메뉴 건너뛰기




Volumn 23, Issue 3-4, 2005, Pages 261-269

Integrated approach for production of recombinant acetylacetone dioxygenase from Acinetobacter johnsonii

Author keywords

Affinity purification; Dke1; Fe2+ cofactor; Non heme metal dependent dioxygenases; Stability

Indexed keywords

CHEMICAL BONDS; CHROMATOGRAPHY; ENZYMES; ESCHERICHIA COLI; IRON; MASS SPECTROMETRY; OXYGEN; PURIFICATION; STOICHIOMETRY; SUBSTRATES;

EID: 28244492851     PISSN: 10242422     EISSN: 10292446     Source Type: Journal    
DOI: 10.1080/10242420500183543     Document Type: Article
Times cited : (8)

References (15)
  • 3
    • 1542378704 scopus 로고    scopus 로고
    • Dioxygen activation at mononuclear non-heme iron active sites: Enzymes, models, and intermediates
    • Costas M, Mehn MP, Jensen MP, Que L, Jr. 2004. Dioxygen activation at mononuclear non-heme iron active sites: enzymes, models, and intermediates. Chem Rev 104:939-986.
    • (2004) Chem. Rev. , vol.104 , pp. 939-986
    • Costas, M.1    Mehn, M.P.2    Jensen, M.P.3    Que Jr., L.4
  • 4
    • 0027442082 scopus 로고
    • Characterization of 2,2′,3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium. Sphingomonas sp. strain RW1
    • Happe B, Eltis LD, Poth H, Hedderich R, Timmis KN. 1993. Characterization of 2,2′,3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium. Sphingomonas sp. strain RW1. J Bacteriol 175:7313-7320.
    • (1993) J. Bacteriol. , vol.175 , pp. 7313-7320
    • Happe, B.1    Eltis, L.D.2    Poth, H.3    Hedderich, R.4    Timmis, K.N.5
  • 5
    • 0346363679 scopus 로고    scopus 로고
    • Diketone-cleaving enzyme Dke1 production by Acinetobacter johnsonii - Optimization of fermentation conditions
    • Hofer H, Mandl T, Steiner W. 2004. Diketone-cleaving enzyme Dke1 production by Acinetobacter johnsonii - optimization of fermentation conditions. J Biotechnol 107:73-81.
    • (2004) J. Biotechnol. , vol.107 , pp. 73-81
    • Hofer, H.1    Mandl, T.2    Steiner, W.3
  • 6
    • 0037465347 scopus 로고    scopus 로고
    • (4-Hydroxyphenyl)-pyruvate dioxygenase from Streptomyces avermitilis: The basis for ordered substrate addition
    • Johnson-Winters K, Purpero VM, Kavana M, Nelson T, Moran GR. 2003. (4-Hydroxyphenyl)-pyruvate dioxygenase from Streptomyces avermitilis: the basis for ordered substrate addition. Biochemistry 42:2072-2080.
    • (2003) Biochemistry , vol.42 , pp. 2072-2080
    • Johnson-Winters, K.1    Purpero, V.M.2    Kavana, M.3    Nelson, T.4    Moran, G.R.5
  • 7
    • 0008899768 scopus 로고    scopus 로고
    • The preparation of protein digests for mass spectrometric sequencing
    • New York: Wiley-Interscience
    • Kinter M, Sherman NE. 2000. The preparation of protein digests for mass spectrometric sequencing. New York: Wiley-Interscience. p 147-165.
    • (2000) , pp. 147-165
    • Kinter, M.1    Sherman, N.E.2
  • 9
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • Lilie H, Schwarz E, Rudolph R. 1998. Advances in refolding of proteins produced in E. coli. Curr Opin Biotechnol 9:497-501.
    • (1998) Curr. Opin. Biotechnol. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 10
    • 0039302669 scopus 로고    scopus 로고
    • Dioxygen activation by enzymes with mononuclear non-heme iron active sites
    • Que L, Jr, Ho RY. 1996. Dioxygen activation by enzymes with mononuclear non-heme iron active sites. Chem Rev 96:2607-2624.
    • (1996) Chem. Rev. , vol.96 , pp. 2607-2624
    • Que Jr., L.1    Ho, R.Y.2
  • 11
    • 0033814033 scopus 로고    scopus 로고
    • Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins
    • Skerra A, Schmidt TG. 2000. Use of the Strep-Tag and streptavidin for detection and purification of recombinant proteins. Methods Enzymol 326:271-304.
    • (2000) Methods Enzymol. , vol.326 , pp. 271-304
    • Skerra, A.1    Schmidt, T.G.2
  • 13
    • 0037325484 scopus 로고    scopus 로고
    • Acetylacetone-cleaving enzyme Dke1: A novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii
    • Straganz GD, Glieder A, Brecker L, Ribbons DW, Steiner W. 2003. Acetylacetone-cleaving enzyme Dke1: a novel C-C-bond-cleaving enzyme from Acinetobacter johnsonii. Biochem J 369:573-581.
    • (2003) Biochem. J. , vol.369 , pp. 573-581
    • Straganz, G.D.1    Glieder, A.2    Brecker, L.3    Ribbons, D.W.4    Steiner, W.5
  • 14
    • 28244501850 scopus 로고    scopus 로고
    • X-ray crystal structure of acetylacetone-cleaving dioxygenase of Acinetobacter johnsonii and NMR evidence for a strong short hydrogen bond in the active site of HbHNL
    • PhD-Thesis, Karl Franzens University of Graz, Graz, Austria
    • Stranzl GR. 2002. X-ray crystal structure of acetylacetone-cleaving dioxygenase of Acinetobacter johnsonii and NMR evidence for a strong short hydrogen bond in the active site of HbHNL. PhD-Thesis, Karl Franzens University of Graz, Graz, Austria.
    • (2002)
    • Stranzl, G.R.1
  • 15
    • 0032567402 scopus 로고    scopus 로고
    • Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl-1, 2-dioxygenase by t-butanol
    • Vaillancourt FH, Han S, Fortin PD, Bolin JT, Eltis LD. 1998. Molecular basis for the stabilization and inhibition of 2,3-dihydroxybiphenyl-1, 2-dioxygenase by t-butanol. J Biol Chem 273:34887-34895.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34887-34895
    • Vaillancourt, F.H.1    Han, S.2    Fortin, P.D.3    Bolin, J.T.4    Eltis, L.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.