메뉴 건너뛰기




Volumn 74, Issue 11, 2008, Pages 3400-3409

Improvement of the glutaryl-7-aminocephalosporanic acid acylase activity of a bacterial γ-glutamyltranspeptidase

Author keywords

[No Author keywords available]

Indexed keywords

AMINATION; AMINES; AMINO ACIDS; BIOCHEMICAL ENGINEERING; ENZYMES; ESCHERICHIA COLI; FOOD ADDITIVES; HEALTH; ORGANIC ACIDS; PAINTING; SEWAGE TREATMENT PLANTS; THREE DIMENSIONAL;

EID: 44949102457     PISSN: 00992240     EISSN: None     Source Type: Journal    
DOI: 10.1128/AEM.02693-07     Document Type: Article
Times cited : (20)

References (38)
  • 2
    • 0017807890 scopus 로고
    • Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid
    • Chang, A. C. Y., and S. N. Cohen. 1978. Construction and characterization of amplifiable multicopy DNA cloning vehicles derived from the P15A cryptic miniplasmid. J. Bacteriol. 134:1141-1156.
    • (1978) J. Bacteriol , vol.134 , pp. 1141-1156
    • Chang, A.C.Y.1    Cohen, S.N.2
  • 3
    • 0029065955 scopus 로고
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistant determinant
    • R cassettes with the option of Flp-catalyzed excision of the antibiotic-resistant determinant. Gene 158:9-14.
    • (1995) Gene , vol.158 , pp. 9-14
    • Cherepanov, P.P.1    Wackernagel, W.2
  • 4
    • 0025780937 scopus 로고
    • Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli
    • Claudio, J. O., H. Suzuki, H. Kumagai, and T. Tochikura. 1991. Excretion and rapid purification of γ-glutamyltranspeptidase from Escherichia coli. J. Ferment. Bioeng. 72:125-127.
    • (1991) J. Ferment. Bioeng , vol.72 , pp. 125-127
    • Claudio, J.O.1    Suzuki, H.2    Kumagai, H.3    Tochikura, T.4
  • 5
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko, K. A., and B. L. Wanner. 2000. One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc. Natl. Acad. Sci. USA 97:6640-6645.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 6
    • 0029151242 scopus 로고
    • Screening and characterization of microorganisms with glutaryl-7ADCA acylase activity
    • Franzosi, G., E. Battistel, I. Gagliardi, and W. Van der Goes. 1995. Screening and characterization of microorganisms with glutaryl-7ADCA acylase activity. Appl. Microbiol. Biotechnol. 43:508-513.
    • (1995) Appl. Microbiol. Biotechnol , vol.43 , pp. 508-513
    • Franzosi, G.1    Battistel, E.2    Gagliardi, I.3    Van der Goes, W.4
  • 7
    • 0023777977 scopus 로고
    • A survey of the kinetic parameters of class C β-lactamase. Cephalosporins and other β-lactam compounds
    • Galleni, M., G. Amicosante, and J. M. Frere. 1988. A survey of the kinetic parameters of class C β-lactamase. Cephalosporins and other β-lactam compounds. Biochem. J. 255:123-129.
    • (1988) Biochem. J , vol.255 , pp. 123-129
    • Galleni, M.1    Amicosante, G.2    Frere, J.M.3
  • 8
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan, D. 1983. Studies on transformation of Escherichia coli with plasmids. J. Mol. Biol. 166:557-580.
    • (1983) J. Mol. Biol , vol.166 , pp. 557-580
    • Hanahan, D.1
  • 9
    • 0028977997 scopus 로고
    • Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit
    • Ikeda, Y., J. Fujii, N. Taniguchi, and A. Meister. 1995. Human γ-glutamyl transpeptidase mutants involving conserved aspartate residues and the unique cysteine residue of the light subunit. J. Biol. Chem. 270:12471-12475.
    • (1995) J. Biol. Chem , vol.270 , pp. 12471-12475
    • Ikeda, Y.1    Fujii, J.2    Taniguchi, N.3    Meister, A.4
  • 10
    • 0034604269 scopus 로고    scopus 로고
    • Identification of catalytic nucleophile of Escherichia coli γ-glutamyltranspeptidase by γ-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile
    • Inoue, M., J. Hiratake, H. Suzuki, H. Kumagai, and K. Sakata. 2000. Identification of catalytic nucleophile of Escherichia coli γ-glutamyltranspeptidase by γ-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile. Biochemistry 39:7764-7771.
    • (2000) Biochemistry , vol.39 , pp. 7764-7771
    • Inoue, M.1    Hiratake, J.2    Suzuki, H.3    Kumagai, H.4    Sakata, K.5
  • 11
    • 0026660909 scopus 로고
    • Nucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain
    • Ishiye, M., and M. Niwa. 1992. Nucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain. Biochim. Biophys. Acta 1132:232-243.
    • (1992) Biochim. Biophys. Acta , vol.1132 , pp. 232-243
    • Ishiye, M.1    Niwa, M.2
  • 12
    • 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
  • 13
    • 0033564384 scopus 로고    scopus 로고
    • In vivo post-translational 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 post-translational 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
  • 14
    • 0014702482 scopus 로고
    • Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains
    • Lindstrom, E. B., H. G. Boman, and B. B. Steele. 1970. Resistance of Escherichia coli to penicillins. VI. Purification and characterization of the chromosomally mediated penicillinase present in ampA-containing strains. J. Bacteriol. 101:218-231.
    • (1970) J. Bacteriol , vol.101 , pp. 218-231
    • Lindstrom, E.B.1    Boman, H.G.2    Steele, B.B.3
  • 15
    • 0037416735 scopus 로고    scopus 로고
    • Salt-tolerant γ-gluramyltranspeptidase from Bacillus subtilis 168 with glutaminase activity
    • Minami, H., H. Suzuki, and H. Kumagai. 2003. Salt-tolerant γ-gluramyltranspeptidase from Bacillus subtilis 168 with glutaminase activity. Enzyme Microb. Technol. 32:431-438.
    • (2003) Enzyme Microb. Technol , vol.32 , pp. 431-438
    • Minami, H.1    Suzuki, H.2    Kumagai, H.3
  • 16
    • 0041707747 scopus 로고    scopus 로고
    • A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity
    • Minami, H., H. Suzuki, and H. Kumagai. 2003. A mutant Bacillus subtilis γ-glutamyltranspeptidase specialized in hydrolysis activity. FEMS Microbiol. Lett. 224:169-173.
    • (2003) FEMS Microbiol. Lett , vol.224 , pp. 169-173
    • Minami, H.1    Suzuki, H.2    Kumagai, H.3
  • 17
    • 36248940234 scopus 로고    scopus 로고
    • Characterization of Helicobacter pylori γ- glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis
    • Morrow, A. L., K. Willams, A. Sand, G. Boanca, and J. J. Barycki. 2007. Characterization of Helicobacter pylori γ- glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis. Biochemistry 46:12407-13414.
    • (2007) Biochemistry , vol.46 , pp. 12407-13414
    • Morrow, A.L.1    Willams, K.2    Sand, A.3    Boanca, G.4    Barycki, J.J.5
  • 18
    • 0023375673 scopus 로고
    • Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: A quantitative predictive treatment
    • Nikaido, H., and S. Normark. 1987. Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamases: a quantitative predictive treatment. Mol. Microbiol. 1:29-36.
    • (1987) Mol. Microbiol , vol.1 , pp. 29-36
    • Nikaido, H.1    Normark, S.2
  • 19
    • 0141514470 scopus 로고    scopus 로고
    • Deacylation activity of cephalosporin acylase to cephalosporin C 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 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
  • 20
    • 33646244528 scopus 로고    scopus 로고
    • Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate
    • Okada, T., H. Suzuki, K. Wada, H. Kumagai, and K. Fukuyama. 2006. Crystal structures of γ-glutamyltranspeptidase from Escherichia coli, a key enzyme in glutathione metabolism, and its reaction intermediate. Proc. Natl. Acad. Sci. USA 103:6471-6476.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6471-6476
    • Okada, T.1    Suzuki, H.2    Wada, K.3    Kumagai, H.4    Fukuyama, K.5
  • 21
    • 34047276293 scopus 로고    scopus 로고
    • Crystal structure of the γ-glutamyltranspcptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism
    • Okada, T., H. Suzuki, K. Wada, H. Kumagai, and K. Fukuyama. 2007. Crystal structure of the γ-glutamyltranspcptidase precursor protein from Escherichia coli. Structural changes upon autocatalytic processing and implications for the maturation mechanism. J. Biol. Chem. 282:2433-2439.
    • (2007) J. Biol. Chem , vol.282 , pp. 2433-2439
    • Okada, T.1    Suzuki, H.2    Wada, K.3    Kumagai, H.4    Fukuyama, K.5
  • 22
    • 0036829913 scopus 로고    scopus 로고
    • Altering the substrate specificity of cephalosporin acylase by directed evolution of the β-subunit
    • Otten, L. G., C. F. Sio, J. Vrielink, R. H. Cool, and W. J. Quax. 2002. Altering the substrate specificity of cephalosporin acylase by directed evolution of the β-subunit. J. Biol. Chem. 277:42121-42127.
    • (2002) J. Biol. Chem , vol.277 , pp. 42121-42127
    • Otten, L.G.1    Sio, C.F.2    Vrielink, J.3    Cool, R.H.4    Quax, W.J.5
  • 23
    • 33644685043 scopus 로고    scopus 로고
    • Spectrophotometric assay for quantitative determination of 7-aminocephalosporanic acid from direct hydrolysis of cephalosporin C
    • Patett, F., and L. Fischer. 2006. Spectrophotometric assay for quantitative determination of 7-aminocephalosporanic acid from direct hydrolysis of cephalosporin C. Anal. Biochem. 350:304-306.
    • (2006) Anal. Biochem , vol.350 , pp. 304-306
    • Patett, F.1    Fischer, L.2
  • 24
    • 0345102428 scopus 로고    scopus 로고
    • The complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamase
    • Powers, R. A., J. Blazquez, G. S. Weston, M. I. Morisini, F. Baquero, and B. K. Shoichet. 1999. The complexed structure and antimicrobial activity of a non-β-lactam inhibitor of AmpC β-lactamase. Protein Sci. 8:2330-2337.
    • (1999) Protein Sci , vol.8 , pp. 2330-2337
    • Powers, R.A.1    Blazquez, J.2    Weston, G.S.3    Morisini, M.I.4    Baquero, F.5    Shoichet, B.K.6
  • 25
    • 0019878056 scopus 로고
    • Characterization of the β-lactamase promoter of pBR322
    • Russell, D. R., and G. N. Bennett. 1981. Characterization of the β-lactamase promoter of pBR322. Nucleic Acids Res. 9:2517-2533.
    • (1981) Nucleic Acids Res , vol.9 , pp. 2517-2533
    • Russell, D.R.1    Bennett, G.N.2
  • 27
    • 0001235624 scopus 로고
    • Isolation and properties of 7β-(4-carboxybutanamido)cephalosporanic acid acylase-producing bacteria
    • Shibuya, Y., K. Matsumoto, and T. Fujii. 1981. Isolation and properties of 7β-(4-carboxybutanamido)cephalosporanic acid acylase-producing bacteria. Agric. Biol. Chem. 45:1561-1567.
    • (1981) Agric. Biol. Chem , vol.45 , pp. 1561-1567
    • Shibuya, Y.1    Matsumoto, K.2    Fujii, T.3
  • 29
    • 24344468705 scopus 로고    scopus 로고
    • The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette
    • Suzuki, H., T. Koyanagi, S. Izuka, A. Onishi, and H. Kumagai. 2005. The yliA, -B, -C, and -D genes of Escherichia coli K-12 encode a novel glutathione importer with an ATP-binding cassette. J. Bacteriol. 187:5861-5867.
    • (2005) J. Bacteriol , vol.187 , pp. 5861-5867
    • Suzuki, H.1    Koyanagi, T.2    Izuka, S.3    Onishi, A.4    Kumagai, H.5
  • 30
    • 0037044805 scopus 로고    scopus 로고
    • Autocatalytic processing of γ-glutamyltranspeptidase
    • Suzuki, H., and H. Kumagai. 2002. Autocatalytic processing of γ-glutamyltranspeptidase. J. Biol. Chem. 277:43536-43543.
    • (2002) J. Biol. Chem , vol.277 , pp. 43536-43543
    • Suzuki, H.1    Kumagai, H.2
  • 31
    • 0023835701 scopus 로고
    • Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase
    • Suzuki, H., H. Kumagai, T. Echigo, and T. Tochikura. 1988. Molecular cloning of Escherichia coli K-12 ggt and rapid isolation of γ-glutamyltranspeptidase. Biochem. Biophys. Res. Commun. 150:33-38.
    • (1988) Biochem. Biophys. Res. Commun , vol.150 , pp. 33-38
    • Suzuki, H.1    Kumagai, H.2    Echigo, T.3    Tochikura, T.4
  • 32
    • 0022891712 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Purification and properties
    • Suzuki, H., H. Kumagai, and T. Tochikura. 1986. γ-Glutamyltranspeptidase from Escherichia coli K-12: purification and properties. J. Bacteriol. 168: 1325-1335.
    • (1986) J. Bacteriol , vol.168 , pp. 1325-1335
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 33
    • 0022908614 scopus 로고
    • γ-Glutamyltranspeptidase from Escherichia coli K-12: Formation and localization
    • Suzuki, H., H. Kumagai, and T. Tochikura. 1986. γ-Glutamyltranspeptidase from Escherichia coli K-12: formation and localization. J. Bacteriol. 168: 1332-1335.
    • (1986) J. Bacteriol , vol.168 , pp. 1332-1335
    • Suzuki, H.1    Kumagai, H.2    Tochikura, T.3
  • 34
    • 8144223543 scopus 로고    scopus 로고
    • A single amino acid substitution converts γ-glutamyltranspeptidasc to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase)
    • Suzuki, H., C. Miwa, S. Ishihara, and H. Kumagai. 2004. A single amino acid substitution converts γ-glutamyltranspeptidasc to a class IV cephalosporin acylase (glutaryl-7-aminocephalosporanic acid acylase). Appl. Environ. Microbiol. 70:6324-6328.
    • (2004) Appl. Environ. Microbiol , vol.70 , pp. 6324-6328
    • Suzuki, H.1    Miwa, C.2    Ishihara, S.3    Kumagai, H.4
  • 35
    • 34147171510 scopus 로고    scopus 로고
    • γ-Glutamyl compounds and their enzymatic production using bacterial γ- glutamyltranspeptidase
    • Suzuki, H., C. Yamada, and K. Kato. 2007. γ-Glutamyl compounds and their enzymatic production using bacterial γ- glutamyltranspeptidase. Amino Acids 32:333-340.
    • (2007) Amino Acids , vol.32 , pp. 333-340
    • Suzuki, H.1    Yamada, C.2    Kato, K.3
  • 36
    • 0031627519 scopus 로고    scopus 로고
    • γ-Glutamyltranspeptidase: Catalytic mechanism and gene expression
    • Taniguchi, N., and Y. Ikeda. 1998. γ-Glutamyltranspeptidase: catalytic mechanism and gene expression. Adv. Enzymol. Relat. Areas Mol. Biol. 72:239-278.
    • (1998) Adv. Enzymol. Relat. Areas Mol. Biol , vol.72 , pp. 239-278
    • Taniguchi, N.1    Ikeda, Y.2
  • 37
    • 0027968068 scopus 로고
    • CLUSTALW: 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. CLUSTALW: 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
  • 38
    • 34147108343 scopus 로고    scopus 로고
    • Construction of recombinant Escherichta coli D11/pMSTO and its use in enzymatic preparation of 7-aminocephalosporanic acid in one pot
    • Zheng, H., T. Zhu, J. Chen, Y. Zhao, W. Jiang, G. Zhao, S. Yang, and Y. Yang. 2007. Construction of recombinant Escherichta coli D11/pMSTO and its use in enzymatic preparation of 7-aminocephalosporanic acid in one pot. J. Biotechnol. 129:400-405.
    • (2007) J. Biotechnol , vol.129 , pp. 400-405
    • Zheng, H.1    Zhu, T.2    Chen, J.3    Zhao, Y.4    Jiang, W.5    Zhao, G.6    Yang, S.7    Yang, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.