메뉴 건너뛰기




Volumn 20, Issue 8, 2013, Pages 1002-1011

N-carbamoylation of 2,4-diaminobutyrate reroutes the outcome in padanamide biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DIAMINOBUTYRIC ACID; CARBAMOYLTRANSFERASE; NONRIBOSOMAL PEPTIDE SYNTHETASE; PADANAMIDE A; PADANAMIDE B; UNCLASSIFIED DRUG;

EID: 84883157334     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2013.06.013     Document Type: Article
Times cited : (23)

References (39)
  • 1
    • 60349101699 scopus 로고    scopus 로고
    • Investigations into viomycin biosynthesis by using heterologous production in Streptomyces lividans
    • J.J. Barkei, B.M. Kevany, E.A. Felnagle, and M.G. Thomas Investigations into viomycin biosynthesis by using heterologous production in Streptomyces lividans ChemBioChem 10 2009 366 376
    • (2009) ChemBioChem , vol.10 , pp. 366-376
    • Barkei, J.J.1    Kevany, B.M.2    Felnagle, E.A.3    Thomas, M.G.4
  • 3
    • 65549086085 scopus 로고    scopus 로고
    • Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis
    • S.K. Choi, S.Y. Park, R. Kim, S.B. Kim, C.H. Lee, J.F. Kim, and S.H. Park Identification of a polymyxin synthetase gene cluster of Paenibacillus polymyxa and heterologous expression of the gene in Bacillus subtilis J. Bacteriol. 191 2009 3350 3358
    • (2009) J. Bacteriol. , vol.191 , pp. 3350-3358
    • Choi, S.K.1    Park, S.Y.2    Kim, R.3    Kim, S.B.4    Lee, C.H.5    Kim, J.F.6    Park, S.H.7
  • 4
    • 76249090018 scopus 로고    scopus 로고
    • PKS and NRPS release mechanisms
    • L. Du, and L. Lou PKS and NRPS release mechanisms Nat. Prod. Rep. 27 2010 255 278
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 255-278
    • Du, L.1    Lou, L.2
  • 7
    • 79960086415 scopus 로고    scopus 로고
    • Crystal structure of the novel PaiB transcriptional regulator from Geobacillus stearothermophilus
    • E.V. Filippova, J.S. Brunzelle, M.E. Cuff, H. Li, A. Joachimiak, and W.F. Anderson Crystal structure of the novel PaiB transcriptional regulator from Geobacillus stearothermophilus Proteins 79 2011 2578 2582
    • (2011) Proteins , vol.79 , pp. 2578-2582
    • Filippova, E.V.1    Brunzelle, J.S.2    Cuff, M.E.3    Li, H.4    Joachimiak, A.5    Anderson, W.F.6
  • 9
    • 84856406381 scopus 로고    scopus 로고
    • Lessons from the past and charting the future of marine natural products drug discovery and chemical biology
    • W.H. Gerwick, and B.S. Moore Lessons from the past and charting the future of marine natural products drug discovery and chemical biology Chem. Biol. 19 2012 85 98
    • (2012) Chem. Biol. , vol.19 , pp. 85-98
    • Gerwick, W.H.1    Moore, B.S.2
  • 10
    • 0037452723 scopus 로고    scopus 로고
    • PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin
    • B. Gust, G.L. Challis, K. Fowler, T. Kieser, and K.F. Chater PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin Proc. Natl. Acad. Sci. USA 100 2003 1541 1546
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1541-1546
    • Gust, B.1    Challis, G.L.2    Fowler, K.3    Kieser, T.4    Chater, K.F.5
  • 12
    • 0025327187 scopus 로고
    • A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production
    • M. Honjo, A. Nakayama, K. Fukazawa, K. Kawamura, K. Ando, M. Hori, and Y. Furutani A novel Bacillus subtilis gene involved in negative control of sporulation and degradative-enzyme production J. Bacteriol. 172 1990 1783 1790
    • (1990) J. Bacteriol. , vol.172 , pp. 1783-1790
    • Honjo, M.1    Nakayama, A.2    Fukazawa, K.3    Kawamura, K.4    Ando, K.5    Hori, M.6    Furutani, Y.7
  • 14
    • 78249286198 scopus 로고    scopus 로고
    • Antibacterials from the sea
    • C.C. Hughes, and W. Fenical Antibacterials from the sea Chemistry 16 2010 12512 12525
    • (2010) Chemistry , vol.16 , pp. 12512-12525
    • Hughes, C.C.1    Fenical, W.2
  • 15
    • 59949101152 scopus 로고    scopus 로고
    • Characterization of the complete zwittermicin A biosynthesis gene cluster from Bacillus cereus
    • B.M. Kevany, D.A. Rasko, and M.G. Thomas Characterization of the complete zwittermicin A biosynthesis gene cluster from Bacillus cereus Appl. Environ. Microbiol. 75 2009 1144 1155
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 1144-1155
    • Kevany, B.M.1    Rasko, D.A.2    Thomas, M.G.3
  • 16
    • 84877674775 scopus 로고    scopus 로고
    • Isolation and structure determination of new siderophore tsukubachelin B from Streptomyces sp. TM-74
    • 10.1080/14786419.14782012.14698412 Published online June 19, 2012
    • S. Kodani, F. Kobayakawa, and M. Hidaki Isolation and structure determination of new siderophore tsukubachelin B from Streptomyces sp. TM-74 Nat. Prod. Res. 27, 2013 775 781 10.1080/14786419.14782012.14698412 Published online June 19, 2012
    • (2013) Nat. Prod. Res. , vol.27 , pp. 775-781
    • Kodani, S.1    Kobayakawa, F.2    Hidaki, M.3
  • 17
    • 84869199212 scopus 로고    scopus 로고
    • Genomics-driven discovery of taiwachelin, a lipopeptide siderophore from Cupriavidus taiwanensis
    • M.F. Kreutzer, and M. Nett Genomics-driven discovery of taiwachelin, a lipopeptide siderophore from Cupriavidus taiwanensis Org. Biomol. Chem. 10 2012 9338 9343
    • (2012) Org. Biomol. Chem. , vol.10 , pp. 9338-9343
    • Kreutzer, M.F.1    Nett, M.2
  • 18
    • 84858668762 scopus 로고    scopus 로고
    • Structure and biosynthetic assembly of cupriachelin, a photoreactive siderophore from the bioplastic producer Cupriavidus necator H16
    • M.F. Kreutzer, H. Kage, and M. Nett Structure and biosynthetic assembly of cupriachelin, a photoreactive siderophore from the bioplastic producer Cupriavidus necator H16 J. Am. Chem. Soc. 134 2012 5415 5422
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 5415-5422
    • Kreutzer, M.F.1    Kage, H.2    Nett, M.3
  • 19
    • 0035951102 scopus 로고    scopus 로고
    • Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases
    • U. Linne, S. Doekel, and M.A. Marahiel Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases Biochemistry 40 2001 15824 15834
    • (2001) Biochemistry , vol.40 , pp. 15824-15834
    • Linne, U.1    Doekel, S.2    Marahiel, M.A.3
  • 22
    • 0030922377 scopus 로고    scopus 로고
    • Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli
    • P. Louis, and E.A. Galinski Characterization of genes for the biosynthesis of the compatible solute ectoine from Marinococcus halophilus and osmoregulated expression in Escherichia coli Microbiology 143 1997 1141 1149
    • (1997) Microbiology , vol.143 , pp. 1141-1149
    • Louis, P.1    Galinski, E.A.2
  • 23
    • 80051740572 scopus 로고    scopus 로고
    • Biosynthesis of himastatin: Assembly line and characterization of three cytochrome P450 enzymes involved in the post-tailoring oxidative steps
    • J. Ma, Z. Wang, H. Huang, M. Luo, D. Zuo, B. Wang, A. Sun, Y.Q. Cheng, C. Zhang, and J. Ju Biosynthesis of himastatin: assembly line and characterization of three cytochrome P450 enzymes involved in the post-tailoring oxidative steps Angew. Chem. Int. Ed. Engl. 50 2011 7797 7802
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 7797-7802
    • Ma, J.1    Wang, Z.2    Huang, H.3    Luo, M.4    Zuo, D.5    Wang, B.6    Sun, A.7    Cheng, Y.Q.8    Zhang, C.9    Ju, J.10
  • 24
    • 9444278428 scopus 로고    scopus 로고
    • Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis
    • M.A. Marahiel, T. Stachelhaus, and H.D. Mootz Modular Peptide Synthetases Involved in Nonribosomal Peptide Synthesis Chem. Rev. 97 1997 2651 2674
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 25
    • 84861618437 scopus 로고    scopus 로고
    • Characterization of madurastatin C1, a novel siderophore from Actinomadura sp
    • E. Mazzei, M. Iorio, S.I. Maffioli, M. Sosio, and S. Donadio Characterization of madurastatin C1, a novel siderophore from Actinomadura sp J. Antibiot. 65 2012 267 269
    • (2012) J. Antibiot. , vol.65 , pp. 267-269
    • Mazzei, E.1    Iorio, M.2    Maffioli, S.I.3    Sosio, M.4    Donadio, S.5
  • 26
    • 34250704344 scopus 로고    scopus 로고
    • Combinatorial biosynthesis for drug development
    • H.G. Menzella, and C.D. Reeves Combinatorial biosynthesis for drug development Curr. Opin. Microbiol. 10 2007 238 245
    • (2007) Curr. Opin. Microbiol. , vol.10 , pp. 238-245
    • Menzella, H.G.1    Reeves, C.D.2
  • 28
    • 79960954444 scopus 로고    scopus 로고
    • Isolation and Characterization of Actinoramides A-C, Highly Modified Peptides from a Marine Streptomyces sp
    • S.J. Nam, C.A. Kauffman, P.R. Jensen, and W. Fenical Isolation and Characterization of Actinoramides A-C, Highly Modified Peptides from a Marine Streptomyces sp Tetrahedron 67 2011 6707 6712
    • (2011) Tetrahedron , vol.67 , pp. 6707-6712
    • Nam, S.J.1    Kauffman, C.A.2    Jensen, P.R.3    Fenical, W.4
  • 30
    • 84861914244 scopus 로고    scopus 로고
    • Hijacking a hydroxyethyl unit from a central metabolic ketose into a nonribosomal peptide assembly line
    • C. Peng, J.Y. Pu, L.Q. Song, X.H. Jian, M.C. Tang, and G.L. Tang Hijacking a hydroxyethyl unit from a central metabolic ketose into a nonribosomal peptide assembly line Proc. Natl. Acad. Sci. USA 109 2012 8540 8545
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 8540-8545
    • Peng, C.1    Pu, J.Y.2    Song, L.Q.3    Jian, X.H.4    Tang, M.C.5    Tang, G.L.6
  • 31
    • 79951595684 scopus 로고    scopus 로고
    • Cloning, sequencing and characterization of the biosynthetic gene cluster of sanglifehrin A, a potent cyclophilin inhibitor
    • X. Qu, N. Jiang, F. Xu, L. Shao, G. Tang, B. Wilkinson, and W. Liu Cloning, sequencing and characterization of the biosynthetic gene cluster of sanglifehrin A, a potent cyclophilin inhibitor Mol. Biosyst. 7 2011 852 861
    • (2011) Mol. Biosyst. , vol.7 , pp. 852-861
    • Qu, X.1    Jiang, N.2    Xu, F.3    Shao, L.4    Tang, G.5    Wilkinson, B.6    Liu, W.7
  • 32
    • 37449003424 scopus 로고    scopus 로고
    • The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate and L-norvaline reveal the enzyme's catalytic mechanism
    • R. Sankaranarayanan, M.M. Cherney, L.T. Cherney, C.R. Garen, F. Moradian, and M.N. James The crystal structures of ornithine carbamoyltransferase from Mycobacterium tuberculosis and its ternary complex with carbamoyl phosphate and L-norvaline reveal the enzyme's catalytic mechanism J. Mol. Biol. 375 2008 1052 1063
    • (2008) J. Mol. Biol. , vol.375 , pp. 1052-1063
    • Sankaranarayanan, R.1    Cherney, M.M.2    Cherney, L.T.3    Garen, C.R.4    Moradian, F.5    James, M.N.6
  • 33
    • 0037384426 scopus 로고    scopus 로고
    • The sypA, sypS, and sypC synthetase genes encode twenty-two modules involved in the nonribosomal peptide synthesis of syringopeptin by Pseudomonas syringae pv. Syringae B301D
    • B.K. Scholz-Schroeder, J.D. Soule, and D.C. Gross The sypA, sypS, and sypC synthetase genes encode twenty-two modules involved in the nonribosomal peptide synthesis of syringopeptin by Pseudomonas syringae pv. syringae B301D Mol. Plant Microbe Interact. 16 2003 271 280
    • (2003) Mol. Plant Microbe Interact. , vol.16 , pp. 271-280
    • Scholz-Schroeder, B.K.1    Soule, J.D.2    Gross, D.C.3
  • 34
    • 79960880056 scopus 로고    scopus 로고
    • Structure and biosynthesis of amychelin, an unusual mixed-ligand siderophore from Amycolatopsis sp. AA4
    • M.R. Seyedsayamdost, M.F. Traxler, S.L. Zheng, R. Kolter, and J. Clardy Structure and biosynthesis of amychelin, an unusual mixed-ligand siderophore from Amycolatopsis sp. AA4 J. Am. Chem. Soc. 133 2011 11434 11437
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 11434-11437
    • Seyedsayamdost, M.R.1    Traxler, M.F.2    Zheng, S.L.3    Kolter, R.4    Clardy, J.5
  • 35
    • 38149064397 scopus 로고    scopus 로고
    • Glyceryl-S-acyl carrier protein as an intermediate in the biosynthesis of tetronate antibiotics
    • Y. Sun, H. Hong, F. Gillies, J.B. Spencer, and P.F. Leadlay Glyceryl-S-acyl carrier protein as an intermediate in the biosynthesis of tetronate antibiotics ChemBioChem 9 2008 150 156
    • (2008) ChemBioChem , vol.9 , pp. 150-156
    • Sun, Y.1    Hong, H.2    Gillies, F.3    Spencer, J.B.4    Leadlay, P.F.5
  • 37
    • 84872517716 scopus 로고    scopus 로고
    • Nahuoic acid A produced by a Streptomyces sp. Isolated from a marine sediment is a selective SAM-competitive inhibitor of the histone methyltransferase SETD8
    • D.E. Williams, D.S. Dalisay, F. Li, J. Amphlett, W. Maneerat, M.A. Chavez, Y.A. Wang, T. Matainaho, W. Yu, and P.J. Brown Nahuoic acid A produced by a Streptomyces sp. isolated from a marine sediment is a selective SAM-competitive inhibitor of the histone methyltransferase SETD8 Org. Lett. 15 2013 414 417
    • (2013) Org. Lett. , vol.15 , pp. 414-417
    • Williams, D.E.1    Dalisay, D.S.2    Li, F.3    Amphlett, J.4    Maneerat, W.5    Chavez, M.A.6    Wang, Y.A.7    Matainaho, T.8    Yu, W.9    Brown, P.J.10
  • 38
    • 0034643859 scopus 로고    scopus 로고
    • The FK520 gene cluster of Streptomyces hygroscopicus var. Ascomyceticus (ATCC 14891) contains genes for biosynthesis of unusual polyketide extender units
    • K. Wu, L. Chung, W.P. Revill, L. Katz, and C.D. Reeves The FK520 gene cluster of Streptomyces hygroscopicus var. ascomyceticus (ATCC 14891) contains genes for biosynthesis of unusual polyketide extender units Gene 251 2000 81 90
    • (2000) Gene , vol.251 , pp. 81-90
    • Wu, K.1    Chung, L.2    Revill, W.P.3    Katz, L.4    Reeves, C.D.5
  • 39
    • 33744771027 scopus 로고    scopus 로고
    • Utilization of the methoxymalonyl-acyl carrier protein biosynthesis locus for cloning the oxazolomycin biosynthetic gene cluster from Streptomyces albus JA3453
    • C. Zhao, J. Ju, S.D. Christenson, W.C. Smith, D. Song, X. Zhou, B. Shen, and Z. Deng Utilization of the methoxymalonyl-acyl carrier protein biosynthesis locus for cloning the oxazolomycin biosynthetic gene cluster from Streptomyces albus JA3453 J. Bacteriol. 188 2006 4142 4147
    • (2006) J. Bacteriol. , vol.188 , pp. 4142-4147
    • Zhao, C.1    Ju, J.2    Christenson, S.D.3    Smith, W.C.4    Song, D.5    Zhou, X.6    Shen, B.7    Deng, Z.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.