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Volumn 7, Issue 10, 2012, Pages

Structural Characterization of the Enzymes Composing the Arginine Deiminase Pathway in Mycoplasma penetrans

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE DEIMINASE; CARBAMATE KINASE; ORNITHINE CARBAMOYLTRANSFERASE;

EID: 84867635948     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047886     Document Type: Article
Times cited : (17)

References (63)
  • 1
    • 0018099097 scopus 로고
    • The mycoplasmas
    • Razin S, (1978) The mycoplasmas. Microbiol Rev 42: 414-470.
    • (1978) Microbiol Rev , vol.42 , pp. 414-470
    • Razin, S.1
  • 2
    • 0031770391 scopus 로고    scopus 로고
    • Molecular biology and pathogenicity of mycoplasmas
    • Razin S, Yogev D, Naot Y, (1998) Molecular biology and pathogenicity of mycoplasmas. Microbiol Mol Biol Rev 62: 1094-156.
    • (1998) Microbiol Mol Biol Rev , vol.62 , pp. 1094-1156
    • Razin, S.1    Yogev, D.2    Naot, Y.3
  • 3
    • 0031441913 scopus 로고    scopus 로고
    • The comparative metabolism of the Mollicutes (Mycoplasmas): the utility for taxonomic classification and the relationship of putative gene annotation and phylogeny to enzymatic function in the smallest free-living cells
    • Pollack JD, Williams MV, McElhaney RN, (1997) The comparative metabolism of the Mollicutes (Mycoplasmas): the utility for taxonomic classification and the relationship of putative gene annotation and phylogeny to enzymatic function in the smallest free-living cells. Critical Rev Microbiol 23: 269-354.
    • (1997) Critical Rev Microbiol , vol.23 , pp. 269-354
    • Pollack, J.D.1    Williams, M.V.2    McElhaney, R.N.3
  • 5
    • 84867659391 scopus 로고
    • Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster
    • Ruepp A, Soppa J, (1993) Fermentative arginine degradation in Halobacterium salinarium (formerly Halobacterium halobium): genes, gene products, and transcripts of the arcRACB gene cluster. Plant Physiol 101: 429-34.
    • (1993) Plant Physiol , vol.101 , pp. 429-434
    • Ruepp, A.1    Soppa, J.2
  • 6
    • 84867646441 scopus 로고
    • Arabidopsis chloroplasts dissimilate L-arginine and L-citrulline for use as N source
    • Ludwig RA, (1992) Arabidopsis chloroplasts dissimilate L-arginine and L-citrulline for use as N source. Mol Biochem Parasitol 51: 29-36.
    • (1992) Mol Biochem Parasitol , vol.51 , pp. 29-36
    • Ludwig, R.A.1
  • 8
    • 0028534943 scopus 로고
    • Subcellular localization of the enzymes of the arginine dihydrolase pathway in Trichomonas vaginalis and Tritrichomonas foetus
    • Yarlett N, Lindmark DG, Goldberg B, Moharrami MA, Bacchi CJ, (1994) Subcellular localization of the enzymes of the arginine dihydrolase pathway in Trichomonas vaginalis and Tritrichomonas foetus. J Eukaryot Microbiol 41: 554-9.
    • (1994) J Eukaryot Microbiol , vol.41 , pp. 554-559
    • Yarlett, N.1    Lindmark, D.G.2    Goldberg, B.3    Moharrami, M.A.4    Bacchi, C.J.5
  • 9
    • 0030767109 scopus 로고    scopus 로고
    • Mycoplasma genes: a case for reflective annotation
    • Pollack JD (1997). Mycoplasma genes: a case for reflective annotation. Trends Microbiol. 5, 413-419.
    • (1997) Trends Microbiol , vol.5 , pp. 413-419
    • Pollack, J.D.1
  • 10
    • 0014208217 scopus 로고
    • The occurrence of a catabolic and an anabolic ornithine carbamoyltransferase in Pseudomonas
    • Stalon V, Ramos F, Piérard A, Wiame JM, (1967) The occurrence of a catabolic and an anabolic ornithine carbamoyltransferase in Pseudomonas. Biochim Biophys Acta 139: 91-7.
    • (1967) Biochim Biophys Acta , vol.139 , pp. 91-97
    • Stalon, V.1    Ramos, F.2    Piérard, A.3    Wiame, J.M.4
  • 11
    • 0021664042 scopus 로고
    • Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: evidence for a four-gene cluster encoding the arginine deiminase pathway
    • Vander Wauven C, Piérard A, Kley-Raymann M, Haas D, (1984) Pseudomonas aeruginosa mutants affected in anaerobic growth on arginine: evidence for a four-gene cluster encoding the arginine deiminase pathway. J Bacteriol 160: 928-34.
    • (1984) J Bacteriol , vol.160 , pp. 928-934
    • Vander Wauven, C.1    Piérard, A.2    Kley-Raymann, M.3    Haas, D.4
  • 12
    • 0033522899 scopus 로고    scopus 로고
    • The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase
    • Uriarte M, Marina A, Ramón-Maiques S, Fita I, Rubio V, (1999) The carbamoyl-phosphate synthetase of Pyrococcus furiosus is enzymologically and structurally a carbamate kinase. J Biol Chem 274: 16295-303.
    • (1999) J Biol Chem , vol.274 , pp. 16295-16303
    • Uriarte, M.1    Marina, A.2    Ramón-Maiques, S.3    Fita, I.4    Rubio, V.5
  • 13
    • 0032549032 scopus 로고    scopus 로고
    • Cloning and expression of a prokaryotic enzyme, arginine deiminase, from a primitive eukaryote Giardia intestinalis
    • Knodler LA, Sekyere EO, Stewart TS, Schofield PJ, Edwards MR, (1998) Cloning and expression of a prokaryotic enzyme, arginine deiminase, from a primitive eukaryote Giardia intestinalis. J Biol Chem 273: 4470-7.
    • (1998) J Biol Chem , vol.273 , pp. 4470-4477
    • Knodler, L.A.1    Sekyere, E.O.2    Stewart, T.S.3    Schofield, P.J.4    Edwards, M.R.5
  • 15
    • 0024584223 scopus 로고
    • Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of Pseudomonas aeruginosa
    • Baur H, Luethi E, Stalon V, Mercenier A, Haas D, (1989) Sequence analysis and expression of the arginine-deiminase and carbamate-kinase genes of Pseudomonas aeruginosa. Eur J Biochem 179: 53-60.
    • (1989) Eur J Biochem , vol.179 , pp. 53-60
    • Baur, H.1    Luethi, E.2    Stalon, V.3    Mercenier, A.4    Haas, D.5
  • 16
    • 0025812353 scopus 로고
    • Anaerobic regulation of transcription initiation in the arcDABC operon of Pseudomonas aeruginosa
    • Gamper M, Zimmermann A, Haas D, (1991) Anaerobic regulation of transcription initiation in the arcDABC operon of Pseudomonas aeruginosa. J Bacteriol 173: 4742-50.
    • (1991) J Bacteriol , vol.173 , pp. 4742-4750
    • Gamper, M.1    Zimmermann, A.2    Haas, D.3
  • 17
    • 0022533828 scopus 로고
    • The arcABC operon required for fermentative growth of Pseudomonas aeruginosa on arginine: Tn5-751-assisted cloning and localization of structural genes
    • Lüthi E, Mercenier A, Haas D, (1986) The arcABC operon required for fermentative growth of Pseudomonas aeruginosa on arginine: Tn5-751-assisted cloning and localization of structural genes. J Gen Microbiol 132: 2667-75.
    • (1986) J Gen Microbiol , vol.132 , pp. 2667-2675
    • Lüthi, E.1    Mercenier, A.2    Haas, D.3
  • 18
    • 0037325045 scopus 로고    scopus 로고
    • P. aeruginosa quorum-sensing systems and virulence
    • Smith RS, Iglewski BH, (2003) P. aeruginosa quorum-sensing systems and virulence. Curr Opin Microbiol 6: 56-60.
    • (2003) Curr Opin Microbiol , vol.6 , pp. 56-60
    • Smith, R.S.1    Iglewski, B.H.2
  • 19
    • 0036652959 scopus 로고    scopus 로고
    • Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production
    • Dillon BJ, Holtsberg FW, Ensor CM, Bomalaski JS, Clark MA, (2002) Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production. Med Sci Monit 8: BR248-53.
    • (2002) Med Sci Monit , vol.8
    • Dillon, B.J.1    Holtsberg, F.W.2    Ensor, C.M.3    Bomalaski, J.S.4    Clark, M.A.5
  • 20
    • 0025353364 scopus 로고
    • Potent growth inhibition of human tumor cells in culture by arginine deiminase purified from a culture medium of a Mycoplasma-infected cell line
    • Miyazaki K, Takaku H, Umeda M, Fujita T, Huang WD, et al. (1990) Potent growth inhibition of human tumor cells in culture by arginine deiminase purified from a culture medium of a Mycoplasma-infected cell line. Cancer Res 50: 4522-7.
    • (1990) Cancer Res , vol.50 , pp. 4522-4527
    • Miyazaki, K.1    Takaku, H.2    Umeda, M.3    Fujita, T.4    Huang, W.D.5
  • 21
    • 0037463235 scopus 로고    scopus 로고
    • Arginine deprivation, growth inhibition and tumour cell death: 2. Enzymatic degradation of arginine in normal and malignant cell cultures
    • Philip R, Campbell E, Wheatley DN, (2003) Arginine deprivation, growth inhibition and tumour cell death: 2. Enzymatic degradation of arginine in normal and malignant cell cultures. Br J Cancer 88: 613-23.
    • (2003) Br J Cancer , vol.88 , pp. 613-623
    • Philip, R.1    Campbell, E.2    Wheatley, D.N.3
  • 22
    • 0020064624 scopus 로고
    • Arginase as an inhibitory principle in liver plasma membranes arresting the growth of various mammalian cells in vitro
    • Terayama H, Koji T, Kontani M, Okumoto T, (1982) Arginase as an inhibitory principle in liver plasma membranes arresting the growth of various mammalian cells in vitro. Biochim Biophys Acta 720: 188-92.
    • (1982) Biochim Biophys Acta , vol.720 , pp. 188-192
    • Terayama, H.1    Koji, T.2    Kontani, M.3    Okumoto, T.4
  • 23
    • 1842639583 scopus 로고    scopus 로고
    • Structural insight into arginine degradation by arginine deiminase, an antibacterial and parasite drug target
    • Galkin A, Kulakova L, Sarikaya E, Lim K, Howard A, et al. (2004) Structural insight into arginine degradation by arginine deiminase, an antibacterial and parasite drug target. J Biol Chem 279: 14001-8.
    • (2004) J Biol Chem , vol.279 , pp. 14001-14008
    • Galkin, A.1    Kulakova, L.2    Sarikaya, E.3    Lim, K.4    Howard, A.5
  • 24
    • 26644450503 scopus 로고    scopus 로고
    • Crystal structures representing the Michaelis complex and the thiouronium reaction intermediate of Pseudomonas aeruginosa arginine deiminase
    • Galkin A, Lu X, Dunaway-Mariano D, Herzberg O, (2005) Crystal structures representing the Michaelis complex and the thiouronium reaction intermediate of Pseudomonas aeruginosa arginine deiminase. J Biol Chem 280: 34080-7.
    • (2005) J Biol Chem , vol.280 , pp. 34080-34087
    • Galkin, A.1    Lu, X.2    Dunaway-Mariano, D.3    Herzberg, O.4
  • 25
    • 1842450302 scopus 로고    scopus 로고
    • Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism
    • Das K, Butler GH, Kwiatkowski V, Clark AD Jr, Yadav P, et al. (2004) Crystal structures of arginine deiminase with covalent reaction intermediates; implications for catalytic mechanism. Structure 12: 657-67.
    • (2004) Structure , vol.12 , pp. 657-667
    • Das, K.1    Butler, G.H.2    Kwiatkowski, V.3    Clark Jr., A.D.4    Yadav, P.5
  • 26
    • 0021967278 scopus 로고
    • Immunological and structural relatedness of catabolic ornithine carbamoyltransferases and the anabolic enzymes of enterobacteria
    • Falmagne P, Portetelle D, Stalon V, (1985) Immunological and structural relatedness of catabolic ornithine carbamoyltransferases and the anabolic enzymes of enterobacteria. J. Bacteriol 161: 714-9.
    • (1985) J. Bacteriol , vol.161 , pp. 714-719
    • Falmagne, P.1    Portetelle, D.2    Stalon, V.3
  • 27
    • 77954143716 scopus 로고    scopus 로고
    • Regulation of CPSase, ACTase, and OCTase genes in Medicago truncatula: Implications for carbamoylphosphate synthesis and allocation to pyrimidine and arginine de novo biosynthesis
    • Brady BS, Hyman BC, Lovatt CJ, (2010) Regulation of CPSase, ACTase, and OCTase genes in Medicago truncatula: Implications for carbamoylphosphate synthesis and allocation to pyrimidine and arginine de novo biosynthesis. Gene 462: 18-25.
    • (2010) Gene , vol.462 , pp. 18-25
    • Brady, B.S.1    Hyman, B.C.2    Lovatt, C.J.3
  • 28
    • 77955624544 scopus 로고    scopus 로고
    • Molecular and biochemical features of the mitochondrial enzyme ornithine transcarbamylase: a possible new role as a signaling factor
    • Díaz-Muñoz M, Hernández-Muñoz R, (2010) Molecular and biochemical features of the mitochondrial enzyme ornithine transcarbamylase: a possible new role as a signaling factor. Curr Med Chem 17: 2253-60.
    • (2010) Curr Med Chem , vol.17 , pp. 2253-2260
    • Díaz-Muñoz, M.1    Hernández-Muñoz, R.2
  • 29
    • 0021274224 scopus 로고
    • Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12
    • Houghton JE, Bencini DA, O'Donovan GA, Wild JR, (1984) Protein differentiation: a comparison of aspartate transcarbamoylase and ornithine transcarbamoylase from Escherichia coli K-12. Proc Natl Acad Sci U S A 81: 4864-8.
    • (1984) Proc Natl Acad Sci U S A , vol.81 , pp. 4864-4868
    • Houghton, J.E.1    Bencini, D.A.2    O'Donovan, G.A.3    Wild, J.R.4
  • 30
    • 0020411609 scopus 로고
    • Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli
    • Honzatko RB, Crawford JL, Monaco HL, Ladner JE, Ewards BF, et al. (1982) Crystal and molecular structures of native and CTP-liganded aspartate carbamoyltransferase from Escherichia coli. J Mol Biol 160: 219-63.
    • (1982) J Mol Biol , vol.160 , pp. 219-263
    • Honzatko, R.B.1    Crawford, J.L.2    Monaco, H.L.3    Ladner, J.E.4    Ewards, B.F.5
  • 31
    • 0028881913 scopus 로고
    • Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase family
    • Villeret V, Tricot C, Stalon V, Dideberg O, (1995) Crystal structure of Pseudomonas aeruginosa catabolic ornithine transcarbamoylase at 3.0-A resolution: a different oligomeric organization in the transcarbamoylase family. Proc Natl Acad Sci U S A 92: 10762-6.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10762-10766
    • Villeret, V.1    Tricot, C.2    Stalon, V.3    Dideberg, O.4
  • 33
    • 70349420814 scopus 로고    scopus 로고
    • Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding
    • de las Rivas B, Fox GC, Angulo I, Ripoll MM, Rodríguez H, et al. (2009) Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: Structural insights into the oligomeric assembly and metal binding. J Mol Biol 393: 425-34.
    • (2009) J Mol Biol , vol.393 , pp. 425-434
    • de las Rivas, B.1    Fox, G.C.2    Angulo, I.3    Ripoll, M.M.4    Rodríguez, H.5
  • 34
    • 0032539795 scopus 로고    scopus 로고
    • The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures
    • Villeret V, Clantin B, Tricot C, Legrain C, Roovers M, et al. (1998) The crystal structure of Pyrococcus furiosus ornithine carbamoyltransferase reveals a key role for oligomerization in enzyme stability at extremely high temperatures. Proc Natl Acad Sci U S A 95: 2801-6.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 2801-2806
    • Villeret, V.1    Clantin, B.2    Tricot, C.3    Legrain, C.4    Roovers, M.5
  • 35
    • 0024998366 scopus 로고
    • Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme
    • Baur H, Tricot C, Stalon V, Haas D, (1990) Converting catabolic ornithine carbamoyltransferase to an anabolic enzyme. J Biol Chem 265: 14728-31.
    • (1990) J Biol Chem , vol.265 , pp. 14728-14731
    • Baur, H.1    Tricot, C.2    Stalon, V.3    Haas, D.4
  • 36
    • 0018405710 scopus 로고
    • Arginine catabolism by microorganisms
    • Abdelal AT, (1979) Arginine catabolism by microorganisms. Annu Rev Microbiol 33: 139-68.
    • (1979) Annu Rev Microbiol , vol.33 , pp. 139-168
    • Abdelal, A.T.1
  • 37
    • 0020422867 scopus 로고
    • Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis
    • Simon JP, Stalon V, (1982) Enzymes of agmatine degradation and the control of their synthesis in Streptococcus faecalis. J Bacteriol 152: 676-81.
    • (1982) J Bacteriol , vol.152 , pp. 676-681
    • Simon, J.P.1    Stalon, V.2
  • 38
    • 31344480412 scopus 로고    scopus 로고
    • Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159
    • Griswold AR, Jameson-Lee M, Burne RA, (2006) Regulation and physiologic significance of the agmatine deiminase system of Streptococcus mutans UA159. J Bacteriol 188: 834-41.
    • (2006) J Bacteriol , vol.188 , pp. 834-841
    • Griswold, A.R.1    Jameson-Lee, M.2    Burne, R.A.3
  • 39
    • 0022545161 scopus 로고
    • Control of enzyme synthesis in the oxalurate catabolic pathway of Streptococcus faecalis ATCC 11700: evidence for the existence of a third carbamate kinase
    • Vander Wauven C, Simon JP, Slos P, Stalon V, (1986) Control of enzyme synthesis in the oxalurate catabolic pathway of Streptococcus faecalis ATCC 11700: evidence for the existence of a third carbamate kinase. Arch Microbiol 145: 386-90.
    • (1986) Arch Microbiol , vol.145 , pp. 386-390
    • Vander Wauven, C.1    Simon, J.P.2    Slos, P.3    Stalon, V.4
  • 40
    • 0032762639 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
    • Cusa E, Obradors N, Baldomà L, Badía J, Aguilar J, (1999) Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J Bacteriol 181: 7479-84.
    • (1999) J Bacteriol , vol.181 , pp. 7479-7484
    • Cusa, E.1    Obradors, N.2    Baldomà, L.3    Badía, J.4    Aguilar, J.5
  • 41
    • 0020955911 scopus 로고
    • The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis
    • Linstead D, Cranshaw MA, (1983) The pathway of arginine catabolism in the parasitic flagellate Trichomonas vaginalis. Mol Biochem Parasitol 8: 241-52.
    • (1983) Mol Biochem Parasitol , vol.8 , pp. 241-252
    • Linstead, D.1    Cranshaw, M.A.2
  • 42
    • 0034595434 scopus 로고    scopus 로고
    • The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases
    • Ramón-Maiques S, Marina A, Uriarte M, Fita I, Rubio V, (2000) The 1.5 A resolution crystal structure of the carbamate kinase-like carbamoyl phosphate synthetase from the hyperthermophilic Archaeon Pyrococcus furiosus, bound to ADP, confirms that this thermostable enzyme is a carbamate kinase, and provides insight into substrate binding and stability in carbamate kinases. J Mol Biol 299: 463-76.
    • (2000) J Mol Biol , vol.299 , pp. 463-476
    • Ramón-Maiques, S.1    Marina, A.2    Uriarte, M.3    Fita, I.4    Rubio, V.5
  • 43
    • 77950517828 scopus 로고    scopus 로고
    • Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria
    • Ramón-Maiques S, Marina A, Guinot A, Gil-Ortiz F, Uriarte M, et al. (2010) Substrate binding and catalysis in carbamate kinase ascertained by crystallographic and site-directed mutagenesis studies: movements and significance of a unique globular subdomain of this key enzyme for fermentative ATP production in bacteria. J Mol Biol 397: 1261-75.
    • (2010) J Mol Biol , vol.397 , pp. 1261-1275
    • Ramón-Maiques, S.1    Marina, A.2    Guinot, A.3    Gil-Ortiz, F.4    Uriarte, M.5
  • 44
    • 0032054533 scopus 로고    scopus 로고
    • Carbamate kinase from Enterococcus faecalis and Enterococcus faecium - cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase
    • Marina A, Uriarte M, Barcelona B, Fresquet V, Cervera J, et al. (1998) Carbamate kinase from Enterococcus faecalis and Enterococcus faecium - cloning of the genes, studies on the enzyme expressed in Escherichia coli, and sequence similarity with N-acetyl-L-glutamate kinase. Eur J Biochem 253: 280-91.
    • (1998) Eur J Biochem , vol.253 , pp. 280-291
    • Marina, A.1    Uriarte, M.2    Barcelona, B.3    Fresquet, V.4    Cervera, J.5
  • 45
    • 84876452478 scopus 로고    scopus 로고
    • PhD Thesis, Universitat Autònoma Barcelona
    • Planell R (2008) PhD Thesis, Universitat Autònoma Barcelona.
    • (2008)
    • Planell, R.1
  • 46
    • 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, (1997) Crystal structure and mechanism of human L-arginine: glycine amidinotransferase: a mitochondrial enzyme involved in creatine biosynthesis. EMBO J 16: 3373-85.
    • (1997) EMBO J , vol.16 , pp. 3373-3385
    • Humm, A.1    Fritsche, E.2    Steinbacher, S.3    Huber, R.4
  • 47
    • 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, et al. (2001) Structural insights into the hydrolysis of cellular nitric oxide synthase inhibitors by dimethylarginine dimethylaminohydrolase. Nat Struct Biol 8: 679-83.
    • (2001) Nat Struct Biol , vol.8 , pp. 679-683
    • Murray-Rust, J.1    Leiper, J.2    McAlister, M.3    Phelan, J.4    Tilley, S.5
  • 48
    • 33846912925 scopus 로고    scopus 로고
    • The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction
    • Llácer JL, Polo LM, Tavárez S, Alarcón B, Hilario R, et al. (2007) The gene cluster for agmatine catabolism of Enterococcus faecalis: study of recombinant putrescine transcarbamylase and agmatine deiminase and a snapshot of agmatine deiminase catalyzing its reaction. J Bacteriol 189: 1254-65.
    • (2007) J Bacteriol , vol.189 , pp. 1254-1265
    • Llácer, J.L.1    Polo, L.M.2    Tavárez, S.3    Alarcón, B.4    Hilario, R.5
  • 49
    • 0347062345 scopus 로고    scopus 로고
    • Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A. Acta Crystallogr D Biol Crystallogr
    • Massant J, Wouters J, Glansdorff N, (2003) Refined structure of Pyrococcus furiosus ornithine carbamoyltransferase at 1.87 A. Acta Crystallogr D Biol Crystallogr. 59: 2140-9.
    • (2003) , vol.59 , pp. 2140-2149
    • Massant, J.1    Wouters, J.2    Glansdorff, N.3
  • 50
    • 0034822181 scopus 로고    scopus 로고
    • Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants
    • Clantin B, Tricot C, Lonhienne T, Stalon V, Villeret V, (2001) Probing the role of oligomerization in the high thermal stability of Pyrococcus furiosus ornithine carbamoyltransferase by site-specific mutants. Eur J Biochem 268: 3937-42.
    • (2001) Eur J Biochem , vol.268 , pp. 3937-3942
    • Clantin, B.1    Tricot, C.2    Lonhienne, T.3    Stalon, V.4    Villeret, V.5
  • 51
    • 0034733518 scopus 로고    scopus 로고
    • Mechanism of inactivation of ornithine transcarbamoylase by Ndelta -(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism
    • Langley DB, Templeton MD, Fields BA, Mitchell RE, Collyer CA, (2000) Mechanism of inactivation of ornithine transcarbamoylase by Ndelta-(N'-Sulfodiaminophosphinyl)-L-ornithine, a true transition state analogue? Crystal structure and implications for catalytic mechanism. J Biol Chem 275: 20012-9.
    • (2000) J Biol Chem , vol.275 , pp. 20012-20019
    • Langley, D.B.1    Templeton, M.D.2    Fields, B.A.3    Mitchell, R.E.4    Collyer, C.A.5
  • 52
    • 37449003424 scopus 로고    scopus 로고
    • The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate and L-norvaline reveal the enzyme's catalytic mechanism
    • Sankaranarayanan R, Cherney MM, Cherney LT, Garen CR, Moradian F, et al. (2008) The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate and L-norvaline reveal the enzyme's catalytic mechanism. J Mol Biol 375: 1052-63.
    • (2008) J Mol Biol , vol.375 , pp. 1052-1063
    • Sankaranarayanan, R.1    Cherney, M.M.2    Cherney, L.T.3    Garen, C.R.4    Moradian, F.5
  • 53
    • 0029864712 scopus 로고    scopus 로고
    • Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Importance of the N-terminal region for dodecameric structure and homotropic carbamoylphosphate cooperativity
    • Nguyen VT, Baker DP, Tricot C, Baur H, Villeret V, et al. (1996) Catabolic ornithine carbamoyltransferase of Pseudomonas aeruginosa. Importance of the N-terminal region for dodecameric structure and homotropic carbamoylphosphate cooperativity. Eur J Biochem 236: 283-93.
    • (1996) Eur J Biochem , vol.236 , pp. 283-293
    • Nguyen, V.T.1    Baker, D.P.2    Tricot, C.3    Baur, H.4    Villeret, V.5
  • 54
    • 0029792918 scopus 로고    scopus 로고
    • Use of a designed fusion protein dissociates allosteric properties from the dodecameric state of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase
    • Mouz N, Tricot C, Ebel C, Petillot Y, Stalon V, et al. (1996) Use of a designed fusion protein dissociates allosteric properties from the dodecameric state of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. Proc Natl Acad Sci U S A 93: 9414-9.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9414-9419
    • Mouz, N.1    Tricot, C.2    Ebel, C.3    Petillot, Y.4    Stalon, V.5
  • 55
    • 2342568994 scopus 로고    scopus 로고
    • Metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: dynamic enzyme-enzyme interactions involved in the formation of the channelling complex
    • Massant J, Glansdorff N, (2004) Metabolic channelling of carbamoyl phosphate in the hyperthermophilic archaeon Pyrococcus furiosus: dynamic enzyme-enzyme interactions involved in the formation of the channelling complex. Biochem Soc Trans 32: 306-9.
    • (2004) Biochem Soc Trans , vol.32 , pp. 306-309
    • Massant, J.1    Glansdorff, N.2
  • 57
    • 32244434642 scopus 로고    scopus 로고
    • Comparative analysis of antibiotic resistance gene markers in Mycoplasma genitalium: application to studies of the minimal gene complement
    • Pich O, Burgos O, Planell R, Querol E, Piñol J, (2006) Comparative analysis of antibiotic resistance gene markers in Mycoplasma genitalium: application to studies of the minimal gene complement. Microbiology 152: 519-527.
    • (2006) Microbiology , vol.152 , pp. 519-527
    • Pich, O.1    Burgos, O.2    Planell, R.3    Querol, E.4    Piñol, J.5
  • 61
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT, (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733.
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


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