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Volumn 76, Issue 10, 1999, Pages 1113-1118

C-terminal His-tagging results in substrate specificity changes of the thioesterase I from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ADDITION REACTIONS; BIOCHEMISTRY; ESCHERICHIA COLI; KINETIC THEORY; ORGANIC COMPOUNDS; PH EFFECTS; TEMPERATURE;

EID: 0033322243     PISSN: 0003021X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11746-999-0082-7     Document Type: Article
Times cited : (24)

References (16)
  • 1
    • 0027255719 scopus 로고
    • Escherichia coli thioesterase I, molecular cloning and sequencing of the structural gene and identification as a periplasmic enzyme
    • Cho, H., and J.E. Cronan Jr., Escherichia coli Thioesterase I, Molecular Cloning and Sequencing of the Structural Gene and Identification as a Periplasmic Enzyme, J. Biol. Chem. 268: 9238-9245 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 9238-9245
    • Cho, H.1    Cronan J.E., Jr.2
  • 2
    • 0027461466 scopus 로고
    • Molecular cloning, sequencing, and mapping of the gene encoding protease I and characterization of protease and protease-defective Escherichia coli mutants
    • Ichihara, S., Y. Kato, C. Matsubara, K. Akasaka, and S. Mizushima, Molecular Cloning, Sequencing, and Mapping of the Gene Encoding Protease I and Characterization of Protease and Protease-Defective Escherichia coli Mutants, J. Bacteriol. 175:1032-1037 (1993).
    • (1993) J. Bacteriol. , vol.175 , pp. 1032-1037
    • Ichihara, S.1    Kato, Y.2    Matsubara, C.3    Akasaka, K.4    Mizushima, S.5
  • 3
    • 0028176615 scopus 로고
    • Protease I of Escherichia coli functions as a thioesterase in vivo
    • Cho, H., and J.E., Cronan Jr., Protease I of Escherichia coli Functions as a Thioesterase in vivo, Ibid. 176:1793-1795 (1994).
    • (1994) J. Bacteriol. , vol.176 , pp. 1793-1795
    • Cho, H.1    Cronan J.E., Jr.2
  • 4
    • 0031566271 scopus 로고    scopus 로고
    • The thioesterase I of Escherichia coli has arylesterase activity and shows stereospecificity for protease substrates
    • Lee, Y.L., J.C. Chen, and J.F. Shaw, The Thioesterase I of Escherichia coli Has Arylesterase Activity and Shows Stereospecificity for Protease Substrates, Biochem. Biophys. Res. Comm. 231:452-456 (1997).
    • (1997) Biochem. Biophys. Res. Comm. , vol.231 , pp. 452-456
    • Lee, Y.L.1    Chen, J.C.2    Shaw, J.F.3
  • 5
    • 0028280199 scopus 로고
    • Nucleotide sequence of a novel arylesterase gene from Vibrio mimicus and characterization of the enzyme expressed in Escherichia coli
    • Shaw, J.F., R.C. Chang, K.H. Chuang, Y.T. Yen, Y.J. Wang, and F.G. Wang, Nucleotide Sequence of a Novel Arylesterase Gene from Vibrio mimicus and Characterization of the Enzyme Expressed in Escherichia coli, Biochem. J. 298:675-680 (1994).
    • (1994) Biochem. J. , vol.298 , pp. 675-680
    • Shaw, J.F.1    Chang, R.C.2    Chuang, K.H.3    Yen, Y.T.4    Wang, Y.J.5    Wang, F.G.6
  • 6
    • 0000251294 scopus 로고
    • Biocatalytic, enantioselective preparations of (R)-and (S)-ethyl 4-chloro-3-hydroxybutanoate, a useful chiral synthon
    • Aragozzini, F., M. Valenti, E. Santaniello, P. Ferraboschi, and P. Grisenti, Biocatalytic, Enantioselective Preparations of (R)-and (S)-Ethyl 4-Chloro-3-hydroxybutanoate, a Useful Chiral Synthon, Biocatalysis 5:325-332 (1992).
    • (1992) Biocatalysis , vol.5 , pp. 325-332
    • Aragozzini, F.1    Valenti, M.2    Santaniello, E.3    Ferraboschi, P.4    Grisenti, P.5
  • 8
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes
    • Upton, C., and J.T. Buckley, A New Family of Lipolytic Enzymes, Trend Biochem. Sci. 20:178-179 (1995).
    • (1995) Trend Biochem. Sci. , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.T.2
  • 9
    • 0032058947 scopus 로고    scopus 로고
    • Multinuclear NMR resonance assignments and the secondary structure of Escherichia coli thioesterase I/protease I - A member of a new subclass of lipolytic enzymes
    • Lin, T.H., C. Chen, R.F. Huang, Y.L. Lee, J.F. Shaw, and T.H. Huang, Multinuclear NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase I/Protease I - A Member of a New Subclass of Lipolytic Enzymes, J. Biomol. NMR 11:363-380 (1998).
    • (1998) J. Biomol. NMR , vol.11 , pp. 363-380
    • Lin, T.H.1    Chen, C.2    Huang, R.F.3    Lee, Y.L.4    Shaw, J.F.5    Huang, T.H.6
  • 10
    • 0026507598 scopus 로고
    • Improved primer designed for PCR-based, site-directed mutagenesis
    • Sharrocks, A.D., and P.E. Shaw, Improved Primer Designed for PCR-Based, Site-Directed Mutagenesis, Nucleic Acids Res. 20:1147 (1992).
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1147
    • Sharrocks, A.D.1    Shaw, P.E.2
  • 11
    • 0031274834 scopus 로고    scopus 로고
    • Facile purification of a C-terminal extended his-tagged Vibrio mimicus arylesterase and characterization of the purified enzyme
    • Lee, Y.L., R.C. Chang, and J.F. Shaw, Facile Purification of a C-Terminal Extended His-Tagged Vibrio mimicus Arylesterase and Characterization of the Purified Enzyme, J. Am. Oil Chem. Soc. 74:1371-1376 (1997).
    • (1997) J. Am. Oil Chem. Soc. , vol.74 , pp. 1371-1376
    • Lee, Y.L.1    Chang, R.C.2    Shaw, J.F.3
  • 12
    • 0020110250 scopus 로고
    • Activity staining of nucleolytic enzymes after sodium dodecyl sulfate-polyacrylamide gel electrophoresis: Use of aqueous isopropanol to remove detergent from gels
    • Blank, A., R.H. Sugiyama, and C. Dekker, Activity Staining of Nucleolytic Enzymes After Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis: Use of Aqueous Isopropanol to Remove Detergent from Gels, Anal. Biochem. 120:267-275 (1982).
    • (1982) Anal. Biochem. , vol.120 , pp. 267-275
    • Blank, A.1    Sugiyama, R.H.2    Dekker, C.3
  • 13
    • 33747379226 scopus 로고
    • Enzyme activity staining
    • edited by S.D. Tanksley, and T.J. Orton, Elsevier Science Publishers, Amsterdam
    • Vallejos, C.E., Enzyme Activity Staining, in Isozymes in Plant Genetics and Breeding, Part A, edited by S.D. Tanksley, and T.J. Orton, Elsevier Science Publishers, Amsterdam, 1983, pp. 500-501.
    • (1983) Isozymes in Plant Genetics and Breeding, Part A , pp. 500-501
    • Vallejos, C.E.1
  • 14
    • 0343427326 scopus 로고
    • Influence of pH on the inactivation kinetics of isoamylase
    • Shaw, J.F., R.S. Pan, and W.H. Hsu, Influence of pH on the Inactivation Kinetics of Isoamylase, Bot. Bull. Acad. Sinica 30:155-159 (1989).
    • (1989) Bot. Bull. Acad. Sinica , vol.30 , pp. 155-159
    • Shaw, J.F.1    Pan, R.S.2    Hsu, W.H.3
  • 16
    • 0028305457 scopus 로고
    • Prediction of pH-dependent properties of proteins
    • Antosiewicz, J., J.A. McCammon, and M.K. Gilson, Prediction of pH-Dependent Properties of Proteins, J. Mol. Biol. 238:415-436 (1994).
    • (1994) J. Mol. Biol. , vol.238 , pp. 415-436
    • Antosiewicz, J.1    McCammon, J.A.2    Gilson, M.K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.