메뉴 건너뛰기




Volumn 19, Issue 8, 2014, Pages 1263-1275

Comparative investigation of the reaction mechanisms of the organophosphate-degrading phosphotriesterases from Agrobacterium radiobacter (OpdA) and Pseudomonas diminuta (OPH)

Author keywords

Binding affinity; Calorimetry; Enzyme kinetics; Magnetic circular dichroism; Site directed mutagenesis

Indexed keywords

ENZYME INHIBITOR; FLUORIDE; ORGANOPHOSPHATE; PHOSPHOTRIESTERASE;

EID: 84938905397     PISSN: 09498257     EISSN: 14321327     Source Type: Journal    
DOI: 10.1007/s00775-014-1183-9     Document Type: Article
Times cited : (47)

References (56)
  • 1
    • 0021532007 scopus 로고
    • Groundwater contamination. 2. Health and enviromental aspects of setting cleanup criteria
    • 1:CAS:528:DyaL2MXmslSktA%3D%3D
    • Block RM, Dragun J, Kalinowski TW (1984) Groundwater contamination. 2. Health and enviromental aspects of setting cleanup criteria. Chem Eng 91:70-73
    • (1984) Chem Eng , vol.91 , pp. 70-73
    • Block, R.M.1    Dragun, J.2    Kalinowski, T.W.3
  • 2
    • 0021529262 scopus 로고
    • Groundwater contamination. 1. Transport and transformation of organic-chemicals
    • 1:CAS:528:DyaL2MXmslSktw%3D%3D
    • Dragun J, Kuffner AC, Schneiter RW (1984) Groundwater contamination. 1. Transport and transformation of organic-chemicals. Chem Eng 91:65-70
    • (1984) Chem Eng , vol.91 , pp. 65-70
    • Dragun, J.1    Kuffner, A.C.2    Schneiter, R.W.3
  • 3
    • 0034007911 scopus 로고    scopus 로고
    • Organophosphates and their impact on the global environment
    • 1:CAS:528:DC%2BD3cXjtV2isLw%3D 10794404
    • Satoh T, Hosokawa M (2000) Organophosphates and their impact on the global environment. Neurotoxicology. 21:223-227
    • (2000) Neurotoxicology. , vol.21 , pp. 223-227
    • Satoh, T.1    Hosokawa, M.2
  • 4
    • 33645472653 scopus 로고    scopus 로고
    • Microbial degradation of organophosphorus compounds
    • 1:CAS:528:DC%2BD28XkslCmtr8%3D 16594965 10.1111/j.1574-6976.2006.00018.x
    • Singh BK, Walker A (2006) Microbial degradation of organophosphorus compounds. FEMS Microbiol Rev 30:428-471
    • (2006) FEMS Microbiol Rev , vol.30 , pp. 428-471
    • Singh, B.K.1    Walker, A.2
  • 5
    • 0347130091 scopus 로고    scopus 로고
    • Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source
    • 1:CAS:528:DC%2BD2cXmvFamsg%3D%3D 321290 14711669 10.1128/AEM.70.1.404-412.2004
    • McLoughlin SY, Jackson C, Liu J-W, Ollis DL (2004) Growth of Escherichia coli coexpressing phosphotriesterase and glycerophosphodiester phosphodiesterase, using paraoxon as the sole phosphorus source. Appl Environ Microbiol. 70:404-412
    • (2004) Appl Environ Microbiol. , vol.70 , pp. 404-412
    • McLoughlin, S.Y.1    Jackson, C.2    Liu, J.-W.3    Ollis, D.L.4
  • 6
    • 0024097524 scopus 로고
    • Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes
    • 1:CAS:528:DyaL1MXktVWls7s%3D 204325 3202637
    • Harper LL, McDaniel CS, Miller CE, Wild JR (1988) Dissimilar plasmids isolated from Pseudomonas diminuta MG and a Flavobacterium sp. (ATCC 27551) contain identical opd genes. Appl Environ Microbiol 54:2586-2589
    • (1988) Appl Environ Microbiol , vol.54 , pp. 2586-2589
    • Harper, L.L.1    McDaniel, C.S.2    Miller, C.E.3    Wild, J.R.4
  • 9
    • 51849117083 scopus 로고    scopus 로고
    • Enzymatic bioremediation: Organophosphate degradation by binuclear metallo-hydrolases
    • 1:CAS:528:DC%2BD1MXotFygsQ%3D%3D
    • Ely F, Foo J-L, Jackson CJ, Gahan LR, Ollis DL, Schenk G (2007) Enzymatic bioremediation: organophosphate degradation by binuclear metallo-hydrolases. Curr Top Biochem Res. 9:63-78
    • (2007) Curr Top Biochem Res. , vol.9 , pp. 63-78
    • Ely, F.1    Foo, J.-L.2    Jackson, C.J.3    Gahan, L.R.4    Ollis, D.L.5    Schenk, G.6
  • 10
    • 78649849947 scopus 로고    scopus 로고
    • The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis
    • 1:CAS:528:DC%2BC3cXhsVOkt7rP 20868365 10.1042/BJ20101054
    • Ely F, Hadler KS, Gahan LR, Guddat LW, Ollis DL, Schenk G (2010) The organophosphate-degrading enzyme from Agrobacterium radiobacter displays mechanistic flexibility for catalysis. Biochem J 432:565-573
    • (2010) Biochem J , vol.432 , pp. 565-573
    • Ely, F.1    Hadler, K.S.2    Gahan, L.R.3    Guddat, L.W.4    Ollis, D.L.5    Schenk, G.6
  • 11
    • 84866417151 scopus 로고    scopus 로고
    • Binuclear metallohydrolases: Complex mechanistic strategies for a simple chemical reaction
    • 1:CAS:528:DC%2BC38XosFemtL4%3D 22698580 10.1021/ar300067g
    • Schenk G, Mitić N, Gahan LR, Ollis DL, McGeary RP, Guddat LW (2012) Binuclear metallohydrolases: complex mechanistic strategies for a simple chemical reaction. Acc Chem Res 45:1593-1603
    • (2012) Acc Chem Res , vol.45 , pp. 1593-1603
    • Schenk, G.1    Mitić, N.2    Gahan, L.R.3    Ollis, D.L.4    McGeary, R.P.5    Guddat, L.W.6
  • 12
    • 2442496666 scopus 로고    scopus 로고
    • Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase
    • 1:CAS:528:DC%2BD2cXjt1ais7k%3D 15134445 10.1021/bi0497805
    • Aubert SD, Li Y, Raushel FM (2004) Mechanism for the hydrolysis of organophosphates by the bacterial phosphotriesterase. Biochemistry 43:5707-5715
    • (2004) Biochemistry , vol.43 , pp. 5707-5715
    • Aubert, S.D.1    Li, Y.2    Raushel, F.M.3
  • 13
    • 0034684248 scopus 로고    scopus 로고
    • Rationally engineered mutants of phosphotriesterase for preparative scale isolation of chiral organophosphates
    • 1:CAS:528:DC%2BD3cXmsl2jtrY%3D 10.1021/ja002546r
    • Wu F, Li W-S, Chen-Goodspeed M, Sogorb MA, Raushel FM (2000) Rationally engineered mutants of phosphotriesterase for preparative scale isolation of chiral organophosphates. J Am Chem Soc 122:10206-10207
    • (2000) J Am Chem Soc , vol.122 , pp. 10206-10207
    • Wu, F.1    Li, W.-S.2    Chen-Goodspeed, M.3    Sogorb, M.A.4    Raushel, F.M.5
  • 14
    • 0029759529 scopus 로고    scopus 로고
    • Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase
    • 1:CAS:528:DyaK28XksFyjurY%3D 8718883 10.1021/bi960663m
    • Hong S-B, Raushel FM (1996) Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase. Biochemistry 35:10904-10912
    • (1996) Biochemistry , vol.35 , pp. 10904-10912
    • Hong, S.-B.1    Raushel, F.M.2
  • 15
    • 0033658178 scopus 로고    scopus 로고
    • Phosphotriesterase: An enzyme in search of its natural substrate
    • 1:CAS:528:DC%2BD3cXjt1Crtrc%3D 10800593
    • Raushel FM, Holden HM (2000) Phosphotriesterase: an enzyme in search of its natural substrate. Adv Enzymol Relat Areas Mol Biol 74:51-73
    • (2000) Adv Enzymol Relat Areas Mol Biol , vol.74 , pp. 51-73
    • Raushel, F.M.1    Holden, H.M.2
  • 16
    • 24044512145 scopus 로고    scopus 로고
    • Protonation of the binuclear metal center within the active site of phosphotriesterase
    • 1:CAS:528:DC%2BD2MXms1Kntbk%3D 16101284 10.1021/bi0506270
    • Samples CR, Howard T, Raushel FM, DeRose VJ (2005) Protonation of the binuclear metal center within the active site of phosphotriesterase. Biochemistry 44:11005-11013
    • (2005) Biochemistry , vol.44 , pp. 11005-11013
    • Samples, C.R.1    Howard, T.2    Raushel, F.M.3    Derose, V.J.4
  • 17
    • 80051552042 scopus 로고    scopus 로고
    • Electronic and geometric structure of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA)
    • 1:CAS:528:DC%2BC3MXksFymtb8%3D 21487938 10.1007/s00775-011-0779-6
    • Ely F, Hadler KS, Mitic N, Gahan L, Ollis DL, Larrabee JA, Schenk G (2011) Electronic and geometric structure of the organophosphate-degrading enzyme from Agrobacterium radiobacter (OpdA). J Biol Inorg Chem 16:777-787
    • (2011) J Biol Inorg Chem , vol.16 , pp. 777-787
    • Ely, F.1    Hadler, K.S.2    Mitic, N.3    Gahan, L.4    Ollis, D.L.5    Larrabee, J.A.6    Schenk, G.7
  • 18
    • 0026748791 scopus 로고
    • Characterization of the zinc binding site of bacterial phosphotriesterase
    • 1:CAS:528:DyaK38XltVOht7s%3D 1320014
    • Omburo G, Kuo J, Mullins L, Raushel F (1992) Characterization of the zinc binding site of bacterial phosphotriesterase. J Biol Chem 267:13278-13283
    • (1992) J Biol Chem , vol.267 , pp. 13278-13283
    • Omburo, G.1    Kuo, J.2    Mullins, L.3    Raushel, F.4
  • 19
    • 81355161239 scopus 로고    scopus 로고
    • Phosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacter
    • 1:CAS:528:DC%2BC3MXhsFOgtbbN 22112835 10.1016/j.jinorgbio.2011.09.015
    • Ely F, Pedroso MM, Gahan LR, Ollis DL, Guddat LW, Schenk G (2012) Phosphate-bound structure of an organophosphate-degrading enzyme from Agrobacterium radiobacter. J Inorg Biochem 106:19-22
    • (2012) J Inorg Biochem , vol.106 , pp. 19-22
    • Ely, F.1    Pedroso, M.M.2    Gahan, L.R.3    Ollis, D.L.4    Guddat, L.W.5    Schenk, G.6
  • 20
    • 77954739001 scopus 로고    scopus 로고
    • Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme
    • 1:CAS:528:DC%2BC3cXotVajsL0%3D 20459397 10.1042/BJ20100233
    • Foo J-L, Jackson CJ, Carr PD, Kim H-K, Schenk G, Gahan LR, Ollis DL (2010) Mutation of outer-shell residues modulates metal ion co-ordination strength in a metalloenzyme. Biochem J 429:313-321
    • (2010) Biochem J , vol.429 , pp. 313-321
    • Foo, J.-L.1    Jackson, C.J.2    Carr, P.D.3    Kim, H.-K.4    Schenk, G.5    Gahan, L.R.6    Ollis, D.L.7
  • 21
  • 22
    • 0026317336 scopus 로고
    • Calorimetric studies of the binding of ferric ions to ovotransferrin and interactions between binding sites
    • 1:CAS:528:DyaK3MXmslektLs%3D 1751486 10.1021/bi00114a008
    • Lin LN, Mason AB, Woodworth RC, Brandts JF (1991) Calorimetric studies of the binding of ferric ions to ovotransferrin and interactions between binding sites. Biochemistry 30:11660-11669
    • (1991) Biochemistry , vol.30 , pp. 11660-11669
    • Lin, L.N.1    Mason, A.B.2    Woodworth, R.C.3    Brandts, J.F.4
  • 23
    • 0027445614 scopus 로고
    • Calorimetric studies of the binding of ferric ions to human serum transferrin
    • 1:CAS:528:DyaK3sXltleku7g%3D 8369310 10.1021/bi00087a019
    • Lin LN, Mason AB, Woodworth RC, Brandts JF (1993) Calorimetric studies of the binding of ferric ions to human serum transferrin. Biochemistry 32:9398-9406
    • (1993) Biochemistry , vol.32 , pp. 9398-9406
    • Lin, L.N.1    Mason, A.B.2    Woodworth, R.C.3    Brandts, J.F.4
  • 25
    • 67349169309 scopus 로고    scopus 로고
    • Grams/AI 9.0 Software
    • Thermo Scientific, Grams/AI 9.0 Software (2009)
    • (2009) Thermo Scientific
  • 26
    • 0034720769 scopus 로고    scopus 로고
    • Self-assembly of the binuclear metal center of phosphotriesterase
    • 1:CAS:528:DC%2BD3cXjsFGqu7w%3D 10858282 10.1021/bi000291o
    • Shim H, Raushel FM (2000) Self-assembly of the binuclear metal center of phosphotriesterase. Biochemistry 39:7357-7364
    • (2000) Biochemistry , vol.39 , pp. 7357-7364
    • Shim, H.1    Raushel, F.M.2
  • 27
    • 84896761223 scopus 로고    scopus 로고
    • Thermodynamics of formation of the insulin hexamer: Metal-stabilized proton-coupled assembly of quaternary structure
    • 1:CAS:528:DC%2BC2cXitVygtLk%3D 24506168 10.1021/bi4016567
    • Carpenter MC, Wilcox DE (2014) Thermodynamics of formation of the insulin hexamer: metal-stabilized proton-coupled assembly of quaternary structure. Biochemistry 53:1296-1301
    • (2014) Biochemistry , vol.53 , pp. 1296-1301
    • Carpenter, M.C.1    Wilcox, D.E.2
  • 28
    • 78649979715 scopus 로고    scopus 로고
    • Application of isothermal titration calorimetry in bioinorganic chemistry
    • 1:CAS:528:DC%2BC3cXhtVCmtLfF 20725755 10.1007/s00775-010-0693-3
    • Grossoehme NE, Spuches AM, Wilcox DE (2010) Application of isothermal titration calorimetry in bioinorganic chemistry. J Biol Inorg Chem 15:1183-1191
    • (2010) J Biol Inorg Chem , vol.15 , pp. 1183-1191
    • Grossoehme, N.E.1    Spuches, A.M.2    Wilcox, D.E.3
  • 29
    • 0034650726 scopus 로고    scopus 로고
    • Exact analysis of competition ligand binding by displacement isothermal titration calorimetry
    • 1:CAS:528:DC%2BD3cXhs1WmsA%3D%3D 10625516 10.1006/abio.1999.4402
    • Sigurskjold BW (2000) Exact analysis of competition ligand binding by displacement isothermal titration calorimetry. Anal Biochem 277:260-266
    • (2000) Anal Biochem , vol.277 , pp. 260-266
    • Sigurskjold, B.W.1
  • 32
    • 84902424172 scopus 로고    scopus 로고
    • AOMX: Angular overlap model computation
    • J.A. McCleverty T.J. Meyer (eds) 2 Elsevier Oxford 10.1016/B0-08-043748-6/01052-5
    • Schonherr T, Artanasov M, Adamsky H (2004) AOMX: angular overlap model computation. In: McCleverty JA, Meyer TJ (eds) Comprehensive coordination chemistry II, vol 2. Elsevier, Oxford, pp 443-455
    • (2004) Comprehensive Coordination Chemistry II , pp. 443-455
    • Schonherr, T.1    Artanasov, M.2    Adamsky, H.3
  • 33
    • 0015522562 scopus 로고
    • Magnetic circular dichroism of cobalt metalloenzyme derivatives
    • 1:CAS:528:DyaE3sXmvVOisw%3D%3D 4622650 10.1016/0006-291X(72)90799-1
    • Kaden TA, Holmquist B, Vallee BL (1972) Magnetic circular dichroism of cobalt metalloenzyme derivatives. Biochem Biophys Res Commun. 46:1654-1659
    • (1972) Biochem Biophys Res Commun. , vol.46 , pp. 1654-1659
    • Kaden, T.A.1    Holmquist, B.2    Vallee, B.L.3
  • 34
    • 4644228869 scopus 로고    scopus 로고
    • Magnetic circular dichroism and cobalt(II) binding equilibrium studies of Escherichia coli methionyl aminopeptidase
    • 1:CAS:528:DC%2BD2cXntFGhs70%3D 15453765 10.1021/ja0485006
    • Larrabee JA, Leung CH, Moore RL, Thamrong-nawasawat T, Wessler BSH (2004) Magnetic circular dichroism and cobalt(II) binding equilibrium studies of Escherichia coli methionyl aminopeptidase. J Am Chem Soc 126:12316-12324
    • (2004) J Am Chem Soc , vol.126 , pp. 12316-12324
    • Larrabee, J.A.1    Leung, C.H.2    Moore, R.L.3    Thamrong-Nawasawat, T.4    Wessler, B.S.H.5
  • 35
    • 0030938540 scopus 로고    scopus 로고
    • Magnetic circular dichroism spectroscopy as a probe of geometric and electronic structure of cobalt(II)-substituted proteins: Ground-state zero-field splitting as a coordination number indicator
    • 1:CAS:528:DyaK2sXivVeku70%3D 10.1021/ja963555w
    • Larrabee JA, Alessi CM, Asiedu ET, Cook JO, Hoerning KR, Klingler LJ, Okin GS, Santee SG, Volkert TL (1997) Magnetic circular dichroism spectroscopy as a probe of geometric and electronic structure of cobalt(II)-substituted proteins: ground-state zero-field splitting as a coordination number indicator. J Am Chem Soc 119:4182-4196
    • (1997) J Am Chem Soc , vol.119 , pp. 4182-4196
    • Larrabee, J.A.1    Alessi, C.M.2    Asiedu, E.T.3    Cook, J.O.4    Hoerning, K.R.5    Klingler, L.J.6    Okin, G.S.7    Santee, S.G.8    Volkert, T.L.9
  • 36
    • 77949371597 scopus 로고    scopus 로고
    • Electronic structure analysis of the dinuclear metal center in the bioremediator glycerophosphodiesterase (GpdQ) from enterobacter aerogenes
    • 1:CAS:528:DC%2BC3cXitFaqtrs%3D 20163105 10.1021/ic901950c
    • Hadler KS, Mitic N, Yip SH-C, Gahan LR, Ollis DL, Schenk G, Larrabee JA (2010) Electronic structure analysis of the dinuclear metal center in the bioremediator glycerophosphodiesterase (GpdQ) from enterobacter aerogenes. Inorg Chem 49:2727-2734
    • (2010) Inorg Chem , vol.49 , pp. 2727-2734
    • Hadler, K.S.1    Mitic, N.2    Yip, S.-C.3    Gahan, L.R.4    Ollis, D.L.5    Schenk, G.6    Larrabee, J.A.7
  • 39
    • 57149089670 scopus 로고    scopus 로고
    • Magnetic circular dichroism study of a dicobalt(II) methionine aminopeptidase/fumagillin complex and dicobalt II/II and II/III model complexes
    • 1:CAS:528:DC%2BD1cXht1Gjtr%2FO 18921993 10.1021/ic8011553
    • Larrabee JA, Chyun S-A, Volwiler AS (2008) Magnetic circular dichroism study of a dicobalt(II) methionine aminopeptidase/fumagillin complex and dicobalt II/II and II/III model complexes. Inorg Chem 47:10499-10508
    • (2008) Inorg Chem , vol.47 , pp. 10499-10508
    • Larrabee, J.A.1    Chyun, S.-A.2    Volwiler, A.S.3
  • 40
    • 0028855016 scopus 로고
    • CO2 is required for the assembly of the binuclear metal center of phosphotriesterase
    • 1:CAS:528:DyaK2MXmvVehu7w%3D 10.1021/ja00133a046
    • Hong S-B, Kuo JM, Mullins LS, Raushel FM (1995) CO2 is required for the assembly of the binuclear metal center of phosphotriesterase. J Am Chem Soc 117:7580-7581
    • (1995) J Am Chem Soc , vol.117 , pp. 7580-7581
    • Hong, S.-B.1    Kuo, J.M.2    Mullins, L.S.3    Raushel, F.M.4
  • 41
    • 0028873117 scopus 로고
    • Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency
    • 1:CAS:528:DyaK2MXmsFSmsLo%3D 10.1021/ja00131a004
    • Kiefer LL, Paterno SA, Fierke CA (1995) Hydrogen bond network in the metal binding site of carbonic anhydrase enhances zinc affinity and catalytic efficiency. J Am Chem Soc 117:6831-6837
    • (1995) J Am Chem Soc , vol.117 , pp. 6831-6837
    • Kiefer, L.L.1    Paterno, S.A.2    Fierke, C.A.3
  • 42
    • 33947388370 scopus 로고    scopus 로고
    • Activation of the binuclear metal center through formation of phosphotriesterase; Inhibitor complexes
    • 1:CAS:528:DC%2BD2sXhvFKqsL4%3D 17315951 10.1021/bi061951d
    • Samples CR, Raushel FM, DeRose VJ (2007) Activation of the binuclear metal center through formation of phosphotriesterase; inhibitor complexes. Biochemistry 46:3435-3442
    • (2007) Biochemistry , vol.46 , pp. 3435-3442
    • Samples, C.R.1    Raushel, F.M.2    Derose, V.J.3
  • 43
    • 26844462157 scopus 로고    scopus 로고
    • Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site
    • 1:CAS:528:DC%2BD2MXhtFekurnE 16188223 10.1016/j.abb.2005.08.012
    • Grimsley JK, Calamini B, Wild JR, Mesecar AD (2005) Structural and mutational studies of organophosphorus hydrolase reveal a cryptic and functional allosteric-binding site. Arch Biochem Biophys 442:169-179
    • (2005) Arch Biochem Biophys , vol.442 , pp. 169-179
    • Grimsley, J.K.1    Calamini, B.2    Wild, J.R.3    Mesecar, A.D.4
  • 44
    • 0030759664 scopus 로고    scopus 로고
    • Fluoride binding in hemoproteins: The importance of the distal cavity structure
    • 1:CAS:528:DyaK2sXkt1Ghsbk%3D 9220982 10.1021/bi970248+
    • Neri F, Kok D, Miller MA, Smulevich G (1997) Fluoride binding in hemoproteins: the importance of the distal cavity structure. Biochemistry 36:8947-8953
    • (1997) Biochemistry , vol.36 , pp. 8947-8953
    • Neri, F.1    Kok, D.2    Miller, M.A.3    Smulevich, G.4
  • 45
    • 0015829998 scopus 로고
    • The effect of fluoride on the spectral and catalytic properties of the three copper-containing oxidases
    • 4354619 10.1111/j.1432-1033.1973.tb02901.x
    • Brändén R, Malmström BG, Vänngård T (1973) The effect of fluoride on the spectral and catalytic properties of the three copper-containing oxidases. Eur J Biochem 36:195
    • (1973) Eur J Biochem , vol.36 , pp. 195
    • Brändén, R.1    Malmström, B.G.2    Vänngård, T.3
  • 46
    • 0034625058 scopus 로고    scopus 로고
    • Fluoride inhibition of Klebsiella aerogenes urease: Mechanistic implications of a pseudo-uncompetitive, slow-binding inhibitor
    • 1:CAS:528:DC%2BD3cXitlKnt7o%3D 10820010 10.1021/bi992287m
    • Todd MJ, Hausinger RP (2000) Fluoride inhibition of Klebsiella aerogenes urease: mechanistic implications of a pseudo-uncompetitive, slow-binding inhibitor. Biochemistry 39:5389-5396
    • (2000) Biochemistry , vol.39 , pp. 5389-5396
    • Todd, M.J.1    Hausinger, R.P.2
  • 47
    • 0037439988 scopus 로고    scopus 로고
    • Substrate inhibition of rat liver and kidney arginase with fluoride
    • 1:CAS:528:DC%2BD3sXpsFOisg%3D%3D 12576287 10.1016/S0162-0134(02)00579-2
    • Tormanen CD (2003) Substrate inhibition of rat liver and kidney arginase with fluoride. J Inorg Biochem 93:243
    • (2003) J Inorg Biochem , vol.93 , pp. 243
    • Tormanen, C.D.1
  • 48
    • 0036186289 scopus 로고    scopus 로고
    • Interaction of anions with rat liver arginase: Specific inhibitory effects of fluoride
    • 1:CAS:528:DC%2BD38XhvVWmsr4%3D 11897356 10.1016/S0162-0134(01)00417-2
    • Pethe S, Boucher JL, Mansuy D (2002) Interaction of anions with rat liver arginase: specific inhibitory effects of fluoride. J Inorg Biochem 88:397-402
    • (2002) J Inorg Biochem , vol.88 , pp. 397-402
    • Pethe, S.1    Boucher, J.L.2    Mansuy, D.3
  • 51
    • 0033520085 scopus 로고    scopus 로고
    • Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III), Mn(II) center in bovine spleen purple acid phosphatase during enzymatic turnover
    • 1:CAS:528:DyaK1MXktlWjt74%3D 10433698 10.1021/bi9904454
    • Merkx M, Pinkse MWH, Averill BA (1999) Evidence for nonbridged coordination of p-nitrophenyl phosphate to the dinuclear Fe(III), Mn(II) center in bovine spleen purple acid phosphatase during enzymatic turnover. Biochemistry 38:9914-9925
    • (1999) Biochemistry , vol.38 , pp. 9914-9925
    • Merkx, M.1    Pinkse, M.W.H.2    Averill, B.A.3
  • 52
    • 33845740664 scopus 로고    scopus 로고
    • Inhibition studies of purple acid phosphatases: Implications for the catalytic mechanism
    • 1:CAS:528:DC%2BD2sXpsVCqtA%3D%3D 10.1590/S0103-50532006000800011
    • Elliott TW, Mitic N, Gahan LR, Guddat LW, Schenk G (2006) Inhibition studies of purple acid phosphatases: implications for the catalytic mechanism. J Braz Chem Soc 17:1558-1565
    • (2006) J Braz Chem Soc , vol.17 , pp. 1558-1565
    • Elliott, T.W.1    Mitic, N.2    Gahan, L.R.3    Guddat, L.W.4    Schenk, G.5
  • 53
    • 0032829740 scopus 로고    scopus 로고
    • Spectroscopic characterization of a ternary phosphatase, substrate, fluoride complex. Mechanistic implications for dinuclear hydrolases
    • 1:CAS:528:DyaK1MXlvFKisLY%3D 10.1021/ja990732v
    • Wang X, Ho RYN, Whiting AK, Que L (1999) Spectroscopic characterization of a ternary phosphatase, substrate, fluoride complex. Mechanistic implications for dinuclear hydrolases. J Am Chem Soc. 121:9235-9236
    • (1999) J Am Chem Soc. , vol.121 , pp. 9235-9236
    • Wang, X.1    Ho, R.Y.N.2    Whiting, A.K.3    Que, L.4
  • 54
    • 40849135696 scopus 로고    scopus 로고
    • Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle
    • 2267794 18234116 10.1186/1472-6807-8-6
    • Schenk G, Elliott TW, Leung E, Carrington LE, Mitić N, Gahan LR, Guddat LW (2008) Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle. BMC Struct Biol 8:6
    • (2008) BMC Struct Biol , vol.8 , pp. 6
    • Schenk, G.1    Elliott, T.W.2    Leung, E.3    Carrington, L.E.4    Mitić, N.5    Gahan, L.R.6    Guddat, L.W.7
  • 55
    • 23944485399 scopus 로고    scopus 로고
    • The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism
    • 1:CAS:528:DC%2BD2MXptVWnu78%3D 10.1016/j.bbapap.2005.06.008
    • Jackson C, Kim H-K, Carr PD, Liu J-W, Ollis DL (2005) The structure of an enzyme-product complex reveals the critical role of a terminal hydroxide nucleophile in the bacterial phosphotriesterase mechanism. Biochimica et Biophysica Acta (BBA) Proteins Proteomics 1752:56-64
    • (2005) Biochimica et Biophysica Acta (BBA) Proteins Proteomics , vol.1752 , pp. 56-64
    • Jackson, C.1    Kim, H.-K.2    Carr, P.D.3    Liu, J.-W.4    Ollis, D.L.5
  • 56
    • 0035814923 scopus 로고    scopus 로고
    • High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta
    • 1:CAS:528:DC%2BD3MXosVGjtQ%3D%3D 11258882 10.1021/bi002661e
    • Benning MM, Shim H, Raushel FM, Holden HM (2001) High resolution X-ray structures of different metal-substituted forms of phosphotriesterase from Pseudomonas diminuta. Biochemistry 40:2712-2722
    • (2001) Biochemistry , vol.40 , pp. 2712-2722
    • Benning, M.M.1    Shim, H.2    Raushel, F.M.3    Holden, H.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.