메뉴 건너뛰기




Volumn 36, Issue 2, 2006, Pages 175-195

Purification and characterization of L,(L/D)-aminopeptidase from guinea pig serum

Author keywords

Guinea pig serum; L,(L D) Aminopeptidase; Mammalian sera; N Acetylmuramyl L alanine amidase (EC 3.5.1.28); Peptidoglycan monomer

Indexed keywords

ALANINE; AMINOPEPTIDASE; OLIGOPEPTIDE; PEPTIDOGLYCAN; PROTEINASE INHIBITOR;

EID: 33644806187     PISSN: 10826068     EISSN: 15322297     Source Type: Journal    
DOI: 10.1080/10826060500534099     Document Type: Article
Times cited : (4)

References (43)
  • 1
    • 33644804448 scopus 로고    scopus 로고
    • Cell walls, bacterial
    • Oliver, S.G., Schaechter, M., Lederberg, J., Alexander, M., Bloom, B.R., Hopwood, D.A., Hull, R., Iglewski, B.H., Laskin, A.I., Eds.; Academic Press: Amsterdam
    • Höltje, J.V. Cell walls, bacterial. In Encyclopedia of Microbiology, 2nd Ed.; Oliver, S.G., Schaechter, M., Lederberg, J., Alexander, M., Bloom, B.R., Hopwood, D.A., Hull, R., Iglewski, B.H., Laskin, A.I., Eds.; Academic Press: Amsterdam, 2000; Vol. 1, 759-771.
    • (2000) Encyclopedia of Microbiology, 2nd Ed. , vol.1 , pp. 759-771
    • Höltje, J.V.1
  • 2
    • 0002249336 scopus 로고
    • Building and breaking of bonds in the cell wall of bacteria - The role for autolysins
    • Nombela, C., Ed.; Elsevier Science Publishing: New York
    • Tomasz, A. Building and breaking of bonds in the cell wall of bacteria - The role for autolysins. In Microbial Cell Wall Synthesis and Autolysis; Nombela, C., Ed.; Elsevier Science Publishing: New York, 1984; 3-12.
    • (1984) Microbial Cell Wall Synthesis and Autolysis , pp. 3-12
    • Tomasz, A.1
  • 3
    • 77956866741 scopus 로고
    • Microbial peptidoglycan (Murein) hydrolases
    • Ghuysen, J.M., Hakenbeck, R., Eds.; Elsevier: Amsterdam
    • Shockman, G.D.; Höltje, J.V. Microbial peptidoglycan (Murein) hydrolases. In Bacterial Cell Wall; Ghuysen, J.M., Hakenbeck, R., Eds.; Elsevier: Amsterdam, 1994; 131-166.
    • (1994) Bacterial Cell Wall , pp. 131-166
    • Shockman, G.D.1    Höltje, J.V.2
  • 5
    • 0015966563 scopus 로고
    • Isolation and study of the composition of a peptidoglycan complex excreted by the biotin-requiring mutant of Brevibacterium divaricatum NRRL-2311 in the presence of penicillin
    • Keglević, D.; Ladešić, B.; Hadžija, O.; Tomašić, J.; Valinger, Z.; Pokorny, M.; Naumski, R. Isolation and study of the composition of a peptidoglycan complex excreted by the biotin-requiring mutant of Brevibacterium divaricatum NRRL-2311 in the presence of penicillin. Eur. J. Biochem. 1974, 42, 389-400.
    • (1974) Eur. J. Biochem. , vol.42 , pp. 389-400
    • Keglević, D.1    Ladešić, B.2    Hadžija, O.3    Tomašić, J.4    Valinger, Z.5    Pokorny, M.6    Naumski, R.7
  • 6
    • 0018359872 scopus 로고
    • Isolation procedure and properties of monomer unit from lysozyme digest of peptidoglycan complex excreted into the medium by penicillin-treated Brevibacterium divaricatum mutant
    • Keglević, D.; Ladešić, B.; Tomašić, J.; Valinger, Z.; Naumski, R. Isolation procedure and properties of monomer unit from lysozyme digest of peptidoglycan complex excreted into the medium by penicillin-treated Brevibacterium divaricatum mutant. Biochim. Biophys. Acta 1979, 585, 273-281.
    • (1979) Biochim. Biophys. Acta , vol.585 , pp. 273-281
    • Keglević, D.1    Ladešić, B.2    Tomašić, J.3    Valinger, Z.4    Naumski, R.5
  • 7
    • 0024296686 scopus 로고
    • Comparative susceptibility of peptidoglycan monomer from Brevibacterium divaricatum and its anhydromuramyl analogue to hydrolysis with N-acetilmuramyl-L-alanine amidase; isolation and characterization of anhydromuramyl-peptidoglycan
    • Tomašić, J.; Sesartić, Lj.; Martin, S.A.; Valinger, Z.; Ladešić, B. Comparative susceptibility of peptidoglycan monomer from Brevibacterium divaricatum and its anhydromuramyl analogue to hydrolysis with N-acetilmuramyl-L-alanine amidase; isolation and characterization of anhydromuramyl-peptidoglycan. J. Chromatogr. 1988, 440, 405-414.
    • (1988) J. Chromatogr. , vol.440 , pp. 405-414
    • Tomašić, J.1    Sesartić, Lj.2    Martin, S.A.3    Valinger, Z.4    Ladešić, B.5
  • 8
    • 0030978556 scopus 로고    scopus 로고
    • Structure and dynamics of a peptidoglycan monomer in aqueous solution using NMR spectroscopy and simulated annealing calculations
    • Matter, H.; Szilagy, L.; Forgo, P.; Marinić, Ž.; Klaić, B. Structure and dynamics of a peptidoglycan monomer in aqueous solution using NMR spectroscopy and simulated annealing calculations. J. Am. Chem. Soc. 1997, 119, 2212-2223.
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 2212-2223
    • Matter, H.1    Szilagy, L.2    Forgo, P.3    Marinić, Ž.4    Klaić, B.5
  • 9
    • 0005137072 scopus 로고
    • Peptidoglycan monomer originating from Brevibacterium divaricatum - Its metabolism and biological activities in the host
    • Shrinner, E., Richmond, M.H., Seibert, G., Schwartz, G., Eds.; VCH: Weinheim
    • Tomašić, J.; Hršak, I. Peptidoglycan monomer originating from Brevibacterium divaricatum - its metabolism and biological activities in the host. In Surface Structures of Microorganisms and Their Interactions with Mammalian Host; Shrinner, E., Richmond, M.H., Seibert, G., Schwartz, G., Eds.; VCH: Weinheim, 1988; 113-121.
    • (1988) Surface Structures of Microorganisms and Their Interactions with Mammalian Host , pp. 113-121
    • Tomašić, J.1    Hršak, I.2
  • 10
    • 0037803776 scopus 로고    scopus 로고
    • Comparative study of the effects of peptidoglycan monomer and structurally related adamantyltripeptides on humoral immune response to ovalbumin in mouse
    • Tomašić, J.; Hanzl-Dujmović, I.; Špoljar, B.; Vranešić, B.; Šantak, M.; Jovičić, A. Comparative study of the effects of peptidoglycan monomer and structurally related adamantyltripeptides on humoral immune response to ovalbumin in mouse. Vaccine 2000, 18, 1236-1243.
    • (2000) Vaccine , vol.18 , pp. 1236-1243
    • Tomašić, J.1    Hanzl-Dujmović, I.2    Špoljar, B.3    Vranešić, B.4    Šantak, M.5    Jovičić, A.6
  • 11
    • 0019230150 scopus 로고
    • 14C-labeled peptidoglycan monomer in mice. I. Identification of the monomer and corresponding pentapeptide in urine
    • 14C-labeled peptidoglycan monomer in mice. I. Identification of the monomer and corresponding pentapeptide in urine. Biochim. Biophys. Acta 1980, 629, 77-82.
    • (1980) Biochim. Biophys. Acta , vol.629 , pp. 77-82
    • Tomašić, J.1    Ladešić, B.2    Valinger, Z.3    Hršak, I.4
  • 13
    • 0020474543 scopus 로고
    • Partial purification and characterization of N-acetylmuramyl-L-alanine amidase from human and mouse serum
    • Valinger, Z.; Ladešić, B.; Tomašić, J. Partial purification and characterization of N-acetylmuramyl-L-alanine amidase from human and mouse serum. Biochim. Biophys. Acta 1982, 701, 63-71.
    • (1982) Biochim. Biophys. Acta , vol.701 , pp. 63-71
    • Valinger, Z.1    Ladešić, B.2    Tomašić, J.3
  • 14
    • 0021689409 scopus 로고
    • Murein hydrolase (N-acetylmuramyl-L-alanine amidase) in human serum
    • Mollner, S.; Braun, V. Murein hydrolase (N-acetylmuramyl-L-alanine amidase) in human serum. Arch. Microbiol. 1984, 140, 171-177.
    • (1984) Arch. Microbiol. , vol.140 , pp. 171-177
    • Mollner, S.1    Braun, V.2
  • 16
    • 0029670071 scopus 로고    scopus 로고
    • Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies
    • Hoijer, M.A.; Meleif, M.J.; Keck, W.; Hazenberg, M.P. Purification and characterization of N-acetylmuramyl-L-alanine amidase from human plasma using monoclonal antibodies. Biochim. Biophys. Acta 1996, 1289, 57-64.
    • (1996) Biochim. Biophys. Acta , vol.1289 , pp. 57-64
    • Hoijer, M.A.1    Meleif, M.J.2    Keck, W.3    Hazenberg, M.P.4
  • 18
    • 0037172929 scopus 로고    scopus 로고
    • Reversed-phase high-performance liquid chromatographic method for the determination of peptidoglycan monomers and structurally related peptides and adamantyltripeptides
    • Krstanović, M.; Frkanec, R.; Vranešić, B.; Ljevaković, D.; Šporec, V.; Tomašić, J. Reversed-phase high-performance liquid chromatographic method for the determination of peptidoglycan monomers and structurally related peptides and adamantyltripeptides. J. Chromatogr. B 2002, 773, 167-174.
    • (2002) J. Chromatogr. B , vol.773 , pp. 167-174
    • Krstanović, M.1    Frkanec, R.2    Vranešić, B.3    Ljevaković, D.4    Šporec, V.5    Tomašić, J.6
  • 19
    • 0037435980 scopus 로고    scopus 로고
    • Adjuvant activity of peptidoglycan monomer and its metabolic products
    • Halassy, B.; Krstanović, M.; Frkanec, R.; Tomašić, J. Adjuvant activity of peptidoglycan monomer and its metabolic products. Vaccine 2003, 21, 971-976.
    • (2003) Vaccine , vol.21 , pp. 971-976
    • Halassy, B.1    Krstanović, M.2    Frkanec, R.3    Tomašić, J.4
  • 20
    • 0018935367 scopus 로고
    • An optimized assay of alanine aminopeptidase activity in urine
    • Jung, K.; Scholz, D. An optimized assay of alanine aminopeptidase activity in urine. Clin. Chem. 1980, 26, 1251-1254.
    • (1980) Clin. Chem. , vol.26 , pp. 1251-1254
    • Jung, K.1    Scholz, D.2
  • 21
    • 0021988172 scopus 로고
    • Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining
    • Heukeshoven, J.; Dernick, R. Simplified method for silver staining of proteins in polyacrylamide gels and the mechanism of silver staining. Electrophoresis 1985, 6, 103-112.
    • (1985) Electrophoresis , vol.6 , pp. 103-112
    • Heukeshoven, J.1    Dernick, R.2
  • 22
    • 0030871373 scopus 로고    scopus 로고
    • Expression and intracellular localization of the human N-acetylmuramyl-L-alanine amidase, a bacterial cell wall-degrading enzyme
    • Hoijer, M.A.; Melief, M.J.; Calafat, J.; Roos, D.; Van den Beemd, R.W.M.; Dongen, J.J.M.; Hazenberg, M.P. Expression and intracellular localization of the human N-acetylmuramyl-L-alanine amidase, a bacterial cell wall-degrading enzyme. Blood 1997, 90, 1246-1254.
    • (1997) Blood , vol.90 , pp. 1246-1254
    • Hoijer, M.A.1    Melief, M.J.2    Calafat, J.3    Roos, D.4    Van Den Beemd, R.W.M.5    Dongen, J.J.M.6    Hazenberg, M.P.7
  • 23
    • 0031435146 scopus 로고    scopus 로고
    • Inflammatory properties of peptidoglycan are decreased after degradation by human N-acetylmuramyl-L-alanine amidase
    • Hoijer, M.A.; Melief, M.J.; Debets, R.; Hazenberg, M.P. Inflammatory properties of peptidoglycan are decreased after degradation by human N-acetylmuramyl-L-alanine amidase. Eur. Cytokine Network 1997, 8, 375-381.
    • (1997) Eur. Cytokine Network , vol.8 , pp. 375-381
    • Hoijer, M.A.1    Melief, M.J.2    Debets, R.3    Hazenberg, M.P.4
  • 24
    • 0031985840 scopus 로고    scopus 로고
    • Differences in N-acetylmuramyl-L-alanine amidase and lysozyme in serum and cerebrospinal fluid of patients with bacterial meningitis
    • Hoijer, M.A.; de Groot, R.; van Lieshout, L.; Jacobs, B.C.; Melief, M.J.; Hazenberg, M.P. Differences in N-acetylmuramyl-L-alanine amidase and lysozyme in serum and cerebrospinal fluid of patients with bacterial meningitis. J. Infect. Dis. 1998, 177, 102-106.
    • (1998) J. Infect. Dis. , vol.177 , pp. 102-106
    • Hoijer, M.A.1    De Groot, R.2    Van Lieshout, L.3    Jacobs, B.C.4    Melief, M.J.5    Hazenberg, M.P.6
  • 25
    • 0034071105 scopus 로고    scopus 로고
    • Enzymes acting on peptides containing D-amino acid
    • Assano, Y.; Lübbehüsen, T.L. Enzymes acting on peptides containing D-amino acid. J. Biosci. Bioeng. 2000, 89, 295-306.
    • (2000) J. Biosci. Bioeng. , vol.89 , pp. 295-306
    • Assano, Y.1    Lübbehüsen, T.L.2
  • 26
    • 0027991987 scopus 로고
    • Penicilin-binding protein 7/8 of Escherichia coli is a D,D-endopeptidase
    • Romies, T.; Höltje, J.V. Penicilin-binding protein 7/8 of Escherichia coli is a D,D-endopeptidase. Eur. J. Biochem. 1994, 224, 597-604.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 597-604
    • Romies, T.1    Höltje, J.V.2
  • 27
    • 0018128025 scopus 로고
    • Purification of penicillin-insensitive D,D-endopeptidase: A new cell wall peptidoglycan-hydrolyzing enzyme in Escherichia coli, and its inhibition by deoxyribonucleic acids
    • Tomioka, S.; Matsuhashi, M. Purification of penicillin-insensitive D,D-endopeptidase: a new cell wall peptidoglycan-hydrolyzing enzyme in Escherichia coli, and its inhibition by deoxyribonucleic acids. Biochem. Biophys. Res. Commun. 1978, 84, 978-984.
    • (1978) Biochem. Biophys. Res. Commun. , vol.84 , pp. 978-984
    • Tomioka, S.1    Matsuhashi, M.2
  • 28
    • 0017359499 scopus 로고
    • Specificity profiles of the membrane-bound γ-D-glutamyl-(L)meso- diaminopimelate endopeptidase and L,D-carboxypeptidase from Bacillus sphearicus 9602
    • Arminjon, F.; Guinand, M.; Vacheron, M.J.; Michel, G. Specificity profiles of the membrane-bound γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase and L,D-carboxypeptidase from Bacillus sphearicus 9602. Eur. J. Biochem. 1977, 73, 557-565.
    • (1977) Eur. J. Biochem. , vol.73 , pp. 557-565
    • Arminjon, F.1    Guinand, M.2    Vacheron, M.J.3    Michel, G.4
  • 29
    • 0018670420 scopus 로고
    • Characterization of a new endopeptidase from sporulating Bacillus sphearicus which is specific for the γ-D-glutamyl-L-lysine and γ-D-glutamyl-(L)meso-diaminopimelate linkages of peptidoglycan substrates
    • Vacheron, M.J.; Guinand, M.; Francon, A.; Michel, G. Characterization of a new endopeptidase from sporulating Bacillus sphearicus which is specific for the γ-D-glutamyl-L-lysine and γ-D-glutamyl-(L)meso-diaminopimelate linkages of peptidoglycan substrates. Eur. J. Biochem. 1979, 100, 189-196.
    • (1979) Eur. J. Biochem. , vol.100 , pp. 189-196
    • Vacheron, M.J.1    Guinand, M.2    Francon, A.3    Michel, G.4
  • 30
    • 0021837555 scopus 로고
    • Purification and partial characterization of the extracellular γ-D-glutamyl-(L)meso-diaminopimelate endopeptidase I from Bacillus sphearicus NCTC 9602
    • Garnier, M.; Vacheron, M.J.; Guinand, M.; Michel, G. Purification and partial characterization of the extracellular γ-D-glutamyl-(L)meso- diaminopimelate endopeptidase I from Bacillus sphearicus NCTC 9602. Eur. J. Biochem. 1985, 148, 539-543.
    • (1985) Eur. J. Biochem. , vol.148 , pp. 539-543
    • Garnier, M.1    Vacheron, M.J.2    Guinand, M.3    Michel, G.4
  • 31
    • 0029122651 scopus 로고
    • Heterogeneous endolysins in Listeria monocytogenes bacteriophages: A new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes
    • Loessner, M.J.; Wendlinger, G.; Scherer, S. Heterogeneous endolysins in Listeria monocytogenes bacteriophages: a new class of enzymes and evidence for conserved holin genes within the siphoviral lysis cassettes. Mol. Microbiol. 1995, 16, 1231-1241.
    • (1995) Mol. Microbiol. , vol.16 , pp. 1231-1241
    • Loessner, M.J.1    Wendlinger, G.2    Scherer, S.3
  • 32
    • 0022599291 scopus 로고
    • L,D-Carboxypeptidase activity in Escherichia coli. I. The L,D-carboxypeptidase activity in ether treated cells
    • Metz, R.; Henning, S.; Hammes, W.P. L,D-Carboxypeptidase activity in Escherichia coli. I. The L,D-carboxypeptidase activity in ether treated cells. Arch. Microbiol. 1986, 144, 175-186.
    • (1986) Arch. Microbiol. , vol.144 , pp. 175-186
    • Metz, R.1    Henning, S.2    Hammes, W.P.3
  • 33
    • 0026513864 scopus 로고
    • Purification of a nocardicin A-sensitive L,D-carboxypeptidase from Escherichia coli by affinity chromatography
    • Ursins, A.; Steinhaus, H.; Höltje, J.V. Purification of a nocardicin A-sensitive L,D-carboxypeptidase from Escherichia coli by affinity chromatography. J. Bacteriol. 1992, 174, 441-446.
    • (1992) J. Bacteriol. , vol.174 , pp. 441-446
    • Ursins, A.1    Steinhaus, H.2    Höltje, J.V.3
  • 34
    • 0028825333 scopus 로고
    • From growth to autolysis: The murein hydrolases in Escherichia coli
    • Höltje, J.V. From growth to autolysis: the murein hydrolases in Escherichia coli. Arch. Microbiol. 1995, 164, 243-254.
    • (1995) Arch. Microbiol. , vol.164 , pp. 243-254
    • Höltje, J.V.1
  • 36
    • 0001985244 scopus 로고    scopus 로고
    • The murein sacculus
    • Neidhardt, F.C., Ed.; ASM Press: Washington
    • Park, J.T. The murein sacculus. In Escherichia coli and Salmonella; Neidhardt, F.C., Ed.; ASM Press: Washington, 1996; 48-57.
    • (1996) Escherichia Coli and Salmonella , pp. 48-57
    • Park, J.T.1
  • 37
    • 0035118119 scopus 로고    scopus 로고
    • Enzymology of elongation and constriction of the murein sacculus of Escherichia coli
    • Höltje, J.V.; Heidrich, C. Enzymology of elongation and constriction of the murein sacculus of Escherichia coli. Biochimie 2001, 83, 103-108.
    • (2001) Biochimie , vol.83 , pp. 103-108
    • Höltje, J.V.1    Heidrich, C.2
  • 38
    • 0037224580 scopus 로고    scopus 로고
    • Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the γ-D-glutamyl-meso-diaminopimelate bond in murein peptides
    • Uehara, T.; Park, J.T. Identification of MpaA, an amidase in Escherichia coli that hydrolyzes the γ-D-glutamyl-meso-diaminopimelate bond in murein peptides. J. Bacteriol. 2003, 185, 679-682.
    • (2003) J. Bacteriol. , vol.185 , pp. 679-682
    • Uehara, T.1    Park, J.T.2
  • 39
    • 0024393970 scopus 로고
    • Properties of novel D-stereospecific aminopeptidase from Ochrobactrum anthropi
    • Asano, Y.; Nakazawa, A.; Kato, Y.; Kondo, K. Properties of novel D-stereospecific aminopeptidase from Ochrobactrum anthropi. J. Biol. Chem. 1989, 264, 14233-14239.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14233-14239
    • Asano, Y.1    Nakazawa, A.2    Kato, Y.3    Kondo, K.4
  • 40
    • 0034067403 scopus 로고    scopus 로고
    • Gene cloning, nucleotide sequencing, and purification and characterization of the stereospecific amino acid amidase from Ochrobactrum anthropi SV3
    • Komeda, H.; Asano, Y. Gene cloning, nucleotide sequencing, and purification and characterization of the stereospecific amino acid amidase from Ochrobactrum anthropi SV3. Eur. J. Biochem. 2000, 267, 2028-2035.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2028-2035
    • Komeda, H.1    Asano, Y.2
  • 41
    • 0014006562 scopus 로고
    • The purification and properties of a particulate renal dipeptidase
    • Campbell, B.J.; Lin, Y-C.; Davis, R.V.; Ballew, E. The purification and properties of a particulate renal dipeptidase. Biochim. Biophys. Acta 1965, 118, 371-386.
    • (1965) Biochim. Biophys. Acta , vol.118 , pp. 371-386
    • Campbell, B.J.1    Lin, Y.-C.2    Davis, R.V.3    Ballew, E.4
  • 42
    • 0030583724 scopus 로고    scopus 로고
    • Purification and kinetic properties of a D-amino acid peptide hydrolyzing enzyme from pig kidney cortex and its tentative identification with renal membrane dipeptidase
    • Watanabe, T.; Kera, Y.; Matsumoto, T.; Yamada, R. Purification and kinetic properties of a D-amino acid peptide hydrolyzing enzyme from pig kidney cortex and its tentative identification with renal membrane dipeptidase. Biochim. Biophys. Acta 1996, 1298, 109-118.
    • (1996) Biochim. Biophys. Acta , vol.1298 , pp. 109-118
    • Watanabe, T.1    Kera, Y.2    Matsumoto, T.3    Yamada, R.4
  • 43
    • 0021361316 scopus 로고
    • Purification and characterization of an enkephalin-degrading aminopeptidase from guinea pig serum
    • Shimumara, M.; Hazato, T.; Katayama, T. Purification and characterization of an enkephalin-degrading aminopeptidase from guinea pig serum. Biochim. Biophys. Acta 1984, 798, 8-13.
    • (1984) Biochim. Biophys. Acta , vol.798 , pp. 8-13
    • Shimumara, M.1    Hazato, T.2    Katayama, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.