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Volumn 8, Issue 4, 2012, Pages 350-357

The radical SAM enzyme AlbA catalyzes thioether bond formation in subtilosin A

Author keywords

[No Author keywords available]

Indexed keywords

ALBA ENZYME; BACTERIOCIN; ENZYME; S ADENOSYLMETHIONINE; SUBTILOSIN A; SULFIDE; UNCLASSIFIED DRUG;

EID: 84858701614     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.798     Document Type: Article
Times cited : (157)

References (50)
  • 2
    • 78049323503 scopus 로고    scopus 로고
    • Naturally occurring circular proteins: Distribution, biosynthesis and evolution
    • Cascales, L. & Craik, D.J. Naturally occurring circular proteins: distribution, biosynthesis and evolution. Org. Biomol. Chem. 8, 5035-5047 (2010).
    • (2010) Org. Biomol. Chem. , vol.8 , pp. 5035-5047
    • Cascales, L.1    Craik, D.J.2
  • 4
    • 0022413987 scopus 로고
    • Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: Isolation, structural analysis, and biogenesis
    • Babasaki, K., Takao, T., Shimonishi, Y. & Kurahashi, K. Subtilosin A, a new antibiotic peptide produced by Bacillus subtilis 168: isolation, structural analysis, and biogenesis. J. Biochem. 98, 585-603 (1985). (Pubitemid 16216406)
    • (1985) Journal of Biochemistry , vol.98 , Issue.3 , pp. 585-603
    • Babasaki, K.1    Takao, T.2    Shimonishi, Y.3    Kurahashi, K.4
  • 6
    • 54249143112 scopus 로고    scopus 로고
    • Spermicidal activity of the safe natural antimicrobial peptide subtilosin
    • Sutyak, K.E. et al. Spermicidal activity of the safe natural antimicrobial peptide subtilosin. Infect. Dis. Obstet. Gynecol. 2008, 540758 (2008).
    • (2008) Infect. Dis. Obstet. Gynecol. 2008 , pp. 540758
    • Sutyak, K.E.1
  • 8
    • 69949088377 scopus 로고    scopus 로고
    • Isolation of a variant of subtilosin A with hemolytic activity
    • Huang, T. et al. Isolation of a variant of subtilosin A with hemolytic activity. J. Bacteriol. 191, 5690-5696 (2009).
    • (2009) J. Bacteriol. , vol.191 , pp. 5690-5696
    • Huang, T.1
  • 9
    • 0037462081 scopus 로고    scopus 로고
    • Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine
    • DOI 10.1021/ja029654t
    • Kawulka, K. et al. Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to α-carbons of phenylalanine and threonine. J. Am. Chem. Soc. 125, 4726-4727 (2003). (Pubitemid 36505362)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.16 , pp. 4726-4727
    • Kawulka, K.1    Sprules, T.2    McKay, R.T.3    Mercier, P.4    Diaper, C.M.5    Zuber, P.6    Vederas, J.C.7
  • 10
    • 1642367862 scopus 로고    scopus 로고
    • Structure of Subtilosin A, A Cyclic Antimicrobial Peptide from Bacillus subtilis with Unusual Sulfur to α-Carbon Cross-Links: Formation and Reduction of α-Thio-α-Amino Acid Derivatives
    • DOI 10.1021/bi0359527
    • Kawulka, K.E. et al. Structure of subtilosin A, a cyclic antimicrobial peptide from Bacillus subtilis with unusual sulfur to α-carbon cross-links: formation and reduction of α-thio-α-amino acid derivatives. Biochemistry 43, 3385-3395 (2004). (Pubitemid 38391695)
    • (2004) Biochemistry , vol.43 , Issue.12 , pp. 3385-3395
    • Kawulka, K.E.1    Sprules, T.2    Diaper, C.M.3    Whittal, R.M.4    McKay, R.T.5    Mercier, P.6    Zuber, P.7    Vederas, J.C.8
  • 11
    • 77957977117 scopus 로고    scopus 로고
    • Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis
    • Liu, W.-T. et al. Imaging mass spectrometry of intraspecies metabolic exchange revealed the cannibalistic factors of Bacillus subtilis. Proc. Natl. Acad. Sci. USA 107, 16286-16290 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16286-16290
    • Liu, W.-T.1
  • 12
    • 70349234326 scopus 로고    scopus 로고
    • Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361
    • Lee, H., Churey, J.J. & Worobo, R.W. Biosynthesis and transcriptional analysis of thurincin H, a tandem repeated bacteriocin genetic locus, produced by Bacillus thuringiensis SF361. FEMS Microbiol. Lett. 299, 205-213 (2009).
    • (2009) FEMS Microbiol. Lett. , vol.299 , pp. 205-213
    • Lee, H.1    Churey, J.J.2    Worobo, R.W.3
  • 13
    • 80052485163 scopus 로고    scopus 로고
    • The 3D solution structure of thurincin H, a cacteriocin with four sulfur to α-carbon crosslinks
    • Sit, C.S., van Belkum, M.J., McKay, R.T., Worobo, R.W. & Vederas, J.C. The 3D solution structure of thurincin H, a cacteriocin with four sulfur to α-carbon crosslinks. Angew. Chem. Int. Edn Engl. 50, 8718-8721 (2011).
    • (2011) Angew. Chem. Int. Edn Engl. , vol.50 , pp. 8718-8721
    • Sit, C.S.1    Van Belkum, M.J.2    McKay, R.T.3    Worobo, R.W.4    Vederas, J.C.5
  • 14
    • 77952679997 scopus 로고    scopus 로고
    • Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against clostridium difficile
    • Rea, M.C. et al. Thuricin CD, a posttranslationally modified bacteriocin with a narrow spectrum of activity against Clostridium difficile. Proc. Natl. Acad. Sci. USA 107, 9352-9357 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 9352-9357
    • Rea, M.C.1
  • 15
    • 79957690316 scopus 로고    scopus 로고
    • The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links
    • Sit, C.S., McKay, R.T., Hill, C., Ross, R.P. & Vederas, J.C. The 3D structure of thuricin CD, a two-component bacteriocin with cysteine sulfur to α-carbon cross-links. J. Am. Chem. Soc. 133, 7680-7683 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 7680-7683
    • Sit, C.S.1    McKay, R.T.2    Hill, C.3    Ross, R.P.4    Vederas, J.C.5
  • 16
    • 0032726081 scopus 로고    scopus 로고
    • Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin
    • Zheng, G., Yan, L.Z., Vederas, J.C. & Zuber, P. Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin. J. Bacteriol. 181, 7346-7355 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 7346-7355
    • Zheng, G.1    Yan, L.Z.2    Vederas, J.C.3    Zuber, P.4
  • 17
    • 0034039083 scopus 로고    scopus 로고
    • Mutational analysis of the sbo-alb locus of Bacillus subtilis: Identification of genes required for subtilosin production and immunity
    • DOI 10.1128/JB.182.11.3266-3273.2000
    • Zheng, G., Hehn, R. & Zuber, P. Mutational analysis of the sbo-alb locus of Bacillus subtilis: identification of genes required for subtilosin production and immunity. J. Bacteriol. 182, 3266-3273 (2000). (Pubitemid 30326945)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3266-3273
    • Zheng, G.1    Hehn, R.2    Zuber, P.3
  • 18
    • 0034087235 scopus 로고    scopus 로고
    • Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis
    • DOI 10.1128/JB.182.11.3274-3277.2000
    • Nakano, M.M., Zheng, G. & Zuber, P. Dual control of sbo-alb operon expression by the Spo0 and ResDE systems of signal transduction under anaerobic conditions in Bacillus subtilis. J. Bacteriol. 182, 3274-3277 (2000). (Pubitemid 30326946)
    • (2000) Journal of Bacteriology , vol.182 , Issue.11 , pp. 3274-3277
    • Nakano, M.M.1    Zheng, G.2    Zuber, P.3
  • 20
    • 0042366189 scopus 로고    scopus 로고
    • Cannibalism by sporulating bacteria
    • DOI 10.1126/science.1086462
    • González-Pastor, J.E., Hobbs, E.C. & Losick, R. Cannibalism by sporulating bacteria. Science 301, 510-513 (2003). (Pubitemid 36900307)
    • (2003) Science , vol.301 , Issue.5632 , pp. 510-513
    • Gonzalez-Pastor, J.E.1    Hobbs, E.C.2    Losick, R.3
  • 21
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia, H.J., Chen, G., Hetzler, B., Reyes-Spindola, J. & Miller, N. Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods. Nucleic Acids Res. 29, 1097-1106 (2001). (Pubitemid 32186195)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 24
    • 0014939344 scopus 로고
    • Lysine 2,3-aminomutase purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme
    • Chirpich, T.P., Zappia, V., Costilow, R.N. & Barker, H.A. Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme. J. Biol. Chem. 245, 1778-1789 (1970).
    • (1970) J. Biol. Chem. , vol.245 , pp. 1778-1789
    • Chirpich, T.P.1    Zappia, V.2    Costilow, R.N.3    Barker, H.A.4
  • 26
    • 0031577321 scopus 로고    scopus 로고
    • Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical
    • DOI 10.1006/bbrc.1997.6952
    • Guianvarc'h, D., Florentin, D., Tse Sum Bui, B., Nunzi, F. & Marquet, A. Biotin synthase, a new member of the family of enzymes which uses S-adenosylmethionine as a source of deoxyadenosyl radical. Biochem. Biophys. Res. Commun. 236, 402-406 (1997). (Pubitemid 27373308)
    • (1997) Biochemical and Biophysical Research Communications , vol.236 , Issue.2 , pp. 402-406
    • Guianvarc'h, D.1    Florentin, D.2    Bui, B.T.S.3    Nunzi, F.4    Marquet, A.5
  • 27
    • 0035902569 scopus 로고    scopus 로고
    • Biotin synthase contains two distinct iron-sulfur cluster binding sites: Chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions
    • DOI 10.1021/bi0104625
    • Ugulava, N.B., Gibney, B.R. & Jarrett, J.T. Biotin synthase contains two distinct iron-sulfur cluster binding sites: chemical and spectroelectrochemical analysis of iron-sulfur cluster interconversions. Biochemistry 40, 8343-8351 (2001). (Pubitemid 32661895)
    • (2001) Biochemistry , vol.40 , Issue.28 , pp. 8343-8351
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 28
    • 0346727529 scopus 로고    scopus 로고
    • Crystal Structure of Biotin Synthase, an S-Adenosylmethionine-Dependent Radical Enzyme
    • DOI 10.1126/science.1088493
    • Berkovitch, F. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science 303, 76-79 (2004). (Pubitemid 38055773)
    • (2004) Science , vol.303 , Issue.5654 , pp. 76-79
    • Berkovitch, F.1    Nicolet, Y.2    Wan, J.T.3    Jarrett, J.T.4    Drennan, C.L.5
  • 29
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein
    • Miller, J.R. et al. Escherichia coli LipA is a lipoyl synthase: in vitro biosynthesis of lipoylated pyruvate dehydrogenase complex from octanoyl-acyl carrier protein. Biochemistry 39, 15166-15178 (2000).
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1
  • 32
    • 33646468635 scopus 로고    scopus 로고
    • Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism
    • Hänzelmann, P. & Schindelin, H. Binding of 5′-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism. Proc. Natl. Acad. Sci. USA 103, 6829-6834 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 6829-6834
    • Hänzelmann, P.1    Schindelin, H.2
  • 33
    • 9144220291 scopus 로고    scopus 로고
    • MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA
    • DOI 10.1074/jbc.M408562200
    • Pierrel, F., Douki, T., Fontecave, M. & Atta, M. MiaB protein is a bifunctional radical-S-adenosylmethionine enzyme involved in thiolation and methylation of tRNA. J. Biol. Chem. 279, 47555-47563 (2004). (Pubitemid 39540900)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , pp. 47555-47563
    • Pierrel, F.1    Douki, T.2    Fontecave, M.3    Atta, M.4
  • 34
    • 34247631048 scopus 로고    scopus 로고
    • MiaB, a bifunctional radical-S-adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters
    • DOI 10.1021/bi7000449
    • Hernández, H.L. et al. MiaB, a bifunctional radical-S- adenosylmethionine enzyme involved in the thiolation and methylation of tRNA, contains two essential [4Fe-4S] clusters. Biochemistry 46, 5140-5147 (2007). (Pubitemid 46683012)
    • (2007) Biochemistry , vol.46 , Issue.17 , pp. 5140-5147
    • Hernandez, H.L.1    Pierrel, F.2    Elleingand, E.3    Garcia-Serres, R.4    Huynh, B.H.5    Johnson, M.K.6    Fontecave, M.7    Atta, M.8
  • 35
    • 70350215875 scopus 로고    scopus 로고
    • Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily
    • Lee, K.-H. et al. Characterization of RimO, a new member of the methylthiotransferase subclass of the radical SAM superfamily. Biochemistry 48, 10162-10174 (2009).
    • (2009) Biochemistry , vol.48 , pp. 10162-10174
    • Lee, K.-H.1
  • 36
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin
    • DOI 10.1021/ja072481t
    • Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D. & Eguchi, T. Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin. J. Am. Chem. Soc. 129, 15147-15155 (2007). (Pubitemid 350247798)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.49 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 37
    • 77951930923 scopus 로고    scopus 로고
    • A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters
    • Grove, T.L., Ahlum, J.H., Sharma, P., Krebs, C. & Booker, S.J. A consensus mechanism for radical SAM-dependent dehydrogenation? BtrN contains two [4Fe-4S] clusters. Biochemistry 49, 3783-3785 (2010).
    • (2010) Biochemistry , vol.49 , pp. 3783-3785
    • Grove, T.L.1    Ahlum, J.H.2    Sharma, P.3    Krebs, C.4    Booker, S.J.5
  • 38
    • 2442499333 scopus 로고    scopus 로고
    • Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB
    • DOI 10.1074/jbc.M313855200
    • Fang, Q., Peng, J. & Dierks, T. Post-translational formylglycine modification of bacterial sulfatases by the radical S-adenosylmethionine protein AtsB. J. Biol. Chem. 279, 14570-14578 (2004). (Pubitemid 38618844)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.15 , pp. 14570-14578
    • Fang, Q.1    Peng, J.2    Dierks, T.3
  • 39
    • 47349101467 scopus 로고    scopus 로고
    • In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
    • DOI 10.1021/bi8004297
    • Grove, T.L., Lee, K.-H., St. Clair, J., Krebs, C. & Booker, S.J. In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters. Biochemistry 47, 7523-7538 (2008). (Pubitemid 351994313)
    • (2008) Biochemistry , vol.47 , Issue.28 , pp. 7523-7538
    • Grove, T.L.1    Lee, K.-H.2    St. Clair, J.3    Krebs, C.4    Booker, S.J.5
  • 40
    • 0020766701 scopus 로고
    • Synthetic routes to iron sulfide (Fe2S2, Fe3S4, Fe4S4, and Fe6S9), clusters from the common precursor tetrakis(ethanethiolate)ferrate2- ion ([Fe(SC2H5)4]2-): Structures and properties of [Fe3S4(SR)4]3- and bis(ethanethiolate)nonathioxohexaferrate4- ion ([Fe6S9(SC2H5)2]4-), examples of the newest types of Fe-S-SR clusters
    • Hagen, K. & Watson, A. Synthetic routes to iron sulfide (Fe2S2, Fe3S4, Fe4S4, and Fe6S9), clusters from the common precursor tetrakis(ethanethiolate)ferrate2- ion ([Fe(SC2H5)4]2-): structures and properties of [Fe3S4(SR)4]3- and bis(ethanethiolate)nonathioxohexaferrate4- ion ([Fe6S9(SC2H5)2]4-), examples of the newest types of Fe-S-SR clusters. J. Am. Chem. Soc. 105, 3905-3913 (1983).
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 3905-3913
    • Hagen, K.1    Watson, A.2
  • 41
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Polynuclear Iron-Sulfur cluster in pyruvate formate-lyase-activating enzyme: Molecular properties of the holoenzyme form
    • DOI 10.1074/jbc.273.9.4897
    • Külzer, R., Pils, T., Kappl, R., Hüttermann, J. & Knappe, J. Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme. Molecular properties of the holoenzyme form. J. Biol. Chem. 273, 4897-4903 (1998). (Pubitemid 28108640)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.9 , pp. 4897-4903
    • Kulzer, R.1    Pils, T.2    Kappl, R.3    Huttermann, J.4    Knappe, J.5
  • 42
    • 0034595376 scopus 로고    scopus 로고
    • Iron-sulfur cluster interconversions in biotin synthase: Dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters
    • DOI 10.1021/bi9926227
    • Ugulava, N.B., Gibney, B.R. & Jarrett, J.T. Iron-sulfur cluster interconversions in biotin synthase: dissociation and reassociation of iron during conversion of [2Fe-2S] to [4Fe-4S] clusters. Biochemistry 39, 5206-5214 (2000). (Pubitemid 30241643)
    • (2000) Biochemistry , vol.39 , Issue.17 , pp. 5206-5214
    • Ugulava, N.B.1    Gibney, B.R.2    Jarrett, J.T.3
  • 43
    • 77950368112 scopus 로고    scopus 로고
    • The antiviral protein viperin is a radical SAM enzyme
    • Duschene, K.S. & Broderick, J.B. The antiviral protein viperin is a radical SAM enzyme. FEBS Lett. 584, 1263-1267 (2010).
    • (2010) FEBS Lett. , vol.584 , pp. 1263-1267
    • Duschene, K.S.1    Broderick, J.B.2
  • 44
    • 56249110190 scopus 로고    scopus 로고
    • Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily
    • Chatterjee, A. et al. Reconstitution of ThiC in thiamine pyrimidine biosynthesis expands the radical SAM superfamily. Nat. Chem. Biol. 4, 758-765 (2008).
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 758-765
    • Chatterjee, A.1
  • 45
    • 79960080501 scopus 로고    scopus 로고
    • Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters
    • Murphy, K. et al. Genome mining for radical SAM protein determinants reveals multiple sactibiotic-like gene clusters. PLoS ONE 6, e20852 (2011).
    • (2011) PLoS ONE , vol.6
    • Murphy, K.1
  • 46
    • 74049115080 scopus 로고    scopus 로고
    • Follow the leader: The use of leader peptides to guide natural product biosynthesis
    • Oman, T.J. & van der Donk, W.A. Follow the leader: the use of leader peptides to guide natural product biosynthesis. Nat. Chem. Biol. 6, 9-18 (2010).
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 9-18
    • Oman, T.J.1    Van Der Donk, W.A.2
  • 47
    • 0942268866 scopus 로고    scopus 로고
    • Lacticin 481: In vitro reconstitution of lantibiotic synthetase activity
    • DOI 10.1126/science.1092600
    • Xie, L., Miller, L., Chatterjee, C. & Averin, O. Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity. Science 303, 679-681 (2004). (Pubitemid 38141635)
    • (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
  • 48
    • 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. 105, 633-684 (2005).
    • (2005) Chem. Rev. , vol.105 , pp. 633-684
    • Chatterjee, C.1    Paul, M.2    Xie, L.3    Van Der Donk, W.A.4
  • 49
    • 0030947388 scopus 로고    scopus 로고
    • Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation
    • DOI 10.1038/42990
    • Roach, P.L., Clifton, I., Hensgens, C. & Shibata, N. Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation. Nature 387, 827-830 (1997). (Pubitemid 27270911)
    • (1997) Nature , vol.387 , Issue.6635 , pp. 827-830
    • Roach, P.L.1    Clifton, I.J.2    Hensgens, C.M.H.3    Shibata, N.4    Schofield, C.J.5    Hajdu, J.6    Baldwin, J.E.7
  • 50
    • 0037072870 scopus 로고    scopus 로고
    • Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli
    • Layer, G., Verfürth, K., Mahlitz, E. & Jahn, D. Oxygen-independent coproporphyrinogen-III oxidase HemN from Escherichia coli. J. Biol. Chem. 277, 34136-34142 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34136-34142
    • Layer, G.1    Verfürth, K.2    Mahlitz, E.3    Jahn, D.4


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