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Volumn 14, Issue 10, 2005, Pages 2702-2712

Parallel interrogation of covalent intermediates in the biosynthesis of gramicidin S using high-resolution mass spectrometry

Author keywords

Covalent intermediates; Fourier transform mass spectrometry; Gramicidin S; Nonribosomal peptide synthesis

Indexed keywords

AMINO ACID; CYANOGEN BROMIDE; GRAMICIDIN S;

EID: 25144485731     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.051553705     Document Type: Article
Times cited : (19)

References (28)
  • 1
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • Belshaw, P.J., Walsh, C.T., and 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
  • 2
    • 0036161991 scopus 로고    scopus 로고
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis
    • Bergendahl, V., Linne, U., and Marahiel, M.A. 2002. Mutational analysis of the C-domain in nonribosomal peptide synthesis. Eur. J. Biochem. 269: 620-629.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 620-629
    • Bergendahl, V.1    Linne, U.2    Marahiel, M.A.3
  • 3
    • 0032863043 scopus 로고    scopus 로고
    • Hydropathic influences on the quantification of equine heart cytochrome c using relative ion abundance measurements by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry
    • Gordon, E.F., Mansoori, B.A., Carroll, C.F., and Muddiman, D.C. 1999. Hydropathic influences on the quantification of equine heart cytochrome c using relative ion abundance measurements by electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry. J. Mass Spectrom. 34: 1055-1062.
    • (1999) J. Mass Spectrom. , vol.34 , pp. 1055-1062
    • Gordon, E.F.1    Mansoori, B.A.2    Carroll, C.F.3    Muddiman, D.C.4
  • 4
    • 6044236054 scopus 로고    scopus 로고
    • Mass spectrometric interrogation of thioester-bound intermediates in the initial stages of epothilone biosynthesis
    • Hicks, L.M., O'Connor, S.E., Mazur, M.T., Walsh, C.T., and Kelleher, N.L. 2004.Mass spectrometric interrogation of thioester-bound intermediates in the initial stages of epothilone biosynthesis. Chem. Biol. 11: 327-335.
    • (2004) Chem. Biol. , vol.11 , pp. 327-335
    • Hicks, L.M.1    O'Connor, S.E.2    Mazur, M.T.3    Walsh, C.T.4    Kelleher, N.L.5
  • 6
    • 0031467961 scopus 로고    scopus 로고
    • Identification of modification sites in large biomolecules by stable isotope labeling and tandem high resolution mass spectrometry
    • Kelleher, N.L., Nicewonger, R.B., Begley, T.P., and McLafferty, F.W. 1997. Identification of modification sites in large biomolecules by stable isotope labeling and tandem high resolution mass spectrometry. J. Biol. Chem. 272: 32215-32220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 32215-32220
    • Kelleher, N.L.1    Nicewonger, R.B.2    Begley, T.P.3    McLafferty, F.W.4
  • 9
    • 0035826653 scopus 로고    scopus 로고
    • Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase
    • Luo, L. and Walsh, C.T. 2001. Kinetic analysis of three activated phenylalanyl intermediates generated by the initiation module PheATE of gramicidin S synthetase. Biochemistry 40: 5329-5337.
    • (2001) Biochemistry , vol.40 , pp. 5329-5337
    • Luo, L.1    Walsh, C.T.2
  • 10
    • 0035861070 scopus 로고    scopus 로고
    • Substrate recognition and selection by the initiation module PheATE of gramicidin S synthetase
    • Luo, L., Burkart, M.D., Stachelhaus, T., and Walsh, C.T. 2001. Substrate recognition and selection by the initiation module PheATE of gramicidin S synthetase. J. Am. Chem. Soc. 123: 11208-11218.
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 11208-11218
    • Luo, L.1    Burkart, M.D.2    Stachelhaus, T.3    Walsh, C.T.4
  • 11
    • 0344823693 scopus 로고    scopus 로고
    • Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase
    • Mazur, M.T., Walsh, C.T., and Kelleher, N.L. 2003. Site-specific observation of acyl intermediate processing in thiotemplate biosynthesis by Fourier transform mass spectrometry: The polyketide module of yersiniabactin synthetase. Biochemistry 42: 13393-13400.
    • (2003) Biochemistry , vol.42 , pp. 13393-13400
    • Mazur, M.T.1    Walsh, C.T.2    Kelleher, N.L.3
  • 12
    • 0000323481 scopus 로고
    • High-resolution tandem FT mass spectrometry above 10 kDa
    • McLafferty, F.W. 1994. High-resolution tandem FT mass spectrometry above 10 kDa. Acc. Chem. Res. 27: 379-386.
    • (1994) Acc. Chem. Res. , vol.27 , pp. 379-386
    • McLafferty, F.W.1
  • 13
    • 6044254962 scopus 로고    scopus 로고
    • Kinetic and regiospecific interrogation of covalent intermediates in the nonribosomal peptide synthesis of yersiniabactin
    • McLoughlin, S. and Kelleher, N.L. 2004. Kinetic and regiospecific interrogation of covalent intermediates in the nonribosomal peptide synthesis of yersiniabactin. J. Am. Chem. Soc. 126: 13265-13275.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 13265-13275
    • McLoughlin, S.1    Kelleher, N.L.2
  • 14
    • 5644231221 scopus 로고    scopus 로고
    • Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FTICR MS)
    • Medzihradszky, K.F., Zhang, X., Chalkley, R.J., Guan, S., McFarland, M.A., Chalmers, M.J., Marshall, A.G., Diaz, R.L., Allis, C.D., and Burlingame, A.L. 2004. Characterization of Tetrahymena histone H2B variants and posttranslational populations by electron capture dissociation (ECD) Fourier transform ion cyclotron mass spectrometry (FTICR MS). Mol. Cell Proteomics 3: 872-886.
    • (2004) Mol. Cell Proteomics , vol.3 , pp. 872-886
    • Medzihradszky, K.F.1    Zhang, X.2    Chalkley, R.J.3    Guan, S.4    McFarland, M.A.5    Chalmers, M.J.6    Marshall, A.G.7    Diaz, R.L.8    Allis, C.D.9    Burlingame, A.L.10
  • 16
    • 1642272372 scopus 로고    scopus 로고
    • Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry
    • Pesavento, J.J., Kim, Y.B., Taylor, G.K., and Kelleher, N.L. 2004. Shotgun annotation of histone modifications: A new approach for streamlined characterization of proteins by top down mass spectrometry. J. Am. Chem. Soc. 126: 3386-3387.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 3386-3387
    • Pesavento, J.J.1    Kim, Y.B.2    Taylor, G.K.3    Kelleher, N.L.4
  • 17
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer, D., Mootz, H.D., Linne, U., and Marahiel, M.A. 2002. Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl. Acad. Sci. 99: 14083-14088.
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 14083-14088
    • Schwarzer, D.1    Mootz, H.D.2    Linne, U.3    Marahiel, M.A.4
  • 18
    • 14844362054 scopus 로고    scopus 로고
    • Molecular mechanisms underlying nonribosomal peptide synthesis: Approaches to new antibiotics
    • Sieber, S.A. and Marahiel, M.A. 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
  • 19
    • 0028908601 scopus 로고
    • Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA
    • Stachelhaus, T. and 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
  • 20
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus, T. and Walsh, C.T. 2000. Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry 39: 5775-5787.
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2
  • 21
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis
    • Stachelhaus, T., Mootz, H.D., Bergendahl, V., and Marahiel, M.A. 1998. Peptide bond formation in nonribosomal peptide biosynthesis. J. Biol. Chem. 273: 22773-22781.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 22
    • 0021824426 scopus 로고
    • Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions
    • Vater, J., Mallow, N., Gerhardt, S., Gadow, A., and Kleinkauf, H. 1985. Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions. Biochemistry 24: 2022-2027.
    • (1985) Biochemistry , vol.24 , pp. 2022-2027
    • Vater, J.1    Mallow, N.2    Gerhardt, S.3    Gadow, A.4    Kleinkauf, H.5
  • 23
    • 0023642127 scopus 로고
    • Formation of D-Phe-Pro-Val-Cyclo-Orn by gramicidin-S synthetase in the absence of L-leucine
    • Vater, J., Schlumbohm, W., Palacz, Z., Salnikow, J., Gadow, A., and Kleinkauf, H. 1987. Formation of D-Phe-Pro-Val-Cyclo-Orn by gramicidin-S synthetase in the absence of L-leucine. Eur. J. Biochem. 163: 297-302.
    • (1987) Eur. J. Biochem. , vol.163 , pp. 297-302
    • Vater, J.1    Schlumbohm, W.2    Palacz, Z.3    Salnikow, J.4    Gadow, A.5    Kleinkauf, H.6
  • 25
    • 0032502031 scopus 로고    scopus 로고
    • Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase
    • Weinreb, P.H., Quadri, L.E.N., Walsh, C.T., and Zuber, P. 1998. Stoichiometry and specificity of in vitro phosphopantetheinylation and aminoacylation of the valine-activating module of surfactin synthetase. Biochemistry 37: 1575-1584.
    • (1998) Biochemistry , vol.37 , pp. 1575-1584
    • Weinreb, P.H.1    Quadri, L.E.N.2    Walsh, C.T.3    Zuber, P.4
  • 26
    • 4644278719 scopus 로고    scopus 로고
    • Type II thioesterase restores activity of a NRPS module stalled with and aminoacyl-S-enzyme that cannot be elongated
    • Yeh, E., Kohli, R.M., Bruner, S.D., and Walsh, C.T. 2004. Type II thioesterase restores activity of a NRPS module stalled with and aminoacyl-S-enzyme that cannot be elongated. Chem. Bio. Chem. 5: 1290-1293.
    • (2004) Chem. Bio. Chem. , vol.5 , pp. 1290-1293
    • Yeh, E.1    Kohli, R.M.2    Bruner, S.D.3    Walsh, C.T.4
  • 27
    • 0029826481 scopus 로고    scopus 로고
    • Characterization of unstable intermediates and oxidized products formed during cyanogen bromide cleavage of peptides and proteins by electrospray mass spectrometry
    • Zhang, X., Dillen, L., Vanhoutte, K., Van Dongen, W., Esmans, E., and Claeys, M. 1996. Characterization of unstable intermediates and oxidized products formed during cyanogen bromide cleavage of peptides and proteins by electrospray mass spectrometry. Anal. Chem. 68: 3422-3430.
    • (1996) Anal. Chem. , vol.68 , pp. 3422-3430
    • Zhang, X.1    Dillen, L.2    Vanhoutte, K.3    Van Dongen, W.4    Esmans, E.5    Claeys, M.6
  • 28
    • 0347123341 scopus 로고    scopus 로고
    • Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry
    • Zhang, L., Freitas, M.A., Wickham, J., Parthun, M.R., Klisovic, M.I., Marcucci, G., and Byrd, J.C. 2004. Differential expression of histone post-translational modifications in acute myeloid and chronic lymphocytic leukemia determined by high-pressure liquid chromatography and mass spectrometry. J. Am. Soc. Mass Spectrom. 15: 77-86.
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 77-86
    • Zhang, L.1    Freitas, M.A.2    Wickham, J.3    Parthun, M.R.4    Klisovic, M.I.5    Marcucci, G.6    Byrd, J.C.7


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