메뉴 건너뛰기




Volumn 44, Issue 24, 2005, Pages 8873-8882

Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BIOSYNTHESIS; DEHYDRATION; ENZYMES; HYDROPHOBICITY; MASS SPECTROMETRY; STATISTICAL METHODS;

EID: 20544436705     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi050081h     Document Type: Article
Times cited : (139)

References (74)
  • 3
    • 0027309021 scopus 로고
    • Characterization of the Lactococcus lactis nisin a operon genes nisP, encoding a subtilin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis
    • Van der Meer, J. R., Polman, J., Beerthuyzen, M. M., Siezen, R., Kuipers, O. P., and de Vos, W. M. (1993) Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis, J. Bacteriol. 175, 2578-2588.
    • (1993) J. Bacteriol. , vol.175 , pp. 2578-2588
    • Van Der Meer, J.R.1    Polman, J.2    Beerthuyzen, M.M.3    Siezen, R.4    Kuipers, O.P.5    De Vos, W.M.6
  • 5
  • 6
    • 0035912883 scopus 로고    scopus 로고
    • Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases
    • Kohli, R. M., Trauger, J. W., Scharzer, D., Marahiel, M. A., and Walsh, C. T. (2001) Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases, Biochemistry 40, 7099-7108.
    • (2001) Biochemistry , vol.40 , pp. 7099-7108
    • Kohli, R.M.1    Trauger, J.W.2    Scharzer, D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 7
    • 0037022301 scopus 로고    scopus 로고
    • The thioesterase domain from a nonribosomal peptide synthetase as a cyclization catalyst for integrin binding peptides
    • Kohli, R. M., Takagi, J., and Walsh, C. T. (2002) The thioesterase domain from a nonribosomal peptide synthetase as a cyclization catalyst for integrin binding peptides, Proc. Natl. Acad. Sci. U.S.A. 99, 1247-1252.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1247-1252
    • Kohli, R.M.1    Takagi, J.2    Walsh, C.T.3
  • 8
    • 0036589245 scopus 로고    scopus 로고
    • Focus on modified microcins: Structural features and mechanisms of action
    • Destoumieux-Garzón, D., Peduzzi, J., and Rebuffat, S. (2002) Focus on modified microcins: structural features and mechanisms of action, Biochimie 84, 511-519.
    • (2002) Biochimie , vol.84 , pp. 511-519
    • Destoumieux-Garzón, D.1    Peduzzi, J.2    Rebuffat, S.3
  • 9
    • 0037335990 scopus 로고    scopus 로고
    • Identification and characterization of two novel clostridial bacteriocins, circularin a and closticin 574
    • Kemperman, R., Kuipers, A., Karsens, H., Nauta, A., Kuipers, O., and Kok, J. (2003) Identification and characterization of two novel clostridial bacteriocins, circularin A and closticin 574, Appl. Environ. Microbiol. 69, 1589-1597.
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 1589-1597
    • Kemperman, R.1    Kuipers, A.2    Karsens, H.3    Nauta, A.4    Kuipers, O.5    Kok, J.6
  • 10
    • 0024605648 scopus 로고
    • Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48, Antimicrob
    • Gálvez, A., Giménez-Gallego, G., Maqueda, M., and Valdivia, E. (1989) Purification and amino acid composition of peptide antibiotic AS-48 produced by Streptococcus (Enterococcus) faecalis subsp. liquefaciens S-48, Antimicrob. Agents Chemother. 33, 437-441.
    • (1989) Agents Chemother. , vol.33 , pp. 437-441
    • Gálvez, A.1    Giménez-Gallego, G.2    Maqueda, M.3    Valdivia, E.4
  • 12
    • 0003107982 scopus 로고
    • Pore formation in bacterial membranes by cationic lantibiotics
    • (Jung, G., and Sahl, H.-G., Eds.), Escom, Leiden
    • Sahl, H.-G. (1991) Pore formation in bacterial membranes by cationic lantibiotics, in Nisin and novel lantibiotics (Jung, G., and Sahl, H.-G., Eds.) pp 347-358, Escom, Leiden.
    • (1991) Nisin and Novel Lantibiotics , pp. 347-358
    • Sahl, H.-G.1
  • 13
    • 0033213354 scopus 로고    scopus 로고
    • Lantibiotics: Biosynthesis, mode of action and applications
    • Van Kraaij, C., de Vos, W. M., Siezen, R. J., and Kuipers, O. P. (1999) Lantibiotics: biosynthesis, mode of action and applications, Nat. Prod. Rep. 16, 575-587.
    • (1999) Nat. Prod. Rep. , vol.16 , pp. 575-587
    • Van Kraaij, C.1    De Vos, W.M.2    Siezen, R.J.3    Kuipers, O.P.4
  • 14
    • 2542445791 scopus 로고    scopus 로고
    • Genetics of lantibiotic biosynthesis
    • (Kelly, J. W., Ed.) Comprehensive Natural Products Chemistry (Barton, D., Nakanishi, K., and Meth-Cohn, O., Eds.), Elsevier, Amsterdam
    • Bierbaum, G. (1999) Genetics of lantibiotic biosynthesis, in Ammo acids, peptides, porphyrins, alkaloids (Kelly, J. W., Ed.) Vol. 4, pp 275-301, Comprehensive Natural Products Chemistry (Barton, D., Nakanishi, K., and Meth-Cohn, O., Eds.), Elsevier, Amsterdam.
    • (1999) Ammo Acids, Peptides, Porphyrins, Alkaloids , vol.4 , pp. 275-301
    • Bierbaum, G.1
  • 15
    • 3843091511 scopus 로고    scopus 로고
    • The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor
    • Kodani, S., Hudson, M. E., Durrant, M. C., Buttner, M. J., Nodwell, J. R., and Willey, J. M. (2004) The SapB morphogen is a lantibiotic-like peptide derived from the product of the developmental gene ramS in Streptomyces coelicolor, Proc. Natl. Acad. Sci. U.S.A., 101, 11448-11453.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11448-11453
    • Kodani, S.1    Hudson, M.E.2    Durrant, M.C.3    Buttner, M.J.4    Nodwell, J.R.5    Willey, J.M.6
  • 16
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins
    • Okeley, N. M., Moushumi, P., Stasser, J. P., Blackburn, N., and van der Donk, W. A. (2003) SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins, Biochemistry 42, 13613-13624.
    • (2003) Biochemistry , vol.42 , pp. 13613-13624
    • Okeley, N.M.1    Moushumi, P.2    Stasser, J.P.3    Blackburn, N.4    Van Der Donk, W.A.5
  • 17
    • 0001860958 scopus 로고
    • Induction of autolysis of Staphylococcus simulans 22 by Pep5 and nisin and influence of the cationic peptides on the activity of the autolytic enzymes
    • (Jung, G., and Sahl, H.-G., Eds.), Escom, Leiden
    • Bierbaum, G., and Sahl, H.-G. (1991) Induction of autolysis of Staphylococcus simulans 22 by Pep5 and nisin and influence of the cationic peptides on the activity of the autolytic enzymes, in Nisin and novel lantibiotics (Jung, G., and Sahl, H.-G., Eds.) pp 386-396, Escom, Leiden.
    • (1991) Nisin and Novel Lantibiotics , pp. 386-396
    • Bierbaum, G.1    Sahl, H.-G.2
  • 18
    • 0015215446 scopus 로고
    • The structure of nisin
    • Gross, E., and Morrell, J. L. (1971) The structure of nisin, J. Am. Chem. Soc. 93, 4634-4635.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 4634-4635
    • Gross, E.1    Morrell, J.L.2
  • 23
    • 0025817859 scopus 로고
    • Lantibiotics-ribosomally synthesized biologically active polypeptides sulfide bridges and α,β didehydroamine acids
    • Jung, G. (1991) Lantibiotics-ribosomally synthesized biologically active polypeptides sulfide bridges and α,β didehydroamine acids, Angew. Chem., Int. Ed. Engl. 30, 1051-1192.
    • (1991) Angew. Chem., Int. Ed. Engl. , vol.30 , pp. 1051-1192
    • Jung, G.1
  • 24
    • 0036692989 scopus 로고    scopus 로고
    • Lantibiotics produced by lactic acid bacteria: Structure, function and applications
    • Twomey, D., Ross, R. P., Ryan, M., Meany, B., and Hill, C. (2002) Lantibiotics produced by lactic acid bacteria: structure, function and applications, Antonie van Leeuwenhoek 82, 165-185.
    • (2002) Antonie Van Leeuwenhoek , vol.82 , pp. 165-185
    • Twomey, D.1    Ross, R.P.2    Ryan, M.3    Meany, B.4    Hill, C.5
  • 25
    • 0029034856 scopus 로고
    • Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermis K7-cloning of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7
    • Van de Kamp, M., van den Hooven, H. W., Konings, R. N. H., Hilbers, C. W., van de Ven, F. J. M., Bierbaum, G., Sahl, H.-G., Kuipers, O. P., Siezen, R. J., and de Vos, W. M. (1995a) Elucidation of the primary structure of the lantibiotic epilancin K7 from Staphylococcus epidermis K7-cloning of the epilancin-K7-encoding gene and NMR analysis of mature epilancin K7, Eur. J. Biochem. 230, 587-600.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 587-600
    • Van De Kamp, M.1    Van Den Hooven, H.W.2    Konings, R.N.H.3    Hilbers, C.W.4    Van De Ven, F.J.M.5    Bierbaum, G.6    Sahl, H.-G.7    Kuipers, O.P.8    Siezen, R.J.9    De Vos, W.M.10
  • 28
    • 2542432896 scopus 로고    scopus 로고
    • NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides
    • Kuipers, A., De Boef, E., Rink, R., Fekken, S., Kluskens, L. D., Driessen, A. J. M., Leenhouts, K., Kuipers, O. P., and Moll, G. N. (2004) NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides, J. Biol. Chem. 279, 22176-22182.
    • (2004) J. Biol. Chem. , vol.279 , pp. 22176-22182
    • Kuipers, A.1    De Boef, E.2    Rink, R.3    Fekken, S.4    Kluskens, L.D.5    Driessen, A.J.M.6    Leenhouts, K.7    Kuipers, O.P.8    Moll, G.N.9
  • 29
    • 0023992075 scopus 로고
    • Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis
    • Simon, D., and Chopin, A. (1988) Construction of a vector plasmid family and its use for molecular cloning in Streptococcus lactis, Biochimie 70, 559-566.
    • (1988) Biochimie , vol.70 , pp. 559-566
    • Simon, D.1    Chopin, A.2
  • 30
    • 0029177438 scopus 로고
    • Transformation of Lactococcus by electroporation
    • Holo, H., and Nes, I. F. (1995) Transformation of Lactococcus by electroporation, Methods Mol. Biol. 47, 195-199.
    • (1995) Methods Mol. Biol. , vol.47 , pp. 195-199
    • Holo, H.1    Nes, I.F.2
  • 31
    • 0016686551 scopus 로고
    • Improved medium for lactic streptococci and their bacteriophages
    • Terzaghi, B. E., and Sandine, W. E. (1975) Improved medium for lactic streptococci and their bacteriophages, Appl. Microbiol. 29, 807-313.
    • (1975) Appl. Microbiol. , vol.29 , pp. 807-1313
    • Terzaghi, B.E.1    Sandine, W.E.2
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H., and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa, Anal. Biochem. 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 33
    • 0029875689 scopus 로고    scopus 로고
    • Detection of modified amino acids in lantibiotic peptide mutacin II by chemical derivation and electrospray ionization-mass spectroscopic analysis
    • Novak, J., Kirk, M., Caufield, P. W., Barnes, S., Morrison, K., and Baker, J. (1996) Detection of modified amino acids in lantibiotic peptide mutacin II by chemical derivation and electrospray ionization-mass spectroscopic analysis, Anal. Biochem. 236, 358-360.
    • (1996) Anal. Biochem. , vol.236 , pp. 358-360
    • Novak, J.1    Kirk, M.2    Caufield, P.W.3    Barnes, S.4    Morrison, K.5    Baker, J.6
  • 34
    • 0022929886 scopus 로고
    • Epidermin: Sequencing a heterdet tetracyclic 21-peptide amide antibiotic
    • Allgaier, H., Jung, G., Werner, R. G., Schneider, U., and Zahner, H. (1986) Epidermin: sequencing a heterdet tetracyclic 21-peptide amide antibiotic, Eur. J. Biochem. 160, 9-22.
    • (1986) Eur. J. Biochem. , vol.160 , pp. 9-22
    • Allgaier, H.1    Jung, G.2    Werner, R.G.3    Schneider, U.4    Zahner, H.5
  • 36
    • 0030198730 scopus 로고    scopus 로고
    • Isolation of a new epidermin variant from two strains of Staphylococcus epidermidis-frequency of lantibiotic production in coagulase-negative staphylococci
    • Israil, A. M., Jack, R. W., Jung, G., and Sahl, H.-G. (1996) Isolation of a new epidermin variant from two strains of Staphylococcus epidermidis- frequency of lantibiotic production in coagulase-negative staphylococci, Zentralbl. Bakteriol. 284, 285-296.
    • (1996) Zentralbl. Bakteriol. , vol.284 , pp. 285-296
    • Israil, A.M.1    Jack, R.W.2    Jung, G.3    Sahl, H.-G.4
  • 37
    • 0033711399 scopus 로고    scopus 로고
    • Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics
    • Smith, L., Novák, J., Rocca, J., McClung, S., Hillman, J. D., and Edison, A. S. (2000) Covalent structure of mutacin 1140 and a novel method for the rapid identification of lantibiotics, Eur. J. Biochem. 267, 6810-1816.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6810-11816
    • Smith, L.1    Novák, J.2    Rocca, J.3    McClung, S.4    Hillman, J.D.5    Edison, A.S.6
  • 38
    • 0032850133 scopus 로고    scopus 로고
    • Purification of mutacin III from group III Streptococcus mutans UA787 and genetic analysis of mutacin III biosynthesis genes
    • Qi, F., Chen, P., and Caufield, P. W. (1999) Purification of mutacin III from group III Streptococcus mutans UA787 and genetic analysis of mutacin III biosynthesis genes, Appl. Environ. Microbiol. 65, 3880-3887.
    • (1999) Appl. Environ. Microbiol. , vol.65 , pp. 3880-3887
    • Qi, F.1    Chen, P.2    Caufield, P.W.3
  • 39
    • 0030744235 scopus 로고    scopus 로고
    • Purification and structure of mutacin B-Ny266: A new lantibiotic produced by Streptococcus mutans
    • Mota-Meira, M., Lacroix, C., Lapointe, G., and Lavoie, M. C. (1997) Purification and structure of mutacin B-Ny266: a new lantibiotic produced by Streptococcus mutans, FEBS Lett. 410, 275-279.
    • (1997) FEBS Lett. , vol.410 , pp. 275-279
    • Mota-Meira, M.1    Lacroix, C.2    Lapointe, G.3    Lavoie, M.C.4
  • 40
    • 0033859933 scopus 로고    scopus 로고
    • Purification and biochemical characterization of mutacin I from the group I strain of Streptococcus mutans, CH43, and genetic analysis of mutacin I biosynthesis genes
    • Qi, F., Chen, P., and Caufield, P. W. (2000) Purification and biochemical characterization of mutacin I from the group I strain of Streptococcus mutans, CH43, and genetic analysis of mutacin I biosynthesis genes, Appl. Environ. Microbiol. 66, 3221-3229.
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 3221-3229
    • Qi, F.1    Chen, P.2    Caufield, P.W.3
  • 41
    • 0036185650 scopus 로고    scopus 로고
    • Two different lantibiotic-like peptides originate from the ericin gene cluster of Bacillus subtilis A1/3
    • Stein, T., Borchert, S., Conrad, B., Feesche, J., Hofemeister, B., Hofemeister, J., and Entian, K.-D. (2002) Two different lantibiotic-like peptides originate from the ericin gene cluster of Bacillus subtilis A1/3, J. Bacteriol. 184, 1703-1711.
    • (2002) J. Bacteriol. , vol.184 , pp. 1703-1711
    • Stein, T.1    Borchert, S.2    Conrad, B.3    Feesche, J.4    Hofemeister, B.5    Hofemeister, J.6    Entian, K.-D.7
  • 43
    • 0026062942 scopus 로고
    • Identification and characterization of the lantibiotic nisin Z, a natural nisin variant
    • Mulders, J. W. M., Boerrigter, I. J., Rollema, H. S., Siezen, R. J., and de Vos, W. M. (1991) Identification and characterization of the lantibiotic nisin Z, a natural nisin variant, Eur. J. Biochem. 301, 581-584.
    • (1991) Eur. J. Biochem. , vol.301 , pp. 581-584
    • Mulders, J.W.M.1    Boerrigter, I.J.2    Rollema, H.S.3    Siezen, R.J.4    De Vos, W.M.5
  • 44
    • 2442436623 scopus 로고    scopus 로고
    • Identification of the lantibiotic NisinQ, a new natural nisin variant produced by Lactococcus lactis 61-64 isolated from a river in Japan
    • Zendo, T., Masanori, F., Ueda, K., Higuchi, T., Nakayama, J., and Sonomoto, K. (2003) Identification of the lantibiotic NisinQ, a new natural nisin variant produced by Lactococcus lactis 61-64 isolated from a river in Japan, Biosci., Biotechnol. Biochem. 67, 1616-1619.
    • (2003) Biosci., Biotechnol. Biochem. , vol.67 , pp. 1616-1619
    • Zendo, T.1    Masanori, F.2    Ueda, K.3    Higuchi, T.4    Nakayama, J.5    Sonomoto, K.6
  • 45
    • 0027248383 scopus 로고
    • Solution structures of the lantibiotics duramycin B and C
    • Zimmermann, N., Freund, S., Fredenhagen, A., and Jung, G. (1993) Solution structures of the lantibiotics duramycin B and C, Eur. J. Biochem. 216, 419-428.
    • (1993) Eur. J. Biochem. , vol.216 , pp. 419-428
    • Zimmermann, N.1    Freund, S.2    Fredenhagen, A.3    Jung, G.4
  • 46
    • 0028929222 scopus 로고
    • Cloning sequencing and production of the lantibiotic mersacidin
    • Bierbaum, G., Brötz, H., Koller, K.-P., and Sahl, H.-G. (1995) Cloning sequencing and production of the lantibiotic mersacidin, FEMS Microbiol. Lett. 127, 121-126.
    • (1995) FEMS Microbiol. Lett. , vol.127 , pp. 121-126
    • Bierbaum, G.1    Brötz, H.2    Koller, K.-P.3    Sahl, H.-G.4
  • 49
    • 0027279657 scopus 로고
    • Isolation and characterization of the lantibiotic salivaricin a and its structural gene sa1A from Streptococcus salivarius 20P3
    • Ross, K. F., Ronson, C. W., and Tagg, J. R. (1993) Isolation and characterization of the lantibiotic salivaricin A and its structural gene sa1A from Streptococcus salivarius 20P3, Appl. Environ. Microbiol. 59, 2014-2021.
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 2014-2021
    • Ross, K.F.1    Ronson, C.W.2    Tagg, J.R.3
  • 50
    • 0029974631 scopus 로고    scopus 로고
    • Variacin, a new lanthionine-containing bacteriocin produced by Micrococcus varians: Comparison to lacticin 481 of Lactococcus lactis
    • Pridmore, D., Rekhif, N., Pittet, A. C., Suri, B., and Mollet, B. (1996) Variacin, a new lanthionine-containing bacteriocin produced by Micrococcus varians: Comparison to lacticin 481 of Lactococcus lactis, Appl. Environ. Microbiol. 62, 1799-1802.
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1799-1802
    • Pridmore, D.1    Rekhif, N.2    Pittet, A.C.3    Suri, B.4    Mollet, B.5
  • 53
    • 0028211139 scopus 로고
    • Elucidation of the structure of SA-FF22 lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22
    • Jack, R. W., Carne, A., Metzger, J., Stefanovic, S., Sahl, H.-G., Jung, G., and Tagg, J. (1994) Elucidation of the structure of SA-FF22 lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22, Eur. J. Biochem. 220, 455-462.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 455-462
    • Jack, R.W.1    Carne, A.2    Metzger, J.3    Stefanovic, S.4    Sahl, H.-G.5    Jung, G.6    Tagg, J.7
  • 54
    • 1542743956 scopus 로고    scopus 로고
    • Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity
    • Martin, N. I., Sprules, T., Carpenter, M. R., Cotter, P. D., Hill, C., Ross, R. P., and Vederas, J. C. (2004) Structural characterization of lacticin 3147, a two-peptide lantibiotic with synergistic activity, Biochemistry 43, 3049-3056.
    • (2004) Biochemistry , vol.43 , pp. 3049-3056
    • Martin, N.I.1    Sprules, T.2    Carpenter, M.R.3    Cotter, P.D.4    Hill, C.5    Ross, R.P.6    Vederas, J.C.7
  • 55
    • 0035081130 scopus 로고    scopus 로고
    • Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics
    • Holo, H., Jeknic, Z., Daeschel, M., Stevanovic, S., and Nes, I. F. (2001) Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics, Microbiology 147, 643-651.
    • (2001) Microbiology , vol.147 , pp. 643-651
    • Holo, H.1    Jeknic, Z.2    Daeschel, M.3    Stevanovic, S.4    Nes, I.F.5
  • 58
    • 0032483367 scopus 로고    scopus 로고
    • Identification and characterization of the structural and transporter genes for and the chemical and biological properties of sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168
    • Paik, S. H., Chakicheria, A., and Hansen, J. N. (1998) Identification and characterization of the structural and transporter genes for and the chemical and biological properties of sublancin 168, a novel lantibiotic produced by Bacillus subtilis 168, J. Biol. Chem. 273, 23134-23142.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23134-23142
    • Paik, S.H.1    Chakicheria, A.2    Hansen, J.N.3
  • 60
    • 0031665461 scopus 로고    scopus 로고
    • Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analyis of its biosynthetic gene cluster
    • Heidrich, C., Pag, U., Josten, M., Metzger, J., Jack, R. W., Bierbaum, G., Jung, G., and Sahl, H.-G. (1998) Isolation, characterization, and heterologous expression of the novel lantibiotic epicidin 280 and analyis of its biosynthetic gene cluster, Appl. Environ. Microbiol. 64, 3140-3146.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 3140-3146
    • Heidrich, C.1    Pag, U.2    Josten, M.3    Metzger, J.4    Jack, R.W.5    Bierbaum, G.6    Jung, G.7    Sahl, H.-G.8
  • 63
    • 0033560968 scopus 로고    scopus 로고
    • Posttranslational modification of nisin. The involvement of NisB in the dehydration process
    • Karakas, S. A., Narbad, A., Horn, N., Dodd, H. M., Parr, A. J., Colquhoun, I., and Gasson, M. J. (1999) Posttranslational modification of nisin. The involvement of NisB in the dehydration process, Eur. J. Biochem. 261, 524-532.
    • (1999) Eur. J. Biochem. , vol.261 , pp. 524-532
    • Karakas, S.A.1    Narbad, A.2    Horn, N.3    Dodd, H.M.4    Parr, A.J.5    Colquhoun, I.6    Gasson, M.J.7
  • 64
    • 0037129424 scopus 로고    scopus 로고
    • Biomimetic stereoselective formation of methyllanthionine
    • Zhou, H., and van der Donk, W. A. (2002) Biomimetic stereoselective formation of methyllanthionine, Org. Lett. 4, 1335-1338.
    • (2002) Org. Lett. , vol.4 , pp. 1335-1338
    • Zhou, H.1    Van Der Donk, W.A.2
  • 65
    • 0034676587 scopus 로고    scopus 로고
    • Facile chemoselective synthesis of dehydroalanine-containing peptides
    • Okeley, N. M., Zhu, Y., and van der Donk, W. A. (2000) Facile chemoselective synthesis of dehydroalanine-containing peptides, Org. Lett. 2, 3603-3606.
    • (2000) Org. Lett. , vol.2 , pp. 3603-3606
    • Okeley, N.M.1    Zhu, Y.2    Van Der Donk, W.A.3
  • 67
    • 0142094530 scopus 로고    scopus 로고
    • Biomimetic studies on the mechanism of stereoselective lathionine formation
    • Zhu, Y., Matt, D., Zhou, H., Averin, O., and van der Donk, W. A. (2003) Biomimetic studies on the mechanism of stereoselective lathionine formation, Org. Biomol. Chem. 1, 3304-3315.
    • (2003) Org. Biomol. Chem. , vol.1 , pp. 3304-3315
    • Zhu, Y.1    Matt, D.2    Zhou, H.3    Averin, O.4    Van Der Donk, W.A.5
  • 71
    • 0030804834 scopus 로고    scopus 로고
    • Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity
    • Van Kraaij, C., Breukink, E., Rollema, H. S., Siezen, R. J., Demel, R. A., De Kruijff, B., and Kuipers, O. P. (1997) Influence of charge differences in the C-terminal part of nisin on antimicrobial activity and signaling capacity, Eur. J. Biochem. 247, 114-120.
    • (1997) Eur. J. Biochem. , vol.247 , pp. 114-120
    • Van Kraaij, C.1    Breukink, E.2    Rollema, H.S.3    Siezen, R.J.4    Demel, R.A.5    De Kruijff, B.6    Kuipers, O.P.7
  • 72
    • 0030923340 scopus 로고    scopus 로고
    • The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane
    • Breukink, E., van Kraaij, C., Demel, R. A., Siezen, R. J., Kuipers, O. P., and de Kruijff, B. (1997) The C-terminal region of nisin is responsible for the initial interaction of nisin with the target membrane, Biochemistry 36, 6968-6976.
    • (1997) Biochemistry , vol.36 , pp. 6968-6976
    • Breukink, E.1    Van Kraaij, C.2    Demel, R.A.3    Siezen, R.J.4    Kuipers, O.P.5    De Kruijff, B.6
  • 73
    • 0024654855 scopus 로고
    • Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic
    • Schnell, N., Entian, K.-D., Götz, F., Hörner, T., Kellner, R., and Jung, G. (1989) Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic, FEMS Microbiol. Lett. 58, 263-268.
    • (1989) FEMS Microbiol. Lett. , vol.58 , pp. 263-268
    • Schnell, N.1    Entian, K.-D.2    Götz, F.3    Hörner, T.4    Kellner, R.5    Jung, G.6
  • 74
    • 0031842742 scopus 로고    scopus 로고
    • Structure-activity study of the lantibiotic mutacinII from Streptococcus mutans T8 by a gene replacement strategy
    • Chen, P., Novak, J., Kirk, M., Barnes, S., Qi, F., and Caufield, P. W. (1998) Structure-activity study of the lantibiotic mutacinII from Streptococcus mutans T8 by a gene replacement strategy, Appl. Environ. Microbiol. 64, 2335-2340.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 2335-2340
    • Chen, P.1    Novak, J.2    Kirk, M.3    Barnes, S.4    Qi, F.5    Caufield, P.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.