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Volumn 45, Issue 2, 2006, Pages 275-287

An improved purification procedure for cyclosporin synthetase

Author keywords

Antibiotic biosynthesis; Cyclosporin synthetase; Fungal biotechnology; In vitro enzymatic biosynthesis; Large scale protein purification; Non ribosomal peptide synthetase; Tolypocladium inflatum

Indexed keywords

CYCLOSPORIN; CYCLOSPORIN A SYNTHETASE; FUNGAL PROTEIN; MULTIENZYME COMPLEX; PEPTIDE SYNTHASE;

EID: 31044444367     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2005.07.012     Document Type: Article
Times cited : (5)

References (48)
  • 1
    • 0035023450 scopus 로고    scopus 로고
    • Multimodular biocatalysts for natural product assembly
    • D. Schwarzer, and M.A. Marahiel Multimodular biocatalysts for natural product assembly Naturwissenschaften 88 2001 93 101
    • (2001) Naturwissenschaften , vol.88 , pp. 93-101
    • Schwarzer, D.1    Marahiel, M.A.2
  • 3
    • 1642304143 scopus 로고    scopus 로고
    • Polyketide and nonribosomal peptide antibiotics: Modularity and versatility
    • C.T. Walsh Polyketide and nonribosomal peptide antibiotics: modularity and versatility Science 303 2004 1805 1810
    • (2004) Science , vol.303 , pp. 1805-1810
    • Walsh, C.T.1
  • 5
    • 0000357083 scopus 로고
    • Tolypocladium, a synonym of Beauveria
    • J.A. von Arx (1986) Tolypocladium, a synonym of Beauveria. Mycotaxonomy 25 (2003) 153-158.
    • (1986) Mycotaxonomy , vol.25 , pp. 153-158
    • Von Arx, J.A.1
  • 6
    • 0006957892 scopus 로고
    • Proposal to reject Pachybasium niveum Rostrup in order to retain the name Tolypocladium inflatum W. Gams for the fungus that produces cyclosporin
    • M.M. Dreyfuss, and W. Gams Proposal to reject Pachybasium niveum Rostrup in order to retain the name Tolypocladium inflatum W. Gams for the fungus that produces cyclosporin Taxon 34 1994 660 661
    • (1994) Taxon , vol.34 , pp. 660-661
    • Dreyfuss, M.M.1    Gams, W.2
  • 7
    • 0017072249 scopus 로고
    • Cyclosporin A, ein immunsuppressiv wirksamer Peptidmetabolit aus Trichoderma polysporum (Link ex Pers.) Rifai
    • Rüegger, M. Kuhn, H. Lichti, H.R. Loosli, R. Huguenin, C. Quiquerez, and A. von Wartburg Cyclosporin A, ein immunsuppressiv wirksamer Peptidmetabolit aus Trichoderma polysporum (Link ex Pers.) Rifai Helv. Chim. Acta 59 1976 1075 1092
    • (1976) Helv. Chim. Acta , vol.59 , pp. 1075-1092
    • Rüegger1    Kuhn, M.2    Lichti, H.3    Loosli, H.R.4    Huguenin, R.5    Quiquerez, C.6    Von Wartburg, A.7
  • 9
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • M.A. Marahiel Protein templates for the biosynthesis of peptide antibiotics Chem. Biol. 4 1997 561 567
    • (1997) Chem. Biol. , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 10
    • 0029688322 scopus 로고    scopus 로고
    • Biosynthesis and mechanism of action of cyclosporins
    • A. Lawen Biosynthesis and mechanism of action of cyclosporins Prog. Med. Chem. 33 1996 53 97
    • (1996) Prog. Med. Chem. , vol.33 , pp. 53-97
    • Lawen, A.1
  • 11
    • 1542755301 scopus 로고    scopus 로고
    • Nonribosomal peptide synthetases as technological platforms for the synthesis of highly modified peptide bioeffectors-cyclosporin synthetase as a complex example
    • M.R. El-Gewely Elsevier Science B.V.
    • T. Velkov, and A. Lawen Nonribosomal peptide synthetases as technological platforms for the synthesis of highly modified peptide bioeffectors-cyclosporin synthetase as a complex example M.R. El-Gewely Biotechnology Annual Review vol. 9 2003 Elsevier Science B.V. 151 197
    • (2003) Biotechnology Annual Review , vol.9 , pp. 151-197
    • Velkov, T.1    Lawen, A.2
  • 12
    • 0025193843 scopus 로고
    • Cyclosporin synthetase. the most complex peptide synthesizing multienzyme polypeptide so far described
    • A. Lawen, and R. Zocher Cyclosporin synthetase. The most complex peptide synthesizing multienzyme polypeptide so far described J. Biol. Chem. 265 1990 11355 11360
    • (1990) J. Biol. Chem. , vol.265 , pp. 11355-11360
    • Lawen, A.1    Zocher, R.2
  • 13
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • G. Weber, K. Schörgendorfer, E. Schneider-Scherzer, and E. Leitner The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame Curr. Genet. 26 1994 120 125
    • (1994) Curr. Genet. , vol.26 , pp. 120-125
    • Weber, G.1    Schörgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 14
    • 0028122932 scopus 로고
    • Mechanism of cyclosporin a biosynthesis. Evidence for synthesis via a single linear undecapeptide precursor
    • J. Dittmann, R.M. Wenger, H. Kleinkauf, and A. Lawen Mechanism of cyclosporin A biosynthesis. Evidence for synthesis via a single linear undecapeptide precursor J. Biol. Chem. 269 1994 2841 2846
    • (1994) J. Biol. Chem. , vol.269 , pp. 2841-2846
    • Dittmann, J.1    Wenger, R.M.2    Kleinkauf, H.3    Lawen, A.4
  • 15
    • 0026766758 scopus 로고
    • Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases
    • B. Schmidt, D. Riesner, A. Lawen, and H. Kleinkauf Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases FEBS Lett. 307 1992 355 360
    • (1992) FEBS Lett. , vol.307 , pp. 355-360
    • Schmidt, B.1    Riesner, D.2    Lawen, A.3    Kleinkauf, H.4
  • 16
    • 0022482553 scopus 로고
    • Cyclosporin and its future
    • J.F. Borel Cyclosporin and its future Prog. Allergy 38 1986 9 18
    • (1986) Prog. Allergy , vol.38 , pp. 9-18
    • Borel, J.F.1
  • 17
    • 0024955297 scopus 로고
    • Pharmacology of cyclosporine (sandimmune). IV. Pharmacological properties in vivo
    • J.F. Borel Pharmacology of cyclosporine (sandimmune). IV. Pharmacological properties in vivo Pharmacol. Rev. 41 1989 259 371
    • (1989) Pharmacol. Rev. , vol.41 , pp. 259-371
    • Borel, J.F.1
  • 19
    • 0024557096 scopus 로고
    • Cyclosporins new analogs by precursor directed biosynthesis
    • R. Traber, H. Hofmann, and H. Kobel Cyclosporins new analogs by precursor directed biosynthesis J. Antibiot. Tokyo 42 1989 591 597
    • (1989) J. Antibiot. Tokyo , vol.42 , pp. 591-597
    • Traber, R.1    Hofmann, H.2    Kobel, H.3
  • 21
    • 0028283317 scopus 로고
    • In vitro biosynthesis of ring-extended cyclosporins
    • A. Lawen, R. Traber, R. Reuille, and M. Ponelle In vitro biosynthesis of ring-extended cyclosporins Biochem. J. 300 1994 395 399
    • (1994) Biochem. J. , vol.300 , pp. 395-399
    • Lawen, A.1    Traber, R.2    Reuille, R.3    Ponelle, M.4
  • 22
    • 0027250118 scopus 로고
    • Substrate specificities of cyclosporin synthetase and peptolide SDZ 214-103 synthetase. Comparison of the substrate specificities of the related multifunctional polypeptides
    • A. Lawen, and R. Traber Substrate specificities of cyclosporin synthetase and peptolide SDZ 214-103 synthetase. Comparison of the substrate specificities of the related multifunctional polypeptides J. Biol. Chem. 268 1993 20452 20465
    • (1993) J. Biol. Chem. , vol.268 , pp. 20452-20465
    • Lawen, A.1    Traber, R.2
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 24
    • 0024959449 scopus 로고
    • Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins
    • G. Fischer, B. Wittmann-Liebold, K. Lang, T. Kiefhaber, and F.X. Schmid Cyclophilin and peptidyl-prolyl cis-trans isomerase are probably identical proteins Nature 337 1989 476 478
    • (1989) Nature , vol.337 , pp. 476-478
    • Fischer, G.1    Wittmann-Liebold, B.2    Lang, K.3    Kiefhaber, T.4    Schmid, F.X.5
  • 25
    • 0025868143 scopus 로고
    • Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay
    • J.L. Kofron, P. Kuzmič, V. Kishore, E. Colón-Bonilla, and D.H. Rich Determination of kinetic constants for peptidyl prolyl cis-trans isomerases by an improved spectrophotometric assay Biochemistry 30 1991 6127 6134
    • (1991) Biochemistry , vol.30 , pp. 6127-6134
    • Kofron, J.L.1    Kuzmič, P.2    Kishore, V.3    Colón-Bonilla, E.4    Rich, D.H.5
  • 26
    • 0038672779 scopus 로고    scopus 로고
    • Photoaffinity labeling of the N-methyltransferase domains of cyclosporin synthetase
    • T. Velkov, and A. Lawen Photoaffinity labeling of the N-methyltransferase domains of cyclosporin synthetase Photochem. Photobiol. 77 2003 129 137
    • (2003) Photochem. Photobiol. , vol.77 , pp. 129-137
    • Velkov, T.1    Lawen, A.2
  • 28
    • 0022516746 scopus 로고
    • Physiological and genetic factors for process development of cyclosporine fermentations
    • S.N. Agathos, J.W. Marshall, C. Morati, R. Parekh, and C. Madhosingh Physiological and genetic factors for process development of cyclosporine fermentations J. Ind. Microbiol. 1 1986 39 48
    • (1986) J. Ind. Microbiol. , vol.1 , pp. 39-48
    • Agathos, S.N.1    Marshall, J.W.2    Morati, C.3    Parekh, R.4    Madhosingh, C.5
  • 30
    • 0025020139 scopus 로고
    • Enhancement of cyclosporin production in a Tolypocladium inflatum strain after epichlorohydrin treatment
    • S.N. Agathos, and R. Parekh Enhancement of cyclosporin production in a Tolypocladium inflatum strain after epichlorohydrin treatment J. Biotechnol. 13 1990 73 81
    • (1990) J. Biotechnol. , vol.13 , pp. 73-81
    • Agathos, S.N.1    Parekh, R.2
  • 31
    • 0026024046 scopus 로고
    • Dynamics of l-valine in relation to the production of cyclosporin a by Tolypocladium inflatum
    • J. Lee, and S.N. Agathos Dynamics of l-valine in relation to the production of cyclosporin A by Tolypocladium inflatum Appl. Microbiol. Biotechnol. 34 1991 513 517
    • (1991) Appl. Microbiol. Biotechnol. , vol.34 , pp. 513-517
    • Lee, J.1    Agathos, S.N.2
  • 33
    • 0035732760 scopus 로고    scopus 로고
    • Structure and localization of cyclosporin synthetase, the key enzyme of cyclosporin biosynthesis in Tolypocladium inflatum
    • M. Hoppert, C. Gentzsch, and K. Schörgendorfer Structure and localization of cyclosporin synthetase, the key enzyme of cyclosporin biosynthesis in Tolypocladium inflatum Arch. Microbiol. 176 2001 285 293
    • (2001) Arch. Microbiol. , vol.176 , pp. 285-293
    • Hoppert, M.1    Gentzsch, C.2    Schörgendorfer, K.3
  • 34
    • 0037428469 scopus 로고    scopus 로고
    • Mapping and molecular modeling of S-adenosyl-l-methionine binding sites in N-methyltransferase domains of the multifunctional polypeptide cyclosporin synthetase
    • T. Velkov, and A. Lawen Mapping and molecular modeling of S-adenosyl-l-methionine binding sites in N-methyltransferase domains of the multifunctional polypeptide cyclosporin synthetase J. Biol. Chem. 278 2003 1137 1148
    • (2003) J. Biol. Chem. , vol.278 , pp. 1137-1148
    • Velkov, T.1    Lawen, A.2
  • 35
    • 84885498181 scopus 로고    scopus 로고
    • Immunosuppressants
    • H.D. Osiewacz Springer-Verlag Berlin Heidelberg
    • H. Kürsteiner, M. Zinner, and U. Kück Immunosuppressants H.D. Osiewacz The Mycota vol. 10 2002 Springer-Verlag Berlin Heidelberg 129 155
    • (2002) The Mycota , vol.10 , pp. 129-155
    • Kürsteiner, H.1    Zinner, M.2    Kück, U.3
  • 36
    • 0021079458 scopus 로고
    • Production of cyclosporin by carrageenan-immobilized Tolypocladium inflatum in an airlift reactor with external loop
    • B.C. Foster, R.T. Coutts, F.M. Pasutto, and J.B. Dossetor Production of cyclosporin by carrageenan-immobilized Tolypocladium inflatum in an airlift reactor with external loop Biotechnol. Lett. 5 1983 693 696
    • (1983) Biotechnol. Lett. , vol.5 , pp. 693-696
    • Foster, B.C.1    Coutts, R.T.2    Pasutto, F.M.3    Dossetor, J.B.4
  • 37
    • 0024634666 scopus 로고
    • Immobilization of Tolypocladium inflatum spores into porous celite beads for cyclosporin production
    • G.T. Chun, and S.N. Agathos Immobilization of Tolypocladium inflatum spores into porous celite beads for cyclosporin production J. Biotechnol. 9 1989 237 254
    • (1989) J. Biotechnol. , vol.9 , pp. 237-254
    • Chun, G.T.1    Agathos, S.N.2
  • 38
    • 0025925357 scopus 로고
    • 10]cyclosporin, a cyclosporin-related peptolide with immunosuppressive activity by a multienzyme polypeptide
    • 10]cyclosporin, a cyclosporin-related peptolide with immunosuppressive activity by a multienzyme polypeptide J. Biol. Chem. 266 1991 15567 15570
    • (1991) J. Biol. Chem. , vol.266 , pp. 15567-15570
    • Lawen, A.1    Traber, R.2    Geyl, D.3
  • 40
    • 0002974228 scopus 로고    scopus 로고
    • Biosynthesis of cyclosporins
    • W.R. Strohl 2nd ed. Marcel Dekker New York, Basel, Hong Kong
    • R. Traber Biosynthesis of cyclosporins W.R. Strohl 2nd ed. Biotechnology of Antibiotics 1997 Marcel Dekker New York, Basel, Hong Kong 279 314
    • (1997) Biotechnology of Antibiotics , pp. 279-314
    • Traber, R.1
  • 44
    • 0029083998 scopus 로고
    • Reversal of multidrug resistance by novel cyclosporin a analogs and the cyclopeptide SDZ 214-103 biosynthesized in vitro
    • K. Schwabe, G. Steinheider, A. Lawen, R. Traber, and A. Hildebrandt Reversal of multidrug resistance by novel cyclosporin A analogs and the cyclopeptide SDZ 214-103 biosynthesized in vitro J. Cancer Res. Clin. Oncol. 121 1995 407 412
    • (1995) J. Cancer Res. Clin. Oncol. , vol.121 , pp. 407-412
    • Schwabe, K.1    Steinheider, G.2    Lawen, A.3    Traber, R.4    Hildebrandt, A.5
  • 45
    • 0001679730 scopus 로고
    • Mechanism of alkaline hydrolysis of S-adenosyl-l-methionine and related sulfonium nucleosides
    • R.T. Borchardt Mechanism of alkaline hydrolysis of S-adenosyl-l- methionine and related sulfonium nucleosides J. Am. Chem. Soc. 101 1979 458 463
    • (1979) J. Am. Chem. Soc. , vol.101 , pp. 458-463
    • Borchardt, R.T.1
  • 46
    • 6344256785 scopus 로고    scopus 로고
    • Insight into the polar reactivity of the onium chalcogen analogues of S-adenosyl-l-methionine
    • D.F. Iwig, and S.J. Booker Insight into the polar reactivity of the onium chalcogen analogues of S-adenosyl-l-methionine Biochemistry 43 2004 13496 13509
    • (2004) Biochemistry , vol.43 , pp. 13496-13509
    • Iwig, D.F.1    Booker, S.J.2
  • 47
    • 0028724354 scopus 로고
    • Potential of fungi in the discovery of novel, low-molecular weight pharmaceuticals
    • M.M. Dreyfuss, and I.H. Chapela Potential of fungi in the discovery of novel, low-molecular weight pharmaceuticals Biotechnology 26 1994 49 80
    • (1994) Biotechnology , vol.26 , pp. 49-80
    • Dreyfuss, M.M.1    Chapela, I.H.2
  • 48
    • 0030484801 scopus 로고    scopus 로고
    • Occurrence of cyclosporins and cyclosporin-like peptolides in fungi
    • R. Traber, and M.M. Dreyfuss Occurrence of cyclosporins and cyclosporin-like peptolides in fungi J. Ind. Microbiol. 17 1996 397 401
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 397-401
    • Traber, R.1    Dreyfuss, M.M.2


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