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Volumn 70, Issue 5, 2004, Pages 2764-2770

Cloning, overexpression, and characterization of a novel thermostable penicillin G acylase from Achromobacter xylosoxidans: Probing the molecular basis for its high thermostability

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CLONING; ESCHERICHIA COLI; GENES; MOLECULAR STRUCTURE; THERMODYNAMIC STABILITY;

EID: 2442653152     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.70.5.2764-2770.2004     Document Type: Article
Times cited : (34)

References (53)
  • 2
    • 0034623981 scopus 로고    scopus 로고
    • Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic Archaea Thermoplasma acidophilum and Pyrococcus furiosus
    • Arnott, M. A., R. A. Michael, C. R. Thompson, D. W. Hough, and M. J. Danson. Thermostability and thermoactivity of citrate synthases from the thermophilic and hyperthermophilic Archaea Thermoplasma acidophilum and Pyrococcus furiosus. J. Mol. Biol. 304:657-668.
    • J. Mol. Biol. , vol.304 , pp. 657-668
    • Arnott, M.A.1    Michael, R.A.2    Thompson, C.R.3    Hough, D.W.4    Danson, M.J.5
  • 4
    • 0034693042 scopus 로고    scopus 로고
    • Structural and genomic correlates of hyperthermostability
    • Cambillau, C., and J. M. Claverie. 2000. Structural and genomic correlates of hyperthermostability. J. Biol. Chem. 42:32383-32386.
    • (2000) J. Biol. Chem. , vol.42 , pp. 32383-32386
    • Cambillau, C.1    Claverie, J.M.2
  • 5
    • 0034677790 scopus 로고    scopus 로고
    • Elucidation of determinants of protein stability through genome sequence analysis
    • Chakravarty, S., and R. Varadarajan. 2000. Elucidation of determinants of protein stability through genome sequence analysis. FEBS Lett. 470:65-69.
    • (2000) FEBS Lett. , vol.470 , pp. 65-69
    • Chakravarty, S.1    Varadarajan, R.2
  • 6
    • 0001050205 scopus 로고
    • Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure
    • Cunningham, B. C., and J. A. Wells. 1987. Improvement in the alkaline stability of subtilisin using an efficient random mutagenesis and screening procedure. Protein Eng. 1:319-325.
    • (1987) Protein Eng. , vol.1 , pp. 319-325
    • Cunningham, B.C.1    Wells, J.A.2
  • 7
    • 0035084965 scopus 로고    scopus 로고
    • Expression of penicillin G acylase from the cloned pac gene of Escherichia coli ATCC 11105
    • Dai, M. H., Y. M. Zhu, Y. L. Yang, E. D. Wang, Y. Xie, G. P. Zhao, and W. H. Jiang. 2001. Expression of penicillin G acylase from the cloned pac gene of Escherichia coli ATCC 11105. Eur. J. Biochem. 268:1298-1303.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 1298-1303
    • Dai, M.H.1    Zhu, Y.M.2    Yang, Y.L.3    Wang, E.D.4    Xie, Y.5    Zhao, G.P.6    Jiang, W.H.7
  • 8
    • 0034191064 scopus 로고    scopus 로고
    • The stability of thermophilic proteins: A study based on comprehensive genome comparison
    • Das, R., and M. Gerstein. 2000. The stability of thermophilic proteins: a study based on comprehensive genome comparison. Funct. Integr. Genomics 1:76-88.
    • (2000) Funct. Integr. Genomics , vol.1 , pp. 76-88
    • Das, R.1    Gerstein, M.2
  • 9
    • 0032573516 scopus 로고    scopus 로고
    • Ligand-induced conformational change in penicillin acylase
    • Done, S. H., J. A. Brannigan, P. C. Moody, and R. E. Hubbard. 1998. Ligand-induced conformational change in penicillin acylase. J. Mol. Biol. 284:463-475.
    • (1998) J. Mol. Biol. , vol.284 , pp. 463-475
    • Done, S.H.1    Brannigan, J.A.2    Moody, P.C.3    Hubbard, R.E.4
  • 12
    • 0000122573 scopus 로고
    • PHYLIP-Phylogeny inference package (version 3.2)
    • Felsenstein, J. 1989. PHYLIP-Phylogeny Inference Package (version 3.2). Cladistics 5:164-166.
    • (1989) Cladistics , vol.5 , pp. 164-166
    • Felsenstein, J.1
  • 13
    • 77957074791 scopus 로고    scopus 로고
    • Rigidity of thermophilic enzymes
    • A. Ballesteros, F. J. Plou, J. L. Iborra, and P. J. Halling (ed.). Elsevier Science, Amsterdam, The Netherlands
    • Fontana, A., V. de Filippis, P. P. de Laureto, E. Scaramella, and M. Zambonin. 1998. Rigidity of thermophilic enzymes, p. 277-294. In A. Ballesteros, F. J. Plou, J. L. Iborra, and P. J. Halling (ed.), Instability and stabilization of biocatalysts. Elsevier Science, Amsterdam, The Netherlands.
    • (1998) Instability and Stabilization of Biocatalysts , pp. 277-294
    • Fontana, A.1    De Filippis, V.2    De Laureto, P.P.3    Scaramella, E.4    Zambonin, M.5
  • 14
    • 0026058195 scopus 로고
    • Microbiology of airway disease in patients with cystic fibrosis
    • Gilligan, P. H. 1991. Microbiology of airway disease in patients with cystic fibrosis. Clin. Microbiol. Rev. 4:35-51.
    • (1991) Clin. Microbiol. Rev. , vol.4 , pp. 35-51
    • Gilligan, P.H.1
  • 15
    • 57849101475 scopus 로고    scopus 로고
    • 19 September, posting date. [Online.] Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada
    • Hancock, R. E. W. 19 September 2001, posting date. Hancock laboratory methods. [Online.] Department of Microbiology and Immunology, University of British Columbia, Vancouver, British Columbia, Canada, http://www.cmdr.ubc.ca/bobh/methodsall.html.
    • (2001) Hancock Laboratory Methods
    • Hancock, R.E.W.1
  • 16
    • 0033214040 scopus 로고
    • Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus
    • Haney, P. J., M. Stees, and J. Konisky. 1994. Analysis of thermal stabilizing interactions in mesophilic and thermophilic adenylate kinases from the genus Methanococcus. J. Biol. Chem. 274:28453-28458.
    • (1994) J. Biol. Chem. , vol.274 , pp. 28453-28458
    • Haney, P.J.1    Stees, M.2    Konisky, J.3
  • 17
    • 0026714968 scopus 로고
    • Role of proline residues in human lysozyme stability: A scanning calorimetric study combined with X-ray structure analysis of proline mutants
    • Herning, T., K. Yutani, K. Inaka, R. Kuroki, M. Matsushima, and M. Kikuchi. 1992. Role of proline residues in human lysozyme stability: a scanning calorimetric study combined with X-ray structure analysis of proline mutants. Biochemistry 31:7077-7085.
    • (1992) Biochemistry , vol.31 , pp. 7077-7085
    • Herning, T.1    Yutani, K.2    Inaka, K.3    Kuroki, R.4    Matsushima, M.5    Kikuchi, M.6
  • 18
    • 0034730417 scopus 로고    scopus 로고
    • Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft
    • Hewitt, L., V. Kasche, K. Lummer, R. J. Lewis, G. N. Murshudov, C. S. Verma, G. G. Dodson, and K. S. Wilson. 2000. Structure of a slow processing precursor penicillin acylase from Escherichia coli reveals the linker peptide blocking the active-site cleft. J. Mol. Biol. 302:887-898.
    • (2000) J. Mol. Biol. , vol.302 , pp. 887-898
    • Hewitt, L.1    Kasche, V.2    Lummer, K.3    Lewis, R.J.4    Murshudov, G.N.5    Verma, C.S.6    Dodson, G.G.7    Wilson, K.S.8
  • 19
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 20
    • 0027672619 scopus 로고
    • Molecular basis of the exclusive low-temperature synthesis of an enzyme in E. coli: Penicillin acylase
    • Keilmann, C., G. Wanner, and A. Bock. 1993. Molecular basis of the exclusive low-temperature synthesis of an enzyme in E. coli: penicillin acylase. Biol. Chem. Hoppe-Seyler 374:983-992.
    • (1993) Biol. Chem. Hoppe-Seyler. , vol.374 , pp. 983-992
    • Keilmann, C.1    Wanner, G.2    Bock, A.3
  • 21
    • 0020999167 scopus 로고
    • Stabilization of enzymes against thermal inactivation
    • Klibanov, A. M. 1983. Stabilization of enzymes against thermal inactivation. Adv. Appl. Microbiol. 29:1-28.
    • (1983) Adv. Appl. Microbiol. , vol.29 , pp. 1-28
    • Klibanov, A.M.1
  • 22
    • 0034017055 scopus 로고    scopus 로고
    • Factors enhancing protein thermostability
    • Kumar, S., C. J. Tsai, and R. Nussinov. 2000. Factors enhancing protein thermostability. Protein Eng. 13:179-191.
    • (2000) Protein Eng. , vol.13 , pp. 179-191
    • Kumar, S.1    Tsai, C.J.2    Nussinov, R.3
  • 23
    • 0034724271 scopus 로고    scopus 로고
    • Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity?
    • Jaenicke, R. 1999. Do ultrastable proteins from hyperthermophiles have high or low conformational rigidity? Proc. Natl. Acad. Sci. USA 97:2962-2964.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2962-2964
    • Jaenicke, R.1
  • 24
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., M. W. MacArthur, D. S. Moss, and J. M. Thornton. 1993. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystal. 26:283-291.
    • (1993) J. Appl. Crystal. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 25
    • 0032884396 scopus 로고    scopus 로고
    • Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri
    • Mcdonough, M. A., H. E. Klei, and J. A. Kelly. 1999. Crystal structure of penicillin G acylase from the Bro1 mutant strain of Providencia rettgeri. Protein Sci. 8:1971-1981.
    • (1999) Protein Sci. , vol.8 , pp. 1971-1981
    • Mcdonough, M.A.1    Klei, H.E.2    Kelly, J.A.3
  • 26
    • 0023149799 scopus 로고
    • Cloning and expression of penicillin acylase genes from overproducing strains of Escherichia coli and Bacillus megaterium
    • Meevootisom, V., and J. R. Saunders. 1987. Cloning and expression of penicillin acylase genes from overproducing strains of Escherichia coli and Bacillus megaterium. Appl. Microbiol. Biotechnol. 25:372-378.
    • (1987) Appl. Microbiol. Biotechnol. , vol.25 , pp. 372-378
    • Meevootisom, V.1    Saunders, J.R.2
  • 27
    • 0026705620 scopus 로고
    • Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene
    • Merino, E., P. Balbas, F. Recillas, B. Becerril, F. Valle, and F. Bolivar. 1992. Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene. Mol. Microbiol. 6:2175-2182.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2175-2182
    • Merino, E.1    Balbas, P.2    Recillas, F.3    Becerril, B.4    Valle, F.5    Bolivar, F.6
  • 30
    • 0036184149 scopus 로고    scopus 로고
    • The effect of proline insertions on the thermostability of a barley α-glucosidase
    • Muslin, E. H., S. E. Clark, and C. A. Henson. 2002. The effect of proline insertions on the thermostability of a barley α-glucosidase. Protein Eng. 15:29-33.
    • (2002) Protein Eng. , vol.15 , pp. 29-33
    • Muslin, E.H.1    Clark, S.E.2    Henson, C.A.3
  • 31
    • 0031406972 scopus 로고    scopus 로고
    • Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix
    • Nakamura, S., T. Tanaka, R. Y. Yada, and S. Nakai. 1997. Improving the thermostability of Bacillus stearothermophilus neutral protease by introducing proline into the active site helix. Protein Eng. 10:1263-1269.
    • (1997) Protein Eng. , vol.10 , pp. 1263-1269
    • Nakamura, S.1    Tanaka, T.2    Yada, R.Y.3    Nakai, S.4
  • 32
    • 0030614959 scopus 로고    scopus 로고
    • Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites
    • Nielsen, H., J. Engelbrecht, S. Brunak, and G. Heijne. 1997. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 10:1-6.
    • (1997) Protein Eng. , vol.10 , pp. 1-6
    • Nielsen, H.1    Engelbrecht, J.2    Brunak, S.3    Heijne, G.4
  • 33
    • 0031718310 scopus 로고    scopus 로고
    • Homology modeling, model and software evaluation: Three related resources
    • Rodriguez, R., G. Chinea, N. Lopez, T. Pons, and G. Vriend. 1998. Homology modeling, model and software evaluation: three related resources. Comput. Appl. Biol. Sci. 14:523-528.
    • (1998) Comput. Appl. Biol. Sci. , vol.14 , pp. 523-528
    • Rodriguez, R.1    Chinea, G.2    Lopez, N.3    Pons, T.4    Vriend, G.5
  • 34
    • 0036205765 scopus 로고    scopus 로고
    • Synergistic activities of macrolide antibiotics against Pseudomonas aeruginosa, Burkholderia cepacia, Stenotrophomonas maltophilia, and Alcaligenes xylosoxidans isolated from patients with cystic fibrosis
    • Saiman, L., Y. Chen, P. S. Gabriel, and C. Knirsch. 2002. Synergistic activities of macrolide antibiotics against Pseudomonas aeruginosa, Burkholderia cepacia, Stenotrophomonas maltophilia, and Alcaligenes xylosoxidans isolated from patients with cystic fibrosis. Antimicrob. Agents Chemother. 46:1105-1107.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 1105-1107
    • Saiman, L.1    Chen, Y.2    Gabriel, P.S.3    Knirsch, C.4
  • 35
    • 0035189010 scopus 로고    scopus 로고
    • Increasing the thermostability of Flavobacterium meningosepticum glycerol kinase by changing Ser329 to Asp in the subunit interface region
    • Sakasegawa, S., H. Takerhara, I. Yoshioka, M. Takahashi, Y. Kagimoto, H. Misaki, H. Sakuraba, and T. Ohshima. 2001. Increasing the thermostability of Flavobacterium meningosepticum glycerol kinase by changing Ser329 to Asp in the subunit interface region. Protein Eng. 4:663-667.
    • (2001) Protein Eng. , vol.4 , pp. 663-667
    • Sakasegawa, S.1    Takerhara, H.2    Yoshioka, I.3    Takahashi, M.4    Kagimoto, Y.5    Misaki, H.6    Sakuraba, H.7    Ohshima, T.8
  • 37
    • 0000903228 scopus 로고    scopus 로고
    • Penicillin acylase: Enzyme production and its application in the manufacture of 6-APA
    • Shewale, J. G., and H. SivaRaman. Penicillin acylase: enzyme production and its application in the manufacture of 6-APA. Process Biochem. 24:146-154.
    • Process Biochem , vol.24 , pp. 146-154
    • Shewale, J.G.1    SivaRaman, H.2
  • 38
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl, M. J. 1993. Recognition of errors in three-dimensional structures of proteins. Proteins 17:355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 39
    • 0025100583 scopus 로고
    • Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105
    • Sizmann, D., C. Keilmann, and A. Böck. 1990. Primary structure requirements for the maturation in vivo of penicillin acylase from Escherichia coli ATCC 11105. Eur. J. Biochem. 192:143-151.
    • (1990) Eur. J. Biochem. , vol.192 , pp. 143-151
    • Sizmann, D.1    Keilmann, C.2    Böck, A.3
  • 41
    • 0001767586 scopus 로고
    • A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases
    • Suzuki, Y., K. Oishi, H. Nakano, and T. Nagayama. 1987. A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-1,6-glucosidases. Appl. Microbiol. Biotechnol. 26:546-551.
    • (1987) Appl. Microbiol. Biotechnol. , vol.26 , pp. 546-551
    • Suzuki, Y.1    Oishi, K.2    Nakano, H.3    Nagayama, T.4
  • 42
    • 0039116206 scopus 로고    scopus 로고
    • Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: Results of a comprehensive survey
    • Szilagyi, A., and P. Zavodszky. 2000. Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. Structure 8:493-504.
    • (2000) Structure , vol.8 , pp. 493-504
    • Szilagyi, A.1    Zavodszky, P.2
  • 43
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson, J. D., D. G. Higgins, and T. J. Gibson. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 44
    • 0036217687 scopus 로고    scopus 로고
    • Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-β-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH
    • Turunen, O., M. Vuorio, F. Fenel, and M. Leisola. 2002. Engineering of multiple arginines into the Ser/Thr surface of Trichoderma reesei endo-1,4-β-xylanase II increases the thermotolerance and shifts the pH optimum towards alkaline pH. Protein Eng. 15:141-145.
    • (2002) Protein Eng. , vol.15 , pp. 141-145
    • Turunen, O.1    Vuorio, M.2    Fenel, F.3    Leisola, M.4
  • 48
    • 0035214616 scopus 로고    scopus 로고
    • Bivalent cations and amino-acid composition contribute to the thermostability of Bacillus licheniformis xylose isomerase
    • Vieille, C., K. L. Epting, R. M. Kelly, and J. G. Zeikus. 2001. Bivalent cations and amino-acid composition contribute to the thermostability of Bacillus licheniformis xylose isomerase. Eur. J. Biochem. 268:6291-6301.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6291-6301
    • Vieille, C.1    Epting, K.L.2    Kelly, R.M.3    Zeikus, J.G.4
  • 49
    • 0011186093 scopus 로고    scopus 로고
    • Protein thermal stability: Hydrogen bonds or internal packing?
    • Vogt, G., and P. Argos. 1997. Protein thermal stability: hydrogen bonds or internal packing? Fold. Des. 2:S40-S46.
    • (1997) Fold. Des. , vol.2
    • Vogt, G.1    Argos, P.2
  • 50
    • 0031580199 scopus 로고    scopus 로고
    • Protein thermal stability, hydrogen bonds, and ion pairs
    • Vogt, G., S. Woell, and P. Argos. 1997. Protein thermal stability, hydrogen bonds, and ion pairs. J. Mol. Biol. 269:631-643.
    • (1997) J. Mol. Biol. , vol.269 , pp. 631-643
    • Vogt, G.1    Woell, S.2    Argos, P.3
  • 51
    • 0034456022 scopus 로고    scopus 로고
    • Recurrent Achromobacter xylosoxidans bacteremia associated with persistent lymph node infection in a patient with hyper-immunoglobulin M syndrome
    • Weitkamp, J. H., Y. W. Tang, D. W. Haas, N. K. Midha, and J. E. Crowe, Jr. 2000. Recurrent Achromobacter xylosoxidans bacteremia associated with persistent lymph node infection in a patient with hyper-immunoglobulin M syndrome. Clin. Infect. Dis. 31:1183-1187.
    • (2000) Clin. Infect. Dis. , vol.31 , pp. 1183-1187
    • Weitkamp, J.H.1    Tang, Y.W.2    Haas, D.W.3    Midha, N.K.4    Crowe Jr., J.E.5
  • 52
    • 0034951829 scopus 로고    scopus 로고
    • Expression and Purification of extracellular penicillin G acylase in Bacillus subtilis
    • Yang, S., H. Huang, Y. Zhang, X. D. Huang, S. Y. Li, Z. Y. Yuan. 2001. Expression and Purification of extracellular penicillin G acylase in Bacillus subtilis. Protein Expr. Purif. 21:60-64.
    • (2001) Protein Expr. Purif. , vol.21 , pp. 60-64
    • Yang, S.1    Huang, H.2    Zhang, Y.3    Huang, X.D.4    Li, S.Y.5    Yuan, Z.Y.6
  • 53
    • 0032867166 scopus 로고    scopus 로고
    • Increasing the thermostability of D-xylose isomerase by introduction of a proline into the turn of a random coil
    • Zhu, G. P., C. Xu, M. K. Teng, L. M. Tao, X. Y. Zhu, C. J. Wu, J. Hang, L. W. Niu, and Y. Z. Wang. 1999. Increasing the thermostability of D-xylose isomerase by introduction of a proline into the turn of a random coil. Protein Eng. 12:635-638.
    • (1999) Protein Eng. , vol.12 , pp. 635-638
    • Zhu, G.P.1    Xu, C.2    Teng, M.K.3    Tao, L.M.4    Zhu, X.Y.5    Wu, C.J.6    Hang, J.7    Niu, L.W.8    Wang, Y.Z.9


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