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Volumn 581, Issue 9, 2007, Pages 1898-1902

Structural characterization of dimeric murine aminoacylase III

Author keywords

3D reconstruction; Deacetylation; Electron microscopy; Kidney; Murine aminoacylase III

Indexed keywords

AMINOACYLASE; AMINOACYLASE 3; DIMER; UNCLASSIFIED DRUG;

EID: 34247231405     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.088     Document Type: Article
Times cited : (11)

References (25)
  • 2
    • 0030850711 scopus 로고    scopus 로고
    • The hog intestinal mucosa acylase I: subcellular localization, isolation, kinetic studies and biological function
    • Giardina T., Biagini A., Dalle Ore F., Ferre E., Reynier M., and Puigserver A. The hog intestinal mucosa acylase I: subcellular localization, isolation, kinetic studies and biological function. Biochemie 79 (1997) 265-273
    • (1997) Biochemie , vol.79 , pp. 265-273
    • Giardina, T.1    Biagini, A.2    Dalle Ore, F.3    Ferre, E.4    Reynier, M.5    Puigserver, A.6
  • 3
    • 0023786992 scopus 로고
    • Further characterization on porcine kidney aminoacylase 1 reveals close similarity to "renal dipeptidase"
    • Heese D., Loffler H.G., and Rohm K.H. Further characterization on porcine kidney aminoacylase 1 reveals close similarity to "renal dipeptidase". Biol. Chem. Hoppe-Seyler 369 (1988) 559-566
    • (1988) Biol. Chem. Hoppe-Seyler , vol.369 , pp. 559-566
    • Heese, D.1    Loffler, H.G.2    Rohm, K.H.3
  • 4
    • 0017404732 scopus 로고
    • Renal aminoacylase, a zink enzyme
    • Kördel W., and Schneider F. Renal aminoacylase, a zink enzyme. Z. Naturforsch. 32C (1977) 342-344
    • (1977) Z. Naturforsch. , vol.32 C , pp. 342-344
    • Kördel, W.1    Schneider, F.2
  • 5
    • 0031853488 scopus 로고    scopus 로고
    • Acylase I-catalyzed deacetylation of N-acetyl-l-cysteines
    • Uttamsingh V., Keller D.A., and Anders M.W. Acylase I-catalyzed deacetylation of N-acetyl-l-cysteines. Chem. Res. Toxicol. 11 (1998) 800-809
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 800-809
    • Uttamsingh, V.1    Keller, D.A.2    Anders, M.W.3
  • 6
    • 0033771350 scopus 로고    scopus 로고
    • The rat kidney acylase 1, characterization and molecular cloning. Differences with other acylases
    • Giardina T., Perrier J., and Puigserver A. The rat kidney acylase 1, characterization and molecular cloning. Differences with other acylases. Eur. J. Biochem. 267 (2000) 6249-6255
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6249-6255
    • Giardina, T.1    Perrier, J.2    Puigserver, A.3
  • 7
    • 28544435766 scopus 로고    scopus 로고
    • Roles of dimerization domain residues in binding and catalysis by aminoacylase-1
    • Lindner H.A., Alary A., Boju L.I., Sulea T., and Menard R. Roles of dimerization domain residues in binding and catalysis by aminoacylase-1. Biochemistry 44 (2005) 15645-15651
    • (2005) Biochemistry , vol.44 , pp. 15645-15651
    • Lindner, H.A.1    Alary, A.2    Boju, L.I.3    Sulea, T.4    Menard, R.5
  • 8
    • 0242414629 scopus 로고    scopus 로고
    • Essential roles of zink ligation and enzyme dimerization for catalysis of the aminoacylase-1/M20 family
    • Lindner H.A., Lunin V.V., Alary A., Hecker R., Cygler M., and Menard R. Essential roles of zink ligation and enzyme dimerization for catalysis of the aminoacylase-1/M20 family. J. Biol. Chem. 278 (2003) 44496-44504
    • (2003) J. Biol. Chem. , vol.278 , pp. 44496-44504
    • Lindner, H.A.1    Lunin, V.V.2    Alary, A.3    Hecker, R.4    Cygler, M.5    Menard, R.6
  • 9
    • 0029006698 scopus 로고
    • Aminoacylase I from porcine kidney: identification and characterization of two major protein domains
    • Palm G.J., and Röhm K.H. Aminoacylase I from porcine kidney: identification and characterization of two major protein domains. J. Prot. Chem. 14 (1995) 233-240
    • (1995) J. Prot. Chem. , vol.14 , pp. 233-240
    • Palm, G.J.1    Röhm, K.H.2
  • 10
    • 0032748868 scopus 로고    scopus 로고
    • Acylase-catalyzed deacetylation of haloalkene-derived mercapturates
    • Uttamsingh V., and Anders M.W. Acylase-catalyzed deacetylation of haloalkene-derived mercapturates. Chem. Res. Toxicol. 12 (1999) 937-942
    • (1999) Chem. Res. Toxicol. , vol.12 , pp. 937-942
    • Uttamsingh, V.1    Anders, M.W.2
  • 13
    • 23044509196 scopus 로고    scopus 로고
    • Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase
    • Perrier J., Durand A., Giardina T., and Puigserver A. Catabolism of intracellular N-terminal acetylated proteins: involvement of acylpeptide hydrolase and acylase. Biochimie 87 (2005) 673-685
    • (2005) Biochimie , vol.87 , pp. 673-685
    • Perrier, J.1    Durand, A.2    Giardina, T.3    Puigserver, A.4
  • 15
    • 0028190695 scopus 로고
    • Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: cysteine conjugate beta-lyase pathway
    • Anders M.W., Dekant W., and Vamvakas S. Formation and fate of nephrotoxic and cytotoxic glutathione S-conjugates: cysteine conjugate beta-lyase pathway. Adv. Pharmacol. 27 (1994) 115-162
    • (1994) Adv. Pharmacol. , vol.27 , pp. 115-162
    • Anders, M.W.1    Dekant, W.2    Vamvakas, S.3
  • 16
    • 0025261923 scopus 로고
    • Cysteine conjugate toxicity, metabolism and binding to macromolecules in isolated rat kidney mitochondria
    • Hayden P.J., and Stevens J.L. Cysteine conjugate toxicity, metabolism and binding to macromolecules in isolated rat kidney mitochondria. Mol. Pharmacol. 37 (1990) 468-476
    • (1990) Mol. Pharmacol. , vol.37 , pp. 468-476
    • Hayden, P.J.1    Stevens, J.L.2
  • 17
    • 0019835064 scopus 로고
    • Purification and characterization of a rat liver enzyme catalyzing N-deacetylation of mercapturic acid conjugates
    • Suzuki S., and Tateishi M. Purification and characterization of a rat liver enzyme catalyzing N-deacetylation of mercapturic acid conjugates. Drug Metabol. Dispos. 9 (1981) 573-577
    • (1981) Drug Metabol. Dispos. , vol.9 , pp. 573-577
    • Suzuki, S.1    Tateishi, M.2
  • 18
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: semiautomated software for high-resolution single-particle reconstructions
    • Ludtke S.J., Baldwin P.R., and Chiu W. EMAN: semiautomated software for high-resolution single-particle reconstructions. J. Struct. Biol. 128 (1999) 82-97
    • (1999) J. Struct. Biol. , vol.128 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 19
    • 0015522277 scopus 로고
    • Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • Udenfriend S., Stein S., Bohlen P., Dairman W., Leimgruber W., and Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 178 (1972) 871-872
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 20
    • 34247235477 scopus 로고    scopus 로고
    • Use of "double-carbon" negative staining technique in biological applications
    • Ryazantsev S. Use of "double-carbon" negative staining technique in biological applications. Microsc. Today April (2001) 16-19
    • (2001) Microsc. Today , Issue.April , pp. 16-19
    • Ryazantsev, S.1
  • 22
    • 1842409555 scopus 로고    scopus 로고
    • Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy
    • Bottcher B., Wynne S.A., and Crowther R.A. Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy. Nature 386 (1997) 88-91
    • (1997) Nature , vol.386 , pp. 88-91
    • Bottcher, B.1    Wynne, S.A.2    Crowther, R.A.3
  • 24
    • 34247203502 scopus 로고    scopus 로고
    • http://www.cgl.ucsf.edu/chimera.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.