메뉴 건너뛰기




Volumn 6, Issue 8, 1999, Pages 493-505

The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases

Author keywords

Adenylation domain; Binding pocket; Nonribosomal peptide synthetase; Signature sequence; Substrate specificity

Indexed keywords


EID: 0033179468     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(99)80082-9     Document Type: Article
Times cited : (1027)

References (41)
  • 1
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel, M.A., Stachelhaus, T. & Mootz, H.D. (1997). Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97, 2651-2673.
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2673
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 3
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane, D.E., Walsh, C.T. & Khosla, C. (1998). Harnessing the biosynthetic code: Combinations, permutations, and mutations. Science 282, 63-68.
    • (1998) Science , vol.282 , pp. 63-68
    • Cane, D.E.1    Walsh, C.T.2    Khosla, C.3
  • 4
    • 0031322936 scopus 로고    scopus 로고
    • Biosynthetic systems for nonribosomal peptide antibiotic assembly
    • Mootz, H.D. & Marahiel, M.A. (1997). Biosynthetic systems for nonribosomal peptide antibiotic assembly. Curr. Opin. Chem. Biol. 1, 543-551.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 543-551
    • Mootz, H.D.1    Marahiel, M.A.2
  • 5
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthesis enzymes for assembly of the virulence-conferring siderophore mycobactin
    • Quadri, L.E.N., Sello, J., Keating, T.A., Weinreb, P.H. & Walsh, C.T. (1998). Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthesis enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5, 631-645.
    • (1998) Chem. Biol. , vol.5 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 6
    • 0032193282 scopus 로고    scopus 로고
    • Iron acquisition in plaque: Molecular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis
    • Gehring, A.M., et al., & Perry, R.D. (1998). Iron acquisition in plaque: Molecular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis. Chem. Biol. 5, 573-586.
    • (1998) Chem. Biol. , vol.5 , pp. 573-586
    • Gehring, A.M.1    Perry, R.D.2
  • 7
    • 0030294470 scopus 로고    scopus 로고
    • A new enzyme superfamily - the phosphopantetheinyl transferases
    • Lambalot, R.H., et al., & Walsh, C.T. (1996). A new enzyme superfamily - the phosphopantetheinyl transferases. Chem. Biol. 3, 923-936.
    • (1996) Chem. Biol. , vol.3 , pp. 923-936
    • Lambalot, R.H.1    Walsh, C.T.2
  • 8
  • 9
    • 0028908601 scopus 로고
    • Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA
    • Stachelhaus, T. & Marahiel, M.A. (1995). Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA. J. Biol. Chem. 270, 6163-6169.
    • (1995) J. Biol. Chem. , vol.270 , pp. 6163-6169
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 10
    • 0030669091 scopus 로고    scopus 로고
    • The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains
    • Mootz, H.D. & Marahiel, M.A. (1997). The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179, 6843-6850.
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 11
    • 0028896569 scopus 로고
    • Expression of an active adenylate-forming domain of peptide synthetases corresponding to acetyl-CoA-synthetases
    • Dieckmann, R., Lee, Y-O., van Liempt, H., von Döhren, H. & Kleinkauf, H. (1995). Expression of an active adenylate-forming domain of peptide synthetases corresponding to acetyl-CoA-synthetases. FEBS Lett. 357, 212-216.
    • (1995) FEBS Lett. , vol.357 , pp. 212-216
    • Dieckmann, R.1    Lee, Y.-O.2    Van Liempt, H.3    Von Döhren, H.4    Kleinkauf, H.5
  • 12
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti, E., Franks, N.P. & Brick, P. (1996). Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4, 287-298.
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 13
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin
    • Conti, E., Stachelhaus, T., Marahiel, M.A. & Brick, P. (1997). Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S. EMBO J. 16, 4174-4183.
    • (1997) S. EMBO J. , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 14
    • 0028226896 scopus 로고
    • Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis
    • Gocht, M. & Marahiel, M.A. (1994). Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis. J. Bacteriol. 176, 2654-2662.
    • (1994) J. Bacteriol. , vol.176 , pp. 2654-2662
    • Gocht, M.1    Marahiel, M.A.2
  • 15
    • 0028964280 scopus 로고
    • A small gene, designated comS, located within the coding region of the fourth amino acid-activation domain of srfA, is required for competence developement in Bacillus subtilis
    • Hamoen, L.W., Eshuis, H., Jongbloed, J., Venema, G. & van Sinderen, D. (1994). A small gene, designated comS, located within the coding region of the fourth amino acid-activation domain of srfA, is required for competence developement in Bacillus subtilis. Mol. Microbiol. 15, 55-63.
    • (1994) Mol. Microbiol. , vol.15 , pp. 55-63
    • Hamoen, L.W.1    Eshuis, H.2    Jongbloed, J.3    Venema, G.4    Van Sinderen, D.5
  • 16
    • 0028949429 scopus 로고
    • Three conserved glycine residues in valine activation of gramicidin S synthetase 2 from Bacillus brevis
    • Saito, M., Hori, K., Kurotsu, T., Kanda, M. & Saito, Y. (1995). Three conserved glycine residues in valine activation of gramicidin S synthetase 2 from Bacillus brevis. J. Biochem. 117, 276-282.
    • (1995) J. Biochem. , vol.117 , pp. 276-282
    • Saito, M.1    Hori, K.2    Kurotsu, T.3    Kanda, M.4    Saito, Y.5
  • 17
    • 0028243638 scopus 로고
    • Identification of the ATP-binding site in tyrocidine synthetase 1 by selective modification with fluorescein 5′-isothiocyanate
    • Pavela-Vrancic, M., Pfeifer, E., Schröder, W., von Döhren, H. & Kleinkauf, H. (1994). Identification of the ATP-binding site in tyrocidine synthetase 1 by selective modification with fluorescein 5′-isothiocyanate. J. Biol. Chem. 269, 14962-14966.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14962-14966
    • Pavela-Vrancic, M.1    Pfeifer, E.2    Schröder, W.3    Von Döhren, H.4    Kleinkauf, H.5
  • 18
    • 0028227188 scopus 로고
    • ATP binding in peptide synthetases: Determination of contact sites of the adenine moiety by photoaffinity labeling of tyrocidine synthetase 1 with 2-azidoadenosine triphosphate
    • Pavela-Vrancic, M., Pfeifer, E., van Liempt, H., Schäfer, H-J., von Döhren, H. & Kleinkauf, H. (1994). ATP binding in peptide synthetases: Determination of contact sites of the adenine moiety by photoaffinity labeling of tyrocidine synthetase 1 with 2-azidoadenosine triphosphate. Biochemistry 33, 6276-6283.
    • (1994) Biochemistry , vol.33 , pp. 6276-6283
    • Pavela-Vrancic, M.1    Pfeifer, E.2    Van Liempt, H.3    Schäfer, H.-J.4    Von Döhren, H.5    Kleinkauf, H.6
  • 19
    • 0039194307 scopus 로고    scopus 로고
    • Streptogramin B biosynthesis in Streptomyces pristinaespiralis and Streptomyces virginae: Molecular characterization of the last structural peptide synthetase gene
    • de Crécy-Lagard, V., et al., & Blanc, V. (1997). Streptogramin B biosynthesis in Streptomyces pristinaespiralis and Streptomyces virginae: Molecular characterization of the last structural peptide synthetase gene. Antimicrob. Agents Chemother. 41, 1904-1909.
    • (1997) Antimicrob. Agents Chemother. , vol.41 , pp. 1904-1909
    • De Crécy-Lagard, V.1    Blanc, V.2
  • 22
    • 0027289507 scopus 로고
    • Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis
    • Cosmina, P., Rodriguez, F., de Ferra, F., Perego, M., Venema, G. & van Sinderen, D. (1993). Sequence and analysis of the genetic locus responsible for surfactin synthesis in Bacillus subtilis. Mol. Microbiol. 8, 821-831.
    • (1993) Mol. Microbiol. , vol.8 , pp. 821-831
    • Cosmina, P.1    Rodriguez, F.2    De Ferra, F.3    Perego, M.4    Venema, G.5    Van Sinderen, D.6
  • 23
    • 0026588298 scopus 로고
    • Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes
    • Turgay, K., Krause, M. & Marahiel, M.A. (1992). Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6, 529-546.
    • (1992) Mol. Microbiol. , Issue.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 25
    • 0032955583 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin
    • Konz, D., Dökel, S. & Marahiel, M.A. (1999). Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. J. Bacteriol. 181, 133-140.
    • (1999) J. Bacteriol. , vol.181 , pp. 133-140
    • Konz, D.1    Dökel, S.2    Marahiel, M.A.3
  • 26
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T., et al., & Barrell, B.G. (1998). Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393, 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Barrell, B.G.2
  • 27
    • 0032033520 scopus 로고    scopus 로고
    • Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic
    • van Wageningen, A.M., et al., & Solenberg, P.J. (1998). Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic. Chem. Biol. 5, 155-162.
    • (1998) Chem. Biol. , vol.5 , pp. 155-162
    • Van Wageningen, A.M.1    Solenberg, P.J.2
  • 28
    • 0032782572 scopus 로고    scopus 로고
    • Structural and functional organization of the fengycin synthetase multienzyme system from Bacillus subtilis b213 and A1/3
    • Steller, S., et al., & Vater, J. (1999). Structural and functional organization of the fengycin synthetase multienzyme system from Bacillus subtilis b213 and A1/3. Chem. Biol. 6, 31-41.
    • (1999) Chem. Biol. , vol.6 , pp. 31-41
    • Steller, S.1    Vater, J.2
  • 29
    • 0015209453 scopus 로고
    • Attempt to map a process evolution of peptide biosynthesis
    • Lipmann, F. (1971). Attempt to map a process evolution of peptide biosynthesis. Science 173, 875-884.
    • (1971) Science , vol.173 , pp. 875-884
    • Lipmann, F.1
  • 30
    • 0027156609 scopus 로고
    • Analysis of a mutant amino acid-activating domain of surfactin synthetase bearing a serine to alanine substitution at the site of carboxyl thioester formation
    • Vollenbroich, D., Kluge, B., D'Souza, C., Zuber, P., & Vater, J. (1993). Analysis of a mutant amino acid-activating domain of surfactin synthetase bearing a serine to alanine substitution at the site of carboxyl thioester formation. FEBS Lett. 325, 220-224.
    • (1993) FEBS Lett. , vol.325 , pp. 220-224
    • Vollenbroich, D.1    Kluge, B.2    D'Souza, C.3    Zuber, P.4    Vater, J.5
  • 31
    • 0027284693 scopus 로고
    • Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase: Effects on surfactin production and competence development in Bacillus subtilis
    • D'Souza, C., Nakano, M.M., Corbell, N. & Zuber, P. (1993). Amino-acylation site mutations in amino acid-activating domains of surfactin synthetase: Effects on surfactin production and competence development in Bacillus subtilis. J. Bacteriol. 175, 3502-3510.
    • (1993) J. Bacteriol. , vol.175 , pp. 3502-3510
    • D'Souza, C.1    Nakano, M.M.2    Corbell, N.3    Zuber, P.4
  • 32
    • 0024243827 scopus 로고
    • Identification of a genetic locus required for biosynthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis
    • Nakano, M.M., Marahiel, M.A. & Zuber, P. (1988). Identification of a genetic locus required for biosynthesis of the lipopeptide antibiotic surfactin in Bacillus subtilis. J. Bacteriol. 170, 5662-5668.
    • (1988) J. Bacteriol. , vol.170 , pp. 5662-5668
    • Nakano, M.M.1    Marahiel, M.A.2    Zuber, P.3
  • 33
    • 84907114378 scopus 로고
    • Peptide antibiotics, β-lactams, and related compounds
    • Kleinkauf, H. & von Döhren, H. (1988). Peptide antibiotics, β-lactams, and related compounds. CRC Crit. Rev. Biotechnol. 8, 1-32.
    • (1988) CRC Crit. Rev. Biotechnol. , vol.8 , pp. 1-32
    • Kleinkauf, H.1    Von Döhren, H.2
  • 34
    • 0027250118 scopus 로고
    • Substrate specificities of cyclosporin synthetase and peptolide SDZ214-103 synthetase
    • Lawen, A. & Traber, R. (1993). Substrate specificities of cyclosporin synthetase and peptolide SDZ214-103 synthetase. J. Biol. Chem. 268, 20452-20465.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20452-20465
    • Lawen, A.1    Traber, R.2
  • 35
    • 0028283317 scopus 로고
    • In vitro biosynthesis of ring-extended cyclosporins
    • Lawen, A., Traber, R., Reuille, R. & Ponelle, M. (1994). In vitro biosynthesis of ring-extended cyclosporins. Biochem. J. 300, 395-399.
    • (1994) Biochem. J. , vol.300 , pp. 395-399
    • Lawen, A.1    Traber, R.2    Reuille, R.3    Ponelle, M.4
  • 37
    • 0000182975 scopus 로고
    • XL1-Blue: A high efficiency plasmid transforming recA E. Coli strain with β-galactosidase selection
    • Bullock, W.O., Fernandez, J.M. & Short, J.M. (1987). XL1-Blue: A high efficiency plasmid transforming recA E. Coli strain with β-galactosidase selection. Biotechniques 5, 376-379.
    • (1987) Biotechniques , Issue.5 , pp. 376-379
    • Bullock, W.O.1    Fernandez, J.M.2    Short, J.M.3
  • 38
    • 0015580176 scopus 로고
    • Chromosomal location of pleiotropic sporulation mutations in Bacillus subtilis
    • Hoch, J.A. & Mathews, J. (1973). Chromosomal location of pleiotropic sporulation mutations in Bacillus subtilis. Genetics 73, 215-228.
    • (1973) Genetics , vol.73 , pp. 215-228
    • Hoch, J.A.1    Mathews, J.2
  • 39
    • 0030292865 scopus 로고    scopus 로고
    • Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases
    • Stachelhaus, T., Hüser, A. & Marahiel, M.A. (1996). Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases. Chem. Biol. 3, 913-921.
    • (1996) Chem. Biol. , vol.3 , pp. 913-921
    • Stachelhaus, T.1    Hüser, A.2    Marahiel, M.A.3
  • 40
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 41
    • 0025342577 scopus 로고
    • Unified approach to alignment and phylogenies
    • Hein, J.J. (1990). Unified approach to alignment and phylogenies. Methods Enzymol. 183, 626-645.
    • (1990) Methods Enzymol. , vol.183 , pp. 626-645
    • Hein, J.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.