메뉴 건너뛰기




Volumn 1824, Issue 5, 2012, Pages 701-710

Differences in amino acid residues in the binding pockets dictate substrate specificities of mouse senescence marker protein-30, human paraoxonase1, and squid diisopropylfluorophosphatase

Author keywords

Catalytic bioscavenger; DFP; Human PON1; Molecular docking; Mouse SMP 30; Squid DFPase

Indexed keywords

AMINO ACID; ARYLDIALKYLPHOSPHATASE 1; CYCLOSARIN; DIISOPROPYL FLUOROPHOSPHATASE; ESTER DERIVATIVE; GLUCONIC ACID; LACTONE DERIVATIVE; METAL ION; REGUCALCIN; SARIN; SOMAN; TABUN;

EID: 84860304042     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2012.02.007     Document Type: Article
Times cited : (17)

References (39)
  • 1
    • 0000249736 scopus 로고
    • Anticholinesterase agents
    • A.G. Gilman, L.S. Goodman, T.W. Rail, F. Murand, Macmillan New York
    • P. Taylor, A.G. Gilman, and L.S. Goodman Anticholinesterase agents A.G. Gilman, L.S. Goodman, T.W. Rail, F. Murand, The Pharmacological Basis of Therapeutics 1985 Macmillan New York 10 129
    • (1985) The Pharmacological Basis of Therapeutics , pp. 10-129
    • Taylor, P.1    Gilman, A.G.2    Goodman, L.S.3
  • 2
    • 0018420337 scopus 로고
    • Relationship between inhibition of acetylcholinesterase and response of the rat phrenic nerve-diaphragm preparation to indirect stimulation at higher frequencies
    • P.F. Heffron, and F. Hobbiger Relationship between inhibition of acetylcholinesterase and response of the rat phrenic nerve-diaphragm preparation to indirect stimulation at higher frequencies Br. J. Pharmacol. 66 1979 323 329
    • (1979) Br. J. Pharmacol. , vol.66 , pp. 323-329
    • Heffron, P.F.1    Hobbiger, F.2
  • 3
    • 0014316316 scopus 로고
    • Effect of a cholinesterase inhibitor when injected into the medulla of the rabbit
    • W.C. Stewart, and E.A. Anderson Effect of a cholinesterase inhibitor when injected into the medulla of the rabbit J. Pharmacol. Exp. Ther. 162 1968 309 318
    • (1968) J. Pharmacol. Exp. Ther. , vol.162 , pp. 309-318
    • Stewart, W.C.1    Anderson, E.A.2
  • 6
    • 0025117439 scopus 로고
    • Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta
    • D.P. Dumas, H.D. Durst, W.G. Landis, F.M. Raushel, and J.R. Wild Inactivation of organophosphorus nerve agents by the phosphotriesterase from Pseudomonas diminuta Arch. Biochem. Biophys. 277 1990 155 159
    • (1990) Arch. Biochem. Biophys. , vol.277 , pp. 155-159
    • Dumas, D.P.1    Durst, H.D.2    Landis, W.G.3    Raushel, F.M.4    Wild, J.R.5
  • 8
    • 0034972434 scopus 로고    scopus 로고
    • Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris
    • E.I. Scharff, J. Koepke, G. Fritzsch, C. Lucke, and H. Ruterjans Crystal structure of diisopropylfluorophosphatase from Loligo vulgaris Structure 9 2001 493 502
    • (2001) Structure , vol.9 , pp. 493-502
    • Scharff, E.I.1    Koepke, J.2    Fritzsch, G.3    Lucke, C.4    Ruterjans, H.5
  • 9
    • 0027248068 scopus 로고
    • A purified recombinant organophosphorus acid anhydrase protects mice against soman
    • C.A. Broomfield A purified recombinant organophosphorus acid anhydrase protects mice against soman Chem. Biol. Interact. 87 1993 279 284
    • (1993) Chem. Biol. Interact. , vol.87 , pp. 279-284
    • Broomfield, C.A.1
  • 10
    • 0025923560 scopus 로고
    • Prophylaxis against organophosphate poisoning by an enzyme hydrolysing organophosphorus compounds in mice
    • Y. Ashani, N. Rothschild, Y. Segall, D. Levanon, and L. Raveh Prophylaxis against organophosphate poisoning by an enzyme hydrolysing organophosphorus compounds in mice Life Sci. 49 1991 367 374
    • (1991) Life Sci. , vol.49 , pp. 367-374
    • Ashani, Y.1    Rothschild, N.2    Segall, Y.3    Levanon, D.4    Raveh, L.5
  • 11
    • 0026696934 scopus 로고
    • Protection against tabun toxicity in mice by prophylaxis with an enzyme hydrolyzing organophosphate esters
    • L. Raveh, Y. Segall, H. Leader, N. Rothschild, D. Levanon, Y. Henis, and Y. Ashani Protection against tabun toxicity in mice by prophylaxis with an enzyme hydrolyzing organophosphate esters Biochem. Pharmacol. 44 1992 397 400
    • (1992) Biochem. Pharmacol. , vol.44 , pp. 397-400
    • Raveh, L.1    Segall, Y.2    Leader, H.3    Rothschild, N.4    Levanon, D.5    Henis, Y.6    Ashani, Y.7
  • 12
    • 0024501160 scopus 로고
    • Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP)
    • J.S. Little, C.A. Broomfield, M.K. Fox-Talbot, L.J. Boucher, B. MacIver, and D.E. Lenz Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP) Biochem. Pharmacol. 38 1989 23 29
    • (1989) Biochem. Pharmacol. , vol.38 , pp. 23-29
    • Little, J.S.1    Broomfield, C.A.2    Fox-Talbot, M.K.3    Boucher, L.J.4    MacIver, B.5    Lenz, D.E.6
  • 14
    • 0030608048 scopus 로고    scopus 로고
    • Isolation and characterization of genomic and cDNA clones encoding mouse senescence marker protein-30 (SMP30)
    • T. Fujita, T. Shirasawa, and N. Maruyama Isolation and characterization of genomic and cDNA clones encoding mouse senescence marker protein-30 (SMP30) Biochim. Biophys. Acta 1308 1996 49 57
    • (1996) Biochim. Biophys. Acta , vol.1308 , pp. 49-57
    • Fujita, T.1    Shirasawa, T.2    Maruyama, N.3
  • 15
    • 84954358029 scopus 로고    scopus 로고
    • The first crystal structure of gluconolactonase important in the glucose secondary metabolic pathways
    • C.N. Chen, K.H. Chin, A.H. Wang, and S.H. Chou The first crystal structure of gluconolactonase important in the glucose secondary metabolic pathways J. Mol. Biol. 384 2008 604 614
    • (2008) J. Mol. Biol. , vol.384 , pp. 604-614
    • Chen, C.N.1    Chin, K.H.2    Wang, A.H.3    Chou, S.H.4
  • 17
    • 77951247315 scopus 로고    scopus 로고
    • Crystal structure of human senescence marker protein 30: Insights linking structural, enzymatic, and physiological functions
    • S. Chakraborti, and B.J. Bahnson Crystal structure of human senescence marker protein 30: insights linking structural, enzymatic, and physiological functions Biochemistry 49 2010 3436 3444
    • (2010) Biochemistry , vol.49 , pp. 3436-3444
    • Chakraborti, S.1    Bahnson, B.J.2
  • 22
    • 0000292524 scopus 로고
    • A note on the kinetics of enzyme action
    • G.E. Briggs, and J.B. Haldane A note on the kinetics of enzyme action Biochem. J. 19 1925 338 339
    • (1925) Biochem. J. , vol.19 , pp. 338-339
    • Briggs, G.E.1    Haldane, J.B.2
  • 23
    • 0026096803 scopus 로고
    • Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities
    • K.N. Gan, A. Smolen, H.W. Eckerson, and B.N. La Du Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities Drug Metab. Dispos. 19 1991 100 106
    • (1991) Drug Metab. Dispos. , vol.19 , pp. 100-106
    • Gan, K.N.1    Smolen, A.2    Eckerson, H.W.3    La Du, B.N.4
  • 24
    • 0034721761 scopus 로고    scopus 로고
    • Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein- associated lactonase and protects low density lipoprotein against oxidation
    • D.I. Draganov, P.L. Stetson, C.E. Watson, S.S. Billecke, and B.N. La Du Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein-associated lactonase and protects low density lipoprotein against oxidation J. Biol. Chem. 275 2000 33435 33442
    • (2000) J. Biol. Chem. , vol.275 , pp. 33435-33442
    • Draganov, D.I.1    Stetson, P.L.2    Watson, C.E.3    Billecke, S.S.4    La Du, B.N.5
  • 26
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 27
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • A. Shevchenko, M. Wilm, O. Vorm, and M. Mann Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels Anal. Chem. 68 1996 850 858
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 28
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • J.K. Eng, A.L. McCormack, and J.R. Yates III An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass. Spectrom. 5 1994 976 989
    • (1994) J. Am. Soc. Mass. Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates Iii, J.R.3
  • 29
    • 0033534765 scopus 로고    scopus 로고
    • Senescence marker protein-30 (SMP30): Structure and biological function
    • T. Fujita Senescence marker protein-30 (SMP30): structure and biological function Biochem. Biophys. Res. Commun. 254 1999 1 4
    • (1999) Biochem. Biophys. Res. Commun. , vol.254 , pp. 1-4
    • Fujita, T.1
  • 30
    • 33749510670 scopus 로고    scopus 로고
    • Binding of a designed substrate analogue to diisopropyl fluorophosphatase: Implications for the phosphotriesterase mechanism
    • M.M. Blum, F. Lohr, A. Richardt, H. Ruterjans, and J.C. Chen Binding of a designed substrate analogue to diisopropyl fluorophosphatase: implications for the phosphotriesterase mechanism J. Am. Chem. Soc. 128 2006 12750 12757
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 12750-12757
    • Blum, M.M.1    Lohr, F.2    Richardt, A.3    Ruterjans, H.4    Chen, J.C.5
  • 31
    • 48449099393 scopus 로고    scopus 로고
    • Characterization of the PON1 active site using modeling simulation, in relation to PON1 lactonase activity
    • H. Tavori, S. Khatib, M. Aviram, and J. Vaya Characterization of the PON1 active site using modeling simulation, in relation to PON1 lactonase activity Bioorg. Med. Chem. 16 2008 7504 7509
    • (2008) Bioorg. Med. Chem. , vol.16 , pp. 7504-7509
    • Tavori, H.1    Khatib, S.2    Aviram, M.3    Vaya, J.4
  • 33
    • 33947619646 scopus 로고    scopus 로고
    • Human paraoxonase: A promising approach for pre-treatment and therapy of organophosphorus poisoning
    • D. Rochu, E. Chabriere, and P. Masson Human paraoxonase: a promising approach for pre-treatment and therapy of organophosphorus poisoning Toxicology 233 2007 47 59
    • (2007) Toxicology , vol.233 , pp. 47-59
    • Rochu, D.1    Chabriere, E.2    Masson, P.3
  • 34
    • 58149380398 scopus 로고    scopus 로고
    • Quantification of hydrolysis of toxic organophosphates and organophosphonates by diisopropyl fluorophosphatase from Loligo vulgaris by in situ Fourier transform infrared spectroscopy
    • J. Gab, M. Melzer, K. Kehe, A. Richardt, and M.M. Blum Quantification of hydrolysis of toxic organophosphates and organophosphonates by diisopropyl fluorophosphatase from Loligo vulgaris by in situ Fourier transform infrared spectroscopy Anal. Biochem. 385 2009 187 193
    • (2009) Anal. Biochem. , vol.385 , pp. 187-193
    • Gab, J.1    Melzer, M.2    Kehe, K.3    Richardt, A.4    Blum, M.M.5
  • 35
    • 58849161928 scopus 로고    scopus 로고
    • Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement
    • M.M. Blum, M. Mustyakimov, H. Ruterjans, K. Kehe, B.P. Schoenborn, P. Langan, and J.C. Chen Rapid determination of hydrogen positions and protonation states of diisopropyl fluorophosphatase by joint neutron and X-ray diffraction refinement Proc. Natl. Acad. Sci. U. S. A. 106 2009 713 718
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 713-718
    • Blum, M.M.1    Mustyakimov, M.2    Ruterjans, H.3    Kehe, K.4    Schoenborn, B.P.5    Langan, P.6    Chen, J.C.7
  • 36
    • 0034958633 scopus 로고    scopus 로고
    • High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris
    • J. Hartleib, and H. Ruterjans High-yield expression, purification, and characterization of the recombinant diisopropylfluorophosphatase from Loligo vulgaris Protein Expr. Purif. 21 2001 210 219
    • (2001) Protein Expr. Purif. , vol.21 , pp. 210-219
    • Hartleib, J.1    Ruterjans, H.2
  • 37
    • 72249111746 scopus 로고    scopus 로고
    • Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design
    • M. Melzer, J.C. Chen, A. Heidenreich, J. Gab, M. Koller, K. Kehe, and M.M. Blum Reversed enantioselectivity of diisopropyl fluorophosphatase against organophosphorus nerve agents by rational design J. Am. Chem. Soc. 131 2009 17226 17232
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17226-17232
    • Melzer, M.1    Chen, J.C.2    Heidenreich, A.3    Gab, J.4    Koller, M.5    Kehe, K.6    Blum, M.M.7
  • 38
    • 21944455433 scopus 로고    scopus 로고
    • Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme
    • V. Katsemi, C. Lucke, J. Koepke, F. Lohr, S. Maurer, G. Fritzsch, and H. Ruterjans Mutational and structural studies of the diisopropylfluorophosphatase from Loligo vulgaris shed new light on the catalytic mechanism of the enzyme Biochemistry 44 2005 9022 9033
    • (2005) Biochemistry , vol.44 , pp. 9022-9033
    • Katsemi, V.1    Lucke, C.2    Koepke, J.3    Lohr, F.4    Maurer, S.5    Fritzsch, G.6    Ruterjans, H.7
  • 39
    • 33646373929 scopus 로고    scopus 로고
    • The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
    • O. Khersonsky, and D.S. Tawfik The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases J. Biol. Chem. 281 2006 7649 7656
    • (2006) J. Biol. Chem. , vol.281 , pp. 7649-7656
    • Khersonsky, O.1    Tawfik, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.