메뉴 건너뛰기




Volumn 81, Issue 10, 2015, Pages 3419-3429

Pseudomycoicidin, a class II Lantibiotic from Bacillus pseudomycoides

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BACTERIA; BACTERIOLOGY; BIOSYNTHESIS; COVALENT BONDS; DEHYDRATION; ENZYMES; ESCHERICHIA COLI; GENE EXPRESSION; GENES; PEPTIDES;

EID: 84930025291     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00299-15     Document Type: Article
Times cited : (37)

References (65)
  • 1
    • 0023912839 scopus 로고
    • Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings
    • Schnell N, Entian KD, Schneider U, Götz F, Zähner H, Kellner R, Jung G. 1988. Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings Nature 333:276-278. http://dx.doi .org/10.1038/333276a0.
    • (1988) Nature , vol.333 , pp. 276-278
    • Schnell, N.1    Entian, K.D.2    Schneider, U.3    Götz, F.4    Zähner, H.5    Kellner, R.6    Jung, G.7
  • 3
    • 0014682230 scopus 로고
    • Synthesis of the antibiotic nisin: formation of lanthionine and beta-methyl-lanthionine
    • Ingram LC. 1969. Synthesis of the antibiotic nisin: formation of lanthionine and beta-methyl-lanthionine Biochim Biophys Acta 184:216-219. http://dx.doi.org/10.1016/0304-4165(69)90121-4.
    • (1969) Biochim Biophys Acta , vol.184 , pp. 216-219
    • Ingram, L.C.1
  • 4
    • 0014942879 scopus 로고
    • A ribosomal mechanism for synthesis of peptides related to nisin
    • Ingram L. 1970. A ribosomal mechanism for synthesis of peptides related to nisin Biochim Biophys Acta 224:263-265. http://dx.doi.org/10.1016/0005-2787(70)90642-8.
    • (1970) Biochim Biophys Acta , vol.224 , pp. 263-265
    • Ingram, L.1
  • 6
    • 0029115380 scopus 로고
    • Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC Evidence for a role of PepC in thioether formation.
    • Meyer C, Bierbaum G, Heidrich C, Reis M, Süling J, Iglesias-Wind MI, Kempter C, Molitor E, Sahl HG. 1995. Nucleotide sequence of the lantibiotic Pep5 biosynthetic gene cluster and functional analysis of PepP and PepC Evidence for a role of PepC in thioether formation. Eur J Biochem 232:478-489.
    • (1995) Eur J Biochem , vol.232 , pp. 478-489
    • Meyer, C.1    Bierbaum, G.2    Heidrich, C.3    Reis, M.4    Süling, J.5    Iglesias-Wind, M.I.6    Kempter, C.7    Molitor, E.8    Sahl, H.G.9
  • 7
    • 0942268866 scopus 로고    scopus 로고
    • Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity
    • Xie L, Miller LM, Chatterjee C, Averin O, Kelleher NL, van der Donk WA. 2004. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity Science 303:679-681. http://dx.doi.org/10.1126/science.1092600.
    • (2004) Science , vol.303 , pp. 679-681
    • Xie, L.1    Miller, L.M.2    Chatterjee, C.3    Averin, O.4    Kelleher, N.L.5    van der Donk, W.A.6
  • 9
    • 35848941716 scopus 로고    scopus 로고
    • Lantibiotics: peptides of diverse structure and function
    • Willey JM, van der Donk WA. 2007. Lantibiotics: peptides of diverse structure and function Annu Rev Microbiol 61:477-501. http://dx.doi .org/10.1146/annurev.micro.61.080706.093501.
    • (2007) Annu Rev Microbiol , vol.61 , pp. 477-501
    • Willey, J.M.1    van der Donk, W.A.2
  • 10
    • 27244436751 scopus 로고    scopus 로고
    • Bacteriocins: developing innate immunity for food
    • Cotter PD, Hill C, Ross RP. 2005. Bacteriocins: developing innate immunity for food Nat Rev Microbiol 3:777-788. http://dx.doi.org/10.1038/nrmicro1273.
    • (2005) Nat Rev Microbiol , vol.3 , pp. 777-788
    • Cotter, P.D.1    Hill, C.2    Ross, R.P.3
  • 11
    • 38949166717 scopus 로고    scopus 로고
    • Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin
    • Lubelski J, Rink R, Khusainov R, Moll GN, Kuipers OP. 2008. Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin Cell Mol Life Sci 65:455-476. http://dx.doi.org/10.1007/s00018-007-7171-2.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 455-476
    • Lubelski, J.1    Rink, R.2    Khusainov, R.3    Moll, G.N.4    Kuipers, O.P.5
  • 12
    • 0033579207 scopus 로고    scopus 로고
    • Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic
    • Breukink E, Wiedemann I, van Kraaij C, Kuipers OP, Sahl H, de Kruijff B. 1999. Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic Science 286:2361-2364. http://dx.doi.org/10.1126/science.286.5448.2361.
    • (1999) Science , vol.286 , pp. 2361-2364
    • Breukink, E.1    Wiedemann, I.2    van Kraaij, C.3    Kuipers, O.P.4    Sahl, H.5    de Kruijff, B.6
  • 13
    • 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 ME, Durrant MC, Buttner MJ, Nodwell JR, Willey JM. 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. http://dx.doi.org/10.1073/pnas.0404220101.
    • (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
  • 14
    • 77953528770 scopus 로고    scopus 로고
    • In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a posttranslational modification
    • Müller WM, Schmiederer T, Ensle P, Süssmuth RD. 2010. In vitro biosynthesis of the prepeptide of type-III lantibiotic labyrinthopeptin A2 including formation of a C-C bond as a posttranslational modification Angew Chem Int Ed Engl 49:2436-2440. http://dx.doi.org/10.1002/anie .200905909.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 2436-2440
    • Müller, W.M.1    Schmiederer, T.2    Ensle, P.3    Süssmuth, R.D.4
  • 16
    • 69449097013 scopus 로고    scopus 로고
    • Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13
    • Dischinger J, Josten M, Szekat C, Sahl HG, Bierbaum G. 2009. Production of the novel two-peptide lantibiotic lichenicidin by Bacillus licheniformis DSM 13 PLoS One 4:e6788. http://dx.doi.org/10.1371/journal .pone.0006788.
    • (2009) PLoS One , vol.4 , pp. e6788
    • Dischinger, J.1    Josten, M.2    Szekat, C.3    Sahl, H.G.4    Bierbaum, G.5
  • 17
    • 69449094338 scopus 로고    scopus 로고
    • Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins
    • Begley M, Cotter PD, Hill C, Ross RP. 2009. Identification of a novel two-peptide lantibiotic, lichenicidin, following rational genome mining for LanM proteins Appl Environ Microbiol 75:5451-5460. http://dx.doi .org/10.1128/AEM.00730-09.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5451-5460
    • Begley, M.1    Cotter, P.D.2    Hill, C.3    Ross, R.P.4
  • 19
    • 77950563372 scopus 로고    scopus 로고
    • Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights
    • Goto Y, Li B, Claesen J, Shi Y, Bibb MJ, van der Donk WA. 2010. Discovery of unique lanthionine synthetases reveals new mechanistic and evolutionary insights PLoS Biol 8:e1000339. http://dx.doi.org/10.1371/journal.pbio.1000339.
    • (2010) PLoS Biol , vol.8 , pp. e1000339
    • Goto, Y.1    Li, B.2    Claesen, J.3    Shi, Y.4    Bibb, M.J.5    van der Donk, W.A.6
  • 21
    • 84879828226 scopus 로고    scopus 로고
    • Designing and producing modified, new-to-nature peptides with antimicrobial activity by use of a combination of various lantibiotic modification enzymes
    • van Heel AJ, Mu D, Montalban-Lopez M, Hendriks D, Kuipers OP. 2013. Designing and producing modified, new-to-nature peptides with antimicrobial activity by use of a combination of various lantibiotic modification enzymes ACS Synth Biol 2:397-404. http://dx.doi.org/10.1021/sb3001084.
    • (2013) ACS Synth Biol , vol.2 , pp. 397-404
    • van Heel, A.J.1    Mu, D.2    Montalban-Lopez, M.3    Hendriks, D.4    Kuipers, O.P.5
  • 22
    • 0035135297 scopus 로고    scopus 로고
    • Heterologous expression of lacticin 3147 in Enterococcus faecalis: comparison of biological activity with cytolysin
    • Ryan MP, McAuliffe O, Ross RP, Hill C. 2001. Heterologous expression of lacticin 3147 in Enterococcus faecalis: comparison of biological activity with cytolysin Lett Appl Microbiol 32:71-77. http://dx.doi.org/10.1046/j .1472-765x.2001.00864.x.
    • (2001) Lett Appl Microbiol , vol.32 , pp. 71-77
    • Ryan, M.P.1    McAuliffe, O.2    Ross, R.P.3    Hill, C.4
  • 23
    • 79251579302 scopus 로고    scopus 로고
    • Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli
    • Caetano T, Krawczyk JM, Mosker E, Süssmuth RD, Mendo S. 2011. Heterologous expression, biosynthesis, and mutagenesis of type II lantibiotics from Bacillus licheniformis in Escherichia coli Chem Biol 18:90-100. http://dx.doi.org/10.1016/j.chembiol.2010.11.010.
    • (2011) Chem Biol , vol.18 , pp. 90-100
    • Caetano, T.1    Krawczyk, J.M.2    Mosker, E.3    Süssmuth, R.D.4    Mendo, S.5
  • 24
    • 84867540731 scopus 로고    scopus 로고
    • Heterologous production of the lantibiotic Ala(0)actagardine in Escherichia coli
    • Shi Y, Bueno A, van der Donk WA. 2012. Heterologous production of the lantibiotic Ala(0)actagardine in Escherichia coli Chem Commun (Cambridge) 48:10966-10968. http://dx.doi.org/10.1039/c2cc36336d.
    • (2012) Chem Commun (Cambridge) , vol.48 , pp. 10966-10968
    • Shi, Y.1    Bueno, A.2    van der Donk, W.A.3
  • 25
    • 79952464869 scopus 로고    scopus 로고
    • Engineering unusual amino acids into peptides using lantibiotic synthetase
    • Nagao J, Shioya K, Harada Y, Okuda K, Zendo T, Nakayama J, Sonomoto K. 2011. Engineering unusual amino acids into peptides using lantibiotic synthetase Methods Mol Biol 705:225-236. http://dx.doi.org /10.1007/978-1-61737-967-3_13.
    • (2011) Methods Mol Biol , vol.705 , pp. 225-236
    • Nagao, J.1    Shioya, K.2    Harada, Y.3    Okuda, K.4    Zendo, T.5    Nakayama, J.6    Sonomoto, K.7
  • 26
    • 80052092565 scopus 로고    scopus 로고
    • Nine posttranslational modifications during the biosynthesis of cinnamycin
    • Okesli A, Cooper LE, Fogle EJ, van der Donk WA. 2011. Nine posttranslational modifications during the biosynthesis of cinnamycin J Am Chem Soc 133:13753-13760. http://dx.doi.org/10.1021/ja205783f.
    • (2011) J Am Chem Soc , vol.133 , pp. 13753-13760
    • Okesli, A.1    Cooper, L.E.2    Fogle, E.J.3    van der Donk, W.A.4
  • 27
    • 0034120975 scopus 로고    scopus 로고
    • Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster
    • Altena K, Guder A, Cramer C, Bierbaum G. 2000. Biosynthesis of the lantibiotic mersacidin: organization of a type B lantibiotic gene cluster Appl Environ Microbiol 66:2565-2571. http://dx.doi.org/10.1128/AEM .66.6.2565-2571.2000.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 2565-2571
    • Altena, K.1    Guder, A.2    Cramer, C.3    Bierbaum, G.4
  • 29
    • 84899122716 scopus 로고    scopus 로고
    • Sonorensin: an antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93
    • Chopra L, Singh G, Choudhary V, Sahoo DK. 2014. Sonorensin: an antimicrobial peptide, belonging to the heterocycloanthracin subfamily of bacteriocins, from a new marine isolate, Bacillus sonorensis MT93 Appl Environ Microbiol 80:2981-2990. http://dx.doi.org/10.1128/AEM .04259-13.
    • (2014) Appl Environ Microbiol , vol.80 , pp. 2981-2990
    • Chopra, L.1    Singh, G.2    Choudhary, V.3    Sahoo, D.K.4
  • 30
    • 65149101910 scopus 로고    scopus 로고
    • A strain-variable bacteriocin in Bacillus anthracis and Bacillus cereus with repeated Cys-Xaa-Xaa motifs
    • Haft DH. 2009. A strain-variable bacteriocin in Bacillus anthracis and Bacillus cereus with repeated Cys-Xaa-Xaa motifs Biol Direct 4:15. http://dx.doi.org/10.1186/1745-6150-4-15.
    • (2009) Biol Direct , vol.4 , pp. 15
    • Haft, D.H.1
  • 31
    • 0031857298 scopus 로고    scopus 로고
    • Bacillus pseudomycoides sp nov.
    • Nakamura LK. 1998. Bacillus pseudomycoides sp nov. Int J Syst Bacteriol 48:1031-1035. http://dx.doi.org/10.1099/00207713-48-3-1031.
    • (1998) Int J Syst Bacteriol , vol.48 , pp. 1031-1035
    • Nakamura, L.K.1
  • 32
    • 84873799110 scopus 로고
    • Studies on lysogenesis I. The mode of phage liberation by lysogenic Escherichia coli.
    • Bertani G. 1951. Studies on lysogenesis I. The mode of phage liberation by lysogenic Escherichia coli. J Bacteriol 62:293-300.
    • (1951) J Bacteriol , vol.62 , pp. 293-300
    • Bertani, G.1
  • 33
    • 67349119801 scopus 로고    scopus 로고
    • Native graS mutation supports the susceptibility of Staphylococcus aureus strain SG511 to antimicrobial peptides
    • Sass P, Bierbaum G. 2009. Native graS mutation supports the susceptibility of Staphylococcus aureus strain SG511 to antimicrobial peptides Int J Med Microbiol 299:313-322. http://dx.doi.org/10.1016/j.ijmm.2008.10.005.
    • (2009) Int J Med Microbiol , vol.299 , pp. 313-322
    • Sass, P.1    Bierbaum, G.2
  • 34
    • 0020265937 scopus 로고    scopus 로고
    • Description of a new species of the genus Staphylococcus: Staphylococcus carnosus
    • Schleifer KH, Fischer U. 2002. Description of a new species of the genus Staphylococcus: Staphylococcus carnosus Int J Syst Bacteriol 32:153-156. http://dx.doi.org/10.1099/00207713-32-2-153.
    • (2002) Int J Syst Bacteriol , vol.32 , pp. 153-156
    • Schleifer, K.H.1    Fischer, U.2
  • 35
    • 0023547233 scopus 로고
    • Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-Lalanine amidase
    • Bierbaum G, Sahl HG. 1987. Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-Lalanine amidase J Bacteriol 169:5452-5458.
    • (1987) J Bacteriol , vol.169 , pp. 5452-5458
    • Bierbaum, G.1    Sahl, H.G.2
  • 36
    • 33846142874 scopus 로고    scopus 로고
    • Lytic activity of recombinant bacteriophage phi11 and phi12 endolysins on whole cells and biofilms of Staphylococcus aureus
    • Sass P, Bierbaum G. 2007. Lytic activity of recombinant bacteriophage phi11 and phi12 endolysins on whole cells and biofilms of Staphylococcus aureus Appl Environ Microbiol 73:347-352. http://dx.doi.org/10.1128/AEM.01616-06.
    • (2007) Appl Environ Microbiol , vol.73 , pp. 347-352
    • Sass, P.1    Bierbaum, G.2
  • 37
    • 84868094646 scopus 로고    scopus 로고
    • Biosynthesis of the class III lantipeptide catenulipeptin
    • Wang H, van der Donk WA. 2012. Biosynthesis of the class III lantipeptide catenulipeptin ACS Chem Biol 7:1529-1535. http://dx.doi.org/10.1021/cb3002446.
    • (2012) ACS Chem Biol , vol.7 , pp. 1529-1535
    • Wang, H.1    van der Donk, W.A.2
  • 38
    • 0028929222 scopus 로고
    • Cloning, sequencing and production of the lantibiotic mersacidin
    • Bierbaum G, Brötz H, Koller KP, Sahl HG. 1995. Cloning, sequencing and production of the lantibiotic mersacidin FEMS Microbiol Lett 127:121-126. http://dx.doi.org/10.1111/j.1574-6968.1995.tb07460.x.
    • (1995) FEMS Microbiol Lett , vol.127 , pp. 121-126
    • Bierbaum, G.1    Brötz, H.2    Koller, K.P.3    Sahl, H.G.4
  • 39
    • 34249747857 scopus 로고    scopus 로고
    • Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity
    • Paul M, Patton GC, van der Donk WA. 2007. Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity Biochemistry 46:6268-6276. http://dx.doi.org/10.1021/bi7000104.
    • (2007) Biochemistry , vol.46 , pp. 6268-6276
    • Paul, M.1    Patton, G.C.2    van der Donk, W.A.3
  • 41
    • 84892517022 scopus 로고    scopus 로고
    • Lantibiotics: promising candidates for future applications in health care
    • Dischinger J, Basi Chipalu S, Bierbaum G. 2014. Lantibiotics: promising candidates for future applications in health care Int J Med Microbiol 304:51-62. http://dx.doi.org/10.1016/j.ijmm.2013.09.003.
    • (2014) Int J Med Microbiol , vol.304 , pp. 51-62
    • Dischinger, J.1    Basi Chipalu, S.2    Bierbaum, G.3
  • 43
    • 34447250021 scopus 로고    scopus 로고
    • Antimicrobial activity of lacticin 3147 against clinical Clostridium difficile strains
    • Rea MC, Clayton E, O'Connor PM, Shanahan F, Kiely B, Ross RP, Hill C. 2007. Antimicrobial activity of lacticin 3147 against clinical Clostridium difficile strains J Med Microbiol 56:940-946. http://dx.doi.org/10.1099/jmm.0.47085-0.
    • (2007) J Med Microbiol , vol.56 , pp. 940-946
    • Rea, M.C.1    Clayton, E.2    O'Connor, P.M.3    Shanahan, F.4    Kiely, B.5    Ross, R.P.6    Hill, C.7
  • 44
    • 61649125590 scopus 로고    scopus 로고
    • Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens
    • Chen XH, Koumoutsi A, Scholz R, Schneider K, Vater J, Süssmuth R, Piel J, Borriss R. 2009. Genome analysis of Bacillus amyloliquefaciens FZB42 reveals its potential for biocontrol of plant pathogens J Biotechnol 140:27-37. http://dx.doi.org/10.1016/j.jbiotec.2008.10.011.
    • (2009) J Biotechnol , vol.140 , pp. 27-37
    • Chen, X.H.1    Koumoutsi, A.2    Scholz, R.3    Schneider, K.4    Vater, J.5    Süssmuth, R.6    Piel, J.7    Borriss, R.8
  • 45
  • 46
    • 18444415756 scopus 로고    scopus 로고
    • Bacillus subtilis antibiotics: structures, syntheses and specific functions
    • Stein T. 2005. Bacillus subtilis antibiotics: structures, syntheses and specific functions Mol Microbiol 56:845-857. http://dx.doi.org/10.1111/j .1365-2958.2005.04587.x.
    • (2005) Mol Microbiol , vol.56 , pp. 845-857
    • Stein, T.1
  • 47
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: the use of leader peptides to guide natural product biosynthesis
    • Oman TJ, van der Donk WA. 2010. Follow the leader: the use of leader peptides to guide natural product biosynthesis Nat Chem Biol 6:9-18. http://dx.doi.org/10.1038/nchembio.286.
    • (2010) Nat Chem Biol , vol.6 , pp. 9-18
    • Oman, T.J.1    van der Donk, W.A.2
  • 49
    • 0346034649 scopus 로고    scopus 로고
    • Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions
    • Schibli DJ, Epand RF, Vogel HJ, Epand RM. 2002. Tryptophan-rich antimicrobial peptides: comparative properties and membrane interactions Biochem Cell Biol 80:667-677. http://dx.doi.org/10.1139/o02-147.
    • (2002) Biochem Cell Biol , vol.80 , pp. 667-677
    • Schibli, D.J.1    Epand, R.F.2    Vogel, H.J.3    Epand, R.M.4
  • 50
    • 33748988741 scopus 로고    scopus 로고
    • Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action
    • Chan DI, Prenner EJ, Vogel HJ. 2006. Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action Biochim Biophys Acta 1758:1184-1202. http://dx.doi.org/10.1016/j.bbamem.2006.04.006.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1184-1202
    • Chan, D.I.1    Prenner, E.J.2    Vogel, H.J.3
  • 51
    • 0037199421 scopus 로고    scopus 로고
    • Mutational analysis of the role of tryptophan residues in an antimicrobial peptide
    • Fimland G, Eijsink VG, Nissen-Meyer J. 2002. Mutational analysis of the role of tryptophan residues in an antimicrobial peptide Biochemistry 41:9508-9515. http://dx.doi.org/10.1021/bi025856q.
    • (2002) Biochemistry , vol.41 , pp. 9508-9515
    • Fimland, G.1    Eijsink, V.G.2    Nissen-Meyer, J.3
  • 53
    • 0014564764 scopus 로고
    • Inactivation of nisin by alphachymotrypsin
    • Jarvis B, Mahoney RR. 1969. Inactivation of nisin by alphachymotrypsin J Dairy Sci 52:1448-1449. http://dx.doi.org/10.3168/jds .S0022-0302(69)86771-8.
    • (1969) J Dairy Sci , vol.52 , pp. 1448-1449
    • Jarvis, B.1    Mahoney, R.R.2
  • 54
    • 0022929886 scopus 로고
    • Epidermin:sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic
    • Allgaier H, Jung G, Werner RG, Schneider U, Zähner H. 1986. Epidermin:sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic Eur J Biochem 160:9-22. http://dx.doi.org/10.1111/j.1432-1033.1986.tb09933.x.
    • (1986) Eur J Biochem , vol.160 , pp. 9-22
    • Allgaier, H.1    Jung, G.2    Werner, R.G.3    Schneider, U.4    Zähner, H.5
  • 55
    • 53649090841 scopus 로고    scopus 로고
    • Structure- activity relationship studies of the two-component lantibiotic haloduracin
    • Cooper LE, McClerren AL, Chary A, van der Donk WA. 2008. Structure- activity relationship studies of the two-component lantibiotic haloduracin Chem Biol 15:1035-1045. http://dx.doi.org/10.1016/j.chembiol .2008.07.020.
    • (2008) Chem Biol , vol.15 , pp. 1035-1045
    • Cooper, L.E.1    McClerren, A.L.2    Chary, A.3    van der Donk, W.A.4
  • 56
    • 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, Nes IF. 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
  • 57
    • 84856182152 scopus 로고    scopus 로고
    • Isolation and characterization of enterocin W, a novel two-peptide lantibiotic produced by Enterococcus faecalis NKR-4-1
    • Sawa N, Wilaipun P, Kinoshita S, Zendo T, Leelawatcharamas V, Nakayama J, Sonomoto K. 2012. Isolation and characterization of enterocin W, a novel two-peptide lantibiotic produced by Enterococcus faecalis NKR-4-1 Appl Environ Microbiol 78:900-903. http://dx.doi.org/10.1128/AEM.06497-11.
    • (2012) Appl Environ Microbiol , vol.78 , pp. 900-903
    • Sawa, N.1    Wilaipun, P.2    Kinoshita, S.3    Zendo, T.4    Leelawatcharamas, V.5    Nakayama, J.6    Sonomoto, K.7
  • 58
    • 84904132570 scopus 로고    scopus 로고
    • Type AII lantibiotic bovicin HJ50 with a rare disulfide bond: structure, structureactivity relationships and mode of action
    • Zhang J, Feng Y, Teng K, Lin Y, Gao Y, Wang J, Zhong J. 2014. Type AII lantibiotic bovicin HJ50 with a rare disulfide bond: structure, structureactivity relationships and mode of action Biochem J 461:497-508. http://dx.doi.org/10.1042/BJ20131524.
    • (2014) Biochem J , vol.461 , pp. 497-508
    • Zhang, J.1    Feng, Y.2    Teng, K.3    Lin, Y.4    Gao, Y.5    Wang, J.6    Zhong, J.7
  • 59
    • 84901278389 scopus 로고    scopus 로고
    • Bovicin HJ50-like lantibiotics, a novel subgroup of lantibiotics featured by an indispensable disulfide bridge
    • Wang J, Ma H, Ge X, Zhang J, Teng K, Sun Z, Zhong J. 2014. Bovicin HJ50-like lantibiotics, a novel subgroup of lantibiotics featured by an indispensable disulfide bridge PLoS One 9:e97121. http://dx.doi.org/10.1371/journal.pone.0097121.
    • (2014) PLoS One , vol.9 , pp. e97121
    • Wang, J.1    Ma, H.2    Ge, X.3    Zhang, J.4    Teng, K.5    Sun, Z.6    Zhong, J.7
  • 60
    • 77950113113 scopus 로고    scopus 로고
    • Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence
    • Majchrzykiewicz JA, Lubelski J, Moll GN, Kuipers A, Bijlsma JJ, Kuipers OP, Rink R. 2010. Production of a class II two-component lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence Antimicrob Agents Chemother 54:1498-1505. http://dx.doi.org/10.1128/AAC.00883-09.
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1498-1505
    • Majchrzykiewicz, J.A.1    Lubelski, J.2    Moll, G.N.3    Kuipers, A.4    Bijlsma, J.J.5    Kuipers, O.P.6    Rink, R.7
  • 61
    • 47249108199 scopus 로고    scopus 로고
    • The importance of the leader sequence for directing lanthionine formation in lacticin 481
    • Patton GC, Paul M, Cooper LE, Chatterjee C, van der Donk WA. 2008. The importance of the leader sequence for directing lanthionine formation in lacticin 481 Biochemistry 47:7342-7351. http://dx.doi.org/10.1021/bi800277d.
    • (2008) Biochemistry , vol.47 , pp. 7342-7351
    • Patton, G.C.1    Paul, M.2    Cooper, L.E.3    Chatterjee, C.4    van der Donk, W.A.5
  • 62
    • 84904895638 scopus 로고    scopus 로고
    • Mechanistic studies on the substrate-tolerant lanthipeptide synthetase ProcM
    • Mukherjee S, van der Donk WA. 2014. Mechanistic studies on the substrate-tolerant lanthipeptide synthetase ProcM J Am Chem Soc 136:10450-10459. http://dx.doi.org/10.1021/ja504692v.
    • (2014) J Am Chem Soc , vol.136 , pp. 10450-10459
    • Mukherjee, S.1    van der Donk, W.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.