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Volumn 24, Issue 3, 2000, Pages 173-180

Membrane-associated echinocandin B deacylase of Actinoplanes utahensis: Purification, heterologous cloning and enzymatic deacylation reaction

Author keywords

Antifungal agent; Echinocandin B deacylase; Evolution technology; Substrate specificity

Indexed keywords

ECHINOCANDIN B; FUNGAL ENZYME; RECOMBINANT ENZYME;

EID: 0034098943     PISSN: 13675435     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.jim.2900796     Document Type: Article
Times cited : (25)

References (23)
  • 1
    • 0023691009 scopus 로고
    • Deacylation of 21978C, an acidic lipopeptide antibiotic complex, by Actinoplanes utahensis
    • 1 Boeck LD, DS Fukuda, BJ Abbott and M Debono. 1988. Deacylation of 21978C, an acidic lipopeptide antibiotic complex, by Actinoplanes utahensis. J Antibiot 41: 1085-1092.
    • (1988) J Antibiot , vol.41 , pp. 1085-1092
    • Boeck, L.D.1    Fukuda, D.S.2    Abbott, B.J.3    Debono, M.4
  • 2
    • 0024603393 scopus 로고
    • Deacylation of echinocandin B by Actinoplanes utahensis
    • 2 Boeck LD, DS Fukuda, BJ Abbott and M Debono. 1989. Deacylation of echinocandin B by Actinoplanes utahensis. J Antibiot 42: 382-388.
    • (1989) J Antibiot , vol.42 , pp. 382-388
    • Boeck, L.D.1    Fukuda, D.S.2    Abbott, B.J.3    Debono, M.4
  • 3
    • 0021849634 scopus 로고
    • Structure of the penicillin acylase gene from Escherichia coli: A periplasmic enzyme that undergoes multiple proteolytic processing
    • 3 Bruns W, J Hoppe, H Tsai, HJ Bruning, F Maywald, J Collins and H Mayer. 1985. Structure of the penicillin acylase gene from Escherichia coli: a periplasmic enzyme that undergoes multiple proteolytic processing. J Mol Appl Genet 3: 36-44.
    • (1985) J Mol Appl Genet , vol.3 , pp. 36-44
    • Bruns, W.1    Hoppe, J.2    Tsai, H.3    Bruning, H.J.4    Maywald, F.5    Collins, J.6    Mayer, H.7
  • 4
    • 0024591140 scopus 로고
    • Characterization of a salt-extractable phosphatidylinositol synthase from rat pituitary-tumour membranes
    • 4 Cubitt AB and MC Gershengorn. 1989. Characterization of a salt-extractable phosphatidylinositol synthase from rat pituitary-tumour membranes. Biochem J 257: 639-644.
    • (1989) Biochem J , vol.257 , pp. 639-644
    • Cubitt, A.B.1    Gershengorn, M.C.2
  • 5
    • 0024519380 scopus 로고
    • Synthesis of new analogs of echinocandin C by enzymatic deacylation and chemical reacylation of the echinocandin B peptide: Synthesis of the antifungal agent cilofungin (LY121019)
    • 5 Debono M, BJ Abbott, DS Fukuda, M Barnhart, KE Willard, RM Molloy, KH Michel, JR Turner, TF Butler and AH Hunt. 1988. Synthesis of new analogs of echinocandin C by enzymatic deacylation and chemical reacylation of the echinocandin B peptide: synthesis of the antifungal agent cilofungin (LY121019). J Antibiot 42: 389-397.
    • (1988) J Antibiot , vol.42 , pp. 389-397
    • Debono, M.1    Abbott, B.J.2    Fukuda, D.S.3    Barnhart, M.4    Willard, K.E.5    Molloy, R.M.6    Michel, K.H.7    Turner, J.R.8    Butler, T.F.9    Hunt, A.H.10
  • 7
    • 0024155609 scopus 로고
    • Anti-Candida activity and toxicology of LY121019, a novel semisynthetic polypeptide antifungal antibiotic
    • 7 Gordee RS, DJ Zeckner, LC Howard, WE Alborn Jr and M Debono. 1988. Anti-Candida activity and toxicology of LY121019, a novel semisynthetic polypeptide antifungal antibiotic. Ann NY Acad Sci 544: 294-309.
    • (1988) Ann NY Acad Sci , vol.544 , pp. 294-309
    • Gordee, R.S.1    Zeckner, D.J.2    Howard, L.C.3    Alborn, W.E.4    Debono, M.5
  • 8
    • 0001320379 scopus 로고
    • Purification and characterization of glycerol 3-phosphate dehydrogenase from two types of Acidiphilium sp
    • 8 Hatta T, K Inagaki, T Sugio, N Kishimoto and T Tano. 1989. Purification and characterization of glycerol 3-phosphate dehydrogenase from two types of Acidiphilium sp. Agr Biol Chem 53: 651-658.
    • (1989) Agr Biol Chem , vol.53 , pp. 651-658
    • Hatta, T.1    Inagaki, K.2    Sugio, T.3    Kishimoto, N.4    Tano, T.5
  • 10
    • 0026669019 scopus 로고
    • Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression in Streptomyces lividans
    • 10 Inokoshi J, H Takeshima, H Ikeda and S Omura. 1992. Cloning and sequencing of the aculeacin A acylase-encoding gene from Actinoplanes utahensis and expression in Streptomyces lividans. Gene 119: 29-35.
    • (1992) Gene , vol.119 , pp. 29-35
    • Inokoshi, J.1    Takeshima, H.2    Ikeda, H.3    Omura, S.4
  • 11
    • 0023220105 scopus 로고
    • Kinetic reaction mechanism for magnesium binding to membrane-bound and soluble catechol O-methyl-transferase
    • 11 Jeffery DR and JA Roth. 1987. Kinetic reaction mechanism for magnesium binding to membrane-bound and soluble catechol O-methyl-transferase. Biochemistry 26: 2955-2958.
    • (1987) Biochemistry , vol.26 , pp. 2955-2958
    • Jeffery, D.R.1    Roth, J.A.2
  • 12
    • 0013688070 scopus 로고
    • Polymyxin acylase: A new enzyme for preparing starting materials for semisynthetic polymyxin antibiotics
    • 12 Kimura Y, H Matsunaga, N Yasuda, T Tatsuki and T Suzuki. 1987. Polymyxin acylase: a new enzyme for preparing starting materials for semisynthetic polymyxin antibiotics. Agr Biol Chem 51: 1617-1623.
    • (1987) Agr Biol Chem , vol.51 , pp. 1617-1623
    • Kimura, Y.1    Matsunaga, H.2    Yasuda, N.3    Tatsuki, T.4    Suzuki, T.5
  • 13
    • 0015956266 scopus 로고
    • Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11105
    • 13 Kutzbach C and E Rauenbusch. 1974. Preparation and general properties of crystalline penicillin acylase from Escherichia coli ATCC 11105. Hoppe-Seyler's Z Physiol Chem 354: 45-53.
    • (1974) Hoppe-Seyler's Z Physiol Chem , vol.354 , pp. 45-53
    • Kutzbach, C.1    Rauenbusch, E.2
  • 14
    • 0021677344 scopus 로고
    • Penicillin acylases: An update
    • 14 Mahajam PB. 1984. Penicillin acylases: an update. Appl Biochem Biotechnol 9: 537-554.
    • (1984) Appl Biochem Biotechnol , vol.9 , pp. 537-554
    • Mahajam, P.B.1
  • 15
    • 0019174497 scopus 로고
    • Substrate specificity of penicillin amidase from E. coli
    • 15 Margolin AL, VK Svedas and IV Berezin. 1980. Substrate specificity of penicillin amidase from E. coli. Biochim Biophys Acta 616: 283-289.
    • (1980) Biochim Biophys Acta , vol.616 , pp. 283-289
    • Margolin, A.L.1    Svedas, V.K.2    Berezin, I.V.3
  • 16
    • 0023585070 scopus 로고
    • Cloning and characterization of the genes for two distinct cephalosporin acylases from a Pseudomonas strain
    • 16 Matsuda A, K Matsuyama, K Yamamoto, S Ichikawa and KI Komatsu. 1987. Cloning and characterization of the genes for two distinct cephalosporin acylases from a Pseudomonas strain. J Bacteriol 169: 5815-5820.
    • (1987) J Bacteriol , vol.169 , pp. 5815-5820
    • Matsuda, A.1    Matsuyama, K.2    Yamamoto, K.3    Ichikawa, S.4    Komatsu, K.I.5
  • 18
    • 0031788664 scopus 로고    scopus 로고
    • Enzymatic deacylation of teicoplanin followed by reductive alkylation: Synthesis and antibacterial activity of new glycopeptides
    • 18 Snyder NJ, RD Cooper, BS Briggs, M Zmijewski, DL Mullen, RE Kaiser and TI Nicas. 1998. Enzymatic deacylation of teicoplanin followed by reductive alkylation: synthesis and antibacterial activity of new glycopeptides. J Antibiot 51: 945-951.
    • (1998) J Antibiot , vol.51 , pp. 945-951
    • Snyder, N.J.1    Cooper, R.D.2    Briggs, B.S.3    Zmijewski, M.4    Mullen, D.L.5    Kaiser, R.E.6    Nicas, T.I.7
  • 19
    • 0000429254 scopus 로고
    • Enzymatic synthesis of β-lactam antibiotics: A thermodynamic background
    • 19 Svedas VK, AL Margolin and IV Berezin. 1980. Enzymatic synthesis of β-lactam antibiotics: a thermodynamic background. Enzyme Microb Technol 2: 138-144.
    • (1980) Enzyme Microb Technol , vol.2 , pp. 138-144
    • Svedas, V.K.1    Margolin, A.L.2    Berezin, I.V.3
  • 20
    • 0024573701 scopus 로고
    • A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: Purification and characterization
    • 20 Takeshima H, J Inokoshi, Y Takada, H Tanaka and S Omura. 1989. A deacylation enzyme for aculeacin A, a neutral lipopeptide antibiotic, from Actinoplanes utahensis: purification and characterization. J Biochem 105: 606-610.
    • (1989) J Biochem , vol.105 , pp. 606-610
    • Takeshima, H.1    Inokoshi, J.2    Takada, Y.3    Tanaka, H.4    Omura, S.5
  • 22
    • 0031470397 scopus 로고    scopus 로고
    • Evolving enzyme technology for pharmaceutical applications: Case studies
    • 22 Yeh WK. 1997. Evolving enzyme technology for pharmaceutical applications: case studies. J Ind Microbiol Biotechnol 19: 334-343.
    • (1997) J Ind Microbiol Biotechnol , vol.19 , pp. 334-343
    • Yeh, W.K.1
  • 23
    • 0023939244 scopus 로고
    • Solubilization and purification of a α-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae
    • 23 Yoshihisa T, Y Ohsumi and Y Anraku. 1988. Solubilization and purification of a α-mannosidase, a marker enzyme of vacuolar membranes in Saccharomyces cerevisiae. J Biol Chem 263: 5158-5163.
    • (1988) J Biol Chem , vol.263 , pp. 5158-5163
    • Yoshihisa, T.1    Ohsumi, Y.2    Anraku, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.