메뉴 건너뛰기




Volumn 12, Issue 8, 2011, Pages 1221-1230

Methodologies and strategies for the bioengineering of lantibiotics

Author keywords

Cyclization; Dehydration; Lantibiotics; Modification enzyme; Peptide engineering; Unusual amino acid

Indexed keywords

ENZYME; LACTICIN 3147; LANB PROTEIN; LANC PROTEIN; LANM PROTEIN; LANT PROTEIN; LANTIBIOTIC; NISIN; NUKACIN ISK 1; UNCLASSIFIED DRUG;

EID: 79960030559     PISSN: 13892010     EISSN: 18734316     Source Type: Journal    
DOI: 10.2174/138920111796117355     Document Type: Article
Times cited : (9)

References (67)
  • 1
    • 0029028865 scopus 로고
    • Maturation pathway of nisin and other lantibiotics: Posttranslationally modified antimicrobial peptides exported by grampositive bacteria
    • de Vos, W. M.; Kuipers, O. P.; van der Meer, J. R.; Siezen, R. J. Maturation pathway of nisin and other lantibiotics: posttranslationally modified antimicrobial peptides exported by grampositive bacteria. Mol. Microbiol., 1995, 17(3), 427-437.
    • (1995) Mol. Microbiol , vol.17 , Issue.3 , pp. 427-437
    • de Vos, W.M.1    Kuipers, O.P.2    van der Meer, J.R.3    Siezen, R.J.4
  • 2
    • 14844340728 scopus 로고    scopus 로고
    • Biosynthesis and mode of action of lantibiotics
    • Chatterjee, C.; Paul, M.; Xie, L.; van der Donk, W. A. Biosynthesis and mode of action of lantibiotics. Chem. Rev., 2005, 105(2), 633-684.
    • (2005) Chem. Rev , vol.105 , Issue.2 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    van der Donk, W.A.4
  • 5
    • 0036257622 scopus 로고    scopus 로고
    • Multiple activities in lantibiotics - models for the design of novel antibiotics
    • Pag, U.; Sahl, H.-G. Multiple activities in lantibiotics - models for the design of novel antibiotics? Curr. Pharm. Des., 2002, 8(9), 815-833.
    • (2002) Curr. Pharm. Des , vol.8 , Issue.9 , pp. 815-833
    • Pag, U.1    Sahl, H.-G.2
  • 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.; Suling, J.; Iglesias-Wind, M. I.; Kempter, C.; Molitor, E.; Sahl, H.-G. 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., 1995, 232(2), 478-489.
    • (1995) Eur. J. Biochem , vol.232 , Issue.2 , pp. 478-489
    • Meyer, C.1    Bierbaum, G.2    Heidrich, C.3    Reis, M.4    Suling, J.5    Iglesias-Wind, M.I.6    Kempter, C.7    Molitor, E.8    Sahl, H.-G.9
  • 7
    • 0033811439 scopus 로고    scopus 로고
    • Lantibiotic biosynthesis: Interactions between prelacticin 481 and its putative modification enzyme, LctM
    • Uguen, P.; Le Pennec, J. P.; Dufour, A. Lantibiotic biosynthesis: interactions between prelacticin 481 and its putative modification enzyme, LctM. J. Bacteriol., 2000, 182(18), 5262-5266.
    • (2000) J. Bacteriol , vol.182 , Issue.18 , pp. 5262-5266
    • Uguen, P.1    Le Pennec, J.P.2    Dufour, A.3
  • 8
    • 12444307516 scopus 로고    scopus 로고
    • Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1
    • Aso, Y.; Nagao, J.; Koga, H.; Okuda, K.; Kanemasa, Y.; Sashihara, T.; Nakayama, J.; Sonomoto, K. Heterologous expression and functional analysis of the gene cluster for the biosynthesis of and immunity to the lantibiotic, nukacin ISK-1. J. Biosci. Bioeng., 2004, 98(6), 429-436.
    • (2004) J. Biosci. Bioeng , vol.98 , Issue.6 , pp. 429-436
    • Aso, Y.1    Nagao, J.2    Koga, H.3    Okuda, K.4    Kanemasa, Y.5    Sashihara, T.6    Nakayama, J.7    Sonomoto, K.8
  • 9
    • 0942268866 scopus 로고    scopus 로고
    • Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
    • Xie, L.; Miller, L. M.; Chatterjee, C.; Averin, O.; Kelleher, N. L.; van der Donk, W. A. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity. Science, 2004, 303(5658), 679-681.
    • (2004) Science , vol.303 , Issue.5658 , 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
  • 10
    • 65249190283 scopus 로고    scopus 로고
    • Lantibiotics: Diverse activities and unique modes of action
    • Asaduzzaman, S. M.; Sonomoto, K. Lantibiotics: diverse activities and unique modes of action. J. Biosci. Bioeng., 2009, 107(5), 475-487.
    • (2009) J. Biosci. Bioeng , vol.107 , Issue.5 , pp. 475-487
    • Asaduzzaman, S.M.1    Sonomoto, K.2
  • 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, G. N.; Kuipers, O. P. Biosynthesis, immunity, regulation, mode of action and engineering of the model lantibiotic nisin. Cell Mol. Life Sci., 2008, 65(3), 455-476.
    • (2008) Cell Mol. Life Sci , vol.65 , Issue.3 , pp. 455-476
    • Lubelski, J.1    Rink, R.2    Khusainov, R.3    Moll, G.N.4    Kuipers, O.P.5
  • 12
    • 15844418684 scopus 로고    scopus 로고
    • Biosynthesis of lantibiotic nisin. Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex
    • Siegers, K.; Heinzmann, S.; Entian, K. D. Biosynthesis of lantibiotic nisin. Posttranslational modification of its prepeptide occurs at a multimeric membrane-associated lanthionine synthetase complex. J. Biol. Chem., 1996, 271(21), 12294-12301.
    • (1996) J. Biol. Chem , vol.271 , Issue.21 , pp. 12294-12301
    • Siegers, K.1    Heinzmann, S.2    Entian, K.D.3
  • 15
    • 33749658643 scopus 로고    scopus 로고
    • Engineering dehydro amino acids and thioethers into peptides using lacticin 481 synthetase
    • Chatterjee, C.; Patton, G. C.; Cooper, L.; Paul, M.; van der Donk, W. A. Engineering dehydro amino acids and thioethers into peptides using lacticin 481 synthetase. Chem. Biol., 2006, 13(10), 1109-1117.
    • (2006) Chem. Biol , vol.13 , Issue.10 , pp. 1109-1117
    • Chatterjee, C.1    Patton, G.C.2    Cooper, L.3    Paul, M.4    van der Donk, W.A.5
  • 16
    • 25444499680 scopus 로고    scopus 로고
    • Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin
    • Kluskens, L. D.; Kuipers, A.; Rink, R.; de Boef, E.; Fekken, S.; Driessen, A. J.; Kuipers, O. P.; Moll, G. N. Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin. Biochemistry, 2005, 44(38), 12827-12834.
    • (2005) Biochemistry , vol.44 , Issue.38 , pp. 12827-12834
    • Kluskens, L.D.1    Kuipers, A.2    Rink, R.3    de Boef, E.4    Fekken, S.5    Driessen, A.J.6    Kuipers, O.P.7    Moll, G.N.8
  • 17
    • 36048994654 scopus 로고    scopus 로고
    • NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides
    • Rink, R.; Kluskens, L. D.; Kuipers, A.; Driessen, A. J.; Kuipers, O. P.; Moll, G. N. NisC, the cyclase of the lantibiotic nisin, can catalyze cyclization of designed nonlantibiotic peptides. Biochemistry, 2007, 46(45), 13179-13189.
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13179-13189
    • Rink, R.1    Kluskens, L.D.2    Kuipers, A.3    Driessen, A.J.4    Kuipers, O.P.5    Moll, G.N.6
  • 18
    • 20544436705 scopus 로고    scopus 로고
    • Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes
    • Rink, R.; Kuipers, A.; de Boef, E.; Leenhouts, K. J.; Driessen, A. J.; Moll, G. N.; Kuipers, O. P. Lantibiotic structures as guidelines for the design of peptides that can be modified by lantibiotic enzymes. Biochemistry, 2005, 44(24), 8873-8882.
    • (2005) Biochemistry , vol.44 , Issue.24 , pp. 8873-8882
    • Rink, R.1    Kuipers, A.2    de Boef, E.3    Leenhouts, K.J.4    Driessen, A.J.5    Moll, G.N.6    Kuipers, O.P.7
  • 19
    • 49449112664 scopus 로고    scopus 로고
    • Influence of shifting positions of Ser, Thr, and Cys residues in prenisin on the efficiency of modification reactions and on the antimicrobial activities of the modified prepeptides
    • Lubelski, J.; Overkamp, W.; Kluskens, L. D.; Moll, G. N.; Kuipers, O. P. Influence of shifting positions of Ser, Thr, and Cys residues in prenisin on the efficiency of modification reactions and on the antimicrobial activities of the modified prepeptides. Appl. Environ. Microbiol., 2008, 74(15), 4680-4685.
    • (2008) Appl. Environ. Microbiol , vol.74 , Issue.15 , pp. 4680-4685
    • Lubelski, J.1    Overkamp, W.2    Kluskens, L.D.3    Moll, G.N.4    Kuipers, O.P.5
  • 20
    • 33644854595 scopus 로고    scopus 로고
    • Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis
    • Li, B.; Yu, J. P.; Brunzelle, J. S.; Moll, G. N.; van der Donk, W. A.; Nair, S. K. Structure and mechanism of the lantibiotic cyclase involved in nisin biosynthesis. Science, 2006, 311(5766), 1464-1467.
    • (2006) Science , vol.311 , Issue.5766 , pp. 1464-1467
    • Li, B.1    Yu, J.P.2    Brunzelle, J.S.3    Moll, G.N.4    van der Donk, W.A.5    Nair, S.K.6
  • 21
    • 0344823660 scopus 로고    scopus 로고
    • SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins
    • Okeley, N. M.; Paul, M.; Stasser, J. P.; Blackburn, N.; van der Donk, W. A. SpaC and NisC, the cyclases involved in subtilin and nisin biosynthesis, are zinc proteins. Biochemistry, 2003, 42(46), 13613-13624.
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13613-13624
    • Okeley, N.M.1    Paul, M.2    Stasser, J.P.3    Blackburn, N.4    van der Donk, W.A.5
  • 22
    • 34547137156 scopus 로고    scopus 로고
    • Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin
    • Li, B.; van der Donk, W. A. Identification of essential catalytic residues of the cyclase NisC involved in the biosynthesis of nisin. J. Biol. Chem., 2007, 282(29), 21169-21175.
    • (2007) J. Biol. Chem , vol.282 , Issue.29 , pp. 21169-21175
    • Li, B.1    van der Donk, W.A.2
  • 23
    • 70350031573 scopus 로고    scopus 로고
    • Directionality and coordination of dehydration and ring formation during biosynthesis of the lantibiotic nisin
    • Lubelski, J.; Khusainov, R.; Kuipers, O. P. Directionality and coordination of dehydration and ring formation during biosynthesis of the lantibiotic nisin. J. Biol. Chem., 2009, 284(38), 25962-25972.
    • (2009) J. Biol. Chem , vol.284 , Issue.38 , pp. 25962-25972
    • Lubelski, J.1    Khusainov, R.2    Kuipers, O.P.3
  • 26
    • 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, G. C.; van der Donk, W. A. Mutants of the zinc ligands of lacticin 481 synthetase retain dehydration activity but have impaired cyclization activity. Biochemistry, 2007, 46(21), 6268-6276.
    • (2007) Biochemistry , vol.46 , Issue.21 , pp. 6268-6276
    • Paul, M.1    Patton, G.C.2    van der Donk, W.A.3
  • 27
    • 47249108199 scopus 로고    scopus 로고
    • The importance of the leader sequence for directing lanthionine formation in lacticin 481
    • Patton, G. C.; Paul, M.; Cooper, L. E.; Chatterjee, C.; van der Donk, W. A. The importance of the leader sequence for directing lanthionine formation in lacticin 481. Biochemistry, 2008, 47(28), 7342-7351.
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7342-7351
    • Patton, G.C.1    Paul, M.2    Cooper, L.E.3    Chatterjee, C.4    van der Donk, W.A.5
  • 28
    • 67650569231 scopus 로고    scopus 로고
    • Mapping and identification of the region and secondary structure required for the maturation of the nukacin ISK-1 prepeptide
    • Nagao, J.; Morinaga, Y.; Islam, M. R.; Asaduzzaman, S. M.; Aso, Y.; Nakayama, J.; Sonomoto, K. Mapping and identification of the region and secondary structure required for the maturation of the nukacin ISK-1 prepeptide. Peptides, 2009, 30(8), 1412-1420.
    • (2009) Peptides , vol.30 , Issue.8 , pp. 1412-1420
    • Nagao, J.1    Morinaga, Y.2    Islam, M.R.3    Asaduzzaman, S.M.4    Aso, Y.5    Nakayama, J.6    Sonomoto, K.7
  • 29
    • 69349105507 scopus 로고    scopus 로고
    • Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry
    • Lee, M. V.; Ihnken, L. A.; You, Y. O.; McClerren, A. L.; van der Donk, W. A.; Kelleher, N. L. Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry. J. Am. Chem. Soc., 2009, 131(34), 12258-12264.
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.34 , pp. 12258-12264
    • Lee, M.V.1    Ihnken, L.A.2    You, Y.O.3    McClerren, A.L.4    van der Donk, W.A.5    Kelleher, N.L.6
  • 30
    • 64249088729 scopus 로고    scopus 로고
    • In vitro studies of lantibiotic biosynthesis
    • Li, B.; Cooper, L. E.; van der Donk, W. A. In vitro studies of lantibiotic biosynthesis. Methods Enzymol., 2009, 458, 533-558.
    • (2009) Methods Enzymol , vol.458 , pp. 533-558
    • Li, B.1    Cooper, L.E.2    van der Donk, W.A.3
  • 31
    • 34548175995 scopus 로고    scopus 로고
    • On the regioselectivity of thioether formation by lacticin 481 synthetase
    • Zhang, X.; Ni, W.; van der Donk, W. A. On the regioselectivity of thioether formation by lacticin 481 synthetase. Org. Lett., 2007, 9(17), 3343-3346.
    • (2007) Org. Lett , vol.9 , Issue.17 , pp. 3343-3346
    • Zhang, X.1    Ni, W.2    van der Donk, W.A.3
  • 32
    • 64249134841 scopus 로고    scopus 로고
    • Using expressed protein ligation to probe the substrate specificity of lantibiotic synthetases
    • Zhang, X.; van der Donk, W. A. Using expressed protein ligation to probe the substrate specificity of lantibiotic synthetases. Methods Enzymol., 2009, 462, 117-134.
    • (2009) Methods Enzymol , vol.462 , pp. 117-134
    • Zhang, X.1    van der Donk, W.A.2
  • 33
    • 77950113113 scopus 로고    scopus 로고
    • Production of a class II twocomponent lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence
    • Majchrzykiewicz, J. A.; Lubelski, J.; Moll, G. N.; Kuipers, A.; Bijlsma, J. J.; Kuipers, O. P.; Rink, R. Production of a class II twocomponent lantibiotic of Streptococcus pneumoniae using the class I nisin synthetic machinery and leader sequence. Antimicrob. Agents Chemother., 2010, 54(4), 1498-1505.
    • (2010) Antimicrob. Agents Chemother , vol.54 , Issue.4 , 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
  • 34
    • 0028871373 scopus 로고
    • Role of the leader and structural regions of prelantibiotic peptides as assessed by expressing nisinsubtilin chimeras in Bacillus subtilis 168, and characterization of their physical, chemical, and antimicrobial properties
    • Chakicherla, A.; Hansen, J. N. Role of the leader and structural regions of prelantibiotic peptides as assessed by expressing nisinsubtilin chimeras in Bacillus subtilis 168, and characterization of their physical, chemical, and antimicrobial properties. J. Biol. Chem., 1995, 270(40), 23533-23539.
    • (1995) J. Biol. Chem , vol.270 , Issue.40 , pp. 23533-23539
    • Chakicherla, A.1    Hansen, J.N.2
  • 35
    • 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, O. P.; Sahl, H.-G.; de Kruijff, B. Use of the cell wall precursor lipid II by a pore-forming peptide antibiotic. Science, 1999, 286(5448), 2361-2364.
    • (1999) Science , vol.286 , Issue.5448 , pp. 2361-2364
    • Breukink, E.1    Wiedemann, I.2    van Kraaij, C.3    Kuipers, O.P.4    Sahl, H.-G.5    de Kruijff, B.6
  • 36
    • 0035910508 scopus 로고    scopus 로고
    • Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity
    • Wiedemann, I.; Breukink, E.; van Kraaij, C.; Kuipers, O. P.; Bierbaum, G.; de Kruijff, B.; Sahl, H.-G. Specific binding of nisin to the peptidoglycan precursor lipid II combines pore formation and inhibition of cell wall biosynthesis for potent antibiotic activity. J. Biol. Chem., 2001, 276(3), 1772-1779.
    • (2001) J. Biol. Chem , vol.276 , Issue.3 , pp. 1772-1779
    • Wiedemann, I.1    Breukink, E.2    van Kraaij, C.3    Kuipers, O.P.4    Bierbaum, G.5    de Kruijff, B.6    Sahl, H.-G.7
  • 38
    • 0029093410 scopus 로고
    • Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering
    • Rollema, H. S.; Kuipers, O. P.; Both, P.; de Vos, W. M.; Siezen, R. J. Improvement of solubility and stability of the antimicrobial peptide nisin by protein engineering. Appl. Environ. Microbiol., 1995, 61(8), 2873-2878.
    • (1995) Appl. Environ. Microbiol , vol.61 , Issue.8 , pp. 2873-2878
    • Rollema, H.S.1    Kuipers, O.P.2    Both, P.3    de Vos, W.M.4    Siezen, R.J.5
  • 40
    • 3142701459 scopus 로고    scopus 로고
    • Sitedirected mutagenesis of the hinge region of nisin Z and properties of nisin Z mutants
    • Yuan, J.; Zhang, Z. Z.; Chen, X. Z.; Yang, W.; Huan, L. D. Sitedirected mutagenesis of the hinge region of nisin Z and properties of nisin Z mutants. Appl. Microbiol. Biotechnol., 2004, 64(6), 806-815.
    • (2004) Appl. Microbiol. Biotechnol , vol.64 , Issue.6 , pp. 806-815
    • Yuan, J.1    Zhang, Z.Z.2    Chen, X.Z.3    Yang, W.4    Huan, L.D.5
  • 41
    • 45149121558 scopus 로고    scopus 로고
    • The generation of nisin variants with enhanced activity against specific gram-positive pathogens
    • Field, D.; Connor, P. M.; Cotter, P. D.; Hill, C.; Ross, R. P. The generation of nisin variants with enhanced activity against specific gram-positive pathogens. Mol. Microbiol., 2008, 69(1), 218-230.
    • (2008) Mol. Microbiol , vol.69 , Issue.1 , pp. 218-230
    • Field, D.1    Connor, P.M.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 42
    • 34648825064 scopus 로고    scopus 로고
    • Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation
    • Rink, R.; Wierenga, J.; Kuipers, A.; Kluskens, L. D.; Driessen, A. J.; Kuipers, O. P.; Moll, G. N. Dissection and modulation of the four distinct activities of nisin by mutagenesis of rings A and B and by C-terminal truncation. Appl. Environ. Microbiol., 2007, 73(18), 5809-5816.
    • (2007) Appl. Environ. Microbiol , vol.73 , Issue.18 , pp. 5809-5816
    • Rink, R.1    Wierenga, J.2    Kuipers, A.3    Kluskens, L.D.4    Driessen, A.J.5    Kuipers, O.P.6    Moll, G.N.7
  • 43
    • 50949089673 scopus 로고    scopus 로고
    • Distinct contributions of the nisin biosynthesis enzymes NisB and NisC and transporter NisT to prenisin production by Lactococcus lactis
    • van den Berg Saparoea, H. B.; Bakkes, P. J.; Moll, G. N.; Driessen, A. J. Distinct contributions of the nisin biosynthesis enzymes NisB and NisC and transporter NisT to prenisin production by Lactococcus lactis. Appl. Environ. Microbiol., 2008, 74(17), 5541-5548.
    • (2008) Appl. Environ. Microbiol , vol.74 , Issue.17 , pp. 5541-5548
    • van den Berg, S.H.B.1    Bakkes, P.J.2    Moll, G.N.3    Driessen, A.J.4
  • 45
    • 66249125663 scopus 로고    scopus 로고
    • Translocation of a thioetherbridged azurin peptide fragment via the sec pathway in Lactococcus lactis
    • Kuipers, A.; Rink, R.; Moll, G. N. Translocation of a thioetherbridged azurin peptide fragment via the sec pathway in Lactococcus lactis. Appl. Environ. Microbiol., 2009, 75(11), 3800-3802.
    • (2009) Appl. Environ. Microbiol , vol.75 , Issue.11 , pp. 3800-3802
    • Kuipers, A.1    Rink, R.2    Moll, G.N.3
  • 47
    • 33748506881 scopus 로고    scopus 로고
    • The mode of action of the lantibiotic lacticin 3147--a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II
    • Wiedemann, I.; Bottiger, T.; Bonelli, R. R.; Wiese, A.; Hagge, S. O.; Gutsmann, T.; Seydel, U.; Deegan, L.; Hill, C.; Ross, P.; Sahl, H.-G. The mode of action of the lantibiotic lacticin 3147--a complex mechanism involving specific interaction of two peptides and the cell wall precursor lipid II. Mol. Microbiol., 2006, 61(2), 285-296.
    • (2006) Mol. Microbiol , vol.61 , Issue.2 , pp. 285-296
    • Wiedemann, I.1    Bottiger, T.2    Bonelli, R.R.3    Wiese, A.4    Hagge, S.O.5    Gutsmann, T.6    Seydel, U.7    Deegan, L.8    Hill, C.9    Ross, P.10    Sahl, H.-G.11
  • 49
    • 33749999203 scopus 로고    scopus 로고
    • Complete alanine scanning of the two-component lantibiotic lacticin 3147: Generating a blueprint for rational drug design
    • Cotter, P. D.; Deegan, L. H.; Lawton, E. M.; Draper, L. A.; O'Connor, P. M.; Hill, C.; Ross, R. P. Complete alanine scanning of the two-component lantibiotic lacticin 3147: generating a blueprint for rational drug design. Mol. Microbiol., 2006, 62(3), 735-747.
    • (2006) Mol. Microbiol , vol.62 , Issue.3 , pp. 735-747
    • Cotter, P.D.1    Deegan, L.H.2    Lawton, E.M.3    Draper, L.A.4    O'Connor, P.M.5    Hill, C.6    Ross, R.P.7
  • 50
    • 34548498172 scopus 로고    scopus 로고
    • A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: Analysis of mutants producing reduced antibacterial activities
    • Field, D.; Collins, B.; Cotter, P. D.; Hill, C.; Ross, R. P. A system for the random mutagenesis of the two-peptide lantibiotic lacticin 3147: analysis of mutants producing reduced antibacterial activities. J. Mol. Microbiol. Biotechnol., 2007, 13(4), 226-234.
    • (2007) J. Mol. Microbiol. Biotechnol , vol.13 , Issue.4 , pp. 226-234
    • Field, D.1    Collins, B.2    Cotter, P.D.3    Hill, C.4    Ross, R.P.5
  • 51
    • 0028144487 scopus 로고
    • The mode of action of SAFF22, a lantibiotic isolated from Streptococcus pyogenes strain FF22
    • Jack, R.; Benz, R.; Tagg, J.; Sahl, H.-G. The mode of action of SAFF22, a lantibiotic isolated from Streptococcus pyogenes strain FF22. Eur. J. Biochem., 1994, 219(1-2), 699-705.
    • (1994) Eur. J. Biochem , vol.219 , Issue.1-2 , pp. 699-705
    • Jack, R.1    Benz, R.2    Tagg, J.3    Sahl, H.-G.4
  • 55
    • 0034330091 scopus 로고    scopus 로고
    • A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: Cloning of the structural gene and identification of the structure
    • Sashihara, T.; Kimura, H.; Higuchi, T.; Adachi, A.; Matsusaki, H.; Sonomoto, K.; Ishizaki, A. A novel lantibiotic, nukacin ISK-1, of Staphylococcus warneri ISK-1: cloning of the structural gene and identification of the structure. Biosci. Biotechnol. Biochem., 2000, 64(11), 2420-2428.
    • (2000) Biosci. Biotechnol. Biochem , vol.64 , Issue.11 , pp. 2420-2428
    • Sashihara, T.1    Kimura, H.2    Higuchi, T.3    Adachi, A.4    Matsusaki, H.5    Sonomoto, K.6    Ishizaki, A.7
  • 58
    • 0038155138 scopus 로고    scopus 로고
    • Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin
    • Szekat, C.; Jack, R. W.; Skutlarek, D.; Farber, H.; Bierbaum, G. Construction of an expression system for site-directed mutagenesis of the lantibiotic mersacidin. Appl. Environ. Microbiol., 2003, 69(7), 3777-3783.
    • (2003) Appl. Environ. Microbiol , vol.69 , Issue.7 , pp. 3777-3783
    • Szekat, C.1    Jack, R.W.2    Skutlarek, D.3    Farber, H.4    Bierbaum, G.5
  • 59
    • 24644468692 scopus 로고    scopus 로고
    • Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli
    • Nagao, J.; Harada, Y.; Shioya, K.; Aso, Y.; Zendo, T.; Nakayama, J.; Sonomoto, K. Lanthionine introduction into nukacin ISK-1 prepeptide by co-expression with modification enzyme NukM in Escherichia coli. Biochem. Biophys. Res. Commun., 2005, 336(2), 507-513.
    • (2005) Biochem. Biophys. Res. Commun , vol.336 , Issue.2 , pp. 507-513
    • Nagao, J.1    Harada, Y.2    Shioya, K.3    Aso, Y.4    Zendo, T.5    Nakayama, J.6    Sonomoto, K.7
  • 60
    • 77950628779 scopus 로고    scopus 로고
    • Characterization of modification enzyme NukM and engineering of a novel thioether bridge in lantibiotic nukacin ISK-1
    • Shioya, K.; Harada, Y.; Nagao, J.; Nakayama, J.; Sonomoto, K. Characterization of modification enzyme NukM and engineering of a novel thioether bridge in lantibiotic nukacin ISK-1. Appl. Microbiol. Biotechnol., 2010, 86(3), 891-899.
    • (2010) Appl. Microbiol. Biotechnol , vol.86 , Issue.3 , pp. 891-899
    • Shioya, K.1    Harada, Y.2    Nagao, J.3    Nakayama, J.4    Sonomoto, K.5
  • 61
    • 70449728115 scopus 로고    scopus 로고
    • ATPdependent leader peptide cleavage by NukT, a bifunctional ABC transporter, during lantibiotic biosynthesis
    • Nishie, M.; Shioya, K.; Nagao, J.; Jikuya, H.; Sonomoto, K. ATPdependent leader peptide cleavage by NukT, a bifunctional ABC transporter, during lantibiotic biosynthesis. J. Biosci. Bioeng., 2009, 108(6), 460-464.
    • (2009) J. Biosci. Bioeng , vol.108 , Issue.6 , pp. 460-464
    • Nishie, M.1    Shioya, K.2    Nagao, J.3    Jikuya, H.4    Sonomoto, K.5
  • 62
    • 65549105876 scopus 로고    scopus 로고
    • Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids
    • Levengood, M. R.; Kerwood, C. C.; Chatterjee, C.; van der Donk, W. A. Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids. Chembiochem, 2009, 10(5), 911-919.
    • (2009) Chembiochem , vol.10 , Issue.5 , pp. 911-919
    • Levengood, M.R.1    Kerwood, C.C.2    Chatterjee, C.3    van der Donk, W.A.4
  • 63
    • 69349083675 scopus 로고    scopus 로고
    • In vitro mutasynthesis of lantibiotic analogues containing nonproteinogenic amino acids
    • Levengood, M. R.; Knerr, P. J.; Oman, T. J.; van der Donk, W. A. In vitro mutasynthesis of lantibiotic analogues containing nonproteinogenic amino acids. J. Am. Chem. Soc., 2009, 131(34), 12024-12025.
    • (2009) J. Am. Chem. Soc , vol.131 , Issue.34 , pp. 12024-12025
    • Levengood, M.R.1    Knerr, P.J.2    Oman, T.J.3    van der Donk, W.A.4
  • 64
    • 33847685140 scopus 로고    scopus 로고
    • On the substrate specificity of dehydration by lacticin 481 synthetase
    • Zhang, X.; van der Donk, W. A. On the substrate specificity of dehydration by lacticin 481 synthetase. J. Am. Chem. Soc., 2007, 129(8), 2212-2213.
    • (2007) J. Am. Chem. Soc , vol.129 , Issue.8 , pp. 2212-2213
    • Zhang, X.1    van der Donk, W.A.2
  • 65
    • 34249111878 scopus 로고    scopus 로고
    • Mechanistic investigations of the dehydration reaction of lacticin 481 synthetase using site-directed mutagenesis
    • You, Y. O.; van der Donk, W. A. Mechanistic investigations of the dehydration reaction of lacticin 481 synthetase using site-directed mutagenesis. Biochemistry, 2007, 46(20), 5991-6000.
    • (2007) Biochemistry , vol.46 , Issue.20 , pp. 5991-6000
    • You, Y.O.1    van der Donk, W.A.2
  • 66
    • 47249093322 scopus 로고    scopus 로고
    • In vitro reconstitution and substrate specificity of a lantibiotic protease
    • Furgerson Ihnken, L. A.; Chatterjee, C.; van der Donk, W. A. In vitro reconstitution and substrate specificity of a lantibiotic protease. Biochemistry, 2008, 47(28), 7352-7363.
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7352-7363
    • Furgerson, I.L.A.1    Chatterjee, C.2    van der Donk, W.A.3
  • 67
    • 65949089371 scopus 로고    scopus 로고
    • Lantibiotics: Mode of action, biosynthesis and bioengineering
    • Bierbaum, G.; Sahl, H.-G. Lantibiotics: mode of action, biosynthesis and bioengineering. Curr. Pharm. Biotechnol., 2009, 10(1), 2-18.
    • (2009) Curr. Pharm. Biotechnol , vol.10 , Issue.1 , pp. 2-18
    • Bierbaum, G.1    Sahl, H.-G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.