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Volumn 52, Issue 3, 2013, Pages 477-487

Structural and mechanistic studies of HpxO, a novel flavin adenine dinucleotide-dependent urate oxidase from Klebsiella pneumoniae

Author keywords

[No Author keywords available]

Indexed keywords

FLAVIN-DEPENDENT; HYDROPEROXIDES; KLEBSIELLA PNEUMONIAE; MECHANISTIC STUDIES; NICOTINAMIDE ADENINE DINUCLEOTIDES; NUCLEOPHILIC ATTACK; OXYGEN TRANSFER; URIC ACIDS; WILD TYPES;

EID: 84872809405     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301262p     Document Type: Article
Times cited : (30)

References (46)
  • 3
    • 62949166438 scopus 로고    scopus 로고
    • Metallo-β-lactamases in Gram-negative bacteria: Introducing the era of pan-resistance?
    • Maltezou, H. C. (2009) Metallo-β-lactamases in Gram-negative bacteria: Introducing the era of pan-resistance? Int. J. Antimicrob. Agents 33, 405.e401-405.e407
    • (2009) Int. J. Antimicrob. Agents , vol.33
    • Maltezou, H.C.1
  • 4
    • 62749195559 scopus 로고    scopus 로고
    • The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria
    • Nordmann, P., Cuzon, G., and Naas, T. (2009) The real threat of Klebsiella pneumoniae carbapenemase-producing bacteria Lancet 9, 228-236
    • (2009) Lancet , vol.9 , pp. 228-236
    • Nordmann, P.1    Cuzon, G.2    Naas, T.3
  • 6
    • 33745962626 scopus 로고    scopus 로고
    • Pyrimidine and Purine Biosynthesis and Degradation in Plants
    • Zrenner, R., Stitt, M., Sonnewald, U., and Boldt, R. (2006) Pyrimidine and Purine Biosynthesis and Degradation in Plants Annu. Rev. Plant Biol. 57, 805-836
    • (2006) Annu. Rev. Plant Biol. , vol.57 , pp. 805-836
    • Zrenner, R.1    Stitt, M.2    Sonnewald, U.3    Boldt, R.4
  • 7
    • 0017122896 scopus 로고
    • Degradation of purines and pyrimidines by microorganisms
    • Vogels, G. D. and Van der Drift, C. (1976) Degradation of purines and pyrimidines by microorganisms Bacteriol. Rev. 40, 403-468
    • (1976) Bacteriol. Rev. , vol.40 , pp. 403-468
    • Vogels, G.D.1    Van Der Drift, C.2
  • 8
    • 57349137274 scopus 로고    scopus 로고
    • The hpx Genetic System for Hypoxanthine Assimilation as a Nitrogen Source in Klebsiella pneumoniae: Gene Organization and Transcriptional Regulation
    • de la Riva, L., Badia, J., Aguilar, J., Bender, R. A., and Baldoma, L. (2008) The hpx Genetic System for Hypoxanthine Assimilation as a Nitrogen Source in Klebsiella pneumoniae: Gene Organization and Transcriptional Regulation J. Bacteriol. 190, 7892-7903
    • (2008) J. Bacteriol. , vol.190 , pp. 7892-7903
    • De La Riva, L.1    Badia, J.2    Aguilar, J.3    Bender, R.A.4    Baldoma, L.5
  • 9
    • 63449129765 scopus 로고    scopus 로고
    • Purine Utilization by Klebsiella oxytoca M5al: Genes for Ring-Oxidizing and -Opening Enzymes
    • Pope, S. D., Chen, L.-L., and Stewart, V. (2009) Purine Utilization by Klebsiella oxytoca M5al: Genes for Ring-Oxidizing and -Opening Enzymes J. Bacteriol. 191, 1006-1017
    • (2009) J. Bacteriol. , vol.191 , pp. 1006-1017
    • Pope, S.D.1    Chen, L.-L.2    Stewart, V.3
  • 10
    • 65249186468 scopus 로고    scopus 로고
    • Biochemical Characterization of the HpxO Enzyme from Klebsiella pneumoniae, a Novel FAD-Dependent Urate Oxidase
    • O'Leary, S. E., Hicks, K. A., Ealick, S. E., and Begley, T. P. (2009) Biochemical Characterization of the HpxO Enzyme from Klebsiella pneumoniae, a Novel FAD-Dependent Urate Oxidase Biochemistry 48, 3033-3035
    • (2009) Biochemistry , vol.48 , pp. 3033-3035
    • O'Leary, S.E.1    Hicks, K.A.2    Ealick, S.E.3    Begley, T.P.4
  • 11
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of FAD-containing proteins
    • Dym, O. and Eisenberg, D. (2001) Sequence-structure analysis of FAD-containing proteins Protein Sci. 10, 1712-1728
    • (2001) Protein Sci. , vol.10 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 12
    • 33745991798 scopus 로고    scopus 로고
    • Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts
    • van Berkel, W. J. H., Kamerbeek, N. M., and Fraaije, M. W. (2006) Flavoprotein monooxygenases, a diverse class of oxidative biocatalysts J. Biotechnol. 124, 670-689
    • (2006) J. Biotechnol. , vol.124 , pp. 670-689
    • Van Berkel, W.J.H.1    Kamerbeek, N.M.2    Fraaije, M.W.3
  • 14
    • 0030991772 scopus 로고    scopus 로고
    • Kinetic Mechanism and Cofactor Content of Soybean Root Nodule Urate Oxidase
    • Kahn, K. and Tipton, P. A. (1997) Kinetic Mechanism and Cofactor Content of Soybean Root Nodule Urate Oxidase Biochemistry 36, 4731-4738
    • (1997) Biochemistry , vol.36 , pp. 4731-4738
    • Kahn, K.1    Tipton, P.A.2
  • 15
    • 0036406502 scopus 로고    scopus 로고
    • Urate oxidase: Single-turnover stopped-flow techniques for detecting two discrete enzyme-bound intermediates
    • Tipton, P. A. (2002) Urate oxidase: Single-turnover stopped-flow techniques for detecting two discrete enzyme-bound intermediates Methods Enzymol. 354, 310-319
    • (2002) Methods Enzymol. , vol.354 , pp. 310-319
    • Tipton, P.A.1
  • 16
    • 0037446748 scopus 로고    scopus 로고
    • General Base Catalysis in the Urate Oxidase Reaction: Evidence for a Novel Thr-Lys Catalytic Diad
    • Imhoff, R. D., Power, N. P., Borrok, M. J., and Tipton, P. A. (2003) General Base Catalysis in the Urate Oxidase Reaction: Evidence for a Novel Thr-Lys Catalytic Diad Biochemistry 42, 4094-4100
    • (2003) Biochemistry , vol.42 , pp. 4094-4100
    • Imhoff, R.D.1    Power, N.P.2    Borrok, M.J.3    Tipton, P.A.4
  • 17
    • 0034669659 scopus 로고    scopus 로고
    • Evidence for Urate Hydroperoxide as an Intermediate in the Urate Oxidase Reaction
    • Sarma, A. D. and Tipton, P. A. (2000) Evidence for Urate Hydroperoxide as an Intermediate in the Urate Oxidase Reaction J. Am. Chem. Soc. 122, 11252-11253
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 11252-11253
    • Sarma, A.D.1    Tipton, P.A.2
  • 18
    • 0026805891 scopus 로고
    • Functional and Evolutionary Relationships among Diverse Oxygenases
    • Harayama, S., Kok, M., and Neidle, E. L. (1992) Functional and Evolutionary Relationships Among Diverse Oxygenases Annu. Rev. Microbiol. 46, 565-601
    • (1992) Annu. Rev. Microbiol. , vol.46 , pp. 565-601
    • Harayama, S.1    Kok, M.2    Neidle, E.L.3
  • 19
    • 77349127553 scopus 로고    scopus 로고
    • Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications
    • Torres Pazmino, D. E., Winkler, M., Glieder, A., and Fraaije, M. W. (2010) Monooxygenases as biocatalysts: Classification, mechanistic aspects and biotechnological applications J. Biotechnol. 146, 9-24
    • (2010) J. Biotechnol. , vol.146 , pp. 9-24
    • Torres Pazmino, D.E.1    Winkler, M.2    Glieder, A.3    Fraaije, M.W.4
  • 20
    • 84906284472 scopus 로고    scopus 로고
    • Flavin-Dependent Enzymes
    • In (Lew, M. and Hung-Wen, L. Eds.) Vol. Section 7.03, pp, Elsevier, Oxford, U.K. - 113
    • Fagan, R. L. and Palfey, B. A. (2010) Flavin-Dependent Enzymes. In Comprehensive Natural Products II (Lew, M. and Hung-Wen, L., Eds.) Vol. 7, Section 7.03, pp 37-113, Elsevier, Oxford, U.K.
    • (2010) Comprehensive Natural Products II , vol.7 , pp. 37
    • Fagan, R.L.1    Palfey, B.A.2
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0001051788 scopus 로고    scopus 로고
    • A novel technique to control the rate of vapour diffusion, giving larger protein crystals
    • Chayen, N. (1997) A novel technique to control the rate of vapour diffusion, giving larger protein crystals J. Appl. Crystallogr. 30, 198-202
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 198-202
    • Chayen, N.1
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • In, pp, Academic Press, San Diego. - 326
    • Otwinowski, Z., Minor, W., and Carter, C. W., Jr. (1997) Processing of X-ray diffraction data collected in oscillation mode. In Methods in Enzymology, pp 307-326, Academic Press, San Diego.
    • (1997) Methods in Enzymology , pp. 307
    • Otwinowski, Z.1    Minor, W.2    Carter Jr., C.W.3
  • 26
    • 4644366388 scopus 로고    scopus 로고
    • HKL2MAP: A graphical user interface for phasing with SHELX programs
    • Pape, T. and Schneider, T. R. (2004) HKL2MAP: A graphical user interface for phasing with SHELX programs J. Appl. Crystallogr. 37, 843-844
    • (2004) J. Appl. Crystallogr. , vol.37 , pp. 843-844
    • Pape, T.1    Schneider, T.R.2
  • 27
  • 30
    • 0028103275 scopus 로고
    • The CCP-4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4 () - 763
    • Collaborative Computational Project Number 4 (1994) The CCP-4 suite: Programs for protein crystallography Acta Crystallogr. D50, 760-763
    • (1994) Acta Crystallogr. , vol.50 , pp. 760
  • 31
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: A program to check the stereochemical quality of protein structures J. Appl. Crystallogr. 26, 283-291
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 35
    • 27744575887 scopus 로고    scopus 로고
    • Properties of p -Hydroxybenzoate Hydroxylase When Stabilized in Its Open Conformation
    • Cole, L. J., Entsch, B., Ortiz-Maldonado, M., and Ballou, D. P. (2005) Properties of p -Hydroxybenzoate Hydroxylase When Stabilized in Its Open Conformation Biochemistry 44, 14807-14817
    • (2005) Biochemistry , vol.44 , pp. 14807-14817
    • Cole, L.J.1    Entsch, B.2    Ortiz-Maldonado, M.3    Ballou, D.P.4
  • 36
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: Conservation mapping in 3D
    • Holm, L. and Rosenstrom, P. (2010) Dali server: Conservation mapping in 3D Nucleic Acids Res. 38, W545-W549
    • (2010) Nucleic Acids Res. , vol.38
    • Holm, L.1    Rosenstrom, P.2
  • 37
    • 84866329633 scopus 로고    scopus 로고
    • Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism
    • Mohanty, S. K., Yu, C.-L., Das, S., Louie, T. M., Gakhar, L., and Subramanian, M. (2012) Delineation of the caffeine C-8 oxidation pathway in Pseudomonas sp. strain CBB1 via characterization of a new trimethyluric acid monooxygenase and genes involved in trimethyluric acid metabolism J. Bacteriol. 194, 3872-3882
    • (2012) J. Bacteriol. , vol.194 , pp. 3872-3882
    • Mohanty, S.K.1    Yu, C.-L.2    Das, S.3    Louie, T.M.4    Gakhar, L.5    Subramanian, M.6
  • 38
    • 0032524753 scopus 로고    scopus 로고
    • The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis
    • Enroth, C., Neujahr, H., Schneider, G., and Lindqvist, Y. (1998) The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis Structure 6, 605-617
    • (1998) Structure , vol.6 , pp. 605-617
    • Enroth, C.1    Neujahr, H.2    Schneider, G.3    Lindqvist, Y.4
  • 39
    • 33751105570 scopus 로고    scopus 로고
    • Crystal Structure of 3-Hydroxybenzoate Hydroxylase from Comamonas testosteroni Has a Large Tunnel for Substrate and Oxygen Access to the Active Site
    • Hiromoto, T., Fujiwara, S., Hosokawa, K., and Yamaguchi, H. (2006) Crystal Structure of 3-Hydroxybenzoate Hydroxylase from Comamonas testosteroni Has a Large Tunnel for Substrate and Oxygen Access to the Active Site J. Mol. Biol. 364, 878-896
    • (2006) J. Mol. Biol. , vol.364 , pp. 878-896
    • Hiromoto, T.1    Fujiwara, S.2    Hosokawa, K.3    Yamaguchi, H.4
  • 40
    • 66049102551 scopus 로고    scopus 로고
    • Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5- carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications
    • McCulloch, K. M., Mukherjee, T., Begley, T. P., and Ealick, S. E. (2009) Structure of the PLP Degradative Enzyme 2-Methyl-3-hydroxypyridine-5-carboxylic Acid Oxygenase from Mesorhizobium loti MAFF303099 and Its Mechanistic Implications Biochemistry 48, 4139-4149
    • (2009) Biochemistry , vol.48 , pp. 4139-4149
    • McCulloch, K.M.1    Mukherjee, T.2    Begley, T.P.3    Ealick, S.E.4
  • 41
    • 42749083544 scopus 로고    scopus 로고
    • Structure of 2,6-Dihydroxypyridine 3-hydroxylase from a Nicotine-degrading Pathway
    • Treiber, N. and Schulz, G. E. (2008) Structure of 2,6-Dihydroxypyridine 3-hydroxylase from a Nicotine-degrading Pathway J. Mol. Biol. 379, 94-104
    • (2008) J. Mol. Biol. , vol.379 , pp. 94-104
    • Treiber, N.1    Schulz, G.E.2
  • 42
    • 20144385856 scopus 로고    scopus 로고
    • Removal of a Methyl Group Causes Global Changes in p -Hydroxybenzoate Hydroxylase
    • Cole, L. J., Gatti, D. L., Entsch, B., and Ballou, D. P. (2005) Removal of a Methyl Group Causes Global Changes in p -Hydroxybenzoate Hydroxylase Biochemistry 44, 8047-8058
    • (2005) Biochemistry , vol.44 , pp. 8047-8058
    • Cole, L.J.1    Gatti, D.L.2    Entsch, B.3    Ballou, D.P.4
  • 45
    • 0029001789 scopus 로고
    • Structure and mechanism of para-hydroxybenzoate hydroxylase
    • Entsch, B. and van Berkel, W. J. (1995) Structure and mechanism of para-hydroxybenzoate hydroxylase FASEB J. 9, 476-483
    • (1995) FASEB J. , vol.9 , pp. 476-483
    • Entsch, B.1    Van Berkel, W.J.2
  • 46
    • 7444239015 scopus 로고    scopus 로고
    • Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: A reassignment of the active-site binding mode
    • Retailleau, P., Colloch, N., Vivares, D., Bonnete, F., Castro, B., El Hajji, M., Mornon, J.-P., Monard, G., and Prange, T. (2004) Complexed and ligand-free high-resolution structures of urate oxidase (Uox) from Aspergillus flavus: A reassignment of the active-site binding mode Acta Crystallogr. D60, 453-462
    • (2004) Acta Crystallogr. , vol.60 , pp. 453-462
    • Retailleau, P.1    Colloch, N.2    Vivares, D.3    Bonnete, F.4    Castro, B.5    El Hajji, M.6    Mornon, J.-P.7    Monard, G.8    Prange, T.9


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