메뉴 건너뛰기




Volumn 36, Issue 12, 2014, Pages 2407-2416

Genetic manipulation of non-ribosomal peptide synthetases to generate novel bioactive peptide products

Author keywords

Biosynthesis; Directed evolution; Domain substitution; Module swapping; Non ribosomal peptide synthetases; Rational engineering; Secondary metabolite

Indexed keywords

ASSEMBLY; ASSEMBLY MACHINES; BIOCHEMISTRY; BIOSYNTHESIS; METABOLITES; RATIONAL FUNCTIONS; SYNTHETIC BIOLOGY;

EID: 84911484355     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-014-1642-y     Document Type: Review
Times cited : (43)

References (52)
  • 1
    • 3342921823 scopus 로고    scopus 로고
    • Characterization and genetic manipulation of peptide synthetases in Pseudomonas aeruginosa PAO1 in order to generate novel pyoverdines
    • PID: 15271355, COI: 1:CAS:528:DC%2BD2cXmtVanu74%3D
    • Ackerley DF, Lamont IL (2004) Characterization and genetic manipulation of peptide synthetases in Pseudomonas aeruginosa PAO1 in order to generate novel pyoverdines. Chem Biol 11:971–980
    • (2004) Chem Biol , vol.11 , pp. 971-980
    • Ackerley, D.F.1    Lamont, I.L.2
  • 2
    • 0037781843 scopus 로고    scopus 로고
    • Substrate specificity of the nonribosomal peptide synthetase PvdD from Pseudomonas aeruginosa
    • PID: 12700264, COI: 1:CAS:528:DC%2BD3sXjt1Gms70%3D
    • Ackerley DF, Caradoc-Davies TT, Lamont IL (2003) Substrate specificity of the nonribosomal peptide synthetase PvdD from Pseudomonas aeruginosa. J Bacteriol 185:2848–2855
    • (2003) J Bacteriol , vol.185 , pp. 2848-2855
    • Ackerley, D.F.1    Caradoc-Davies, T.T.2    Lamont, I.L.3
  • 3
    • 80855147553 scopus 로고    scopus 로고
    • Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery
    • PID: 21826462, COI: 1:CAS:528:DC%2BC3MXhtlGhtrnO
    • Baltz RH (2011) Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery. J Ind Microbiol Biotechnol 38:1747–1760
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 1747-1760
    • Baltz, R.H.1
  • 4
    • 84901840278 scopus 로고    scopus 로고
    • Creating functional engineered variants of the single-module non-ribosomal peptide synthetase IndC by T domain exchange
    • PID: 24457530, COI: 1:CAS:528:DC%2BC2cXptlKkt7g%3D
    • Beer R, Herbst K, Ignatiadis N et al (2014) Creating functional engineered variants of the single-module non-ribosomal peptide synthetase IndC by T domain exchange. Mol BioSyst 10:1709–1718
    • (2014) Mol BioSyst , vol.10 , pp. 1709-1718
    • Beer, R.1    Herbst, K.2    Ignatiadis, N.3
  • 5
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • PID: 10205056, COI: 1:CAS:528:DyaK1MXisFOkt7c%3D
    • Belshaw PJ, Walsh CT, Stachelhaus T (1999) Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. Science 284:486–489
    • (1999) Science , vol.284 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3
  • 6
    • 84867330853 scopus 로고    scopus 로고
    • Improving known classes of antibiotics: an optimistic approach for the future
    • PID: 22748801, COI: 1:CAS:528:DC%2BC38XpsVOmtr0%3D
    • Bush K (2012) Improving known classes of antibiotics: an optimistic approach for the future. Curr Opin Pharmacol 12:527–534
    • (2012) Curr Opin Pharmacol , vol.12 , pp. 527-534
    • Bush, K.1
  • 7
    • 77957370432 scopus 로고    scopus 로고
    • Diversity of monomers in nonribosomal peptides: towards the prediction of origin and biological activity
    • PID: 20693331, COI: 1:CAS:528:DC%2BC3cXhsFCitbvK
    • Caboche S, Leclère V, Pupin M et al (2010) Diversity of monomers in nonribosomal peptides: towards the prediction of origin and biological activity. J Bacteriol 192:5143–5150
    • (2010) J Bacteriol , vol.192 , pp. 5143-5150
    • Caboche, S.1    Leclère, V.2    Pupin, M.3
  • 8
    • 84906330279 scopus 로고    scopus 로고
    • Ackerley DF: Biosynthesis of novel pyoverdines by domain substitution in a non-ribosomal peptide synthetase of Pseudomonas aeruginosa. Appl Environ Microbiol
    • Calcott MJ, Owen JG, Lamont IL, Ackerley DF (2014) Biosynthesis of novel pyoverdines by domain substitution in a non-ribosomal peptide synthetase of Pseudomonas aeruginosa. Appl Environ Microbiol doi:10.1128/AEM.01453-14
    • (2014) Lamont IL
    • Calcott, M.J.1    Owen, J.G.2
  • 9
    • 84906353352 scopus 로고    scopus 로고
    • Prediction of monomer isomery in Florine: a workflow dedicated to nonribosomal peptide discovery
    • PID: 24465643
    • Caradec T, Pupin M, Vanvlassenbroeck A et al (2014) Prediction of monomer isomery in Florine: a workflow dedicated to nonribosomal peptide discovery. PLoS ONE 9:e85667
    • (2014) PLoS ONE , vol.9 , pp. e85667
    • Caradec, T.1    Pupin, M.2    Vanvlassenbroeck, A.3
  • 10
    • 62649153772 scopus 로고    scopus 로고
    • Computational structure-based redesign of enzyme activity
    • PID: 19228942, COI: 1:CAS:528:DC%2BD1MXjt1Gks7k%3D
    • Chen C-Y, Georgiev I, Anderson AC, Donald BR (2009) Computational structure-based redesign of enzyme activity. Proc Natl Acad Sci USA 106:3764–3769
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3764-3769
    • Chen, C.-Y.1    Georgiev, I.2    Anderson, A.C.3    Donald, B.R.4
  • 11
    • 33747345019 scopus 로고    scopus 로고
    • In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex
    • PID: 16931339, COI: 1:CAS:528:DC%2BD28XoslOhu7g%3D
    • Chiocchini C, Linne U, Stachelhaus T (2006) In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex. Chem Biol 13:899–908
    • (2006) Chem Biol , vol.13 , pp. 899-908
    • Chiocchini, C.1    Linne, U.2    Stachelhaus, T.3
  • 12
    • 84859643888 scopus 로고    scopus 로고
    • Structure guided approaches toward exploiting and manipulating nonribosomal peptide and polyketide biosynthetic pathways
    • PID: 22369855, COI: 1:CAS:528:DC%2BC38XjtVyhsLs%3D
    • Condurso HL, Bruner SD (2012) Structure guided approaches toward exploiting and manipulating nonribosomal peptide and polyketide biosynthetic pathways. Curr Opin Chem Biol 16:162–169
    • (2012) Curr Opin Chem Biol , vol.16 , pp. 162-169
    • Condurso, H.L.1    Bruner, S.D.2
  • 13
    • 53449085206 scopus 로고    scopus 로고
    • Non-ribosomal peptide synthetase module fusions to produce derivatives of daptomycin in Streptomyces roseosporus
    • PID: 18757821, COI: 1:CAS:528:DC%2BD1cXhtF2gtbvJ
    • Doekel S, Coëffet-Le Gal M-F, Gu J-Q et al (2008) Non-ribosomal peptide synthetase module fusions to produce derivatives of daptomycin in Streptomyces roseosporus. Microbiology 154:2872–2880
    • (2008) Microbiology , vol.154 , pp. 2872-2880
    • Doekel, S.1    Coëffet-Le Gal, M.-F.2    Gu, J.-Q.3
  • 14
    • 0345305853 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases for the production of α-l-aspartyl-l-phenylalanine, a precursor for the high-intensity sweetener aspartame
    • PID: 14622284, COI: 1:CAS:528:DC%2BD3sXpt1Knsbw%3D
    • Duerfahrt T, Doekel S, Sonke T et al (2003) Construction of hybrid peptide synthetases for the production of α-l-aspartyl-l-phenylalanine, a precursor for the high-intensity sweetener aspartame. Eur J Biochem 270:4555–4563
    • (2003) Eur J Biochem , vol.270 , pp. 4555-4563
    • Duerfahrt, T.1    Doekel, S.2    Sonke, T.3
  • 15
    • 0033782162 scopus 로고    scopus 로고
    • Aminoacyl-SNACs as small-molecule substrates for the condensation domains of nonribosomal peptide synthetases
    • PID: 11033080, COI: 1:CAS:528:DC%2BD3cXotVWitr0%3D
    • Ehmann DE, Trauger JW, Stachelhaus T, Walsh CT (2000) Aminoacyl-SNACs as small-molecule substrates for the condensation domains of nonribosomal peptide synthetases. Chem Biol 7:765–772
    • (2000) Chem Biol , vol.7 , pp. 765-772
    • Ehmann, D.E.1    Trauger, J.W.2    Stachelhaus, T.3    Walsh, C.T.4
  • 16
    • 0037199494 scopus 로고    scopus 로고
    • Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics
    • PID: 12135394, COI: 1:CAS:528:DC%2BD38XkvFCltr8%3D
    • Eppelmann K, Stachelhaus T, Marahiel MA (2002) Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics. Biochemistry 41:9718–9726
    • (2002) Biochemistry , vol.41 , pp. 9718-9726
    • Eppelmann, K.1    Stachelhaus, T.2    Marahiel, M.A.3
  • 17
    • 79957450871 scopus 로고    scopus 로고
    • Directed evolution of the nonribosomal peptide synthetase AdmK generates new andrimid derivatives in vivo
    • PID: 21609841, COI: 1:CAS:528:DC%2BC3MXmslOksL0%3D
    • Evans BS, Chen Y, Metcalf WW et al (2011) Directed evolution of the nonribosomal peptide synthetase AdmK generates new andrimid derivatives in vivo. Chem Biol 18:601–607
    • (2011) Chem Biol , vol.18 , pp. 601-607
    • Evans, B.S.1    Chen, Y.2    Metcalf, W.W.3
  • 18
    • 42549160616 scopus 로고    scopus 로고
    • Nonribosomal peptide synthetases involved in the production of medically relevant natural products
    • PID: 18217713, COI: 1:CAS:528:DC%2BD1cXhtVyitb0%3D
    • Felnagle EA, Jackson EE, Chan YA et al (2008) Nonribosomal peptide synthetases involved in the production of medically relevant natural products. Mol Pharm 5:191–211
    • (2008) Mol Pharm , vol.5 , pp. 191-211
    • Felnagle, E.A.1    Jackson, E.E.2    Chan, Y.A.3
  • 19
    • 33748631825 scopus 로고    scopus 로고
    • Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms
    • PID: 16895337, COI: 1:CAS:528:DC%2BD28XmvFCqurw%3D
    • Fischbach MA, Walsh CT (2006) Assembly-line enzymology for polyketide and nonribosomal peptide antibiotics: logic, machinery, and mechanisms. Chem Rev 106:3468–3496
    • (2006) Chem Rev , vol.106 , pp. 3468-3496
    • Fischbach, M.A.1    Walsh, C.T.2
  • 20
    • 34547547069 scopus 로고    scopus 로고
    • Directed evolution can rapidly improve the activity of chimeric assembly-line enzymes
    • PID: 17620609, COI: 1:CAS:528:DC%2BD2sXosVClsLc%3D
    • Fischbach MA, Lai JR, Roche ED et al (2007) Directed evolution can rapidly improve the activity of chimeric assembly-line enzymes. Proc Natl Acad Sci USA 104:11951–11956
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11951-11956
    • Fischbach, M.A.1    Lai, J.R.2    Roche, E.D.3
  • 21
    • 42449155111 scopus 로고    scopus 로고
    • The evolution of gene collectives: how natural selection drives chemical innovation
    • PID: 18216259, COI: 1:CAS:528:DC%2BD1cXktlSrtrs%3D
    • Fischbach MA, Walsh CT, Clardy J (2008) The evolution of gene collectives: how natural selection drives chemical innovation. Proc Natl Acad Sci USA 105:4601–4608
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 4601-4608
    • Fischbach, M.A.1    Walsh, C.T.2    Clardy, J.3
  • 22
    • 8144230760 scopus 로고    scopus 로고
    • Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains
    • PID: 15498872, COI: 1:CAS:528:DC%2BD2cXhtVWisL3F
    • Hahn M, Stachelhaus T (2004) Selective interaction between nonribosomal peptide synthetases is facilitated by short communication-mediating domains. Proc Natl Acad Sci USA 101:15585–15590
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 15585-15590
    • Hahn, M.1    Stachelhaus, T.2
  • 23
    • 84862812362 scopus 로고    scopus 로고
    • Site-directed modification of the adenylation domain of the fusaricidin nonribosomal peptide synthetase for enhanced production of fusaricidin analogs
    • PID: 22450515, COI: 1:CAS:528:DC%2BC38XotFais70%3D
    • Han JW, Kim EY, Lee JM et al (2012) Site-directed modification of the adenylation domain of the fusaricidin nonribosomal peptide synthetase for enhanced production of fusaricidin analogs. Biotechnol Lett 34:1327–1334
    • (2012) Biotechnol Lett , vol.34 , pp. 1327-1334
    • Han, J.W.1    Kim, E.Y.2    Lee, J.M.3
  • 24
    • 84870062242 scopus 로고    scopus 로고
    • Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology
    • PID: 22802156, COI: 1:CAS:528:DC%2BC38XhtlCjsbnN
    • Hur GH, Vickery CR, Burkart MD (2012) Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology. Nat Prod Rep 29:1074–1098
    • (2012) Nat Prod Rep , vol.29 , pp. 1074-1098
    • Hur, G.H.1    Vickery, C.R.2    Burkart, M.D.3
  • 25
    • 33747799316 scopus 로고    scopus 로고
    • A biosynthetic gene cluster for the acetyl-CoA carboxylase inhibitor andrimid
    • PID: 16910643, COI: 1:CAS:528:DC%2BD28XnsF2gs7g%3D
    • Jin M, Fischbach MA, Clardy J (2006) A biosynthetic gene cluster for the acetyl-CoA carboxylase inhibitor andrimid. J Am Chem Soc 128:10660–10661
    • (2006) J Am Chem Soc , vol.128 , pp. 10660-10661
    • Jin, M.1    Fischbach, M.A.2    Clardy, J.3
  • 26
    • 84859957277 scopus 로고    scopus 로고
    • Merging chemical synthesis and biosynthesis: a new chapter in the total synthesis of natural products and natural product libraries
    • PID: 22441812, COI: 1:CAS:528:DC%2BC38Xkt1yktLg%3D
    • Kirschning A, Hahn F (2012) Merging chemical synthesis and biosynthesis: a new chapter in the total synthesis of natural products and natural product libraries. Angew Chem Int Ed Engl 51:4012–4022
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 4012-4022
    • Kirschning, A.1    Hahn, F.2
  • 27
    • 77957754232 scopus 로고    scopus 로고
    • Expression and purification of an adenylation domain from a eukaryotic nonribosomal peptide synthetase: using structural genomics tools for a challenging target
    • PID: 20716446, COI: 1:CAS:528:DC%2BC3cXht1OmtbzE
    • Lee TV, Lott JS, Johnson RD, Arcus VL (2010) Expression and purification of an adenylation domain from a eukaryotic nonribosomal peptide synthetase: using structural genomics tools for a challenging target. Protein Expr Purif 74:162–168
    • (2010) Protein Expr Purif , vol.74 , pp. 162-168
    • Lee, T.V.1    Lott, J.S.2    Johnson, R.D.3    Arcus, V.L.4
  • 28
    • 0035951102 scopus 로고    scopus 로고
    • Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases
    • PID: 11747460, COI: 1:CAS:528:DC%2BD3MXos1Cjsb8%3D
    • Linne U, Doekel S, Marahiel MA (2001) Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases. Biochemistry 40:15824–15834
    • (2001) Biochemistry , vol.40 , pp. 15824-15834
    • Linne, U.1    Doekel, S.2    Marahiel, M.A.3
  • 29
    • 73349085562 scopus 로고    scopus 로고
    • Working outside the protein-synthesis rules: insights into non-ribosomal peptide synthesis
    • COI: 1:CAS:528:DC%2BD1MXhtlOku7%2FI
    • Marahiel MA (2009) Working outside the protein-synthesis rules: insights into non-ribosomal peptide synthesis. J Peptide Sci 15:799–807
    • (2009) J Peptide Sci , vol.15 , pp. 799-807
    • Marahiel, M.A.1
  • 30
    • 0034705130 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases by module and domain fusions
    • PID: 10811885, COI: 1:CAS:528:DC%2BD3cXjvFaktLY%3D
    • Mootz HD, Schwarzer D, Marahiel MA (2000) Construction of hybrid peptide synthetases by module and domain fusions. Proc Natl Acad Sci USA 97:5848–5853
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5848-5853
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 31
    • 33751218042 scopus 로고    scopus 로고
    • Combinatorial biosynthesis of novel antibiotics related to daptomycin
    • PID: 17090667, COI: 1:CAS:528:DC%2BD28Xht1Kqu7bE
    • Nguyen KT, Ritz D, Gu J-Q et al (2006) Combinatorial biosynthesis of novel antibiotics related to daptomycin. Proc Natl Acad Sci USA 103:17462–17467
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 17462-17467
    • Nguyen, K.T.1    Ritz, D.2    Gu, J.-Q.3
  • 32
    • 77950101233 scopus 로고    scopus 로고
    • Genetically engineered lipopeptide antibiotics related to A54145 and daptomycin with improved properties
    • PID: 20086142, COI: 1:CAS:528:DC%2BC3cXksFOis7o%3D
    • Nguyen KT, He X, Alexander DC et al (2010) Genetically engineered lipopeptide antibiotics related to A54145 and daptomycin with improved properties. Antimicrob Agents Chemother 54:1404–1413
    • (2010) Antimicrob Agents Chemother , vol.54 , pp. 1404-1413
    • Nguyen, K.T.1    He, X.2    Alexander, D.C.3
  • 33
    • 84885183690 scopus 로고    scopus 로고
    • Combating multidrug-resistant bacteria: current strategies for the discovery of novel antibacterials
    • PID: 24038605
    • O’Connell KMG, Hodgkinson JT, Sore HF et al (2013) Combating multidrug-resistant bacteria: current strategies for the discovery of novel antibacterials. Angew Chem Int Ed Engl 52:10706–10733
    • (2013) Angew Chem Int Ed Engl , vol.52 , pp. 10706-10733
    • O’Connell, K.M.G.1    Hodgkinson, J.T.2    Sore, H.F.3
  • 34
    • 84859988527 scopus 로고    scopus 로고
    • A functional screen for recovery of 4′-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries
    • PID: 22356582, COI: 1:CAS:528:DC%2BC38XhtVant7fF
    • Owen JG, Robins KJ, Parachin NS, Ackerley DF (2012) A functional screen for recovery of 4′-phosphopantetheinyl transferase and associated natural product biosynthesis genes from metagenome libraries. Environ Microbiol 14:1198–1209
    • (2012) Environ Microbiol , vol.14 , pp. 1198-1209
    • Owen, J.G.1    Robins, K.J.2    Parachin, N.S.3    Ackerley, D.F.4
  • 35
    • 26944502019 scopus 로고    scopus 로고
    • Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs)
    • PID: 16221976, COI: 1:CAS:528:DC%2BD2MXht1OmsbjI
    • Rausch C, Weber T, Kohlbacher O et al (2005) Specificity prediction of adenylation domains in nonribosomal peptide synthetases (NRPS) using transductive support vector machines (TSVMs). Nucleic Acids Res 33:5799–5808
    • (2005) Nucleic Acids Res , vol.33 , pp. 5799-5808
    • Rausch, C.1    Weber, T.2    Kohlbacher, O.3
  • 36
    • 84903366227 scopus 로고    scopus 로고
    • BioBrick assembly standards and techniques and associated software tools
    • PID: 24395353
    • Røkke G, Korvald E, Pahr J et al (2014) BioBrick assembly standards and techniques and associated software tools. Methods Mol Biol 1116:1–24
    • (2014) Methods Mol Biol , vol.1116 , pp. 1-24
    • Røkke, G.1    Korvald, E.2    Pahr, J.3
  • 37
    • 79959936207 scopus 로고    scopus 로고
    • NRPSpredictor2—a web server for predicting NRPS adenylation domain specificity
    • PID: 21558170
    • Rottig M, Medema MH, Blin K et al (2011) NRPSpredictor2—a web server for predicting NRPS adenylation domain specificity. Nucleic Acids Res 39:W362–W367
    • (2011) Nucleic Acids Res , vol.39 , pp. W362-W367
    • Rottig, M.1    Medema, M.H.2    Blin, K.3
  • 38
    • 0031932153 scopus 로고    scopus 로고
    • Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping
    • PID: 9520265, COI: 1:CAS:528:DyaK1cXitVOltbY%3D
    • Schneider A, Stachelhaus T, Marahiel MA (1998) Targeted alteration of the substrate specificity of peptide synthetases by rational module swapping. Mol Gen Genet 257:308–318
    • (1998) Mol Gen Genet , vol.257 , pp. 308-318
    • Schneider, A.1    Stachelhaus, T.2    Marahiel, M.A.3
  • 39
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics
    • PID: 15700962, COI: 1:CAS:528:DC%2BD2MXkvFSktw%3D%3D
    • Sieber SA, Marahiel MA (2005) Molecular mechanisms underlying nonribosomal peptide synthesis: approaches to new antibiotics. Chem Rev 105:715–738
    • (2005) Chem Rev , vol.105 , pp. 715-738
    • Sieber, S.A.1    Marahiel, M.A.2
  • 40
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • PID: 7604280, COI: 1:CAS:528:DyaK2MXmsl2jurc%3D
    • Stachelhaus T, Schneider A, Marahiel MA (1995) Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science 269:69–72
    • (1995) Science , vol.269 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 41
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • PID: 10421756, COI: 1:CAS:528:DyaK1MXlsVynsLY%3D
    • Stachelhaus T, Mootz HD, Marahiel MA (1999) The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem Biol 6:493–505
    • (1999) Chem Biol , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 42
    • 0028211466 scopus 로고
    • Detection of 4′-phosphopantetheine at the thioester binding site for l-valine of gramicidinS synthetase 2
    • PID: 8119405, COI: 1:CAS:528:DyaK2cXitl2isr4%3D
    • Stein T, Vater J, Kruft V et al (1994) Detection of 4′-phosphopantetheine at the thioester binding site for l-valine of gramicidinS synthetase 2. FEBS Lett 340:39–44
    • (1994) FEBS Lett , vol.340 , pp. 39-44
    • Stein, T.1    Vater, J.2    Kruft, V.3
  • 43
    • 24644474790 scopus 로고    scopus 로고
    • Utility of epimerization domains for the redesign of nonribosomal peptide synthetases
    • PID: 16128819, COI: 1:CAS:528:DC%2BD2MXhtVWisrjJ
    • Stein DB, Linne U, Marahiel MA (2005) Utility of epimerization domains for the redesign of nonribosomal peptide synthetases. FEBS J 272:4506–4520
    • (2005) FEBS J , vol.272 , pp. 4506-4520
    • Stein, D.B.1    Linne, U.2    Marahiel, M.A.3
  • 44
    • 33845948267 scopus 로고    scopus 로고
    • Redesigning the PheA domain of gramicidin synthetase leads to a new understanding of the enzyme’s mechanism and selectivity
    • PID: 17176071, COI: 1:CAS:528:DC%2BD28XhtlChurjN
    • Stevens BW, Lilien RH, Georgiev I et al (2006) Redesigning the PheA domain of gramicidin synthetase leads to a new understanding of the enzyme’s mechanism and selectivity. Biochemistry 45:15495–15504
    • (2006) Biochemistry , vol.45 , pp. 15495-15504
    • Stevens, B.W.1    Lilien, R.H.2    Georgiev, I.3
  • 45
    • 77951294519 scopus 로고    scopus 로고
    • Nonribosomal peptide synthetases: structures and dynamics
    • PID: 20153164, COI: 1:CAS:528:DC%2BC3cXks1Sjsbc%3D
    • Strieker M, Tanovic A, Marahiel MA (2010) Nonribosomal peptide synthetases: structures and dynamics. Curr Opin Struct Biol 20:234–240
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 234-240
    • Strieker, M.1    Tanovic, A.2    Marahiel, M.A.3
  • 46
    • 48749083335 scopus 로고    scopus 로고
    • Crystal structure of the termination module of a nonribosomal peptide synthetase
    • PID: 18583577, COI: 1:CAS:528:DC%2BD1cXptVKnu70%3D
    • Tanovic A, Samel SA, Essen L-O, Marahiel MA (2008) Crystal structure of the termination module of a nonribosomal peptide synthetase. Science 321:659–663
    • (2008) Science , vol.321 , pp. 659-663
    • Tanovic, A.1    Samel, S.A.2    Essen, L.-O.3    Marahiel, M.A.4
  • 47
    • 84863822575 scopus 로고    scopus 로고
    • Introduction of a non-natural amino acid into a nonribosomal peptide antibiotic by modification of adenylation domain specificity
    • PID: 22711659, COI: 1:CAS:528:DC%2BC38XoslGrs70%3D
    • Thirlway J, Lewis R, Nunns L et al (2012) Introduction of a non-natural amino acid into a nonribosomal peptide antibiotic by modification of adenylation domain specificity. Angew Chem Int Ed Engl 51:7181–7184
    • (2012) Angew Chem Int Ed Engl , vol.51 , pp. 7181-7184
    • Thirlway, J.1    Lewis, R.2    Nunns, L.3
  • 48
    • 1942489379 scopus 로고    scopus 로고
    • Active-site modifications of adenylation domains lead to hydrolysis of upstream nonribosomal peptidyl thioester intermediates
    • PID: 15099062, COI: 1:CAS:528:DC%2BD2cXisl2itrw%3D
    • Uguru GC, Milne C, Borg M et al (2004) Active-site modifications of adenylation domains lead to hydrolysis of upstream nonribosomal peptidyl thioester intermediates. J Am Chem Soc 126:5032–5033
    • (2004) J Am Chem Soc , vol.126 , pp. 5032-5033
    • Uguru, G.C.1    Milne, C.2    Borg, M.3
  • 49
    • 80055091843 scopus 로고    scopus 로고
    • Directed evolution of a gatekeeper domain in nonribosomal peptide synthesis
    • PID: 22035798, COI: 1:CAS:528:DC%2BC3MXhtl2rt73L
    • Villiers B, Hollfelder F (2011) Directed evolution of a gatekeeper domain in nonribosomal peptide synthesis. Chem Biol 18:1290–1299
    • (2011) Chem Biol , vol.18 , pp. 1290-1299
    • Villiers, B.1    Hollfelder, F.2
  • 50
    • 0034004081 scopus 로고    scopus 로고
    • Recombinant acylheptapeptide lichenysin: high level of production by Bacillus subtilis cells
    • PID: 10939247, COI: 1:CAS:528:DC%2BD3cXislWju7w%3D
    • Yakimov MM, Giuliano L, Timmis KN, Golyshin PN (2000) Recombinant acylheptapeptide lichenysin: high level of production by Bacillus subtilis cells. J Mol Microbiol Biotechnol 2:217–224
    • (2000) J Mol Microbiol Biotechnol , vol.2 , pp. 217-224
    • Yakimov, M.M.1    Giuliano, L.2    Timmis, K.N.3    Golyshin, P.N.4
  • 51
    • 84872934815 scopus 로고    scopus 로고
    • Engineering the substrate specificity of the DhbE adenylation domain by yeast cell surface display
    • PID: 23352143, COI: 1:CAS:528:DC%2BC3sXhs1egur0%3D
    • Zhang K, Nelson KM, Bhuripanyo K et al (2013) Engineering the substrate specificity of the DhbE adenylation domain by yeast cell surface display. Chem Biol 20:92–101
    • (2013) Chem Biol , vol.20 , pp. 92-101
    • Zhang, K.1    Nelson, K.M.2    Bhuripanyo, K.3
  • 52
    • 34547409782 scopus 로고    scopus 로고
    • Directed evolution of aryl carrier proteins in the enterobactin synthetase
    • PID: 17606920, COI: 1:CAS:528:DC%2BD2sXotVaks7k%3D
    • Zhou Z, Lai JR, Walsh CT (2007) Directed evolution of aryl carrier proteins in the enterobactin synthetase. Proc Natl Acad Sci USA 104:11621–11626
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 11621-11626
    • Zhou, Z.1    Lai, J.R.2    Walsh, C.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.