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Volumn 15, Issue 3, 2010, Pages 291-301

Determination of the active site of sphingobium chlorophenolicum 2,6-dichlorohydroquinone dioxygenase (PcpA)

Author keywords

2,6 Dichlorohydroquinone; Homology model; Hydroquinone dioxygenase; PcpA; Sphingobium chlorophenolicum

Indexed keywords

ALANINE; BACTERIAL ENZYME; DIOXYGENASE; HYDROQUINONE DERIVATIVE; IRON; PHENYLALANINE;

EID: 77949261552     PISSN: 09498257     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00775-009-0602-9     Document Type: Article
Times cited : (23)

References (93)
  • 1
    • 0028708533 scopus 로고
    • 10.1007/BF00696467 7765840
    • M Schlömann 1994 Biodegradation 5 301 321 10.1007/BF00696467 7765840
    • (1994) Biodegradation , vol.5 , pp. 301-321
    • Schlömann, M.1
  • 2
    • 0028672054 scopus 로고
    • 10.1007/BF00696470 1:CAS:528:DyaK2MXjvVKms7o%3D 7765843
    • V Brenner JJ Arensdorf DD Focht 1994 Biodegradation 5 359 377 10.1007/BF00696470 1:CAS:528:DyaK2MXjvVKms7o%3D 7765843
    • (1994) Biodegradation , vol.5 , pp. 359-377
    • Brenner, V.1    Arensdorf, J.J.2    Focht, D.D.3
  • 3
    • 0029613290 scopus 로고
    • Cleaning up our own backyard: Developing new catabolic pathways to degrade pollutants
    • DOI 10.1016/1074-5521(95)90081-0
    • J Minshull 1995 Chem Biol 2 775 780 10.1016/1074-5521(95)90081-0 1:CAS:528:DyaK28Xlt1Grsg%3D%3D 8807809 (Pubitemid 3014701)
    • (1995) Chemistry and Biology , vol.2 , Issue.12 , pp. 775-780
    • Minshull, J.1
  • 4
    • 0031756487 scopus 로고    scopus 로고
    • Development of hybrid strains for the mineralization of chloroaromatics by patchwork assembly
    • DOI 10.1146/annurev.micro.52.1.287
    • W Reineke 1998 Annu Rev Microbiol 52 287 331 10.1146/annurev.micro.52.1. 287 1:CAS:528:DyaK1cXms1GiurY%3D 9891800 (Pubitemid 28481194)
    • (1998) Annual Review of Microbiology , vol.52 , pp. 287-331
    • Reineke, W.1
  • 5
    • 0032795933 scopus 로고    scopus 로고
    • 10.1016/S0167-7799(98)01295-5 1:CAS:528:DyaK1MXlt1Kjsbs%3D
    • KN Timmis DH Pieper 1999 Trends Biotechnol 17 201 204 10.1016/S0167-7799(98)01295-5 1:CAS:528:DyaK1MXlt1Kjsbs%3D
    • (1999) Trends Biotechnol , vol.17 , pp. 201-204
    • Timmis, K.N.1    Pieper, D.H.2
  • 6
    • 0034082905 scopus 로고    scopus 로고
    • Engineering dioxygenases for efficient degradation of environmental pollutants
    • DOI 10.1016/S0958-1669(00)00091-4
    • K Furukawa 2000 Curr Opin Biotechnol 11 244 249 10.1016/S0958-1669(00) 00091-4 1:CAS:528:DC%2BD3cXksVGks78%3D 10851151 (Pubitemid 30326470)
    • (2000) Current Opinion in Biotechnology , vol.11 , Issue.3 , pp. 244-249
    • Furukawa, K.1
  • 7
    • 0034075043 scopus 로고    scopus 로고
    • Engineering bacteria for bioremediation
    • DOI 10.1016/S0958-1669(00)00094-X
    • DH Pieper W Reineke 2000 Curr Opin Biotechnol 11 262 270 10.1016/S0958-1669(00)00094-X 1:CAS:528:DC%2BD3cXksVGks7o%3D 10851148 (Pubitemid 30326473)
    • (2000) Current Opinion in Biotechnology , vol.11 , Issue.3 , pp. 262-270
    • Pieper, D.H.1    Reineke, W.2
  • 8
    • 0032885089 scopus 로고    scopus 로고
    • PcpA, which is involved in the degradation of pentachlorophenol in Sphingomonas chlorophenolica ATCC39723, is a novel type of ring-cleavage dioxygenase
    • DOI 10.1016/S0014-5793(99)01305-8, PII S0014579399013058
    • Y Ohtsubo K Miyauchi K Kanda T Hatta H Kiyohara T Senda Y Nagata Y Mitsui M Takagi 1999 FEBS Lett 459 395 398 10.1016/S0014-5793(99)01305-8 1:CAS:528:DyaK1MXmvVKjsLo%3D 10526172 (Pubitemid 29467375)
    • (1999) FEBS Letters , vol.459 , Issue.3 , pp. 395-398
    • Ohtsubo, Y.1    Miyauchi, K.2    Kanda, K.3    Hatta, T.4    Kiyohara, H.5    Senda, T.6    Nagata, Y.7    Mitsui, Y.8    Takagi, M.9
  • 9
    • 0033564297 scopus 로고    scopus 로고
    • Evidence that pcpA encodes 2,6-dichlorohydroquinone dioxygenase, the ring cleavage enzyme required for pentachlorophenol degradation in Sphingomonas chlorophenolica strain ATCC 39723
    • DOI 10.1021/bi990103y
    • L Xu K Resing SL Lawson PC Babbitt SD Copley 1999 Biochemistry 38 7659 7669 10.1021/bi990103y 1:CAS:528:DyaK1MXjt1aqurk%3D 10387005 (Pubitemid 29289338)
    • (1999) Biochemistry , vol.38 , Issue.24 , pp. 7659-7669
    • Xu, L.1    Resing, K.2    Lawson, S.L.3    Babbitt, P.C.4    Copley, S.D.5
  • 10
    • 0033590113 scopus 로고    scopus 로고
    • Characterization of 2,6-dichloro-p-hydroquinone 1,2-dioxygenase (PcpA) of Sphingomonas chlorophenolica ATCC 39723
    • DOI 10.1006/bbrc.1999.1805
    • L Xun J Bohuslavek M Cai 1999 Biochem Biophys Res Commun 266 322 325 10.1006/bbrc.1999.1805 1:CAS:528:DyaK1MXnvFeku7c%3D 10600501 (Pubitemid 30028666)
    • (1999) Biochemical and Biophysical Research Communications , vol.266 , Issue.2 , pp. 322-325
    • Xun, L.1    Bohuslavek, J.2    Cai, M.3
  • 11
    • 13244265506 scopus 로고    scopus 로고
    • Identification and characterization of genes involved in the downstream degradation pathway of γ-hexachlorocyclohexane in Sphingomonas paucimobilis UT26
    • DOI 10.1128/JB.187.3.847-853.2005
    • R Endo M Kamakura K Miyauchi M Fukuda Y Ohtsubo M Tsuda Y Nagata 2005 J Bacteriol 187 847 853 10.1128/JB.187.3.847-853.2005 1:CAS:528: DC%2BD2MXhtFyis78%3D 15659662 (Pubitemid 40189758)
    • (2005) Journal of Bacteriology , vol.187 , Issue.3 , pp. 847-853
    • Endo, R.1    Kamakura, M.2    Miyauchi, K.3    Fukuda, M.4    Ohtsubo, Y.5    Tsuda, M.6    Nagata, Y.7
  • 15
    • 0036718377 scopus 로고    scopus 로고
    • Organization and regulation of pentachlorophenol-degrading genes in Sphingobium chlorophenolicum ATCC 39723
    • DOI 10.1128/JB.184.17.4672-4680.2002
    • M Cai LY Xun 2002 J Bacteriol 184 4672 4680 10.1128/JB.184.17.4672-4680. 2002 1:CAS:528:DC%2BD38Xmt12gurs%3D 12169590 (Pubitemid 34898253)
    • (2002) Journal of Bacteriology , vol.184 , Issue.17 , pp. 4672-4680
    • Cai, M.1    Xun, L.2
  • 16
    • 3543063259 scopus 로고    scopus 로고
    • Genome Shuffling Improves Degradation of the Anthropogenic Pesticide Pentachlorophenol by Sphingobium chlorophenolicum ATCC 39723
    • DOI 10.1128/AEM.70.4.2391-2397.2004
    • MH Dai SD Copley 2004 Appl Environ Microbiol 70 2391 2397 10.1128/AEM.70.4.2391-2397.2004 1:CAS:528:DC%2BD2cXjtlOhs78%3D 15066836 (Pubitemid 38500543)
    • (2004) Applied and Environmental Microbiology , vol.70 , Issue.4 , pp. 2391-2397
    • Dai, M.1    Copley, S.D.2
  • 20
    • 17644419814 scopus 로고    scopus 로고
    • J-L Ramos (eds). Kluwer/Plenum New York
    • Vaillancourt FH, Bolin JT, Eltis L (2004) In: Ramos J-L (ed) Pseudomonas, vol 3. Kluwer/Plenum, New York, pp 359-396
    • (2004) Pseudomonas , vol.3 , pp. 359-396
    • Vaillancourt, F.H.1    Bolin, J.T.2    Eltis, L.3
  • 21
    • 43049091488 scopus 로고    scopus 로고
    • 10.1016/j.cbpa.2007.12.007 1:CAS:528:DC%2BD1cXlslKlsLk%3D 18249197
    • TDH Bugg S Ramaswamy 2008 Curr Opin Chem Biol 12 134 140 10.1016/j.cbpa.2007.12.007 1:CAS:528:DC%2BD1cXlslKlsLk%3D 18249197
    • (2008) Curr Opin Chem Biol , vol.12 , pp. 134-140
    • Bugg, T.D.H.1    Ramaswamy, S.2
  • 22
    • 0029846961 scopus 로고    scopus 로고
    • 1:CAS:528:DyaK28XmtFOks7g%3D 8830689
    • LD Eltis JT Bolin 1996 J Bacteriol 178 5930 5937 1:CAS:528: DyaK28XmtFOks7g%3D 8830689
    • (1996) J Bacteriol , vol.178 , pp. 5930-5937
    • Eltis, L.D.1    Bolin, J.T.2
  • 23
  • 24
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2,3- dihydroxybiphenyl 1,2-dioxygenase by t-butanol
    • DOI 10.1074/jbc.273.52.34887
    • FH Vaillancourt S Han PD Fortin JT Bolin LD Eltis 1998 J Biol Chem 273 34887 34895 10.1074/jbc.273.52.34887 1:CAS:528:DyaK1MXisFWqsw%3D%3D 9857017 (Pubitemid 29028184)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.52 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5
  • 29
    • 0033556265 scopus 로고    scopus 로고
    • An archetypical extradiol-cleaving catecholic dioxygenase: The crystal structure of catechol 2,3-dioxygenase (metapyrocatechase) from Pseudomonas putida mt-2
    • DOI 10.1016/S0969-2126(99)80006-9
    • A Kita S-I Kita I Fujisawa K Inaka T Ishida K Horiike M Nozaki K Miki 1999 Structure 7 25 34 10.1016/S0969-2126(99)80006-9 1:CAS:528: DyaK1MXhtFGqtro%3D 10368270 (Pubitemid 29159179)
    • (1999) Structure , vol.7 , Issue.1 , pp. 25-34
    • Kita, A.1    Kita, S.-I.2    Fujisawa, I.3    Inaka, K.4    Ishida, T.5    Horiike, K.6    Nozaki, M.7    Miki, K.8
  • 30
    • 0028835678 scopus 로고
    • 10.1021/ja00134a041 1:CAS:528:DyaK2MXmvVegsLY%3D
    • J Sanvoisin GJ Langley TDH Bugg 1995 J Am Chem Soc 117 7836 7837 10.1021/ja00134a041 1:CAS:528:DyaK2MXmvVegsLY%3D
    • (1995) J Am Chem Soc , vol.117 , pp. 7836-7837
    • Sanvoisin, J.1    Langley, G.J.2    Bugg, T.D.H.3
  • 31
    • 0029836348 scopus 로고    scopus 로고
    • Cis-trans isomerization of a cyclopropyl radical trap catalyzed by extradiol catechol dioxygenases: Evidence for a semiquinone intermediate
    • DOI 10.1021/ja9607704
    • EL Spence GJ Langley TDH Bugg 1996 J Am Chem Soc 118 8336 8343 10.1021/ja9607704 1:CAS:528:DyaK28XkvFCmtrw%3D (Pubitemid 26305255)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.35 , pp. 8336-8343
    • Spence, E.L.1    Langley, G.J.2    Bugg, T.D.H.3
  • 33
    • 0038627547 scopus 로고    scopus 로고
    • 1:CAS:528:DC%2BD3sXjvFCjsb0%3D 12761662
    • RJ Deeth TDH Bugg 2003 J Biol Inorg Chem 8 409 418 1:CAS:528: DC%2BD3sXjvFCjsb0%3D 12761662
    • (2003) J Biol Inorg Chem , vol.8 , pp. 409-418
    • Deeth, R.J.1    Bugg, T.D.H.2
  • 34
    • 3242811958 scopus 로고    scopus 로고
    • Mechanism for catechol ring-cleavage by non-heme iron extradiol dioxygenases
    • DOI 10.1021/ja0493805
    • PEM Siegbahn F Haeffner 2004 J Am Chem Soc 126 8919 8932 10.1021/ja0493805 1:CAS:528:DC%2BD2cXltlClsL4%3D 15264822 (Pubitemid 38971065)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.29 , pp. 8919-8932
    • Siegbahn, P.E.M.1    Haeffner, F.2
  • 36
    • 34247534094 scopus 로고    scopus 로고
    • 2+ dioxygenase superoxo, alkylperoxo, and bound product intermediates
    • DOI 10.1126/science.1134697
    • EG Kovaleva JD Lipscomb 2007 Science 316 453 457 10.1126/science.1134697 1:CAS:528:DC%2BD2sXktlSkurg%3D 17446402 (Pubitemid 46651494)
    • (2007) Science , vol.316 , Issue.5823 , pp. 453-457
    • Kovaleva, E.G.1    Lipscomb, J.D.2
  • 38
    • 0025216788 scopus 로고
    • 1:CAS:528:DyaK3cXksFCkurg%3D 2156846
    • MR Harpel JD Lipscomb 1990 J Biol Chem 265 6301 6311 1:CAS:528: DyaK3cXksFCkurg%3D 2156846
    • (1990) J Biol Chem , vol.265 , pp. 6301-6311
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 39
    • 0025676272 scopus 로고
    • 1:CAS:528:DyaK3MXis1Cr 2266121
    • MR Harpel JD Lipscomb 1990 J Biol Chem 265 22187 22196 1:CAS:528:DyaK3MXis1Cr 2266121
    • (1990) J Biol Chem , vol.265 , pp. 22187-22196
    • Harpel, M.R.1    Lipscomb, J.D.2
  • 41
    • 0032478603 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of 1-hydroxy-2-naphthoate dioxygenase from Nocardioides sp. KP7
    • DOI 10.1074/jbc.273.14.8332
    • T Iwabuchi S Harayama 1998 J Biol Chem 273 8332 8336 10.1074/jbc.273.14. 8332 1:CAS:528:DyaK1cXitlOitbs%3D 9525941 (Pubitemid 28168892)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.14 , pp. 8332-8336
    • Iwabuchi, T.1    Harayama, S.2
  • 42
    • 0035161039 scopus 로고    scopus 로고
    • Direct ring fission of salicylate by a salicylate 1,2-dioxygenase activity from Pseudaminobacter salicylatoxidans
    • DOI 10.1128/JB.183.23.6936-6942.2001
    • J-P Hintner C Lechner U Rigert AE Kuhm T Storm T Reemtsma A Stolz 2001 J Bacteriol 183 6936 6942 10.1128/JB.183.23.6936-6942.2001 1:CAS:528: DC%2BD3MXovVSjt74%3D 11698383 (Pubitemid 33064208)
    • (2001) Journal of Bacteriology , vol.183 , Issue.23 , pp. 6936-6942
    • Hintner, J.-P.1    Lechner, C.2    Riegert, U.3    Kuhm, A.E.4    Storm, T.5    Reemtsma, T.6    Stolz, A.7
  • 43
    • 4444269290 scopus 로고    scopus 로고
    • Biochemical and molecular characterization of a ring fission dioxygenase with the ability to oxidise (substituted) salicylate(s) from Pseudaminobacter salicylatoxidans
    • DOI 10.1074/jbc.M313500200
    • J-P Hintner T Remtsma A Stolz 2004 J Biol Chem 279 37250 37260 10.1074/jbc.M313500200 1:CAS:528:DC%2BD2cXntFSgtLY%3D 15220336 (Pubitemid 39195431)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.36 , pp. 37250-37260
    • Hintner, J.-P.1    Reemtsma, T.2    Stolz, A.3
  • 44
    • 33748498955 scopus 로고    scopus 로고
    • Structural and biochemical characterization of gentisate 1,2-dioxygenase from Escherichia coli O157:H7
    • DOI 10.1111/j.1365-2958.2006.05334.x
    • MA Adams VK Singh BO Keller ZC Jia 2006 Mol Microbiol 61 1469 1484 10.1111/j.1365-2958.2006.05334.x 1:CAS:528:DC%2BD28XhtFensbvN 16930152 (Pubitemid 44359376)
    • (2006) Molecular Microbiology , vol.61 , Issue.6 , pp. 1469-1484
    • Adams, M.A.1    Singh, V.K.2    Keller, B.O.3    Jia, Z.4
  • 45
    • 0029132294 scopus 로고
    • 10.1074/jbc.270.36.21199 1:CAS:528:DyaK2MXnvFKlsL0%3D 7673153
    • JM Fernandez-Canon MA Penalva 1995 J Biol Chem 270 21199 21205 10.1074/jbc.270.36.21199 1:CAS:528:DyaK2MXnvFKlsL0%3D 7673153
    • (1995) J Biol Chem , vol.270 , pp. 21199-21205
    • Fernandez-Canon, J.M.1    Penalva, M.A.2
  • 46
    • 0028921205 scopus 로고
    • 10.1111/j.1432-1033.1995.00425.x 1:CAS:528:DyaK2MXktFyjurs%3D 7705358
    • SR Schmidt CR Muller W Kress 1995 Eur J Biochem 228 425 430 10.1111/j.1432-1033.1995.00425.x 1:CAS:528:DyaK2MXktFyjurs%3D 7705358
    • (1995) Eur J Biochem , vol.228 , pp. 425-430
    • Schmidt, S.R.1    Muller, C.R.2    Kress, W.3
  • 47
    • 0028865857 scopus 로고
    • 10.1016/1357-2725(95)00091-3 1:CAS:528:DyaK2MXhtVSit7vN 8581831
    • S Hudecova Z Strakova O Krizanova 1995 Int J Biochem Cell Biol 27 1357 1363 10.1016/1357-2725(95)00091-3 1:CAS:528:DyaK2MXhtVSit7vN 8581831
    • (1995) Int J Biochem Cell Biol , vol.27 , pp. 1357-1363
    • Hudecova, S.1    Strakova, Z.2    Krizanova, O.3
  • 51
    • 0029858048 scopus 로고    scopus 로고
    • 1:CAS:528:DyaK28Xms1WitbY%3D 8892823
    • U Lendenmann JC Spain 1996 J Bacteriol 178 6227 6232 1:CAS:528: DyaK28Xms1WitbY%3D 8892823
    • (1996) J Bacteriol , vol.178 , pp. 6227-6232
    • Lendenmann, U.1    Spain, J.C.2
  • 52
    • 0032721192 scopus 로고    scopus 로고
    • Genetic and biochemical comparison of 2-aminophenol 1,6-dioxygenase of Pseudomonas pseudoalcaligenes JS45 to meta-cleavage dioxygenases: Divergent evolution of 2-aminophenol meta-cleavage pathway
    • DOI 10.1007/s002030050787
    • JK Davis Z He CC Somerville JC Spain 1999 Arch Microbiol 172 330 339 10.1007/s002030050787 1:CAS:528:DyaK1MXnt1Gnu7o%3D 10550475 (Pubitemid 29496281)
    • (1999) Archives of Microbiology , vol.172 , Issue.5 , pp. 330-339
    • Davis, J.K.1    He, Z.2    Somerville, C.C.3    Spain, J.C.4
  • 55
    • 19644363211 scopus 로고    scopus 로고
    • Structural studies on 3-hydroxyanthranilate-3,4-dioxygenase: The catalytic mechanism of a complex oxidation involved in NAD biosynthesis
    • DOI 10.1021/bi047353l
    • Y Zhang KL Colabroy TP Begley SE Ealick 2005 Biochemistry 44 7632 7643 10.1021/bi047353l 1:CAS:528:DC%2BD2MXjslKlsrg%3D 15909978 (Pubitemid 40740747)
    • (2005) Biochemistry , vol.44 , Issue.21 , pp. 7632-7643
    • Zhang, Y.1    Colabroy, K.L.2    Begley, T.P.3    Ealick, S.E.4
  • 63
    • 0024234855 scopus 로고
    • CLUSTAL: A package for performing multiple sequence alignment on a microcomputer
    • DOI 10.1016/0378-1119(88)90330-7
    • DG Higgins PM Sharp 1988 Gene 73 237 244 10.1016/0378-1119(88)90330-7 1:CAS:528:DyaL1MXhtV2ns74%3D 3243435 (Pubitemid 19033800)
    • (1988) Gene , vol.73 , Issue.1 , pp. 237-244
    • Higgins, D.G.1    Sharp, P.M.2
  • 64
    • 0027968068 scopus 로고
    • 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D 7984417
    • JD Thompson DG Higgins TJ Gibson 1994 Nucleic Acids Res 22 4673 4680 10.1093/nar/22.22.4673 1:CAS:528:DyaK2MXitlSgu74%3D 7984417
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 65
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • DOI 10.1093/nar/25.24.4876
    • JD Thompson TJ Gibson F Plewniak F Jeanmougin DG Higgins 1997 Nucleic Acids Res 25 4876 4882 10.1093/nar/25.24.4876 1:CAS:528:DyaK1cXntFyntQ%3D%3D 9396791 (Pubitemid 28022245)
    • (1997) Nucleic Acids Research , vol.25 , Issue.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 67
    • 0023375195 scopus 로고
    • 1:STN:280:DyaL1c7ovFSjsA%3D%3D 3447015
    • N Saitou M Nei 1987 Mol Biol Evol 4 406 425 1:STN:280: DyaL1c7ovFSjsA%3D%3D 3447015
    • (1987) Mol Biol Evol , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 68
    • 0032420333 scopus 로고    scopus 로고
    • JPred: A consensus secondary structure prediction server
    • DOI 10.1093/bioinformatics/14.10.892
    • JA Cuff ME Clamp AS Siddiqui M Finlay GJ Barton 1998 Bioinformatics 14 892 893 10.1093/bioinformatics/14.10.892 1:CAS:528:DyaK1MXht1yisb4%3D 9927721 (Pubitemid 29041548)
    • (1998) Bioinformatics , vol.14 , Issue.10 , pp. 892-893
    • Cuff, J.A.1    Clamp, M.E.2    Siddiqui, A.S.3    Finlay, M.4    Barton, G.J.5
  • 69
    • 0033810049 scopus 로고    scopus 로고
    • 10.1110/ps.9.9.1753 1:CAS:528:DC%2BD3cXntFamsL8%3D 11045621
    • A Fiser RKG Do A Sali 2000 Protein Sci 9 1753 1773 10.1110/ps.9.9.1753 1:CAS:528:DC%2BD3cXntFamsL8%3D 11045621
    • (2000) Protein Sci , vol.9 , pp. 1753-1773
    • Fiser, A.1    Do, R.K.G.2    Sali, A.3
  • 70
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • A Sali TL Blundell 1993 J Mol Biol 234 779 815 10.1006/jmbi.1993.1626 1:CAS:528:DyaK2cXnt1ylug%3D%3D 8254673 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 72
    • 0026610767 scopus 로고
    • 10.1038/356083a0 1:STN:280:DyaK387mvVWluw%3D%3D 1538787
    • R Luthy JU Bowie D Eisenberg 1992 Nature 356 83 85 10.1038/356083a0 1:STN:280:DyaK387mvVWluw%3D%3D 1538787
    • (1992) Nature , vol.356 , pp. 83-85
    • Luthy, R.1    Bowie, J.U.2    Eisenberg, D.3
  • 74
    • 0004136246 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press Cold Spring Harbor
    • Sambrook J, Russell D (2001) Molecular cloning. Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (2001) Molecular Cloning
    • Sambrook, J.1    Russell, D.2
  • 75
    • 14844294424 scopus 로고    scopus 로고
    • 10.1016/j.pep.2005.01.016 1:CAS:528:DC%2BD2MXjsFCktLw%3D 15915565
    • FW Studier 2005 Protein Expr Purif 41 207 234 10.1016/j.pep.2005.01.016 1:CAS:528:DC%2BD2MXjsFCktLw%3D 15915565
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 78
    • 0034649338 scopus 로고    scopus 로고
    • Mechanistic diversity in a metalloenzyme superfamily
    • DOI 10.1021/bi001814v
    • RN Armstrong 2000 Biochemistry 39 13625 13632 10.1021/bi001814v 1:CAS:528:DC%2BD3cXnsVanurk%3D 11076500 (Pubitemid 30826598)
    • (2000) Biochemistry , vol.39 , Issue.45 , pp. 13625-13632
    • Armstrong, R.N.1
  • 81
    • 0030927104 scopus 로고    scopus 로고
    • Crystal structure of human glyoxalase I - evidence for gene duplication and 3D domain swapping
    • DOI 10.1093/emboj/16.12.3386
    • AD Cameron B Olin M Ridderstrom B Mannervik TA Jones 1997 EMBO J 16 3386 3395 10.1093/emboj/16.12.3386 1:CAS:528:DyaK2sXktlCjtr4%3D 9218781 (Pubitemid 27250034)
    • (1997) EMBO Journal , vol.16 , Issue.12 , pp. 3386-3395
    • Cameron, A.D.1    Olin, B.2    Ridderstrom, M.3    Mannervik, B.4    Jones, T.A.5
  • 82
    • 0034254431 scopus 로고    scopus 로고
    • Determination of the structure of Escherichia coli glyoxalase I suggests a structural basis for differential metal activation
    • DOI 10.1021/bi000856g
    • MM He SL Clugston JF Honek BW Matthews 2000 Biochemistry 39 8719 8727 10.1021/bi000856g 1:CAS:528:DC%2BD3cXksVagtbw%3D 10913283 (Pubitemid 30602781)
    • (2000) Biochemistry , vol.39 , Issue.30 , pp. 8719-8727
    • He, M.M.1    Clugston, S.L.2    Honek, J.F.3    Matthews, B.W.4
  • 84
    • 0030770294 scopus 로고    scopus 로고
    • 10.1016/S0065-3233(08)60319-8 1:CAS:528:DyaK2sXotVyktrs%3D 9338079
    • MP Schlunegger MJ Bennett D Eisenberg 1997 Adv Protein Chem 50 61 122 10.1016/S0065-3233(08)60319-8 1:CAS:528:DyaK2sXotVyktrs%3D 9338079
    • (1997) Adv Protein Chem , vol.50 , pp. 61-122
    • Schlunegger, M.P.1    Bennett, M.J.2    Eisenberg, D.3
  • 85
    • 0032555193 scopus 로고    scopus 로고
    • Active monomeric and dimeric forms of pseudomonas putida glyoxalase I: Evidence for 3D domain swapping
    • DOI 10.1021/bi980868q
    • AP Saint-Jean KR Phillips DJ Creighton MJ Stone 1998 Biochemistry 37 10345 10353 10.1021/bi980868q 1:CAS:528:DyaK1cXktFKqtLc%3D 9671502 (Pubitemid 28357555)
    • (1998) Biochemistry , vol.37 , Issue.29 , pp. 10345-10353
    • Saint-Jean, A.P.1    Phillips, K.R.2    Creighton, D.J.3    Stone, M.J.4
  • 88
    • 0141732267 scopus 로고    scopus 로고
    • Conversion of extradiol aromatic ring-cleaving homoprotocatechuate 2,3-dioxygenase into an intradiol cleaving enzyme
    • DOI 10.1021/ja0368103
    • SL Groce JD Lipscomb 2003 J Am Chem Soc 125 11780 11781 10.1021/ja0368103 1:CAS:528:DC%2BD3sXmvVGhu78%3D 14505375 (Pubitemid 37175388)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.39 , pp. 11780-11781
    • Groce, S.L.1    Lipscomb, J.D.2
  • 89
    • 18544362332 scopus 로고    scopus 로고
    • Aromatic ring cleavage by homoprotocatechuate 2,3-dioxygenase: Role of His200 in the kinetics of interconversion of reaction cycle intermediates
    • DOI 10.1021/bi050180v
    • SL Groce JD Lipscomb 2005 Biochemistry 44 7175 7188 10.1021/bi050180v 1:CAS:528:DC%2BD2MXjtlGltbY%3D 15882056 (Pubitemid 40656662)
    • (2005) Biochemistry , vol.44 , Issue.19 , pp. 7175-7188
    • Groce, S.L.1    Lipscomb, J.D.2


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