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Volumn 187, Issue 1-3, 2010, Pages 370-372

Lactonases with oragnophosphatase activity: Structural and evolutionary perspectives

Author keywords

DFPase; Paraxonase; Phosphotriesterase

Indexed keywords

AMIDASE; ARYLDIALKYLPHOSPHATASE 1; ARYLDIALKYLPHOSPHATASE 2; ARYLESTERASE; ASCORBIC ACID; BACTERIAL ENZYME; CALCIUM ION; COBALT; DIISOPROPYL FLUOROPHOSPHATASE; DYFLOS; GLUCONOLACTONASE; LACTONE DERIVATIVE; LIVER ENZYME; LONG CHAIN FATTY ACID; MAGNESIUM; MANGANESE; N ACYLHOMOSERINE LACTONE; ORGANOPHOSPHATE INSECTICIDE; PARAOXON; PHOSPHOTRIESTERASE; REGUCALCIN; SARIN; SOMAN; ZINC; ARYLDIALKYLPHOSPHATASE; DIISOPROPYL-FLUOROPHOSPHATASE; HYDROLASE;

EID: 77955516506     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2010.01.039     Document Type: Article
Times cited : (64)

References (32)
  • 1
    • 84872639802 scopus 로고
    • An enzyme in animal tissues capable of hydrolyzing the phosphorus-fluoride bond of alkyl fluorophosphates
    • Mazur A. An enzyme in animal tissues capable of hydrolyzing the phosphorus-fluoride bond of alkyl fluorophosphates. J. Biol. Chem. 1946, 164:271-289.
    • (1946) J. Biol. Chem. , vol.164 , pp. 271-289
    • Mazur, A.1
  • 2
    • 70350567023 scopus 로고
    • Serum esterases. II. An enzyme hydrolysing diethyl p-nitrophenyl acetate (E600) and its identity with A-esterase of mammalian sera
    • Aldridge W.N. Serum esterases. II. An enzyme hydrolysing diethyl p-nitrophenyl acetate (E600) and its identity with A-esterase of mammalian sera. Biochem. J. 1953, 53:117-124.
    • (1953) Biochem. J. , vol.53 , pp. 117-124
    • Aldridge, W.N.1
  • 4
    • 0030293198 scopus 로고    scopus 로고
    • The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin
    • Davies H.G., Richter R.J., Keifer M., Broomfield C.A., Sowalla J., Furlong C.E. The effect of the human serum paraoxonase polymorphism is reversed with diazoxon, soman and sarin. Nat. Genet. 1996, 14:334-336.
    • (1996) Nat. Genet. , vol.14 , pp. 334-336
    • Davies, H.G.1    Richter, R.J.2    Keifer, M.3    Broomfield, C.A.4    Sowalla, J.5    Furlong, C.E.6
  • 7
    • 25444456889 scopus 로고    scopus 로고
    • Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily
    • Roodveldt C., Tawfik D.S. Shared promiscuous activities and evolutionary features in various members of the amidohydrolase superfamily. Biochemistry 2005, 44:12728-12736.
    • (2005) Biochemistry , vol.44 , pp. 12728-12736
    • Roodveldt, C.1    Tawfik, D.S.2
  • 8
    • 33751221972 scopus 로고    scopus 로고
    • The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase
    • Afriat L., Roodveldt C., Manco G., Tawfik D.S. The latent promiscuity of newly identified microbial lactonases is linked to a recently diverged phosphotriesterase. Biochemistry 2006, 45:13677-13686.
    • (2006) Biochemistry , vol.45 , pp. 13677-13686
    • Afriat, L.1    Roodveldt, C.2    Manco, G.3    Tawfik, D.S.4
  • 9
    • 0029937118 scopus 로고    scopus 로고
    • The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family
    • Primo-Parmo S.L., Sorenson R.C., Teiber J., La Du B.N. The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics 1996, 33:498-507.
    • (1996) Genomics , vol.33 , pp. 498-507
    • Primo-Parmo, S.L.1    Sorenson, R.C.2    Teiber, J.3    La Du, B.N.4
  • 11
    • 21244491480 scopus 로고    scopus 로고
    • Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities
    • Draganov D.I., Teiber J.F., Speelman A., Osawa Y., Sunahara R., La Du B.N. Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J. Lipid Res. 2005, 46:1239-1247.
    • (2005) J. Lipid Res. , vol.46 , pp. 1239-1247
    • Draganov, D.I.1    Teiber, J.F.2    Speelman, A.3    Osawa, Y.4    Sunahara, R.5    La Du, B.N.6
  • 12
    • 0042261695 scopus 로고    scopus 로고
    • Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3
    • Teiber J.F., Draganov D.I., La Du B.N. Lactonase and lactonizing activities of human serum paraoxonase (PON1) and rabbit serum PON3. Biochem. Pharmacol. 2003, 66:887-896.
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 887-896
    • Teiber, J.F.1    Draganov, D.I.2    La Du, B.N.3
  • 13
    • 77955518309 scopus 로고    scopus 로고
    • PONs' natural substrates-the key to their physiological roles
    • Springer, Dordrecht, B. Mackness, M. Mackness, M. Aviram, G. Paragh (Eds.)
    • Draganov D.I., Teiber J.F. PONs' natural substrates-the key to their physiological roles. The Paraoxonases: Their Role in Disease Development and Xenobiotic Metabolism 2008, 297-306. Springer, Dordrecht. B. Mackness, M. Mackness, M. Aviram, G. Paragh (Eds.).
    • (2008) The Paraoxonases: Their Role in Disease Development and Xenobiotic Metabolism , pp. 297-306
    • Draganov, D.I.1    Teiber, J.F.2
  • 14
    • 0034721761 scopus 로고    scopus 로고
    • Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein-associated lactonase and protects low density lipoprotein against oxidation
    • Draganov D.I., Stetson P.L., Watson C.E., Billecke S.S., La Du B.N. Rabbit serum paraoxonase 3 (PON3) is a high density lipoprotein-associated lactonase and protects low density lipoprotein against oxidation. J. Biol. Chem. 2000, 275:33435-33442.
    • (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
  • 16
    • 17644367506 scopus 로고    scopus 로고
    • Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase
    • Khersonsky O., Tawfik D.S. Structure-reactivity studies of serum paraoxonase PON1 suggest that its native activity is lactonase. Biochemistry 2005, 44:6371-6382.
    • (2005) Biochemistry , vol.44 , pp. 6371-6382
    • Khersonsky, O.1    Tawfik, D.S.2
  • 18
    • 33646373929 scopus 로고    scopus 로고
    • The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases
    • Khersonsky O., Tawfik D.S. The histidine 115-histidine 134 dyad mediates the lactonase activity of mammalian serum paraoxonases. J. Biol. Chem. 2006, 281:7649-7656.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7649-7656
    • Khersonsky, O.1    Tawfik, D.S.2
  • 19
    • 18444379944 scopus 로고    scopus 로고
    • Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates
    • Yeung D.T., Lenz D.E., Cerasoli D.M. Analysis of active-site amino-acid residues of human serum paraoxonase using competitive substrates. FEBS J. 2005, 272:2225-2230.
    • (2005) FEBS J. , vol.272 , pp. 2225-2230
    • Yeung, D.T.1    Lenz, D.E.2    Cerasoli, D.M.3
  • 20
    • 70350513002 scopus 로고    scopus 로고
    • Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes
    • Otto T.C., Harsch C.K., Yeung D.T., Magliery T.J., Cerasoli D.M., Lenz D.E. Dramatic differences in organophosphorus hydrolase activity between human and chimeric recombinant mammalian paraoxonase-1 enzymes. Biochemistry 2009, 48:10416-10422.
    • (2009) Biochemistry , vol.48 , pp. 10416-10422
    • Otto, T.C.1    Harsch, C.K.2    Yeung, D.T.3    Magliery, T.J.4    Cerasoli, D.M.5    Lenz, D.E.6
  • 21
    • 77955509686 scopus 로고    scopus 로고
    • Paraoxonase 1 (PON1) as a potential catalytic scavenger in the prophylaxis and treatment of organophosphate poisoning
    • Publishing House of the Union of Scientist in Bulgaria, Sofia, A. Monov, C. Dishovski (Eds.)
    • Draganov D. Paraoxonase 1 (PON1) as a potential catalytic scavenger in the prophylaxis and treatment of organophosphate poisoning. Medical Aspects of Chemical and Biological Terrorism-Chemical Terrorism and Traumatism 2005, 227-246. Publishing House of the Union of Scientist in Bulgaria, Sofia. A. Monov, C. Dishovski (Eds.).
    • (2005) Medical Aspects of Chemical and Biological Terrorism-Chemical Terrorism and Traumatism , pp. 227-246
    • Draganov, D.1
  • 22
    • 61649102440 scopus 로고    scopus 로고
    • Human paraoxonase 1: a potential bioscavenger of oraganophosphorus nerve agents
    • Springer, Dordrecht, B. Mackness, M. Mackness, M. Aviram, G. Paragh (Eds.)
    • Yeung D.T., Lenz D.E., Cerasoli D.M. Human paraoxonase 1: a potential bioscavenger of oraganophosphorus nerve agents. The Paraoxonases: Their Role in Disease Development and Xenobiotic Metabolism 2008, 151-170. Springer, Dordrecht. B. Mackness, M. Mackness, M. Aviram, G. Paragh (Eds.).
    • (2008) The Paraoxonases: Their Role in Disease Development and Xenobiotic Metabolism , pp. 151-170
    • Yeung, D.T.1    Lenz, D.E.2    Cerasoli, D.M.3
  • 23
    • 0024501160 scopus 로고
    • Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP)
    • Little J.S., Broomfield C.A., Fox-Talbot M.K., Boucher L.J., MacIver B., Lenz D.E. Partial characterization of an enzyme that hydrolyzes sarin, soman, tabun, and diisopropyl phosphorofluoridate (DFP). Biochem. Pharmacol. 1989, 38:23-29.
    • (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
  • 26
    • 84954358029 scopus 로고    scopus 로고
    • The first crystal structure of gluconolactonase important in the glucose secondary metabolic pathways
    • Chen C.-N., Chin K.-H., Wang A.H.-J., Chou S.-H. The first crystal structure of gluconolactonase important in the glucose secondary metabolic pathways. J. Mol. Biol. 2008, 384:604-614.
    • (2008) J. Mol. Biol. , vol.384 , pp. 604-614
    • Chen, C.-N.1    Chin, K.-H.2    Wang, A.H.-J.3    Chou, S.-H.4
  • 27
    • 77955516004 scopus 로고    scopus 로고
    • di Targiany, et al., this volume.
    • di Targiany, et al., this volume.
  • 28
  • 31
    • 0036226347 scopus 로고    scopus 로고
    • Novel sequences propel familiar folds
    • Jawad Z., Paoli M. Novel sequences propel familiar folds. Structure 2002, 10:447-454.
    • (2002) Structure , vol.10 , pp. 447-454
    • Jawad, Z.1    Paoli, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.