.E. Membrane amine oxidase cloning and identification as a major protein in the adipocyte plasma membrane. J. Biol. Chem. 1997, 267:9388-9392.
    • (1997) J. Biol. Chem. , vol.267 , pp. 9388-9392
    • Morris, N.J.1    Ducret, A.2    Aebersold, R.3    Ross, S.A.4    Keller, S.R.5    Lienhard, G.E.6
  • 8
    • 0035028044 scopus 로고    scopus 로고
    • Semicarbazide-sensitive amine oxidase substrate stimulate glucose transport and inhibits lypolysis in human adipocytes
    • Morin N., Lizcano J.M., Fontana E., et al. Semicarbazide-sensitive amine oxidase substrate stimulate glucose transport and inhibits lypolysis in human adipocytes. J. Pharmacol. Exp. Ther. 2001, 297:563-572.
    • (2001) J. Pharmacol. Exp. Ther. , vol.297 , pp. 563-572
    • Morin, N.1    Lizcano, J.M.2    Fontana, E.3
  • 9
    • 1242341261 scopus 로고    scopus 로고
    • Semicarbazide-sensitive amine oxidase activity exerts insulin-like effects on glucose metabolism and insulin-signaling pathways in adipose cells
    • Zorzano A., Abella A., Marti L., Carpéné C., Palacin M., Testar X. Semicarbazide-sensitive amine oxidase activity exerts insulin-like effects on glucose metabolism and insulin-signaling pathways in adipose cells. Biochim. Biophys. Acta 2003, 1647:3-9.
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 3-9
    • Zorzano, A.1    Abella, A.2    Marti, L.3    Carpéné, C.4    Palacin, M.5    Testar, X.6
  • 10
    • 0037380453 scopus 로고    scopus 로고
    • Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 activity exerts an antidiabetic action in Goto-Kakizaki rats
    • Abella A., Marti L., Camps M., et al. Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 activity exerts an antidiabetic action in Goto-Kakizaki rats. Diabetes 2003, 52:1004-1013.
    • (2003) Diabetes , vol.52 , pp. 1004-1013
    • Abella, A.1    Marti, L.2    Camps, M.3
  • 11
    • 33847018785 scopus 로고    scopus 로고
    • Oral insulin-mimetic compounds that act independently of insulin
    • Garcia-Vicente S., Yraola F., Marti L., et al. Oral insulin-mimetic compounds that act independently of insulin. Diabetes 2007, 56:486-493.
    • (2007) Diabetes , vol.56 , pp. 486-493
    • Garcia-Vicente, S.1    Yraola, F.2    Marti, L.3
  • 13
    • 52049102508 scopus 로고    scopus 로고
    • Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1: recent developments concerning substrates and inhibitors of a promising therapeutic target
    • Dunkel P., Gelain A., Barlocco D., et al. Semicarbazide-sensitive amine oxidase/vascular adhesion protein-1: recent developments concerning substrates and inhibitors of a promising therapeutic target. Curr. Med. Chem. 2008, 15:1827-1839.
    • (2008) Curr. Med. Chem. , vol.15 , pp. 1827-1839
    • Dunkel, P.1    Gelain, A.2    Barlocco, D.3
  • 14
    • 0027462875 scopus 로고
    • Oxidative deamination of methylamine by semicarbazide-sensitive amine oxidase lead to cytotoxic damage in endothelial cells. Possible consequences for diabetes
    • Yu P.H., Zuo D.M. Oxidative deamination of methylamine by semicarbazide-sensitive amine oxidase lead to cytotoxic damage in endothelial cells. Possible consequences for diabetes. Diabetes 1993, 42:594-603.
    • (1993) Diabetes , vol.42 , pp. 594-603
    • Yu, P.H.1    Zuo, D.M.2
  • 15
    • 0036033536 scopus 로고    scopus 로고
    • Semicarbazide-sensitive amine oxidase in aortic smooth muscle cells mediates synthesis of a methylglyoxal-AGE: implications for vascular complications in diabetes
    • Mathys K.C., Ponnampalam S.N., Padival S., Nagaraj R.H. Semicarbazide-sensitive amine oxidase in aortic smooth muscle cells mediates synthesis of a methylglyoxal-AGE: implications for vascular complications in diabetes. Biochem. Biophys. Res. Commun. 2002, 297:863-869.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 863-869
    • Mathys, K.C.1    Ponnampalam, S.N.2    Padival, S.3    Nagaraj, R.H.4
  • 16
    • 4544262245 scopus 로고    scopus 로고
    • Exploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity
    • Marti L., Abella A., De la Cruz X., Garcia-Vicente S., et al. Exploring the binding mode of semicarbazide-sensitive amine oxidase/VAP-1: identification of novel substrates with insulin-like activity. J. Med. Chem. 2004, 47:4865-4874.
    • (2004) J. Med. Chem. , vol.47 , pp. 4865-4874
    • Marti, L.1    Abella, A.2    De la Cruz, X.3    Garcia-Vicente, S.4
  • 17
    • 0346040359 scopus 로고    scopus 로고
    • Synthesis of 4-methyl-thio-phenyl-propylamine and the evaluation of its interaction with different amine oxidases
    • Gallardo-Godoy A., Hernandez M., Sanz E., Unzeta M. Synthesis of 4-methyl-thio-phenyl-propylamine and the evaluation of its interaction with different amine oxidases. Bioorg. Med. Chem. 2004, 12:273-279.
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 273-279
    • Gallardo-Godoy, A.1    Hernandez, M.2    Sanz, E.3    Unzeta, M.4
  • 18
    • 33750138764 scopus 로고    scopus 로고
    • New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: analysis by SARs and omputaional docking
    • Yraola F., Garcia-Vicente S., Fernandez-Recio J., et al. New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: analysis by SARs and omputaional docking. J. Med. Chem. 2006, 49:6197-6208.
    • (2006) J. Med. Chem. , vol.49 , pp. 6197-6208
    • Yraola, F.1    Garcia-Vicente, S.2    Fernandez-Recio, J.3
  • 19
    • 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
  • 20
    • 0031573408 scopus 로고    scopus 로고
    • A one-step fluorimetric method for the continuous measurement of monoamine oxidase activity
    • Zhou M., Panchuck-Voloshina N.A. A one-step fluorimetric method for the continuous measurement of monoamine oxidase activity. Anal. Biochem. 1997, 253:169-174.
    • (1997) Anal. Biochem. , vol.253 , pp. 169-174
    • Zhou, M.1    Panchuck-Voloshina, N.A.2
  • 21
    • 0028202998 scopus 로고
    • A sensitive spectrophotometry-based method for the determination of the rate of hydrogen peroxide generation in biological systems
    • Di Paolo M.L., Scarpa M., Rigo A. A sensitive spectrophotometry-based method for the determination of the rate of hydrogen peroxide generation in biological systems. J. Biochem. Biophys. Methods 1994, 28:205-214.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 205-214
    • Di Paolo, M.L.1    Scarpa, M.2    Rigo, A.3
  • 22
    • 0014954224 scopus 로고
    • Mechanistic studies of beef plasma amine oxidase
    • Oi S., Inamasu M., Yasunobu K.T. Mechanistic studies of beef plasma amine oxidase. Biochemistry 1970, 9:3378-3383.
    • (1970) Biochemistry , vol.9 , pp. 3378-3383
    • Oi, S.1    Inamasu, M.2    Yasunobu, K.T.3
  • 23
    • 34250857669 scopus 로고    scopus 로고
    • The effect of buffer cations on interactions between mammalian copper-containing amine oxidases and their substrates
    • Holt A., Degenhardt O.S., Berry P.D., et al. The effect of buffer cations on interactions between mammalian copper-containing amine oxidases and their substrates. J. Neural. Transm 2007, 114:733-741.
    • (2007) J. Neural. Transm , vol.114 , pp. 733-741
    • Holt, A.1    Degenhardt, O.S.2    Berry, P.D.3
  • 25
    • 0022366913 scopus 로고
    • Solvent isotope effects and the pH dependence of laccase activity under steady-state conditions
    • Koudelka G.B., Hansen F.B., Ettinger M.J. Solvent isotope effects and the pH dependence of laccase activity under steady-state conditions. J. Biol. Chem. 1985, 260:15561-15565.
    • (1985) J. Biol. Chem. , vol.260 , pp. 15561-15565
    • Koudelka, G.B.1    Hansen, F.B.2    Ettinger, M.J.3
  • 27
    • 0031021044 scopus 로고    scopus 로고
    • The effect of ionic strength and specific anions on substrate binding and hydrolytic activities of Na, K-ATPase
    • Norby J., Esmann M. The effect of ionic strength and specific anions on substrate binding and hydrolytic activities of Na, K-ATPase. J. Gen. Physiol. 1997, 109:555-570.
    • (1997) J. Gen. Physiol. , vol.109 , pp. 555-570
    • Norby, J.1    Esmann, M.2
  • 28
    • 11644261806 scopus 로고    scopus 로고
    • Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function
    • Morris G.M., Goodsell D.S., Halliday R.S., et al. Automated docking using a Lamarckian genetic algorithm and an empirical binding free energy function. J. Comput. Chem. 1998, 19:1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, R.S.3
  • 29
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • Singh U.C., Kollman P.A. An approach to computing electrostatic charges for molecules. J. Comput. Chem. 1984, 5:129-145.
    • (1984) J. Comput. Chem. , vol.5 , pp. 129-145
    • Singh, U.C.1    Kollman, P.A.2
  • 30
    • 3042524904 scopus 로고
    • A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model
    • Bayly C.I., Cieplak P., Cornell W.D., Kollman P.A. A well-behaved electrostatic potential based method using charge restraints for deriving atomic charges: the RESP model. J. Phys. Chem. 1993, 97:10269-10280.
    • (1993) J. Phys. Chem. , vol.97 , pp. 10269-10280
    • Bayly, C.I.1    Cieplak, P.2    Cornell, W.D.3    Kollman, P.A.4
  • 31
    • 49149147973 scopus 로고
    • Iterative partial equalization of orbital electronegativity - a rapid access to atomic charges
    • Gasteiger J., Marsili M. Iterative partial equalization of orbital electronegativity - a rapid access to atomic charges. Tetrahedron 1980, 36:3219-3228.
    • (1980) Tetrahedron , vol.36 , pp. 3219-3228
    • Gasteiger, J.1    Marsili, M.2
  • 33
    • 0029011701 scopus 로고
    • A second generation force field for the simulation of proteins, nucleic acids, and organic molecules
    • Cornell W.D., P.Cieplak, Bayly C.I., et al. A second generation force field for the simulation of proteins, nucleic acids, and organic molecules. J. Am. Chem. Soc. 1995, 117:5179-5197.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 5179-5197
    • Cornell, W.D.1    P.Cieplak2    Bayly, C.I.3
  • 34
    • 77953542353 scopus 로고    scopus 로고
    • DeLano Scientific LLC, South San Francisco, CA
    • DeLano W.L. PyMOL Incentive Product 2006, DeLano Scientific LLC, South San Francisco, CA.
    • (2006) PyMOL Incentive Product
    • DeLano, W.L.1
  • 35
    • 1642309250 scopus 로고    scopus 로고
    • Molecular basis for the binding of competitive inhibitors of maize polyamine oxidase
    • Cona A., Manetti F., Leone R., et al. Molecular basis for the binding of competitive inhibitors of maize polyamine oxidase. Biochemistry 2004, 43:3426-3435.
    • (2004) Biochemistry , vol.43 , pp. 3426-3435
    • Cona, A.1    Manetti, F.2    Leone, R.3
  • 36
    • 33644785135 scopus 로고    scopus 로고
    • Inhibition of polyamine and spermine oxidases by polyamine analogues
    • Bianchi M., Polticelli F., Ascenzi P., et al. Inhibition of polyamine and spermine oxidases by polyamine analogues. FEBS J. 2006, 273:1115-1123.
    • (2006) FEBS J. , vol.273 , pp. 1115-1123
    • Bianchi, M.1    Polticelli, F.2    Ascenzi, P.3
  • 37
    • 0025887806 scopus 로고
    • Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism
    • Hartman C., Klinman J.P. Structure-function studies of substrate oxidation by bovine serum amine oxidase: relationship to cofactor structure and mechanism. Biochemistry 1991, 30:4605-4611.
    • (1991) Biochemistry , vol.30 , pp. 4605-4611
    • Hartman, C.1    Klinman, J.P.2
  • 38
    • 0037626151 scopus 로고    scopus 로고
    • Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates
    • Di Paolo M.L., Stevanato R., Corazza A., et al. Electrostatic compared with hydrophobic interactions between bovine serum amine oxidase and its substrates. Biochem. J. 2003, 371:549-556.
    • (2003) Biochem. J. , vol.371 , pp. 549-556
    • Di Paolo, M.L.1    Stevanato, R.2    Corazza, A.3
  • 39
    • 34548042737 scopus 로고    scopus 로고
    • N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: a kinetic and spectroscopic study
    • Di Paolo M.L., Pesce C., Lunelli M., Scarpa M., Rigo A. N-alkanamines as substrates to probe the hydrophobic region of bovine serum amine oxidase active site: a kinetic and spectroscopic study. Arch. Biochem. Biophys. 2007, 465:50-60.
    • (2007) Arch. Biochem. Biophys. , vol.465 , pp. 50-60
    • Di Paolo, M.L.1    Pesce, C.2    Lunelli, M.3    Scarpa, M.4    Rigo, A.5
  • 40
  • 41
    • 0036942343 scopus 로고    scopus 로고
    • Human kidney diamine oxidase: heterologous expression, purification, and characterization
    • Elmore B.O., Bollinger J.A., Dooley D.M. Human kidney diamine oxidase: heterologous expression, purification, and characterization. J. Biol. Inorg. Chem. 2002, 6:565-579.
    • (2002) J. Biol. Inorg. Chem. , vol.6 , pp. 565-579
    • Elmore, B.O.1    Bollinger, J.A.2    Dooley, D.M.3
  • 42
    • 70350064739 scopus 로고    scopus 로고
    • Structure and inhibition of human diamine oxidase
    • McGrath A.P., Hilmer K.M., Collyer C.A., et al. Structure and inhibition of human diamine oxidase. Biochemistry 2009, 48:9810-9822.
    • (2009) Biochemistry , vol.48 , pp. 9810-9822
    • McGrath, A.P.1    Hilmer, K.M.2    Collyer, C.A.3
  • 44
    • 33845664843 scopus 로고    scopus 로고
    • Inhibition of plant amine oxidases by novel series of diamine derivatives
    • Stánská J., Šebela M., Tarkowski P., et al. Inhibition of plant amine oxidases by novel series of diamine derivatives. Biochimie 2007, 89:135-144.
    • (2007) Biochimie , vol.89 , pp. 135-144
    • Stánská, J.1    Šebela, M.2    Tarkowski, P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.