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Volumn 39, Issue 10, 2011, Pages 1939-1945

Characterization and crystallization of mouse aldehyde oxidase 3: From mouse liver to Escherichia coli heterologous protein expression

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE OXIDASE; ALDEHYDE OXIDASE 3; DIMER; IRON; IRON SULFUR PROTEIN; MOLYBDENUM; RECOMBINANT ALDEHYDE OXIDASE 3; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

EID: 80053139530     PISSN: 00909556     EISSN: 1521009X     Source Type: Journal    
DOI: 10.1124/dmd.111.040873     Document Type: Article
Times cited : (32)

References (34)
  • 1
    • 36949026168 scopus 로고    scopus 로고
    • Construction and expression of mutant cDNAs responsible for genetic polymorphism in aldehyde oxidase in donryu strain rats
    • Adachi M, Itoh K, Masubuchi A, Watanabe N, and Tanaka Y (2007) Construction and expression of mutant cDNAs responsible for genetic polymorphism in aldehyde oxidase in Donryu strain rats. J Biochem Mol Biol 40:1021-1027. (Pubitemid 350242290)
    • (2007) Journal of Biochemistry and Molecular Biology , vol.40 , Issue.6 , pp. 1021-1027
    • Adachi, M.1    Itoh, K.2    Masubuchi, A.3    Watanabe, N.4    Tanaka, Y.5
  • 2
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 74949128363 scopus 로고    scopus 로고
    • The use of ionic liquids as crystallization additives allowed to overcome nanodrop scaling up problems: A success case for producing diffractionquality crystals of nitrate reductase
    • Coelho C, Trincão J, and Romão MJ (2010) The use of ionic liquids as crystallization additives allowed to overcome nanodrop scaling up problems: a success case for producing diffractionquality crystals of nitrate reductase. J Cryst Growth 312:714-719.
    • (2010) J Cryst Growth , vol.312 , pp. 714-719
    • Coelho, C.1    Trincão, J.2    Romão, M.J.3
  • 5
    • 79960719085 scopus 로고    scopus 로고
    • Increasing recognition of the importance of aldehyde oxidase in drug development and discovery
    • doi:10.3109/03602532.2011.560606
    • Garattini E and Terao M (2011) Increasing recognition of the importance of aldehyde oxidase in drug development and discovery. Drug Metab Rev doi:10.3109/03602532.2011.560606.
    • (2011) Drug Metab Rev
    • Garattini, E.1    Terao, M.2
  • 6
    • 42449117257 scopus 로고    scopus 로고
    • Mammalian aldehyde oxidases: Genetics, evolution and biochemistry
    • Garattini E, Fratelli M, and Terao M (2008) Mammalian aldehyde oxidases: genetics, evolution and biochemistry. Cell Mol Life Sci 65:1019-1048.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1019-1048
    • Garattini, E.1    Fratelli, M.2    Terao, M.3
  • 7
    • 0037954564 scopus 로고    scopus 로고
    • Mammalian molybdo-flavoenzymes, an expanding family of proteins: Structure, genetics, regulation, function and pathophysiology
    • DOI 10.1042/BJ20030121
    • Garattini E, Mendel R, Romão MJ, Wright R, and Terao M (2003) Mammalian molybdoflavoenzymes, an expanding family of proteins: structure, genetics, regulation, function and pathophysiology. Biochem J 372:15-32. (Pubitemid 36609603)
    • (2003) Biochemical Journal , vol.372 , Issue.1 , pp. 15-32
    • Garattini, E.1    Mendel, R.2    Romao, M.J.3    Wright, R.4    Terao, M.5
  • 8
    • 0000273676 scopus 로고    scopus 로고
    • The Mononuclear Molybdenum Enzymes
    • Hille R (1996) The Mononuclear Molybdenum Enzymes. Chem Rev 96:2757-2816.
    • (1996) Chem Rev , vol.96 , pp. 2757-2816
    • Hille, R.1
  • 9
    • 0033560621 scopus 로고    scopus 로고
    • Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli
    • DOI 10.1006/abbi.1999.1129
    • Huang DY, Furukawa A, and Ichikawa Y (1999) Molecular cloning of retinal oxidase/aldehyde oxidase cDNAs from rabbit and mouse livers and functional expression of recombinant mouse retinal oxidase cDNA in Escherichia coli. Arch Biochem Biophys 364:264-272. (Pubitemid 29394280)
    • (1999) Archives of Biochemistry and Biophysics , vol.364 , Issue.2 , pp. 264-272
    • Huang, D.-Y.1    Furukawa, A.2    Ichikawa, Y.3
  • 10
    • 0018175048 scopus 로고
    • Aldehyde oxidase and xanthine oxidase-functional and evolutionary relationships
    • Krenitsky TA (1978) Aldehyde oxidase and xanthine oxidase-functional and evolutionary relationships. Biochem Pharmacol 27:2763-2764.
    • (1978) Biochem Pharmacol , vol.27 , pp. 2763-2764
    • Krenitsky, T.A.1
  • 11
    • 0015359969 scopus 로고
    • A comparison of the specificities of xanthine oxidase and aldehyde oxidase
    • Krenitsky TA, Neil SM, Elion GB, and Hitchings GH (1972) A comparison of the specificities of xanthine oxidase and aldehyde oxidase. Arch Biochem Biophys 150:585-599.
    • (1972) Arch Biochem Biophys , vol.150 , pp. 585-599
    • Krenitsky, T.A.1    Neil, S.M.2    Elion, G.B.3    Hitchings, G.H.4
  • 12
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of phage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of phage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0014963075 scopus 로고
    • On the mechanism of inactivation of xanthine oxidase by cyanide
    • Massey V and Edmondson D (1970) On the mechanism of inactivation of xanthine oxidase by cyanide. J Biol Chem 245:6595-6598.
    • (1970) J Biol Chem , vol.245 , pp. 6595-6598
    • Massey, V.1    Edmondson, D.2
  • 16
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews BW (1968) Solvent content of protein crystals. J Mol Biol 33:491-497.
    • (1968) J Mol Biol , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 17
    • 44949262935 scopus 로고    scopus 로고
    • Mammalian xanthine oxidoreductase - Mechanism of transition from xanthine dehydrogenase to xanthine oxidase
    • DOI 10.1111/j.1742-4658.2008.06489.x
    • Nishino T, Okamoto K, Eger BT, Pai EF, and Nishino T (2008) Mammalian xanthine oxidoreductase - mechanism of transition from xanthine dehydrogenase to xanthine oxidase. FEBS J 275:3278-3289. (Pubitemid 351813552)
    • (2008) FEBS Journal , vol.275 , Issue.13 , pp. 3278-3289
    • Nishino, T.1    Okamoto, K.2    Eger, B.T.3    Pai, E.F.4    Nishino, T.5
  • 18
    • 46749134762 scopus 로고    scopus 로고
    • Mechanism of inhibition of xanthine oxidoreductase by allopurinol: Crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol
    • DOI 10.1080/15257770802146577, PII 794699692
    • Okamoto K, Eger BT, Nishino T, Pai EF, and Nishino T (2008) Mechanism of inhibition of xanthine oxidoreductase by allopurinol: crystal structure of reduced bovine milk xanthine oxidoreductase bound with oxipurinol. Nucleosides Nucleotides Nucleic Acids 27:888-893. (Pubitemid 351948548)
    • (2008) Nucleosides, Nucleotides and Nucleic Acids , vol.27 , Issue.6-7 , pp. 888-893
    • Okamoto, K.1    Eger, B.T.2    Nishino, T.3    Pai, E.F.4    Nishino, T.5
  • 19
    • 0029882611 scopus 로고    scopus 로고
    • Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli
    • DOI 10.1111/j.1365-2958.1996.tb02525.x
    • Palmer T, Santini CL, Iobbi-Nivol C, Eaves DJ, Boxer DH, and Giordano G (1996) Involvement of the narJ and mob gene products in distinct steps in the biosynthesis of the molybdoenzyme nitrate reductase in Escherichia coli. Mol Microbiol 20:875-884. (Pubitemid 26174891)
    • (1996) Molecular Microbiology , vol.20 , Issue.4 , pp. 875-884
    • Palmer, T.1    Santini, C.-L.2    Iobbi-Nivol, C.3    Eaves, D.J.4    Boxer, D.H.5    Giordano, G.6
  • 20
    • 0035846965 scopus 로고    scopus 로고
    • Xanthine dehydrogenase from Pseudomonas putida 86: Specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization
    • DOI 10.1016/S0167-4838(00)00214-4, PII S0167483800002144
    • Parschat K, Canne C, Hüttermann J, Kappl R, and Fetzner S (2001) Xanthine dehydrogenase from Pseudomonas putida 86: specificity, oxidation-reduction potentials of its redox-active centers, and first EPR characterization. Biochim Biophys Acta 1544:151-165. (Pubitemid 32121854)
    • (2001) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1544 , Issue.1-2 , pp. 151-165
    • Parschat, K.1    Canne, C.2    Huttermann, J.3    Kappl, R.4    Fetzner, S.5
  • 21
    • 0026707916 scopus 로고
    • Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii
    • Pérez-Vicente R, Alamillo JM, Cárdenas J, and Pineda M (1992) Purification and substrate inactivation of xanthine dehydrogenase from Chlamydomonas reinhardtii. Biochim Biophys Acta 1117:159-166.
    • (1992) Biochim Biophys Acta , vol.1117 , pp. 159-166
    • Pérez-Vicente, R.1    Alamillo, J.M.2    Cárdenas, J.3    Pineda, M.4
  • 22
    • 78650379608 scopus 로고    scopus 로고
    • Aldehyde oxidase: An enzyme of emerging importance in drug discovery
    • Pryde DC, Dalvie D, Hu Q, Jones P, Obach RS, and Tran TD (2010) Aldehyde oxidase: an enzyme of emerging importance in drug discovery. J Med Chem 53:8441-8460.
    • (2010) J Med Chem , vol.53 , pp. 8441-8460
    • Pryde, D.C.1    Dalvie, D.2    Hu, Q.3    Jones, P.4    Obach, R.S.5    Tran, T.D.6
  • 23
    • 79951480123 scopus 로고    scopus 로고
    • R Development Core Team R Foundation for Statistical Computing, Vienna, Austria
    • R Development Core Team (2010) R: A Language and Environment for Statistical Computing, R Foundation for Statistical Computing, Vienna, Austria.
    • (2010) R: A Language and Environment for Statistical Computing
  • 24
    • 45749124348 scopus 로고    scopus 로고
    • The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins
    • DOI 10.1021/bi800477u
    • Schmitz J, Chowdhury MM, Hänzelmann P, Nimtz M, Lee EY, Schindelin H, and Leimkühler S (2008) The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry 47:6479-6489. (Pubitemid 351874239)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6479-6489
    • Schmitz, J.1    Chowdhury, M.M.2    Hanzelmann, P.3    Nimtz, M.4    Lee, E.-Y.5    Schindelin, H.6    Leimkuhler, S.7
  • 27
    • 0001651375 scopus 로고
    • Novel method for accurate g measurements in electron-spin resonance
    • Stesmans A and Van Gorp G (1989) Novel method for accurate g measurements in electron-spin resonance. Rev Sci Instrum 60:2949-2952.
    • (1989) Rev Sci Instrum , vol.60 , pp. 2949-2952
    • Stesmans, A.1    Van Gorp, G.2
  • 28
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • DOI 10.1016/j.jmr.2005.08.013, PII S1090780705002892
    • Stoll S and Schweiger A (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178:42-55. (Pubitemid 41774010)
    • (2006) Journal of Magnetic Resonance , vol.178 , Issue.1 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 29
    • 0034669320 scopus 로고    scopus 로고
    • Optimization of expression of human sulfite oxidase and its molybdenum domain
    • Temple CA, Graf TN, and Rajagopalan KV (2000) Optimization of expression of human sulfite oxidase and its molybdenum domain. Arch Biochem Biophys 383:281-287.
    • (2000) Arch Biochem Biophys , vol.383 , pp. 281-287
    • Temple, C.A.1    Graf, T.N.2    Rajagopalan, K.V.3
  • 31
    • 0035824605 scopus 로고    scopus 로고
    • Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1
    • Terao M, Kurosaki M, Marini M, Vanoni MA, Saltini G, Bonetto V, Bastone A, Federico C, Saccone S, Fanelli R, et al. (2001) Purification of the aldehyde oxidase homolog 1 (AOH1) protein and cloning of the AOH1 and aldehyde oxidase homolog 2 (AOH2) genes. Identification of a novel molybdo-flavoprotein gene cluster on mouse chromosome 1. J Biol Chem 276:46347-46363.
    • (2001) J Biol Chem , vol.276 , pp. 46347-46363
    • Terao, M.1    Kurosaki, M.2    Marini, M.3    Vanoni, M.A.4    Saltini, G.5    Bonetto, V.6    Bastone, A.7    Federico, C.8    Saccone, S.9    Fanelli, R.10
  • 32
    • 1542365400 scopus 로고    scopus 로고
    • Regulation and biochemistry of mouse molybdo-flavoenzymes: The DBA/2 mouse is selectively deficient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purification and characterization of aldehyde oxidase
    • DOI 10.1074/jbc.M308137200
    • Vila R, Kurosaki M, Barzago MM, Kolek M, Bastone A, Colombo L, Salmona M, Terao M, and Garattini E (2004) Regulation and biochemistry of mouse molybdo-flavoenzymes. The DBA/2 mouse is selectively deficient in the expression of aldehyde oxidase homologues 1 and 2 and represents a unique source for the purification and characterization of aldehyde oxidase. J Biol Chem 279:8668-8683. (Pubitemid 38295922)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8668-8683
    • Vila, R.1    Kurosaki, M.2    Barzago, M.M.3    Kolek, M.4    Bastone, A.5    Colombo, L.6    Salmona, M.7    Terao, M.8    Garattini, E.9
  • 33
    • 0020478588 scopus 로고
    • Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases
    • Wahl RC and Rajagopalan KV (1982) Evidence for the inorganic nature of the cyanolyzable sulfur of molybdenum hydroxylases. J Biol Chem 257:1354-1359.
    • (1982) J Biol Chem , vol.257 , pp. 1354-1359
    • Wahl, R.C.1    Rajagopalan, K.V.2
  • 34
    • 0020478852 scopus 로고
    • Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases
    • Wahl RC, Warner CK, Finnerty V, and Rajagopalan KV (1982) Drosophila melanogaster ma-l mutants are defective in the sulfuration of desulfo Mo hydroxylases. J Biol Chem 257:3958-3962.
    • (1982) J Biol Chem , vol.257 , pp. 3958-3962
    • Wahl, R.C.1    Warner, C.K.2    Finnerty, V.3    Rajagopalan, K.V.4


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