메뉴 건너뛰기




Volumn 35, Issue 2, 2004, Pages 373-380

Isolation of aminoglycoside nucleotidyltransferase(2″)-Ia from inclusion bodies as active, monomeric enzyme

Author keywords

Aminoglycosides; Antibiotics; Enzymatic modification; Inclusion bodies; Protein isolation

Indexed keywords

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; FORMICIDAE; PSEUDOMONAS; PSEUDOMONAS AERUGINOSA;

EID: 2642580087     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2004.02.003     Document Type: Article
Times cited : (20)

References (24)
  • 1
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • D. Moazed, H.F. Noller, Interaction of antibiotics with functional sites in 16S ribosomal RNA, Nature 327 (1987) 389-394.
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 2
    • 0002881670 scopus 로고
    • Aminoglycoside-aminocyclitol antibiotics and their modifying enzymes
    • V. Lorian (Ed.), Williams and Williams, Baltimore
    • J.E. Davies, Aminoglycoside-aminocyclitol antibiotics and their modifying enzymes, in: V. Lorian (Ed.), Antibiotics in Laboratory Medicine, Williams and Williams, Baltimore, 1991, pp. 691-713.
    • (1991) Antibiotics in Laboratory Medicine , pp. 691-713
    • Davies, J.E.1
  • 3
    • 0032538956 scopus 로고    scopus 로고
    • Structural origins of gentamicin antibiotic action
    • S. Yoshizawa, D. Fourmy, J.D. Puglisi, Structural origins of gentamicin antibiotic action, EMBO J. 17 (1998) 6437-6448.
    • (1998) EMBO J. , vol.17 , pp. 6437-6448
    • Yoshizawa, S.1    Fourmy, D.2    Puglisi, J.D.3
  • 4
    • 0034426097 scopus 로고    scopus 로고
    • Aminoglycosides: Perspectives on mechanisms of action and resistance and strategies to counter resistance
    • L.P. Kotra, J. Haddad, S. Mobashery, Aminoglycosides: perspectives on mechanisms of action and resistance and strategies to counter resistance, Antimicrob. Agents Chemother. 44 (2000) 3249-3256.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 3249-3256
    • Kotra, L.P.1    Haddad, J.2    Mobashery, S.3
  • 5
    • 0027478123 scopus 로고
    • Molecular genetics of aminoglycoside resistant genes and familial relationships of the aminoglycoside-modifying enzymes
    • K.J. Shaw, P.N. Rather, R.S. Hare, G.H. Miller, Molecular genetics of aminoglycoside resistant genes and familial relationships of the aminoglycoside-modifying enzymes, Microbiol. Rev. 57 (1993) 138-163.
    • (1993) Microbiol. Rev. , vol.57 , pp. 138-163
    • Shaw, K.J.1    Rather, P.N.2    Hare, R.S.3    Miller, G.H.4
  • 7
    • 0032555691 scopus 로고    scopus 로고
    • Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase
    • E. Wolf, A. Vassilev, Y. Makino, A. Sali, Y. Nakatani, S.K. Burley, Crystal structure of a GCN5-related N-acetyltransferase: Serratia marcescens aminoglycoside 3-N-acetyltransferase, Cell 94 (1998) 439-449.
    • (1998) Cell , vol.94 , pp. 439-449
    • Wolf, E.1    Vassilev, A.2    Makino, Y.3    Sali, A.4    Nakatani, Y.5    Burley, S.K.6
  • 8
    • 2642584838 scopus 로고    scopus 로고
    • Resistance to aminoglycoside antibiotics: Function meets structure
    • A. Van Broekhaven et al. (Eds.), Kliewer Academic Publishers, Amsterdam
    • G.D. Wright, A.M. Berghuis, Resistance to aminoglycoside antibiotics: function meets structure, in: A. Van Broekhaven et al. (Eds.), Novel Frontiers in the Production of Compounds for Biomedical Use, Kliewer Academic Publishers, Amsterdam, 2001, pp. 85-98.
    • (2001) Novel Frontiers in the Production of Compounds for Biomedical Use , pp. 85-98
    • Wright, G.D.1    Berghuis, A.M.2
  • 10
    • 0016367512 scopus 로고
    • Gentamicin:adenine mononucleotide transferase: Partial purification, characterization, and use in the clinical quantitation of gentamicin
    • A.L. Smith, D.H. Smith, Gentamicin:adenine mononucleotide transferase: partial purification, characterization, and use in the clinical quantitation of gentamicin, J. Infect. Dis. 129 (1974) 391-401.
    • (1974) J. Infect. Dis. , vol.129 , pp. 391-401
    • Smith, A.L.1    Smith, D.H.2
  • 11
    • 0020065933 scopus 로고
    • Purification and properties of 2 gentamicin-modifying enzymes, coded by a single plasmid PPK237 originating from Pseudomonas aeruginosa
    • F. Angelatou, S.B. Litsas, P. Kontomichalou, Purification and properties of 2 gentamicin-modifying enzymes, coded by a single plasmid PPK237 originating from Pseudomonas aeruginosa, J. Antibiot. 35 (1982) 235-244.
    • (1982) J. Antibiot. , vol.35 , pp. 235-244
    • Angelatou, F.1    Litsas, S.B.2    Kontomichalou, P.3
  • 12
    • 0021349419 scopus 로고
    • Relationship between aminoglycoside 2″-O-nucleotidyltransferase activity and aminoglycoside resistance
    • G.P.A. Bongaerts, L. Molendijk, Relationship between aminoglycoside 2″-O-nucleotidyltransferase activity and aminoglycoside resistance, Antimicrob. Agents Chemother. 25 (1984) 234-237.
    • (1984) Antimicrob. Agents Chemother. , vol.25 , pp. 234-237
    • Bongaerts, G.P.A.1    Molendijk, L.2
  • 13
    • 0032190686 scopus 로고    scopus 로고
    • Advances in refolding of proteins produced in E. coli
    • H. Lilie, E. Schwarz, R. Rudolph, Advances in refolding of proteins produced in E. coli, Curr. Opin. Biotech. 9 (1998) 497-501.
    • (1998) Curr. Opin. Biotech. , vol.9 , pp. 497-501
    • Lilie, H.1    Schwarz, E.2    Rudolph, R.3
  • 14
    • 0032855077 scopus 로고    scopus 로고
    • Inhibition of aggregation side reactions during in vitro protein refolding
    • E. De Bernardez Clark, E. Schwarz, R. Rudolph, Inhibition of aggregation side reactions during in vitro protein refolding, Methods Enzymol. 309 (1999) 217-236.
    • (1999) Methods Enzymol. , vol.309 , pp. 217-236
    • De Bernardez Clark, E.1    Schwarz, E.2    Rudolph, R.3
  • 15
    • 0345636051 scopus 로고    scopus 로고
    • Practical considerations in refolding proteins from inclusion bodies
    • K. Tsumoto, D. Ejima, I. Kumagai, T. Arakawa, Practical considerations in refolding proteins from inclusion bodies, Protein Expr. Purif. 28 (2003) 1-8.
    • (2003) Protein Expr. Purif. , vol.28 , pp. 1-8
    • Tsumoto, K.1    Ejima, D.2    Kumagai, I.3    Arakawa, T.4
  • 16
    • 0035912790 scopus 로고    scopus 로고
    • Cloning, overexpression, and purification of aminoglycoside antibiotic nucleotidyltransferase (2″)-Ia: Conformational studies with bound substrates
    • D.R. Ekman, E.L. DiGiammarino, E. Wright, E.D. Witter, E.H. Serpersu, Cloning, overexpression, and purification of aminoglycoside antibiotic nucleotidyltransferase (2″)-Ia: conformational studies with bound substrates, Biochemistry 40 (2001) 7017-7024.
    • (2001) Biochemistry , vol.40 , pp. 7017-7024
    • Ekman, D.R.1    DiGiammarino, E.L.2    Wright, E.3    Witter, E.D.4    Serpersu, E.H.5
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford, A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72 (1976) 248-258.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-258
    • Bradford, M.M.1
  • 18
    • 0000003981 scopus 로고
    • Assay for inorganic phosphate
    • B.N. Ames, Assay for inorganic phosphate, Methods Enzymol. 7 (1965) 115-118.
    • (1965) Methods Enzymol. , vol.7 , pp. 115-118
    • Ames, B.N.1
  • 19
    • 0023047203 scopus 로고
    • Nucleotide sequence of the AAD(2″) aminoglycoside adenyltransferase determinant aadB. Evolutionary relationship of this region with those surrounding aadA in R538-I and dhfrII in R388
    • F.H. Cameron, D.J. Groot Obbink, V.P. Ackerman, R.M. Hall, Nucleotide sequence of the AAD(2″) aminoglycoside adenyltransferase determinant aadB. Evolutionary relationship of this region with those surrounding aadA in R538-I and dhfrII in R388, Nucleic Acids Res. 14 (1986) 8625-8635.
    • (1986) Nucleic Acids Res. , vol.14 , pp. 8625-8635
    • Cameron, F.H.1    Groot Obbink, D.J.2    Ackerman, V.P.3    Hall, R.M.4
  • 20
    • 0017717867 scopus 로고
    • Resistance of bacteria to the newer aminoglycoside antibiotics: An epidemiological and enzymatic study
    • M. Devaud, F.H. Kayser, U. Huber, Resistance of bacteria to the newer aminoglycoside antibiotics: An epidemiological and enzymatic study, J. Antibiot. 30 (1977) 655-664.
    • (1977) J. Antibiot. , vol.30 , pp. 655-664
    • Devaud, M.1    Kayser, F.H.2    Huber, U.3
  • 21
    • 0023937023 scopus 로고
    • Substrate specificities and structure-activity relationships for the nucleotidylation of antibiotics catalyzed by aminoglycoside nucleotidyltransferase 2″-I
    • C.A. Gates, D.B. Northrop, Substrate specificities and structure-activity relationships for the nucleotidylation of antibiotics catalyzed by aminoglycoside nucleotidyltransferase 2″-I, Biochemistry 27 (1988) 3820-3825.
    • (1988) Biochemistry , vol.27 , pp. 3820-3825
    • Gates, C.A.1    Northrop, D.B.2
  • 22
    • 0021268095 scopus 로고
    • Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: Nucleotide specificity, pH optimum, and the separation of two electrophoretic variants
    • J.E. Van Pelt, D.B. Northrop, Purification and properties of gentamicin nucleotidyltransferase from Escherichia coli: nucleotide specificity, pH optimum, and the separation of two electrophoretic variants, Arch. Biochem. Biophys. 230 (1984) 250-263.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 250-263
    • Van Pelt, J.E.1    Northrop, D.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.