메뉴 건너뛰기




Volumn 341, Issue 1, 2004, Pages 171-184

Characterization and manipulation of the Pseudomonas aeruginosa dimethylarginine dimethylaminohydrolase monomer-dimer equilibrium

Author keywords

ADMA, asymmetric dimethylarginine; AMA, asymmetric methylarginine; analytical ultracentrifugation; ASA, accessible surface area; AUC, analytical ultracentrifugation; dimethyl arginine; heteronuclear NMR; portain self association; site directed mutagenesis

Indexed keywords

ARGININE; BACTERIAL ENZYME; DIMER; DIMETHYLARGININASE; ENZYME VARIANT; GLUTAMIC ACID; HISTIDINE; MONOMER;

EID: 4143092645     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.05.057     Document Type: Article
Times cited : (14)

References (39)
  • 1
    • 0033566683 scopus 로고    scopus 로고
    • Biological significance of endogenous methylarginines that inhibit nitric oxide synthases
    • Leiper J., Vallance P. Biological significance of endogenous methylarginines that inhibit nitric oxide synthases. Cardiovasc. Res. 43:1999;542-548
    • (1999) Cardiovasc. Res. , vol.43 , pp. 542-548
    • Leiper, J.1    Vallance, P.2
  • 2
    • 0014940650 scopus 로고
    • ε-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine
    • ε-mono-, di-, and trimethyllysine, and glucosylgalactosyl- and galactosyl-delta-hydroxylysine from human urine. J. Biol. Chem. 245:1970;5751-5758
    • (1970) J. Biol. Chem. , vol.245 , pp. 5751-5758
    • Kakimoto, Y.1    Akazawa, S.2
  • 3
    • 0035936406 scopus 로고    scopus 로고
    • Plasma concentration of asymmetrical dimethylarginine and mortality in patients with end-stage renal disease: A prospective study
    • Zoccali C., Bode-Böger S., Mallamaci F., Benedetto F., Tripepi G., Malatino L., et al. Plasma concentration of asymmetrical dimethylarginine and mortality in patients with end-stage renal disease: a prospective study. Lancet. 358:2001;2113-2117
    • (2001) Lancet , vol.358 , pp. 2113-2117
    • Zoccali, C.1    Bode-Böger, S.2    Mallamaci, F.3    Benedetto, F.4    Tripepi, G.5    Malatino, L.6
  • 4
    • 0024340138 scopus 로고
    • G-dimethylarginine dimethylaminohydrolase, from rat kidney
    • G-dimethylarginine dimethylaminohydrolase, from rat kidney. J. Biol. Chem. 264:1989;10205-10209
    • (1989) J. Biol. Chem. , vol.264 , pp. 10205-10209
    • Ogawa, T.1    Kimoto, M.2    Sasaoka, K.3
  • 5
    • 0026548912 scopus 로고
    • Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure
    • Vallance P., Leone A., Calver A., Collier J., Moncada S. Accumulation of an endogenous inhibitor of nitric oxide synthesis in chronic renal failure. Lancet. 339:1992;572-575
    • (1992) Lancet , vol.339 , pp. 572-575
    • Vallance, P.1    Leone, A.2    Calver, A.3    Collier, J.4    Moncada, S.5
  • 7
    • 0033214074 scopus 로고    scopus 로고
    • Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases
    • Leiper J.M., Parry H., Kimoto M., Ogawa T., Russell R.J., Whitley G.S. Identification of two human dimethylarginine dimethylaminohydrolases with distinct tissue distributions and homology with microbial arginine deiminases. Biochem. J. 343:1999;209-214
    • (1999) Biochem. J. , vol.343 , pp. 209-214
    • Leiper, J.M.1    Parry, H.2    Kimoto, M.3    Ogawa, T.4    Russell, R.J.5    Whitley, G.S.6
  • 8
    • 0032864893 scopus 로고    scopus 로고
    • Identification of microbial dimethylarginine dimethylaminohydrolase enzymes
    • Santa-Maria J., Vallance P., Charles I.G., Leiper J.M. Identification of microbial dimethylarginine dimethylaminohydrolase enzymes. Mol. Microbiol. 33:1999;1278-1279
    • (1999) Mol. Microbiol. , vol.33 , pp. 1278-1279
    • Santa-Maria, J.1    Vallance, P.2    Charles, I.G.3    Leiper, J.M.4
  • 9
    • 0034885255 scopus 로고    scopus 로고
    • Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase
    • Murray-Rust J., Leiper J., McAlister M., Phelan J., Tilley S., Santa-Maria J. Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase. Nature Struct. Biol. 8:2001;679-683
    • (2001) Nature Struct. Biol. , vol.8 , pp. 679-683
    • Murray-Rust, J.1    Leiper, J.2    McAlister, M.3    Phelan, J.4    Tilley, S.5    Santa-Maria, J.6
  • 10
    • 0030978412 scopus 로고    scopus 로고
    • Crystal structure and mechanism of human L-arginine: Glycine amidinotransferase: A mitochondrial enzyme involved in creatine biosynthesis
    • Humm A., Fritsche E., Steinbacher S., Huber R. Crystal structure and mechanism of human L-arginine : glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J. 16:1997;3373-3385
    • (1997) EMBO J. , vol.16 , pp. 3373-3385
    • Humm, A.1    Fritsche, E.2    Steinbacher, S.3    Huber, R.4
  • 11
    • 0032559012 scopus 로고    scopus 로고
    • Crystal structure of L-arginine: Inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: An enzyme involved in streptomycin biosynthesis
    • Fritsche E., Bergner A., Humm A., Piepersberg W., Huber R. Crystal structure of L-arginine : inosamine-phosphate amidinotransferase StrB1 from Streptomyces griseus: an enzyme involved in streptomycin biosynthesis. Biochemistry. 37:1998;17664-17672
    • (1998) Biochemistry , vol.37 , pp. 17664-17672
    • Fritsche, E.1    Bergner, A.2    Humm, A.3    Piepersberg, W.4    Huber, R.5
  • 12
    • 0034872508 scopus 로고    scopus 로고
    • An elusive propeller-like fold
    • Paoli M. An elusive propeller-like fold. Nature Struct. Biol. 8:2001;744-745
    • (2001) Nature Struct. Biol. , vol.8 , pp. 744-745
    • Paoli, M.1
  • 13
    • 0036883907 scopus 로고    scopus 로고
    • Blocking NO synthesis: How, where and why?
    • Vallance P., Leiper J. Blocking NO synthesis: how, where and why? Nature Rev. Drug. Disc. 1:2002;939-950
    • (2002) Nature Rev. Drug. Disc. , vol.1 , pp. 939-950
    • Vallance, P.1    Leiper, J.2
  • 14
    • 0141928674 scopus 로고    scopus 로고
    • TROSY in NMR studies of the structure and function of large biological macromolecules
    • Fernandez C., Wider G. TROSY in NMR studies of the structure and function of large biological macromolecules. Curr. Opin. Struct. Biol. 13:2003;570-580
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 570-580
    • Fernandez, C.1    Wider, G.2
  • 15
    • 0034306122 scopus 로고    scopus 로고
    • TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution
    • Riek R., Pervushin K., Wüthrich K. TROSY and CRINEPT: NMR with large molecular and supramolecular structures in solution. Trends Biochem. Sci. 25:2000;462-468
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 462-468
    • Riek, R.1    Pervushin, K.2    Wüthrich, K.3
  • 16
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker S.B., Hajduk P.J., Meadows R.P., Fesik S.W. Discovering high-affinity ligands for proteins: SAR by NMR. Science. 274:1996;1531-1534
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 18
    • 0037189901 scopus 로고    scopus 로고
    • Four-dimensional NMR spectroscopy of a 723-residue protein: Chemical shift assignments and secondary structure of malate synthase G
    • Tugarinov V., Muhandiram R., Ayed A., Kay L.E. Four-dimensional NMR spectroscopy of a 723-residue protein: chemical shift assignments and secondary structure of malate synthase G. J. Am. Chem. Soc. 124:2002;10025-10035
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10025-10035
    • Tugarinov, V.1    Muhandiram, R.2    Ayed, A.3    Kay, L.E.4
  • 19
    • 0031595590 scopus 로고    scopus 로고
    • 15N multidimensional NMR to study the structure and dynamics of proteins
    • 15N multidimensional NMR to study the structure and dynamics of proteins. Annu. Rev. Biophys. Biomol. Struct. 27:1998;357-406
    • (1998) Annu. Rev. Biophys. Biomol. Struct. , vol.27 , pp. 357-406
    • Gardner, K.H.1    Kay, L.E.2
  • 20
    • 0034993094 scopus 로고    scopus 로고
    • Protein folds propelled by diversity
    • Paoli M. Protein folds propelled by diversity. Prog. Biophys. Mol. Biol. 76:2001;103-130
    • (2001) Prog. Biophys. Mol. Biol. , vol.76 , pp. 103-130
    • Paoli, M.1
  • 21
    • 0242558716 scopus 로고    scopus 로고
    • Beta propellers: Structural rigidity and functional diversity
    • Fulop V., Jones D.T. Beta propellers: structural rigidity and functional diversity. Curr. Opin. Struct. Biol. 9:1999;715-721
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 715-721
    • Fulop, V.1    Jones, D.T.2
  • 23
    • 0000521134 scopus 로고
    • Spin-echo water suppression for the generation of pure-phase two-dimensional NMR-spectra
    • Sklenar V., Bax A. Spin-echo water suppression for the generation of pure-phase two-dimensional NMR-spectra. J. Magn. Reson. 74:1987;469-479
    • (1987) J. Magn. Reson. , vol.74 , pp. 469-479
    • Sklenar, V.1    Bax, A.2
  • 24
    • 0027350599 scopus 로고
    • Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS
    • Anglister J., Grzesiek S., Ren H., Klee C.B., Bax A. Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. J. Biomol. NMR. 3:1993;121-126
    • (1993) J. Biomol. NMR , vol.3 , pp. 121-126
    • Anglister, J.1    Grzesiek, S.2    Ren, H.3    Klee, C.B.4    Bax, A.5
  • 25
    • 0024449503 scopus 로고
    • 15N inverse detected heteronuclear NMR spectroscopy: Application to staphylococcal nuclease
    • 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease. Biochemistry. 28:1989;8972-8979
    • (1989) Biochemistry , vol.28 , pp. 8972-8979
    • Kay, L.E.1    Torchia, D.A.2    Bax, A.3
  • 26
    • 0028865843 scopus 로고
    • 3D domain swapping: A mechanism for oligomer assembly
    • Bennett M.J., Schlunegger M.P., Eisenberg D. 3D domain swapping: a mechanism for oligomer assembly. Protein Sci. 4:1995;2455-2468
    • (1995) Protein Sci. , vol.4 , pp. 2455-2468
    • Bennett, M.J.1    Schlunegger, M.P.2    Eisenberg, D.3
  • 28
    • 0030963093 scopus 로고    scopus 로고
    • Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
    • Tjandra N., Garrett D.S., Gronenborn A.M., Bax A., Clore G.M. Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy. Nature Struct. Biol. 4:1997;443-449
    • (1997) Nature Struct. Biol. , vol.4 , pp. 443-449
    • Tjandra, N.1    Garrett, D.S.2    Gronenborn, A.M.3    Bax, A.4    Clore, G.M.5
  • 29
    • 0142183439 scopus 로고    scopus 로고
    • Large-scale millisecond intersubunit dynamics in the B subunit homopentamer of the toxin derived from Escherichia coli O157
    • Yung A., Bruce Turnbull W., Kalverda A.P., Thompson G.S., Homans S.W., Kitov P., Bundle D.R. Large-scale millisecond intersubunit dynamics in the B subunit homopentamer of the toxin derived from Escherichia coli O157. J. Am. Chem. Soc. 125:2003;13058-13062
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 13058-13062
    • Yung, A.1    Bruce Turnbull, W.2    Kalverda, A.P.3    Thompson, G.S.4    Homans, S.W.5    Kitov, P.6    Bundle, D.R.7
  • 31
    • 0034669530 scopus 로고    scopus 로고
    • A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline
    • Knipp M., VaŤák M. A colorimetric 96-well microtiter plate assay for the determination of enzymatically formed citrulline. Anal. Biochem. 286:2000;257-264
    • (2000) Anal. Biochem. , vol.286 , pp. 257-264
    • Knipp, M.1    Vaťák, M.2
  • 32
    • 0023049766 scopus 로고
    • Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences
    • Perkins S.J. Protein volumes and hydration effects. The calculations of partial specific volumes, neutron scattering matchpoints and 280-nm absorption coefficients for proteins and glycoproteins from amino acid sequences. Eur. J. Biochem. 157:1986;169-180
    • (1986) Eur. J. Biochem. , vol.157 , pp. 169-180
    • Perkins, S.J.1
  • 34
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay L.E., Keifer P., Saarinen T. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114:1992;10663-10665
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 35
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR. 4:1994;845-858
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4
  • 36
    • 0032852490 scopus 로고    scopus 로고
    • NMR exchange broadening arising from specific low affinity protein self-association: Analysis of nitrogen-15 nuclear relaxation for rat CD2 domain
    • Pfuhl M., Chen H.A., Kristensen S.M., Driscoll P.C. NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain. J. Biomol. NMR. 14:1999;307-320
    • (1999) J. Biomol. NMR , vol.14 , pp. 307-320
    • Pfuhl, M.1    Chen, H.A.2    Kristensen, S.M.3    Driscoll, P.C.4
  • 37
    • 0034625316 scopus 로고    scopus 로고
    • Backbone dynamics of the C-terminal SH2 domain of the p85α subunit of phosphoinositide 3-kinase: Effect of phosphotyrosine-peptide binding and characterization of slow conformational exchange processes
    • Kristensen S.M., Siegal G., Sankar A., Driscoll P.C. Backbone dynamics of the C-terminal SH2 domain of the p85α subunit of phosphoinositide 3-kinase: effect of phosphotyrosine-peptide binding and characterization of slow conformational exchange processes. J. Mol. Biol. 299:2000;771-788
    • (2000) J. Mol. Biol. , vol.299 , pp. 771-788
    • Kristensen, S.M.1    Siegal, G.2    Sankar, A.3    Driscoll, P.C.4
  • 38
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P.J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 39
    • 0026319199 scopus 로고
    • Protein folding and association, insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association, insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.