메뉴 건너뛰기




Volumn 281, Issue 18, 2014, Pages 4307-4318

Structural and redox properties of the small laccase Ssl1 from Streptomyces sviceus

Author keywords

bacterial laccase; multicopper oxidase; trinuclear cluster; two domain laccase; type 1 copper center

Indexed keywords

ALIZARIN; COPPER ION; ENZYME VARIANT; INDIGO CARMINE; LACCASE; SMALL LACCASE SSL1; SYRINGOL; TYPE 1 COPPER SITE; TYPE 2 COPPER SITE; TYPE 3 COPPER SITE; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; COORDINATION COMPOUND; COPPER;

EID: 84909952385     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12755     Document Type: Article
Times cited : (53)

References (42)
  • 1
  • 4
    • 84892261428 scopus 로고    scopus 로고
    • Laccases: Biological functions, molecular structure and industrial applications
    • (Polaina J. & MacCabe A. Eds), Springer, The Netherlands
    • Alcalde M, (2007) Laccases: biological functions, molecular structure and industrial applications. In Industrial Enzymes (, Polaina J, &, MacCabe A, eds), pp. 461-476. Springer, The Netherlands.
    • (2007) Industrial Enzymes , pp. 461-476
    • Alcalde, M.1
  • 5
    • 75749150899 scopus 로고    scopus 로고
    • LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii
    • Uthandi S, Saad B, Humbard MA, &, Maupin-Furlow JA, (2010) LccA, an archaeal laccase secreted as a highly stable glycoprotein into the extracellular medium by Haloferax volcanii. Appl Environ Microbiol 76, 733-743.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 733-743
    • Uthandi, S.1    Saad, B.2    Humbard, M.A.3    Maupin-Furlow, J.A.4
  • 8
    • 0030025889 scopus 로고    scopus 로고
    • A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability
    • Xu F, Shin W, Brown SH, Wahleithner JA, Sundaram UM, &, Solomon EI, (1996) A study of a series of recombinant fungal laccases and bilirubin oxidase that exhibit significant differences in redox potential, substrate specificity, and stability. Biochim Biophys Acta 1292, 303-311.
    • (1996) Biochim Biophys Acta , vol.1292 , pp. 303-311
    • Xu, F.1    Shin, W.2    Brown, S.H.3    Wahleithner, J.A.4    Sundaram, U.M.5    Solomon, E.I.6
  • 10
    • 43249105591 scopus 로고    scopus 로고
    • An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates
    • Tadesse MA, D'Annibale A, Galli C, Gentili P, &, Sergi F, (2008) An assessment of the relative contributions of redox and steric issues to laccase specificity towards putative substrates. Org Biomol Chem 6, 868-878.
    • (2008) Org Biomol Chem , vol.6 , pp. 868-878
    • Tadesse, M.A.1    D'Annibale, A.2    Galli, C.3    Gentili, P.4    Sergi, F.5
  • 11
    • 80051483501 scopus 로고    scopus 로고
    • Crystal structure of an ascomycete fungal laccase from Thielavia arenaria - Common structural features of asco-laccases
    • Kallio JP, Gasparetti C, Andberg M, Boer H, Koivula A, Kruus K, Rouvinen J, &, Hakulinen N, (2011) Crystal structure of an ascomycete fungal laccase from Thielavia arenaria-common structural features of asco-laccases. FEBS J 278, 2283-2295.
    • (2011) FEBS J , vol.278 , pp. 2283-2295
    • Kallio, J.P.1    Gasparetti, C.2    Andberg, M.3    Boer, H.4    Koivula, A.5    Kruus, K.6    Rouvinen, J.7    Hakulinen, N.8
  • 13
    • 0037020063 scopus 로고    scopus 로고
    • Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers
    • Piontek K, Antorini M, &, Choinowski T, (2002) Crystal structure of a laccase from the fungus Trametes versicolor at 1.90-A resolution containing a full complement of coppers. J Biol Chem 277, 37663-37669.
    • (2002) J Biol Chem , vol.277 , pp. 37663-37669
    • Piontek, K.1    Antorini, M.2    Choinowski, T.3
  • 15
    • 4344699077 scopus 로고    scopus 로고
    • Characterization of SLAC: A small laccase from Streptomyces coelicolor with unprecedented activity
    • Machczynski MC, Vijgenboom E, Samyn B, &, Canters GW, (2004) Characterization of SLAC: a small laccase from Streptomyces coelicolor with unprecedented activity. Protein Sci 13, 2388-2397.
    • (2004) Protein Sci , vol.13 , pp. 2388-2397
    • Machczynski, M.C.1    Vijgenboom, E.2    Samyn, B.3    Canters, G.W.4
  • 17
    • 84871450755 scopus 로고    scopus 로고
    • Characterization of the alkaline laccase Ssl1 from Streptomyces sviceus with unusual properties discovered by genome mining
    • Gunne M, &, Urlacher VB, (2012) Characterization of the alkaline laccase Ssl1 from Streptomyces sviceus with unusual properties discovered by genome mining. PLoS One 7, e52360.
    • (2012) PLoS One , vol.7 , pp. e52360
    • Gunne, M.1    Urlacher, V.B.2
  • 18
    • 0037632906 scopus 로고    scopus 로고
    • Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus
    • Endo K, Hayashi Y, Hibi T, Hosono K, Beppu T, &, Ueda K, (2003) Enzymological characterization of EpoA, a laccase-like phenol oxidase produced by Streptomyces griseus. J Biochem 133, 671-677.
    • (2003) J Biochem , vol.133 , pp. 671-677
    • Endo, K.1    Hayashi, Y.2    Hibi, T.3    Hosono, K.4    Beppu, T.5    Ueda, K.6
  • 20
    • 33745747078 scopus 로고    scopus 로고
    • Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: Structural, biochemical, enzymatic and stability studies
    • Durao P, Bento I, Fernandes AT, Melo EP, Lindley PF, &, Martins LO, (2006) Perturbations of the T1 copper site in the CotA laccase from Bacillus subtilis: structural, biochemical, enzymatic and stability studies. J Biol Inorg Chem 11, 514-526.
    • (2006) J Biol Inorg Chem , vol.11 , pp. 514-526
    • Durao, P.1    Bento, I.2    Fernandes, A.T.3    Melo, E.P.4    Lindley, P.F.5    Martins, L.O.6
  • 21
    • 44449110619 scopus 로고    scopus 로고
    • Proximal mutations at the type 1 copper site of CotA laccase: Spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants
    • Durao P, Chen Z, Silva CS, Soares CM, Pereira MM, Todorovic S, Hildebrandt P, Bento I, Lindley PF, &, Martins LO, (2008) Proximal mutations at the type 1 copper site of CotA laccase: spectroscopic, redox, kinetic and structural characterization of I494A and L386A mutants. Biochem J 412, 339-346.
    • (2008) Biochem J , vol.412 , pp. 339-346
    • Durao, P.1    Chen, Z.2    Silva, C.S.3    Soares, C.M.4    Pereira, M.M.5    Todorovic, S.6    Hildebrandt, P.7    Bento, I.8    Lindley, P.F.9    Martins, L.O.10
  • 22
    • 79953842858 scopus 로고    scopus 로고
    • Design parameters for tuning the type 1 Cu multicopper oxidase redox potential: Insight from a combination of first principles and empirical molecular dynamics simulations
    • Hong G, Ivnitski DM, Johnson GR, Atanassov P, &, Pachter R, (2011) Design parameters for tuning the type 1 Cu multicopper oxidase redox potential: insight from a combination of first principles and empirical molecular dynamics simulations. J Am Chem Soc 133, 4802-4809.
    • (2011) J Am Chem Soc , vol.133 , pp. 4802-4809
    • Hong, G.1    Ivnitski, D.M.2    Johnson, G.R.3    Atanassov, P.4    Pachter, R.5
  • 23
    • 61849150510 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction analysis of a putative two-domain-type laccase from a metagenome
    • Komori H, Miyazaki K, &, Higuchi Y, (2009) Crystallization and preliminary X-ray diffraction analysis of a putative two-domain-type laccase from a metagenome. Acta Crystallogr Sect F Struct Biol Cryst Commun 65, 264-266.
    • (2009) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.65 , pp. 264-266
    • Komori, H.1    Miyazaki, K.2    Higuchi, Y.3
  • 24
    • 0142169403 scopus 로고    scopus 로고
    • Novel types of two-domain multi-copper oxidases: Possible missing links in the evolution
    • Nakamura K, Kawabata T, Yura K, &, Go N, (2003) Novel types of two-domain multi-copper oxidases: possible missing links in the evolution. FEBS Lett 553, 239-244.
    • (2003) FEBS Lett , vol.553 , pp. 239-244
    • Nakamura, K.1    Kawabata, T.2    Yura, K.3    Go, N.4
  • 25
    • 3042694367 scopus 로고    scopus 로고
    • Determinants of the relative reduction potentials of type-1 copper sites in proteins
    • Li H, Webb SP, Ivanic J, &, Jensen JH, (2004) Determinants of the relative reduction potentials of type-1 copper sites in proteins. J Am Chem Soc 126, 8010-8019.
    • (2004) J Am Chem Soc , vol.126 , pp. 8010-8019
    • Li, H.1    Webb, S.P.2    Ivanic, J.3    Jensen, J.H.4
  • 28
    • 39649112653 scopus 로고    scopus 로고
    • Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor
    • Gallaway J, Wheeldon I, Rincon R, Atanassov P, Banta S, &, Barton SC, (2008) Oxygen-reducing enzyme cathodes produced from SLAC, a small laccase from Streptomyces coelicolor. Biosens Bioelectron 23, 1229-1235.
    • (2008) Biosens Bioelectron , vol.23 , pp. 1229-1235
    • Gallaway, J.1    Wheeldon, I.2    Rincon, R.3    Atanassov, P.4    Banta, S.5    Barton, S.C.6
  • 29
    • 79952095532 scopus 로고    scopus 로고
    • Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type i copper center in Escherichia coli CueO and the deletion mutant Δα5-7 CueO
    • Kataoka K, Hirota S, Maeda Y, Kogi H, Shinohara N, Sekimoto M, &, Sakurai T, (2011) Enhancement of laccase activity through the construction and breakdown of a hydrogen bond at the type I copper center in Escherichia coli CueO and the deletion mutant Δα5-7 CueO. Biochemistry 50, 558-565.
    • (2011) Biochemistry , vol.50 , pp. 558-565
    • Kataoka, K.1    Hirota, S.2    Maeda, Y.3    Kogi, H.4    Shinohara, N.5    Sekimoto, M.6    Sakurai, T.7
  • 30
    • 0030589040 scopus 로고    scopus 로고
    • Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: A highly oxidizing cupredoxin with extreme acid stability
    • Walter RL, Ealick SE, Friedman AM, Blake RC, Proctor P, &, Shoham M, (1996) Multiple wavelength anomalous diffraction (MAD) crystal structure of rusticyanin: a highly oxidizing cupredoxin with extreme acid stability. J Mol Biol 263, 730-751.
    • (1996) J Mol Biol , vol.263 , pp. 730-751
    • Walter, R.L.1    Ealick, S.E.2    Friedman, A.M.3    Blake, R.C.4    Proctor, P.5    Shoham, M.6
  • 31
    • 0000449668 scopus 로고
    • + for calculation of one-electron redox potentials of antioxidants
    • + for calculation of one-electron redox potentials of antioxidants. J Phys Chem 95, 10824-10827.
    • (1991) J Phys Chem , vol.95 , pp. 10824-10827
    • Jovanovic, S.V.1    Tosic, M.2    Simic, M.G.3
  • 32
    • 0032312967 scopus 로고    scopus 로고
    • Voltammetric behavior of alizarin red S adsorbed on electrochemically pretreated glassy carbon electrodes
    • Dai H-P, &, Shiu K-K, (1998) Voltammetric behavior of alizarin red S adsorbed on electrochemically pretreated glassy carbon electrodes. Electrochim Acta 43, 2709-2715.
    • (1998) Electrochim Acta , vol.43 , pp. 2709-2715
    • Dai, H.-P.1    Shiu, K.-K.2
  • 33
    • 65649097276 scopus 로고    scopus 로고
    • Crystal structure of a two-domain multicopper oxidase: Implications for the evolution of multicopper blue proteins
    • Lawton TJ, Sayavedra-Soto LA, Arp DJ, &, Rosenzweig AC, (2009) Crystal structure of a two-domain multicopper oxidase: implications for the evolution of multicopper blue proteins. J Biol Chem 284, 10174-10180.
    • (2009) J Biol Chem , vol.284 , pp. 10174-10180
    • Lawton, T.J.1    Sayavedra-Soto, L.A.2    Arp, D.J.3    Rosenzweig, A.C.4
  • 34
    • 70349631652 scopus 로고    scopus 로고
    • Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine
    • Choi M, Sukumar N, Liu A, &, Davidson VL, (2009) Defining the role of the axial ligand of the type 1 copper site in amicyanin by replacement of methionine with leucine. Biochemistry 48, 9174-9184.
    • (2009) Biochemistry , vol.48 , pp. 9174-9184
    • Choi, M.1    Sukumar, N.2    Liu, A.3    Davidson, V.L.4
  • 35
    • 70449090691 scopus 로고    scopus 로고
    • Rationally tuning the reduction potential of a single cupredoxin beyond the natural range
    • Marshall NM, Garner DK, Wilson TD, Gao YG, Robinson H, Nilges MJ, &, Lu Y, (2009) Rationally tuning the reduction potential of a single cupredoxin beyond the natural range. Nature 462, 113-116.
    • (2009) Nature , vol.462 , pp. 113-116
    • Marshall, N.M.1    Garner, D.K.2    Wilson, T.D.3    Gao, Y.G.4    Robinson, H.5    Nilges, M.J.6    Lu, Y.7
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project N
    • Collaborative Computational Project N (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 40
    • 0031033309 scopus 로고    scopus 로고
    • Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases
    • Xu F, (1997) Effects of redox potential and hydroxide inhibition on the pH activity profile of fungal laccases. J Biol Chem 272, 924-928.
    • (1997) J Biol Chem , vol.272 , pp. 924-928
    • Xu, F.1
  • 41
    • 0034629250 scopus 로고    scopus 로고
    • Laccase activity tests and laccase inhibitors
    • Johannes C, &, Majcherczyk A, (2000) Laccase activity tests and laccase inhibitors. J Biotechnol 78, 193-199.
    • (2000) J Biotechnol , vol.78 , pp. 193-199
    • Johannes, C.1    Majcherczyk, A.2
  • 42
    • 0027096634 scopus 로고
    • Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators
    • Wariishi H, Valli K, &, Gold MH, (1992) Manganese(II) oxidation by manganese peroxidase from the basidiomycete Phanerochaete chrysosporium. Kinetic mechanism and role of chelators. J Biol Chem 267, 23688-23695.
    • (1992) J Biol Chem , vol.267 , pp. 23688-23695
    • Wariishi, H.1    Valli, K.2    Gold, M.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.