메뉴 건너뛰기




Volumn 275, Issue 21, 2008, Pages 5343-5354

Role of DptE and DptF in the lipidation reaction of daptomycin

Author keywords

Acidic lipopeptide antibiotics; AMP ligase; Daptomycin; Lipidation reaction; Nonribosomal peptide synthetases

Indexed keywords

A 54145; ACYL CARRIER PROTEIN; ADENOSINE TRIPHOSPHATE; ANTIBIOTIC AGENT; DAPTOMYCIN; FATTY ACID; LIPOPEPTIDE; LONG CHAIN FATTY ACID; PEPTIDE SYNTHASE; UNCLASSIFIED DRUG;

EID: 53849091701     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06664.x     Document Type: Article
Times cited : (64)

References (44)
  • 1
    • 21044448952 scopus 로고    scopus 로고
    • Daptomycin biosynthesis in Streptomyces roseosporus: Cloning and analysis of the gene cluster and revision of peptide stereochemistry
    • Miao V, Coeffet-Legal MF, Brian P, Brost R, Penn J, Whiting A, Martin S, Ford R, Parr I, Bouchard M et al. (2005) Daptomycin biosynthesis in Streptomyces roseosporus: cloning and analysis of the gene cluster and revision of peptide stereochemistry. Microbiology 151, 1507 1523.
    • (2005) Microbiology , vol.151 , pp. 1507-1523
    • Miao, V.1    Coeffet-Legal, M.F.2    Brian, P.3    Brost, R.4    Penn, J.5    Whiting, A.6    Martin, S.7    Ford, R.8    Parr, I.9    Bouchard, M.10
  • 3
    • 0025325794 scopus 로고
    • A54145, a new lipopeptide antibiotic complex: Microbial and chemical modification
    • Fukuda DS, Debono M, Molloy RM Mynderse JS (1990) A54145, a new lipopeptide antibiotic complex: microbial and chemical modification. J Antibiot 43, 601 606.
    • (1990) J Antibiot , vol.43 , pp. 601-606
    • Fukuda, D.S.1    Debono, M.2    Molloy, R.M.3    Mynderse, J.S.4
  • 5
    • 21344467263 scopus 로고    scopus 로고
    • An acyl-CoA dehydrogenase is involved in the formation of the Delta cis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis
    • Heinzelmann E, Berger S, Muller C, Hartner T, Poralla K, Wohlleben W Schwartz D (2005) An acyl-CoA dehydrogenase is involved in the formation of the Delta cis3 double bond in the acyl residue of the lipopeptide antibiotic friulimicin in Actinoplanes friuliensis. Microbiology 151, 1963 1974.
    • (2005) Microbiology , vol.151 , pp. 1963-1974
    • Heinzelmann, E.1    Berger, S.2    Muller, C.3    Hartner, T.4    Poralla, K.5    Wohlleben, W.6    Schwartz, D.7
  • 6
    • 0033856211 scopus 로고    scopus 로고
    • Friulimicins: Novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. II. Isolation and structural characterization
    • Vertesy L, Ehlers E, Kogler H, Kurz M, Meiwes J, Seibert G, Vogel M Hammann P (2000) Friulimicins: novel lipopeptide antibiotics with peptidoglycan synthesis inhibiting activity from Actinoplanes friuliensis sp. nov. II. Isolation and structural characterization. J Antibiot 53, 816 827.
    • (2000) J Antibiot , vol.53 , pp. 816-827
    • Vertesy, L.1    Ehlers, E.2    Kogler, H.3    Kurz, M.4    Meiwes, J.5    Seibert, G.6    Vogel, M.7    Hammann, P.8
  • 7
    • 29244459093 scopus 로고    scopus 로고
    • Natural products to drugs: Daptomycin and related lipopeptide antibiotics
    • Baltz RH, Miao V Wrigley SK (2005) Natural products to drugs: daptomycin and related lipopeptide antibiotics. Nat Prod Rep 22, 717 741.
    • (2005) Nat Prod Rep , vol.22 , pp. 717-741
    • Baltz, R.H.1    Miao, V.2    Wrigley, S.K.3
  • 8
    • 33748262119 scopus 로고    scopus 로고
    • Chemoenzymatic design of acidic lipopeptide hybrids: New insights into the structure-activity relationship of daptomycin and A54145
    • Kopp F, Grunewald J, Mahlert C Marahiel MA (2006) Chemoenzymatic design of acidic lipopeptide hybrids: new insights into the structure-activity relationship of daptomycin and A54145. Biochemistry 45, 10474 10481.
    • (2006) Biochemistry , vol.45 , pp. 10474-10481
    • Kopp, F.1    Grunewald, J.2    Mahlert, C.3    Marahiel, M.A.4
  • 11
    • 0037524493 scopus 로고    scopus 로고
    • Nonribosomal peptides: From genes to products
    • Schwarzer D, Finking R Marahiel MA (2003) Nonribosomal peptides: from genes to products. Nat Prod Rep 20, 275 287.
    • (2003) Nat Prod Rep , vol.20 , pp. 275-287
    • Schwarzer, D.1    Finking, R.2    Marahiel, M.A.3
  • 12
    • 37549038629 scopus 로고    scopus 로고
    • Where chemistry meets biology: The chemoenzymatic synthesis of nonribosomal peptides and polyketides
    • Kopp F Marahiel MA (2007) Where chemistry meets biology: the chemoenzymatic synthesis of nonribosomal peptides and polyketides. Curr Opin Biotechnol 18, 513 520.
    • (2007) Curr Opin Biotechnol , vol.18 , pp. 513-520
    • Kopp, F.1    Marahiel, M.A.2
  • 13
    • 34250710858 scopus 로고    scopus 로고
    • Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution
    • Rausch C, Hoof I, Weber T, Wohlleben W Huson DH (2007) Phylogenetic analysis of condensation domains in NRPS sheds light on their functional evolution. BMC Evol Biol 7, 78.
    • (2007) BMC Evol Biol , vol.7 , pp. 78
    • Rausch, C.1    Hoof, I.2    Weber, T.3    Wohlleben, W.4    Huson, D.H.5
  • 14
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • Trivedi OA, Arora P, Sridharan V, Tickoo R, Mohanty D Gokhale RS (2004) Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 428, 441 445.
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 15
    • 0017043386 scopus 로고
    • Activation of long chain fatty acids with acyl carrier protein: Demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli
    • Ray TK Cronan JE Jr. (1976) Activation of long chain fatty acids with acyl carrier protein: demonstration of a new enzyme, acyl-acyl carrier protein synthetase, in Escherichia coli. Proc Natl Acad Sci USA 73, 4374 4378.
    • (1976) Proc Natl Acad Sci USA , vol.73 , pp. 4374-4378
    • Ray, T.K.1    Cronan Jr., J.E.2
  • 17
    • 0031040894 scopus 로고    scopus 로고
    • Mutational analysis of a fatty acyl-coenzyme a synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity
    • Black PN, Zhang Q, Weimar JD DiRusso CC (1997) Mutational analysis of a fatty acyl-coenzyme A synthetase signature motif identifies seven amino acid residues that modulate fatty acid substrate specificity. J Biol Chem 272, 4896 4903.
    • (1997) J Biol Chem , vol.272 , pp. 4896-4903
    • Black, P.N.1    Zhang, Q.2    Weimar, J.D.3    Dirusso, C.C.4
  • 18
    • 0015580995 scopus 로고
    • Palmitoyl-coenzyme a synthetase. Mechanism of reaction
    • Bar-Tana J, Rose G, Brandes R Shapiro B (1973) Palmitoyl-coenzyme A synthetase. Mechanism of reaction. Biochem J 131, 199 209.
    • (1973) Biochem J , vol.131 , pp. 199-209
    • Bar-Tana, J.1    Rose, G.2    Brandes, R.3    Shapiro, B.4
  • 19
    • 0015802872 scopus 로고
    • Palmitoyl-coenzyme a synthetase. Isolation of an enzyme-bound intermediate
    • Bar-Tana J, Rose G Shapiro B (1973) Palmitoyl-coenzyme A synthetase. Isolation of an enzyme-bound intermediate. Biochem J 135, 411 416.
    • (1973) Biochem J , vol.135 , pp. 411-416
    • Bar-Tana, J.1    Rose, G.2    Shapiro, B.3
  • 20
    • 33749607080 scopus 로고    scopus 로고
    • Complementation of daptomycin dptA and dptD deletion mutations in trans and production of hybrid lipopeptide antibiotics
    • Coeffet-Le Gal MF, Thurston L, Rich P, Miao V Baltz RH (2006) Complementation of daptomycin dptA and dptD deletion mutations in trans and production of hybrid lipopeptide antibiotics. Microbiology 152, 2993 3001.
    • (2006) Microbiology , vol.152 , pp. 2993-3001
    • Coeffet-Le Gal, M.F.1    Thurston, L.2    Rich, P.3    Miao, V.4    Baltz, R.H.5
  • 21
    • 3242738305 scopus 로고    scopus 로고
    • The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units
    • Tang Y, Koppisch AT Khosla C (2004) The acyltransferase homologue from the initiation module of the R1128 polyketide synthase is an acyl-ACP thioesterase that edits acetyl primer units. Biochemistry 43, 9546 9555.
    • (2004) Biochemistry , vol.43 , pp. 9546-9555
    • Tang, Y.1    Koppisch, A.T.2    Khosla, C.3
  • 22
    • 0034930478 scopus 로고    scopus 로고
    • Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-polyketide antitumor drug bleomycin
    • Sanchez C, Du L, Edwards DJ, Toney MD Shen B (2001) Cloning and characterization of a phosphopantetheinyl transferase from Streptomyces verticillus ATCC15003, the producer of the hybrid peptide-polyketide antitumor drug bleomycin. Chem Biol 8, 725 738.
    • (2001) Chem Biol , vol.8 , pp. 725-738
    • Sanchez, C.1    Du, L.2    Edwards, D.J.3    Toney, M.D.4    Shen, B.5
  • 23
    • 33750972299 scopus 로고    scopus 로고
    • Impact of epimerization domains on the intermodular transfer of enzyme-bound intermediates in nonribosomal peptide synthesis
    • Stein DB, Linne U, Hahn M Marahiel MA (2006) Impact of epimerization domains on the intermodular transfer of enzyme-bound intermediates in nonribosomal peptide synthesis. Chembiochem 7, 1807 1814.
    • (2006) Chembiochem , vol.7 , pp. 1807-1814
    • Stein, D.B.1    Linne, U.2    Hahn, M.3    Marahiel, M.A.4
  • 24
    • 2942560272 scopus 로고    scopus 로고
    • In vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli
    • Gruenewald S, Mootz HD, Stehmeier P Stachelhaus T (2004) In vivo production of artificial nonribosomal peptide products in the heterologous host Escherichia coli. Appl Environ Microbiol 70, 3282 3291.
    • (2004) Appl Environ Microbiol , vol.70 , pp. 3282-3291
    • Gruenewald, S.1    Mootz, H.D.2    Stehmeier, P.3    Stachelhaus, T.4
  • 25
    • 4444335028 scopus 로고    scopus 로고
    • The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase
    • Morgan-Kiss RM Cronan JE (2004) The Escherichia coli fadK (ydiD) gene encodes an anerobically regulated short chain acyl-CoA synthetase. J Biol Chem 279, 37324 37333.
    • (2004) J Biol Chem , vol.279 , pp. 37324-37333
    • Morgan-Kiss, R.M.1    Cronan, J.E.2
  • 26
    • 33846833440 scopus 로고    scopus 로고
    • Functional characterization of the acyl-[acyl carrier protein] ligase in the Cryptosporidium parvum giant polyketide synthase
    • Fritzler JM Zhu G (2007) Functional characterization of the acyl-[acyl carrier protein] ligase in the Cryptosporidium parvum giant polyketide synthase. Int J Parasitol 37, 307 316.
    • (2007) Int J Parasitol , vol.37 , pp. 307-316
    • Fritzler, J.M.1    Zhu, G.2
  • 28
    • 34548602373 scopus 로고    scopus 로고
    • Mechanistic studies of the long chain acyl-CoA synthetase Faa1p from Saccharomyces cerevisiae
    • Li H, Melton EM, Quackenbush S, DiRusso CC Black PN (2007) Mechanistic studies of the long chain acyl-CoA synthetase Faa1p from Saccharomyces cerevisiae. Biochim Biophys Acta 1771, 1246 1253.
    • (2007) Biochim Biophys Acta , vol.1771 , pp. 1246-1253
    • Li, H.1    Melton, E.M.2    Quackenbush, S.3    Dirusso, C.C.4    Black, P.N.5
  • 29
    • 34547099608 scopus 로고    scopus 로고
    • Chain initiation in the leinamycin-producing hybrid nonribosomal peptide/polyketide synthetase from Streptomyces atroolivaceus S-140. Discrete, monofunctional adenylation enzyme and peptidyl carrier protein that directly load d-alanine
    • Tang GL, Cheng YQ Shen B (2007) Chain initiation in the leinamycin-producing hybrid nonribosomal peptide/polyketide synthetase from Streptomyces atroolivaceus S-140. Discrete, monofunctional adenylation enzyme and peptidyl carrier protein that directly load d-alanine. J Biol Chem 282, 20273 20282.
    • (2007) J Biol Chem , vol.282 , pp. 20273-20282
    • Tang, G.L.1    Cheng, Y.Q.2    Shen, B.3
  • 32
    • 48649093119 scopus 로고    scopus 로고
    • Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase
    • Reger AS, Wu R, Dunaway-Mariano D Gulick AM (2008) Structural characterization of a 140 degrees domain movement in the two-step reaction catalyzed by 4-chlorobenzoate:CoA ligase. Biochemistry 47, 8016 8025.
    • (2008) Biochemistry , vol.47 , pp. 8016-8025
    • Reger, A.S.1    Wu, R.2    Dunaway-Mariano, D.3    Gulick, A.M.4
  • 33
    • 21644469444 scopus 로고    scopus 로고
    • Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC precursors for polyketide biosynthesis
    • Arora P, Vats A, Saxena P, Mohanty D Gokhale RS (2005) Promiscuous fatty acyl CoA ligases produce acyl-CoA and acyl-SNAC precursors for polyketide biosynthesis. J Am Chem Soc 127, 9388 9389.
    • (2005) J Am Chem Soc , vol.127 , pp. 9388-9389
    • Arora, P.1    Vats, A.2    Saxena, P.3    Mohanty, D.4    Gokhale, R.S.5
  • 34
    • 36549060587 scopus 로고    scopus 로고
    • Versatility of polyketide synthases in generating metabolic diversity
    • Gokhale RS, Sankaranarayanan R Mohanty D (2007) Versatility of polyketide synthases in generating metabolic diversity. Curr Opin Struct Biol 17, 736 743.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 736-743
    • Gokhale, R.S.1    Sankaranarayanan, R.2    Mohanty, D.3
  • 35
    • 34249002570 scopus 로고    scopus 로고
    • The loading module of mycosubtilin: An adenylation domain with fatty acid selectivity
    • Hansen DB, Bumpus SB, Aron ZD, Kelleher NL Walsh CT (2007) The loading module of mycosubtilin: an adenylation domain with fatty acid selectivity. J Am Chem Soc 129, 6366 6367.
    • (2007) J Am Chem Soc , vol.129 , pp. 6366-6367
    • Hansen, D.B.1    Bumpus, S.B.2    Aron, Z.D.3    Kelleher, N.L.4    Walsh, C.T.5
  • 36
    • 34250356414 scopus 로고    scopus 로고
    • FenF: Servicing the Mycosubtilin synthetase assembly line in trans
    • Aron ZD, Fortin PD, Calderone CT Walsh CT (2007) FenF: servicing the Mycosubtilin synthetase assembly line in trans. Chembiochem 8, 613 616.
    • (2007) Chembiochem , vol.8 , pp. 613-616
    • Aron, Z.D.1    Fortin, P.D.2    Calderone, C.T.3    Walsh, C.T.4
  • 37
    • 39749169353 scopus 로고    scopus 로고
    • Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes
    • Kopp F, Linne U, Oberthur M Marahiel MA (2008) Harnessing the chemical activation inherent to carrier protein-bound thioesters for the characterization of lipopeptide fatty acid tailoring enzymes. J Am Chem Soc 130, 2656 2666.
    • (2008) J Am Chem Soc , vol.130 , pp. 2656-2666
    • Kopp, F.1    Linne, U.2    Oberthur, M.3    Marahiel, M.A.4
  • 38
    • 4444252771 scopus 로고    scopus 로고
    • Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein
    • Steller S, Sokoll A, Wilde C, Bernhard F, Franke P Vater J (2004) Initiation of surfactin biosynthesis and the role of the SrfD-thioesterase protein. Biochemistry 43, 11331 11343.
    • (2004) Biochemistry , vol.43 , pp. 11331-11343
    • Steller, S.1    Sokoll, A.2    Wilde, C.3    Bernhard, F.4    Franke, P.5    Vater, J.6
  • 39
    • 41549135295 scopus 로고    scopus 로고
    • Purification and gene cloning of a dehydrogenase from Lactobacillus brevis that catalyzes a reaction involved in aflatoxin biosynthesis
    • Sakuno E, Kameyama M, Nakajima H Yabe K (2008) Purification and gene cloning of a dehydrogenase from Lactobacillus brevis that catalyzes a reaction involved in aflatoxin biosynthesis. Biosci Biotechnol Biochem 72, 724 734.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 724-734
    • Sakuno, E.1    Kameyama, M.2    Nakajima, H.3    Yabe, K.4
  • 41
    • 33847112437 scopus 로고    scopus 로고
    • Aminoacyl-coenzyme a synthesis catalyzed by adenylation domains
    • Linne U, Schafer A, Stubbs MT Marahiel MA (2007) Aminoacyl-coenzyme A synthesis catalyzed by adenylation domains. FEBS Lett 581, 905 910.
    • (2007) FEBS Lett , vol.581 , pp. 905-910
    • Linne, U.1    Schafer, A.2    Stubbs, M.T.3    Marahiel, M.A.4
  • 43
    • 0035813125 scopus 로고    scopus 로고
    • 4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis
    • Mootz HD, Finking R Marahiel MA (2001) 4'-phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis. J Biol Chem 276, 37289 37298.
    • (2001) J Biol Chem , vol.276 , pp. 37289-37298
    • Mootz, H.D.1    Finking, R.2    Marahiel, M.A.3
  • 44
    • 43049113173 scopus 로고    scopus 로고
    • Delta-amino group hydroxylation of l-ornithine during coelichelin biosynthesis
    • Pohlmann V Marahiel MA (2008) Delta-amino group hydroxylation of l-ornithine during coelichelin biosynthesis. Org Biomol Chem 6, 1843 1848.
    • (2008) Org Biomol Chem , vol.6 , pp. 1843-1848
    • Pohlmann, V.1    Marahiel, M.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.