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Volumn 71, Issue 9, 2005, Pages 5290-5296

Improving the activity and stability of GL-7-ACA acylase CA130 by site-directed mutagenesis

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYSIS; CRYSTAL STRUCTURE; GENES; MUTAGENESIS;

EID: 25144504061     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.71.9.5290-5296.2005     Document Type: Article
Times cited : (15)

References (37)
  • 1
    • 0031919546 scopus 로고    scopus 로고
    • Recent trends in enzymatic conversion of cephalosporin C to 7-aminocephalosporinic acid
    • Anupama, P., and K. Harish. 1998. Recent trends in enzymatic conversion of cephalosporin C to 7-aminocephalosporinic acid. Crit. Rev. Biotechnol. 18:1-12.
    • (1998) Crit. Rev. Biotechnol. , vol.18 , pp. 1-12
    • Anupama, P.1    Harish, K.2
  • 3
    • 0344121229 scopus 로고    scopus 로고
    • Analysis of a substrate specificity switch residue of cephalosporin acylase
    • Charles, F. S., L. G. Otten, R. H. Cool, and W. J. Quax. 2003. Analysis of a substrate specificity switch residue of cephalosporin acylase. Biochem. Biophys. Res. Commun. 312:755-760.
    • (2003) Biochem. Biophys. Res. Commun. , vol.312 , pp. 755-760
    • Charles, F.S.1    Otten, L.G.2    Cool, R.H.3    Quax, W.J.4
  • 6
    • 0030228409 scopus 로고    scopus 로고
    • Recombinant Acremonium chrysogenum strains for the industrial production of cephalosporin
    • Diez, B., E. Mellado, R. Fouces, M. Rodriguez, and J. L. Barredo. 1996. Recombinant Acremonium chrysogenum strains for the industrial production of cephalosporin. Microbiologia 12:359-370.
    • (1996) Microbiologia , vol.12 , pp. 359-370
    • Diez, B.1    Mellado, E.2    Fouces, R.3    Rodriguez, M.4    Barredo, J.L.5
  • 7
    • 0027462173 scopus 로고
    • Principals of protein stability derived from protein engineering experiments
    • Fersht, A. R., and L. Serrano. 1993. Principals of protein stability derived from protein engineering experiments. Curr. Opin. Struct. Biol. 3:75-83.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 75-83
    • Fersht, A.R.1    Serrano, L.2
  • 8
    • 0036137006 scopus 로고    scopus 로고
    • Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C
    • Fritz-Wolf, K., K. P. Koller, G. Lange, A. Liesum, K. Sauber, H. Schreuder, W. Aretz, and W. Kabsch. 2002. Structure-based prediction of modifications in glutarylamidase to allow single-step enzymatic production of 7-aminocephalosporanic acid from cephalosporin C. Protein Sci. 11:92-103.
    • (2002) Protein Sci. , vol.11 , pp. 92-103
    • Fritz-Wolf, K.1    Koller, K.P.2    Lange, G.3    Liesum, A.4    Sauber, K.5    Schreuder, H.6    Aretz, W.7    Kabsch, W.8
  • 9
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., H. D. Hunt, R. M. Horton, J. K. Pullen, and L. R. Pease. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77:51-59.
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 10
    • 0031171841 scopus 로고    scopus 로고
    • Heterologous protein production in Acremonium chrysogenum: Expression of bacterial cephalosporin C acylase and human thrombomodulin genes
    • Honda, G., A. Matsuda, M. Zushi, S. Yamamoto, and K. Komatsu. 1997. Heterologous protein production in Acremonium chrysogenum: expression of bacterial cephalosporin C acylase and human thrombomodulin genes. Biosci. Biotechnol. Biochem. 61:948-955.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 948-955
    • Honda, G.1    Matsuda, A.2    Zushi, M.3    Yamamoto, S.4    Komatsu, K.5
  • 11
    • 0037155858 scopus 로고    scopus 로고
    • Affinity alkylation of the Trp-B4 residue of the beta-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130
    • Huang, X., R. Zeng, X. Ding, X. Mao, Y. Ding, Z. Rao, Y. Xie, W. Jiang, and G. Zhao. 2002. Affinity alkylation of the Trp-B4 residue of the beta-subunit of the glutaryl 7-aminocephalosporanic acid acylase of Pseudomonas sp. 130. J. Biol. Chem. 277:10256-10264.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10256-10264
    • Huang, X.1    Zeng, R.2    Ding, X.3    Mao, X.4    Ding, Y.5    Rao, Z.6    Xie, Y.7    Jiang, W.8    Zhao, G.9
  • 12
    • 0029017864 scopus 로고
    • High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176
    • Ishii, Y., Y. Saito, T. Fujimura, H. Sasaki, Y. Noguchi, H. Yamada, M. Niwa, and K. Shimomura. 1995. High-level production, chemical modification and site-directed mutagenesis of a cephalosporin C acylase from Pseudomonas strain N176. Eur. J. Biochem. 230:773-778.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 773-778
    • Ishii, Y.1    Saito, Y.2    Fujimura, T.3    Sasaki, H.4    Noguchi, Y.5    Yamada, H.6    Niwa, M.7    Shimomura, K.8
  • 13
    • 14744269262 scopus 로고
    • Construction of a 7-aminocephalosporanic acid (7ACA) biosynthetic operon and direct production of 7ACA in Acremonium chrysogenum
    • Isogai, T., M. Fukagawa, I. Aramori, M. Iwami, H. Kojo, T. Ono, Y. Ueda, M. Kohsaka, and H. Imanaka. 1991. Construction of a 7-aminocephalosporanic acid (7ACA) biosynthetic operon and direct production of 7ACA in Acremonium chrysogenum. Biotechnology 9:188-191.
    • (1991) Biotechnology , vol.9 , pp. 188-191
    • Isogai, T.1    Fukagawa, M.2    Aramori, I.3    Iwami, M.4    Kojo, H.5    Ono, T.6    Ueda, Y.7    Kohsaka, M.8    Imanaka, H.9
  • 14
    • 0035843166 scopus 로고    scopus 로고
    • Improving enzymes by using them in organic solvents
    • Kibanov, A. M. 2001. Improving enzymes by using them in organic solvents. Nature 409:241-246.
    • (2001) Nature , vol.409 , pp. 241-246
    • Kibanov, A.M.1
  • 15
    • 0035930509 scopus 로고    scopus 로고
    • Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for posttranslational modification
    • Kim, S., and Y. Kim. 2001. Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for posttranslational modification. J. Biol. Chem. 276:48376-48381.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48376-48381
    • Kim, S.1    Kim, Y.2
  • 16
    • 0035542860 scopus 로고    scopus 로고
    • Structure of cephalosporin acylase in complex with glutaryl-7- aminocephalosporanic acid and glutarate: Insight into the basis of its substrate specificity
    • Kim, Y., and W. G. Hol. 2001. Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity. Chem. Biol. 8:1253-1264.
    • (2001) Chem. Biol. , vol.8 , pp. 1253-1264
    • Kim, Y.1    Hol, W.G.2
  • 17
    • 0034435442 scopus 로고    scopus 로고
    • The 2.0 Å crystal structure of cephalosporin acylase
    • Kim, Y., K. Yoon, Y. Khang, S. Turley, and W. G. Hol. 2000. The 2.0 Å crystal structure of cephalosporin acylase. Struct. Fold Des. 8:1059-1068.
    • (2000) Struct. Fold Des. , vol.8 , pp. 1059-1068
    • Kim, Y.1    Yoon, K.2    Khang, Y.3    Turley, S.4    Hol, W.G.5
  • 18
    • 0031654539 scopus 로고    scopus 로고
    • An acidic glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas nitroreducens
    • Lee, Y. H., T. S. Chang, H. J. Liu, and W. S. Chu. 1998. An acidic glutaryl-7-amino cephalosporanic acid acylase from Pseudomonas nitroreducens. Biotechnol. Appl. Biochem. 28(Pt. 2):113-118.
    • (1998) Biotechnol. Appl. Biochem. , vol.28 , Issue.PART 2 , pp. 113-118
    • Lee, Y.H.1    Chang, T.S.2    Liu, H.J.3    Chu, W.S.4
  • 19
    • 0033564384 scopus 로고    scopus 로고
    • In vivo posttranslational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130
    • Li, Y., J. Chen, W. Jiang, X. Mao, G. Zhao, and E. Wang. 1999. In vivo posttranslational processing and subunit reconstitution of cephalosporin acylase from Pseudomonas sp. 130. Eur. J. Biochem. 262:713-719.
    • (1999) Eur. J. Biochem. , vol.262 , pp. 713-719
    • Li, Y.1    Chen, J.2    Jiang, W.3    Mao, X.4    Zhao, G.5    Wang, E.6
  • 20
    • 17144454968 scopus 로고    scopus 로고
    • Overproduction and purification of glutaryl 7-amino cephalosporanic acid acylase
    • Li, Y., W. Jiang, Y. Yang, G. Zhao, and E. Wang. 1998. Overproduction and purification of glutaryl 7-amino cephalosporanic acid acylase. Protein Expr. Purif. 12:233-238.
    • (1998) Protein Expr. Purif. , vol.12 , pp. 233-238
    • Li, Y.1    Jiang, W.2    Yang, Y.3    Zhao, G.4    Wang, E.5
  • 22
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site directed mutations that decrease the entropy of unfolding
    • Matthews, B., H. Nicholson, and W. Becktel. 1987. Enhanced protein thermostability from site directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. USA 84:6663-6667.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6663-6667
    • Matthews, B.1    Nicholson, H.2    Becktel, W.3
  • 23
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K., and J. M. Thornton. 1994. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 24
    • 0141514470 scopus 로고    scopus 로고
    • Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side chain conformations of active-site residues
    • Oh, B., M. Kim, J. Yoon, K. Chung, Y. Shin, D. Lee, and Y. Kim. 2003. Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side chain conformations of active-site residues. Biochem. Biophys. Res. Commun. 310:19-27.
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 19-27
    • Oh, B.1    Kim, M.2    Yoon, J.3    Chung, K.4    Shin, Y.5    Lee, D.6    Kim, Y.7
  • 25
    • 0029932580 scopus 로고    scopus 로고
    • Analysis of protein conformational characteristics related to thermostability
    • Querol, E., J. A. Perez-Pons, and A. Mozo-Villarias. 1996. Analysis of protein conformational characteristics related to thermostability. Protein Eng. 9:265-271.
    • (1996) Protein Eng. , vol.9 , pp. 265-271
    • Querol, E.1    Perez-Pons, J.A.2    Mozo-Villarias, A.3
  • 26
    • 0023646665 scopus 로고
    • Rational modification of enzyme catalysis by engineering surface charge
    • Russell, A. J., and A. R. Fersht. 1987. Rational modification of enzyme catalysis by engineering surface charge. Nature 328:496-500.
    • (1987) Nature , vol.328 , pp. 496-500
    • Russell, A.J.1    Fersht, A.R.2
  • 27
    • 0029742772 scopus 로고    scopus 로고
    • Oxidative modification of a cephalosporin C acylase from Pseudomonas sp. strain N176 and site-directed mutagenesis of the gene
    • Saito, Y., T. Fujimura, Y. Ishii, Y. Noguchi, T. Miura, M. Niwa, and K. Shimomura. 1996. Oxidative modification of a cephalosporin C acylase from Pseudomonas sp. strain N176 and site-directed mutagenesis of the gene. Appl. Environ. Microbiol. 62:2919-2925.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2919-2925
    • Saito, Y.1    Fujimura, T.2    Ishii, Y.3    Noguchi, Y.4    Miura, T.5    Niwa, M.6    Shimomura, K.7
  • 29
    • 0025325983 scopus 로고
    • The "megaprimer" method of site-directed mutagenesis
    • Sarkar, G., and S. S. Sommer. 1990. The "megaprimer" method of site-directed mutagenesis. BioTechniques 8:404-407.
    • (1990) BioTechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 30
    • 0033898359 scopus 로고    scopus 로고
    • Environmentally safe production of 7-aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum
    • Velasco, J., J. Luis-Adrio, M. Angel-Moreno, B. Diez, G. Soler, and J. L. Barredo. 2000. Environmentally safe production of 7- aminodeacetoxycephalosporanic acid (7-ADCA) using recombinant strains of Acremonium chrysogenum. Nat. Biotechnol. 18:857-861.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 857-861
    • Velasco, J.1    Luis-Adrio, J.2    Angel-Moreno, M.3    Diez, B.4    Soler, G.5    Barredo, J.L.6
  • 31
    • 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
  • 34
    • 0003047342 scopus 로고
    • Cloning of GL-7-ACA acylase from Pseudomonas sp. 130 and its expression in Escherichia coli
    • Yang, Y. L., and D. F. Yun. 1991. Cloning of GL-7-ACA acylase from Pseudomonas sp. 130 and its expression in Escherichia coli. Chin. J. Biotechnol. 7:99-107.
    • (1991) Chin. J. Biotechnol. , vol.7 , pp. 99-107
    • Yang, Y.L.1    Yun, D.F.2
  • 35
    • 20444368066 scopus 로고    scopus 로고
    • Mutagenesis of N-terminal amino acid residues in beta-subunit of glutaryl-7-amino-cephalosporanic acid acylase C130
    • Zhang, N., X. M. Ding, X. Huang, E. D. Wang, Y. L. Yang, G. P. Zhao, and W. H. Jiang. 2001. Mutagenesis of N-terminal amino acid residues in beta-subunit of glutaryl-7-amino-cephalosporanic acid acylase C130. Acta Biochim. Biophys. Sinica 33:671-676.
    • (2001) Acta Biochim. Biophys. Sinica , vol.33 , pp. 671-676
    • Zhang, N.1    Ding, X.M.2    Huang, X.3    Wang, E.D.4    Yang, Y.L.5    Zhao, G.P.6    Jiang, W.H.7
  • 36
    • 0345802689 scopus 로고    scopus 로고
    • Affinity-labeled glutaryl-7-amino cephalosporanic acid acylase C130 can hydrolyze the inhibitor during crystallization
    • Zhang, W., X. Huang, G. Zhao, and W. Jiang. 2004. Affinity-labeled glutaryl-7-amino cephalosporanic acid acylase C130 can hydrolyze the inhibitor during crystallization. Biochem. Biophys. Res. Commun. 313:555-558.
    • (2004) Biochem. Biophys. Res. Commun. , vol.313 , pp. 555-558
    • Zhang, W.1    Huang, X.2    Zhao, G.3    Jiang, W.4
  • 37
    • 0038404505 scopus 로고    scopus 로고
    • A rapid and specific method to screen environmental microorganisms for cephalosporin acylase activity
    • Zhu, S., Y. Yang, G. Zhao, and W. Jiang. 2003. A rapid and specific method to screen environmental microorganisms for cephalosporin acylase activity. J. Microbiol. Methods 54:131-135.
    • (2003) J. Microbiol. Methods , vol.54 , pp. 131-135
    • Zhu, S.1    Yang, Y.2    Zhao, G.3    Jiang, W.4


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