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Volumn 58, Issue , 2004, Pages 453-488

Biosynthesis of nonribosomal peptides

Author keywords

4 phosphopantetheinyl transferases; Biosynthetic strategies; Hybrid genes; Nonribosomal peptide synthetases; Tailoring enzymes

Indexed keywords

4' PHOSPHOPANTETHEINYL TRANSFERASE; BACTERIAL ENZYME; FATTY ACID SYNTHASE; FUNGAL ENZYME; HYBRID PROTEIN; NONRIBOSOMAL PEPTIDE SYNTHETASE; PEPTIDE; PEPTIDE SYNTHASE; PEPTIDYL CARRIER PROTEIN; POLYKETIDE SYNTHASE; RIBOSOME PROTEIN; THIOL ESTER HYDROLASE; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; CARRIER PROTEIN; MULTIENZYME COMPLEX;

EID: 9244234513     PISSN: 00664227     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.micro.58.030603.123615     Document Type: Review
Times cited : (690)

References (184)
  • 1
    • 77956910736 scopus 로고
    • Acyl-CoA carboxylase
    • ed. PD Boyer. New York: Academic
    • Alberts A, Vagelos PR. 1972. Acyl-CoA carboxylase. In The Enzymes, ed. PD Boyer, pp. 37-82. New York: Academic
    • (1972) The Enzymes , pp. 37-82
    • Alberts, A.1    Vagelos, P.R.2
  • 2
    • 0042626159 scopus 로고    scopus 로고
    • Structure of gramicidin A in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data
    • Allen TW, Andersen OS, Roux B. 2003. Structure of gramicidin A in a lipid bilayer environment determined using molecular dynamics simulations and solid-state NMR data. J. Am. Chem. Soc. 125:9868-77
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 9868-9877
    • Allen, T.W.1    Andersen, O.S.2    Roux, B.3
  • 3
    • 0028943591 scopus 로고
    • Amide exchange rates in Escherichia coli acyl carrier protein: Correlation with protein structure and dynamics
    • Andrec M, Hill RB, Prestegard JH. 1995. Amide exchange rates in Escherichia coli acyl carrier protein: correlation with protein structure and dynamics. Protein Sci. 4:983-93
    • (1995) Protein Sci. , vol.4 , pp. 983-993
    • Andrec, M.1    Hill, R.B.2    Prestegard, J.H.3
  • 4
    • 0030962189 scopus 로고    scopus 로고
    • Structural and functional considerations of the aminoacylation reaction
    • Arnez JG, Moras D. 1997. Structural and functional considerations of the aminoacylation reaction. Trends Biochem. Sci. 22:203-6
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 203-206
    • Arnez, J.G.1    Moras, D.2
  • 5
    • 0033574774 scopus 로고    scopus 로고
    • Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis
    • Belshaw PJ, Walsh CT, Stachelhaus T. 1999. Aminoacyl-CoAs as probes of condensation domain selectivity in nonribosomal peptide synthesis. Science 284:486-89
    • (1999) Science , vol.284 , pp. 486-489
    • Belshaw, P.J.1    Walsh, C.T.2    Stachelhaus, T.3
  • 6
    • 0036161991 scopus 로고    scopus 로고
    • Mutational analysis of the C-domain in nonribosomal peptide synthesis
    • Bergendahl V, Linne U, Marahiel MA. 2002. Mutational analysis of the C-domain in nonribosomal peptide synthesis. Eur. J. Biochem. 269:620-29
    • (2002) Eur. J. Biochem. , vol.269 , pp. 620-629
    • Bergendahl, V.1    Linne, U.2    Marahiel, M.A.3
  • 7
    • 0028058149 scopus 로고
    • Molecular and biochemical analyses of fatty acid transport, metabolism, and gene regulation in Escherichia coli
    • Black PN, DiRusso CC. 1994. Molecular and biochemical analyses of fatty acid transport, metabolism, and gene regulation in Escherichia coli. Biochim. Biophys. Acta. 1210:123-45
    • (1994) Biochim. Biophys. Acta , vol.1210 , pp. 123-145
    • Black, P.N.1    DiRusso, C.C.2
  • 8
    • 0036120595 scopus 로고    scopus 로고
    • Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE
    • Bruner SD, Weber T, Kohli RM, Schwarzer D, Marahiel MA, et al. 2002. Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE. Structure 10:301-10
    • (2002) Structure , vol.10 , pp. 301-310
    • Bruner, S.D.1    Weber, T.2    Kohli, R.M.3    Schwarzer, D.4    Marahiel, M.A.5
  • 10
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
    • Cane DE, Walsh CT. 1999. The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases. Chem. Biol. 6:R319-25
    • (1999) Chem. Biol. , vol.6
    • Cane, D.E.1    Walsh, C.T.2
  • 11
    • 0032475992 scopus 로고    scopus 로고
    • Harnessing the biosynthetic code: Combinations, permutations, and mutations
    • Cane DE, Walsh CT, 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
  • 12
    • 0029116455 scopus 로고
    • Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis
    • Chen CL, Chang LK, Chang YS, Liu ST, Tschen JS. 1995. Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis. Mol. Gen. Genet. 248:121-25
    • (1995) Mol. Gen. Genet. , vol.248 , pp. 121-125
    • Chen, C.L.1    Chang, L.K.2    Chang, Y.S.3    Liu, S.T.4    Tschen, J.S.5
  • 13
    • 0034837369 scopus 로고    scopus 로고
    • Epothilone biosynthesis: Assembly of the methylthiazolylcarboxy starter unit on the EpoB subunit
    • Chen H, O'Connor S, Cane DE, Walsh CT. 2001. Epothilone biosynthesis: assembly of the methylthiazolylcarboxy starter unit on the EpoB subunit. Chem. Biol. 8:899-912
    • (2001) Chem. Biol. , vol.8 , pp. 899-912
    • Chen, H.1    O'Connor, S.2    Cane, D.E.3    Walsh, C.T.4
  • 14
    • 0034675957 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: An essential enzyme in bacterial fatty acid biosynthesis
    • Chirgadze NY, Briggs SL, McAllister KA, Fischl AS, Zhao G. 2000. Crystal structure of Streptococcus pneumoniae acyl carrier protein synthase: an essential enzyme in bacterial fatty acid biosynthesis. EMBO J. 19:5281-87
    • (2000) EMBO J. , vol.19 , pp. 5281-5287
    • Chirgadze, N.Y.1    Briggs, S.L.2    McAllister, K.A.3    Fischl, A.S.4    Zhao, G.5
  • 15
    • 0030584662 scopus 로고    scopus 로고
    • Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes
    • Conti E, Franks NP, Brick P. 1996. Crystal structure of firefly luciferase throws light on a superfamily of adenylate-forming enzymes. Structure 4:287-98
    • (1996) Structure , vol.4 , pp. 287-298
    • Conti, E.1    Franks, N.P.2    Brick, P.3
  • 16
    • 0030756031 scopus 로고    scopus 로고
    • Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S
    • Conti E, Stachelhaus T, Marahiel MA, Brick P. 1997. Structural basis for the activation of phenylalanine in the nonribosomal biosynthesis of gramicidin S. EMBO J. 16:4174-83
    • (1997) EMBO J. , vol.16 , pp. 4174-4183
    • Conti, E.1    Stachelhaus, T.2    Marahiel, M.A.3    Brick, P.4
  • 17
    • 0019588236 scopus 로고
    • Pyochelin: Novel structure of an iron-chelating growth promotor for Pseudomonas aeruginosa
    • Cox CD. 1981. Pyochelin: novel structure of an iron-chelating growth promotor for Pseudomonas aeruginosa. Proc. Natl. Acad. Sci. USA 78:4256-60
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , pp. 4256-4260
    • Cox, C.D.1
  • 18
    • 0024404842 scopus 로고
    • Genetics and molecular biology of siderophore-mediated iron transport in bacteria
    • Crosa JH. 1989. Genetics and molecular biology of siderophore-mediated iron transport in bacteria. Microbiol. Rev. 53:517-30
    • (1989) Microbiol. Rev. , vol.53 , pp. 517-530
    • Crosa, J.H.1
  • 19
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT. 2002. Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol. Mol. Biol. Rev. 66:223-49
    • (2002) Microbiol. Mol. Biol. Rev. , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 20
    • 0030972114 scopus 로고    scopus 로고
    • Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3 (2)
    • Crump MP, Crosby J, Dempsey CE, Parkinson JA, Murray M, et al. 1997. Solution structure of the actinorhodin polyketide synthase acyl carrier protein from Streptomyces coelicolor A3 (2). Biochemistry 36:6000-8
    • (1997) Biochemistry , vol.36 , pp. 6000-6008
    • Crump, M.P.1    Crosby, J.2    Dempsey, C.E.3    Parkinson, J.A.4    Murray, M.5
  • 21
    • 0015819138 scopus 로고
    • Inhibition of fatty acid synthesis by the antibiotic cerulenin, specific inactivation of β-ketoacyl-acyl carrier protein synthase
    • D'Agnolo G, Rosenfeld IS, Awaya J, Omura S, Vagelos PR. 1973. Inhibition of fatty acid synthesis by the antibiotic cerulenin, specific inactivation of β-ketoacyl-acyl carrier protein synthase. Biochim. Biophys. Acta. 326:155-56
    • (1973) Biochim. Biophys. Acta , vol.326 , pp. 155-156
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Awaya, J.3    Omura, S.4    Vagelos, P.R.5
  • 22
    • 0016734774 scopus 로고
    • Multiple forms of β-ketoacyl-acyl carrier protein synthase in Escherichia coli
    • D'Agnolo G, Rosenfeld IS, Vagelos PR. 1975. Multiple forms of β-ketoacyl-acyl carrier protein synthase in Escherichia coli. J. Biol. Chem. 250:5289-94
    • (1975) J. Biol. Chem. , vol.250 , pp. 5289-5294
    • D'Agnolo, G.1    Rosenfeld, I.S.2    Vagelos, P.R.3
  • 23
    • 0034651317 scopus 로고    scopus 로고
    • The 1.8 Å crystal structure and active-site architecture of β-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli
    • Davies C, Heath RJ, White SW, Rock CO. 2000. The 1.8 Å crystal structure and active-site architecture of β-ketoacyl-acyl carrier protein synthase III (FabH) from Escherichia coli. Structure 8:185-95
    • (2000) Structure , vol.8 , pp. 185-195
    • Davies, C.1    Heath, R.J.2    White, S.W.3    Rock, C.O.4
  • 24
  • 25
    • 0028896569 scopus 로고
    • Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases
    • Dieckmann R, Lee YO, vanLiempt H, von Döhren H, Kleinkauf H. 1995. Expression of an active adenylate-forming domain of peptide synthetases corresponding to acyl-CoA-synthetases. FEBS Lett. 357:212-16
    • (1995) FEBS Lett. , vol.357 , pp. 212-216
    • Dieckmann, R.1    Lee, Y.O.2    VanLiempt, H.3    Von Döhren, H.4    Kleinkauf, H.5
  • 26
    • 0034125798 scopus 로고    scopus 로고
    • Dipeptide formation on engineered hybrid peptide synthetases
    • Doekel S, Marahiel MA. 2000. Dipeptide formation on engineered hybrid peptide synthetases. Chem. Biol. 7:373-84
    • (2000) Chem. Biol. , vol.7 , pp. 373-384
    • Doekel, S.1    Marahiel, M.A.2
  • 27
    • 0033603539 scopus 로고    scopus 로고
    • Phylogenetic classification and the universal tree
    • Doolittle WF. 1999. Phylogenetic classification and the universal tree. Science 284:2124-28
    • (1999) Science , vol.284 , pp. 2124-2128
    • Doolittle, W.F.1
  • 28
    • 0043244862 scopus 로고    scopus 로고
    • BlmIII and BlmIV nonribosomal peptide synthetase-catalyzed biosynthesis of the bleomycin bithiazole moiety involving both in cis and in trans aminoacylation
    • Du L, Chen M, Zhang Y, Shen B. 2003. BlmIII and BlmIV nonribosomal peptide synthetase-catalyzed biosynthesis of the bleomycin bithiazole moiety involving both in cis and in trans aminoacylation. Biochemistry 42:9731-49
    • (2003) Biochemistry , vol.42 , pp. 9731-9749
    • Du, L.1    Chen, M.2    Zhang, Y.3    Shen, B.4
  • 29
    • 0033835373 scopus 로고    scopus 로고
    • The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC 15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase
    • Du L, Sanchez C, Chen M, Edwards DJ, Shen B. 2000. The biosynthetic gene cluster for the antitumor drug bleomycin from Streptomyces verticillus ATCC 15003 supporting functional interactions between nonribosomal peptide synthetases and a polyketide synthase. Chem. Biol. 7:623-42
    • (2000) Chem. Biol. , vol.7 , pp. 623-642
    • Du, L.1    Sanchez, C.2    Chen, M.3    Edwards, D.J.4    Shen, B.5
  • 30
    • 0345305853 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases for the production of alpha-L-aspartyl-L-phenylalanine, a precursor for the high-intensity sweetener aspartame
    • Duerfahrt T, Doekel S, Sonke T, Quaedflieg PJLM, Marahiel MA. 2003. Construction of hybrid peptide synthetases for the production of alpha-L-aspartyl-L-phenylalanine, a precursor for the high-intensity sweetener aspartame. Eur. J. Biochem. 270:4555-63
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4555-4563
    • Duerfahrt, T.1    Doekel, S.2    Sonke, T.3    Quaedflieg, P.J.L.M.4    Marahiel, M.A.5
  • 31
    • 1542380023 scopus 로고    scopus 로고
    • Rational design of a bimodular model system for the investigation of heterocyclization in nonribosomal peptide biosynthesis
    • Duerfahrt T, Eppelmann K, Müller R, Marahiel MA. 2004. Rational design of a bimodular model system for the investigation of heterocyclization in nonribosomal peptide biosynthesis. Chem. Biol. 11:261-71
    • (2004) Chem. Biol. , vol.11 , pp. 261-271
    • Duerfahrt, T.1    Eppelmann, K.2    Müller, R.3    Marahiel, M.A.4
  • 32
    • 0033545834 scopus 로고    scopus 로고
    • Lysine biosynthesis in Saccharomycescerevisiae: Mechanism of α-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5
    • Ehmann DE, Gehring AM, Walsh CT. 1999. Lysine biosynthesis in Saccharomycescerevisiae: mechanism of α-aminoadipate reductase (Lys2) involves posttranslational phosphopantetheinylation by Lys5. Biochemistry 38:6171-77
    • (1999) Biochemistry , vol.38 , pp. 6171-6177
    • Ehmann, D.E.1    Gehring, A.M.2    Walsh, C.T.3
  • 33
    • 0034646227 scopus 로고    scopus 로고
    • The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: Sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates
    • Ehmann DE, Shaw-Reid CA, Losey HC, Walsh CT. 2000. The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Proc. Natl. Acad. Sci. USA 97:2509-14
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2509-2514
    • Ehmann, D.E.1    Shaw-Reid, C.A.2    Losey, H.C.3    Walsh, C.T.4
  • 34
    • 0037199494 scopus 로고    scopus 로고
    • Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics
    • Eppelmann K, Stachelhaus T, Marahiel MA. 2002. Exploitation of the selectivity-conferring code of nonribosomal peptide synthetases for the rational design of novel peptide antibiotics. Biochemistry 41:9718-26
    • (2002) Biochemistry , vol.41 , pp. 9718-9726
    • Eppelmann, K.1    Stachelhaus, T.2    Marahiel, M.A.3
  • 35
    • 0025158208 scopus 로고
    • Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs
    • Eriani G, Delarue M, Poch O, Gangloff J, Moras D. 1990. Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs. Nature 347:203-6
    • (1990) Nature , vol.347 , pp. 203-206
    • Eriani, G.1    Delarue, M.2    Poch, O.3    Gangloff, J.4    Moras, D.5
  • 36
    • 0036007872 scopus 로고    scopus 로고
    • Marine natural products
    • Faulkner DJ. 2002. Marine natural products. Nat. Prod. Rep. 19:1-48
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 1-48
    • Faulkner, D.J.1
  • 37
    • 0034111426 scopus 로고    scopus 로고
    • A novel function of yeast fatty acid synthase. Subunit α is capable of self-pantetheinylation
    • Fichtischerer F, Wellein C, Mittag M, Schweizer E. 2000. A novel function of yeast fatty acid synthase. Subunit α is capable of self-pantetheinylation. Eur. J. Biochem. 267:2666-71
    • (2000) Eur. J. Biochem. , vol.267 , pp. 2666-2671
    • Fichtischerer, F.1    Wellein, C.2    Mittag, M.3    Schweizer, E.4
  • 38
    • 0038457084 scopus 로고    scopus 로고
    • Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus
    • Findlow SC, Winsor C, Simpson TJ, Crosby J, Crump MP. 2003. Solution structure and dynamics of oxytetracycline polyketide synthase acyl carrier protein from Streptomyces rimosus. Biochemistry 42:8423-33
    • (2003) Biochemistry , vol.42 , pp. 8423-8433
    • Findlow, S.C.1    Winsor, C.2    Simpson, T.J.3    Crosby, J.4    Crump, M.P.5
  • 39
    • 0141795294 scopus 로고    scopus 로고
    • Amino acyl-adenylate substrate analogues for the inhibition of adenylation domains of non-ribosomal peptide synthetases
    • Finking R, Neumüller A, Solsbacher J, Konz D, Kretzschmar G, et al. 2003. Amino acyl-adenylate substrate analogues for the inhibition of adenylation domains of non-ribosomal peptide synthetases. ChemBiol. Chem. 4:903-6
    • (2003) ChemBiol. Chem. , vol.4 , pp. 903-906
    • Finking, R.1    Neumüller, A.2    Solsbacher, J.3    Konz, D.4    Kretzschmar, G.5
  • 40
    • 0348087044 scopus 로고    scopus 로고
    • Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore metabolism in Pseudomonas aeruginosa
    • Finking R, Solsbacher J, Konz D, Schobert M, Schäfer A, et al. 2002. Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore metabolism in Pseudomonas aeruginosa. J. Biol. Chem. 277:50293-302
    • (2002) J. Biol. Chem. , vol.277 , pp. 50293-50302
    • Finking, R.1    Solsbacher, J.2    Konz, D.3    Schobert, M.4    Schäfer, A.5
  • 41
    • 0035929665 scopus 로고    scopus 로고
    • Site-directed mutagenesis of acyl carrier protein reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity
    • Flaman AS, Chen JM, Van Iderstine SC, Byers DM. 2001. Site-directed mutagenesis of acyl carrier protein reveals amino acid residues involved in ACP structure and acyl-ACP synthetase activity. J. Biol. Chem. 276:35934-39
    • (2001) J. Biol. Chem. , vol.276 , pp. 35934-35939
    • Flaman, A.S.1    Chen, J.M.2    Van Iderstine, S.C.3    Byers, D.M.4
  • 42
    • 0033955033 scopus 로고    scopus 로고
    • Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli
    • Flugel RS, Hwangbo Y, Lambalot RH, Cronan JE Jr, Walsh CT. 2000. Holo-(acyl carrier protein) synthase and phosphopantetheinyl transfer in Escherichia coli. J. Biol. Chem. 275:959-68
    • (2000) J. Biol. Chem. , vol.275 , pp. 959-968
    • Flugel, R.S.1    Hwangbo, Y.2    Lambalot, R.H.3    Cronan Jr., J.E.4    Walsh, C.T.5
  • 43
    • 0031784872 scopus 로고    scopus 로고
    • Structural basis for the inhibition of firefly luciferase by a general anesthetic
    • Franks NP, Jenkins A, Conti E, Lieb WR, Brick P. 1998. Structural basis for the inhibition of firefly luciferase by a general anesthetic. Biophys. J. 75:2205-11
    • (1998) Biophys. J. , vol.75 , pp. 2205-2211
    • Franks, N.P.1    Jenkins, A.2    Conti, E.3    Lieb, W.R.4    Brick, P.5
  • 45
    • 0019275308 scopus 로고
    • Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthase I and II of Escherichia coli
    • Garwin JL, Klages AL, Cronan JE Jr. 1980. Structural, enzymatic, and genetic studies of β-ketoacyl-acyl carrier protein synthase I and II of Escherichia coli. J. Biol. Chem. 255:11949-56
    • (1980) J. Biol. Chem. , vol.255 , pp. 11949-11956
    • Garwin, J.L.1    Klages, A.L.2    Cronan Jr., J.E.3
  • 46
    • 0030738431 scopus 로고    scopus 로고
    • Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
    • Gehring AM, Bradley KA, Walsh CT. 1997. Enterobactin biosynthesis in Escherichia coli: Isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 36:8495-503
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gehring, A.M.1    Bradley, K.A.2    Walsh, C.T.3
  • 47
    • 0032193282 scopus 로고    scopus 로고
    • Iron acquisition in plague: Modular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis
    • Gehring AM, DeMoll E, Fetherston JD, Mori I, Mayhew GF, et al. 1998. Iron acquisition in plague: modular logic in enzymatic biogenesis of yersiniabactin by Yersinia pestis. Chem. Biol. 5:573-86
    • (1998) Chem. Biol. , vol.5 , pp. 573-586
    • Gehring, A.M.1    DeMoll, E.2    Fetherston, J.D.3    Mori, I.4    Mayhew, G.F.5
  • 48
    • 0030936547 scopus 로고    scopus 로고
    • Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase
    • Gehring AM, Lambalot RH, Vogel KW, Drueckhammer DG, Walsh CT. 1997. Ability of Streptomyces spp. acyl carrier proteins and coenzyme A analogs to serve as substrates in vitro for E. coli holo-ACP synthase. Chem. Biol. 4:17-24
    • (1997) Chem. Biol. , vol.4 , pp. 17-24
    • Gehring, A.M.1    Lambalot, R.H.2    Vogel, K.W.3    Drueckhammer, D.G.4    Walsh, C.T.5
  • 49
    • 0032544193 scopus 로고    scopus 로고
    • The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis
    • Gehring AM, Mori I, Perry RD, Walsh CT. 1998. The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 37:11637-50. Erratum. 1998. Biochemistry 37:17104
    • (1998) Biochemistry , vol.37 , pp. 11637-11650
    • Gehring, A.M.1    Mori, I.2    Perry, R.D.3    Walsh, C.T.4
  • 50
    • 0032400509 scopus 로고    scopus 로고
    • Erratum
    • Gehring AM, Mori I, Perry RD, Walsh CT. 1998. The nonribosomal peptide synthetase HMWP2 forms a thiazoline ring during biogenesis of yersiniabactin, an iron-chelating virulence factor of Yersinia pestis. Biochemistry 37:11637-50. Erratum. 1998. Biochemistry 37:17104
    • (1998) Biochemistry , vol.37 , pp. 17104
  • 51
    • 0032562142 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
    • Gehring AM, Mori I, Walsh CT. 1998. Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 37:2648-59
    • (1998) Biochemistry , vol.37 , pp. 2648-2659
    • Gehring, A.M.1    Mori, I.2    Walsh, C.T.3
  • 52
    • 0014289968 scopus 로고
    • The activation of amino acids for biosynthesis of gramicidin S
    • Gevers W, Kleinkauf H, Lipmann F. 1968. The activation of amino acids for biosynthesis of gramicidin S. Proc. Natl. Acad. Sci. USA 60:269-76
    • (1968) Proc. Natl. Acad. Sci. USA , vol.60 , pp. 269-276
    • Gevers, W.1    Kleinkauf, H.2    Lipmann, F.3
  • 53
    • 0036037587 scopus 로고    scopus 로고
    • Enniatin synthetase is a monomer with extended structure: Evidence for an intramolecular reaction mechanism
    • Glinski M, Urbanke C, Hornbogen T, Zocher R. 2002. Enniatin synthetase is a monomer with extended structure: evidence for an intramolecular reaction mechanism. Arch. Mircrobiol. 178:267-73
    • (2002) Arch. Mircrobiol. , vol.178 , pp. 267-273
    • Glinski, M.1    Urbanke, C.2    Hornbogen, T.3    Zocher, R.4
  • 54
    • 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 MA. 1994. Analysis of core sequences in the D-Phe activating domain of the multifunctional peptide synthetase TycA by site-directed mutagenesis. J. Bacteriol. 176:2654-62
    • (1994) J. Bacteriol. , vol.176 , pp. 2654-2662
    • Gocht, M.1    Marahiel, M.A.2
  • 55
    • 0032562129 scopus 로고    scopus 로고
    • Functional orientation of the acyltransferase domain in a module of the erythromycin polyketide synthase
    • Gokhale RS, Lau J, Cane DE, Khosla C. 1998. Functional orientation of the acyltransferase domain in a module of the erythromycin polyketide synthase. Biochemistry 37:2524-28
    • (1998) Biochemistry , vol.37 , pp. 2524-2528
    • Gokhale, R.S.1    Lau, J.2    Cane, D.E.3    Khosla, C.4
  • 56
    • 0033574768 scopus 로고    scopus 로고
    • Dissecting and exploiting intermodular communication in polyketide synthases
    • Gokhale RS, Tsuji SY, Cane DE, Khosla C. 1999. Dissecting and exploiting intermodular communication in polyketide synthases. Science 284:482-85
    • (1999) Science , vol.284 , pp. 482-485
    • Gokhale, R.S.1    Tsuji, S.Y.2    Cane, D.E.3    Khosla, C.4
  • 58
    • 0016285541 scopus 로고
    • Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyl-transferase, and carboxyl carrier protein components
    • Guchhait RB, Polakis SE, Dimroth P, Stoll E, Moss J, Lane MD. 1974. Acetyl coenzyme A carboxylase system of Escherichia coli. Purification and properties of the biotin carboxylase, carboxyl-transferase, and carboxyl carrier protein components. J. Biol. Chem. 249:6633-45
    • (1974) J. Biol. Chem. , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 59
    • 0032484013 scopus 로고    scopus 로고
    • Characterization of the syringomycin synthetase gene cluster. A link between prokaryotic and eukaryotic peptide synthetases
    • Guenzi E, Galli G, Grgurina I, Gross DC, Grandi G. 1998. Characterization of the syringomycin synthetase gene cluster. A link between prokaryotic and eukaryotic peptide synthetases. J. Biol. Chem. 273:32857-63
    • (1998) J. Biol. Chem. , vol.273 , pp. 32857-32863
    • Guenzi, E.1    Galli, G.2    Grgurina, I.3    Gross, D.C.4    Grandi, G.5
  • 60
    • 0032486407 scopus 로고    scopus 로고
    • Coordinate transcription and physical linkage of domains in surfactin synthetase are not essential for proper assembly and activity of the multienzyme complex
    • Guenzi E, Galli G, Grgurina I, Pace E, Ferranti P, Grandi G. 1998. Coordinate transcription and physical linkage of domains in surfactin synthetase are not essential for proper assembly and activity of the multienzyme complex. J. Biol. Chem. 273:14403-10
    • (1998) J. Biol. Chem. , vol.273 , pp. 14403-14410
    • Guenzi, E.1    Galli, G.2    Grgurina, I.3    Pace, E.4    Ferranti, P.5    Grandi, G.6
  • 61
    • 0016351434 scopus 로고
    • Mutants of Escherichia coli with temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase
    • Harder M, Ladenson RC, Schimmel SD, Silbert DF. 1974. Mutants of Escherichia coli with temperature-sensitive malonyl coenzyme A-acyl carrier protein transacylase. J. Biol. Chem. 249:7468-75
    • (1974) J. Biol. Chem. , vol.249 , pp. 7468-7475
    • Harder, M.1    Ladenson, R.C.2    Schimmel, S.D.3    Silbert, D.F.4
  • 62
    • 0033636188 scopus 로고    scopus 로고
    • The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin A production and pathogenicity
    • Healy FG, Wach M, Krasnoff SB, Gibson DM, Loria R. 2000. The txtAB genes of the plant pathogen Streptomyces acidiscabies encode a peptide synthetase required for phytotoxin thaxtomin A production and pathogenicity. Mol. Microbiol. 38:794-804
    • (2000) Mol. Microbiol. , vol.38 , pp. 794-804
    • Healy, F.G.1    Wach, M.2    Krasnoff, S.B.3    Gibson, D.M.4    Loria, R.5
  • 63
    • 0037469129 scopus 로고    scopus 로고
    • Dimeric structure of the six-domain VibF subunit of vibriobactin synthetase: Mutant domain activity regain and ultracentrifugation studies
    • Hillson NJ, Walsh CT. 2003. Dimeric structure of the six-domain VibF subunit of vibriobactin synthetase: mutant domain activity regain and ultracentrifugation studies. Biochemistry 42:766-75
    • (2003) Biochemistry , vol.42 , pp. 766-775
    • Hillson, N.J.1    Walsh, C.T.2
  • 64
    • 0028272082 scopus 로고
    • Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis
    • Hoffmann K, Schneider-Scherzer E, Kleinkauf H, Zocher R. 1994. Purification and characterization of eucaryotic alanine racemase acting as key enzyme in cyclosporin biosynthesis. J. Biol. Chem. 269:12710-14
    • (1994) J. Biol. Chem. , vol.269 , pp. 12710-12714
    • Hoffmann, K.1    Schneider-Scherzer, E.2    Kleinkauf, H.3    Zocher, R.4
  • 65
    • 0023813070 scopus 로고
    • Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations
    • Holak TA, Kearsley SK, Kim Y, Prestegard JH. 1988. Three-dimensional structure of acyl carrier protein determined by NMR pseudoenergy and distance geometry calculations. Biochemistry 27:6135-42
    • (1988) Biochemistry , vol.27 , pp. 6135-6142
    • Holak, T.A.1    Kearsley, S.K.2    Kim, Y.3    Prestegard, J.H.4
  • 66
    • 0001747786 scopus 로고    scopus 로고
    • Genetic contributions to understanding polyketide synthases
    • Hopwood DA. 1997. Genetic contributions to understanding polyketide synthases. Chem. Rev. 97:2465-97
    • (1997) Chem. Rev. , vol.97 , pp. 2465-2497
    • Hopwood, D.A.1
  • 67
    • 0024470350 scopus 로고
    • Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1 gene
    • Hori K, Yamamoto Y, Minetoki T, Kurotsu T, Kanda M, et al. 1989. Molecular cloning and nucleotide sequence of the gramicidin S synthetase 1 gene. J. Biochem. 106:639-45
    • (1989) J. Biochem. , vol.106 , pp. 639-645
    • Hori, K.1    Yamamoto, Y.2    Minetoki, T.3    Kurotsu, T.4    Kanda, M.5
  • 69
    • 0000991019 scopus 로고    scopus 로고
    • Biosynthesis of coenzymes and prosthetic groups
    • ed. FC Neidhard. New York: ASM Press
    • Jackowski S. 1996. Biosynthesis of coenzymes and prosthetic groups. In E. coli and Salmonella. Cellular and Molecular Biology, ed. FC Neidhard, pp. 687-94. New York: ASM Press
    • (1996) E. coli and Salmonella. Cellular and Molecular Biology , pp. 687-694
    • Jackowski, S.1
  • 70
    • 0037330531 scopus 로고    scopus 로고
    • Engineering of an active animal fatty acid synthase dimer with only one competent subunit
    • Joshi AK, Rangan VS, Witkowski A, Smith S. 2003. Engineering of an active animal fatty acid synthase dimer with only one competent subunit. Chem. Biol. 10:169-73
    • (2003) Chem. Biol. , vol.10 , pp. 169-173
    • Joshi, A.K.1    Rangan, V.S.2    Witkowski, A.3    Smith, S.4
  • 71
    • 0031050460 scopus 로고    scopus 로고
    • Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro
    • Joshi AK, Witkowski A, Smith S. 1997. Mapping of functional interactions between domains of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 36:2316-22
    • (1997) Biochemistry , vol.36 , pp. 2316-2322
    • Joshi, A.K.1    Witkowski, A.2    Smith, S.3
  • 72
    • 0042858246 scopus 로고    scopus 로고
    • Cloning, expression and characterization of a human 4′- phosphopantetheinyl transferase with broad substrate specificity
    • Joshi AK, Zhang L, Rangan VS, Smith S. 2003. Cloning, expression and characterization of a human 4′-phosphopantetheinyl transferase with broad substrate specificity. J. Biol. Chem. 278:33142-49
    • (2003) J. Biol. Chem. , vol.278 , pp. 33142-33149
    • Joshi, A.K.1    Zhang, L.2    Rangan, V.S.3    Smith, S.4
  • 73
    • 0029797581 scopus 로고    scopus 로고
    • Evidence for two catalytically independent clusters of active sites in a functional modular polyketide synthase
    • Kao CM, Pieper R, Cane DE, Khosla C. 1996. Evidence for two catalytically independent clusters of active sites in a functional modular polyketide synthase. Biochemistry 35:12363-68
    • (1996) Biochemistry , vol.35 , pp. 12363-12368
    • Kao, C.M.1    Pieper, R.2    Cane, D.E.3    Khosla, C.4
  • 74
    • 0242668745 scopus 로고    scopus 로고
    • A new redox-cofactor vitamin for mammals
    • Kasahara T, Tadafumi K. 2003. A new redox-cofactor vitamin for mammals. Nature 422:832
    • (2003) Nature , vol.422 , pp. 832
    • Kasahara, T.1    Tadafumi, K.2
  • 75
    • 0001436716 scopus 로고    scopus 로고
    • Manipulation of modular polyketide synthases
    • Katz L. 1997. Manipulation of modular polyketide synthases. Chem. Rev. 97:2557-76
    • (1997) Chem. Rev. , vol.97 , pp. 2557-2576
    • Katz, L.1
  • 76
    • 0034687759 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH
    • Keating TA, Marshall CG, Walsh CT. 2000. Reconstitution and characterization of the Vibrio cholerae vibriobactin synthetase from VibB, VibE, VibF, and VibH. Biochemistry 39:15522-30
    • (2000) Biochemistry , vol.39 , pp. 15522-15530
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 77
    • 0034687767 scopus 로고    scopus 로고
    • Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase homologous to nonribosomal peptide synthetase condensation domains
    • Keating TA, Marshall CG, Walsh CT. 2000. Vibriobactin biosynthesis in Vibrio cholerae: VibH is an amide synthase homologous to nonribosomal peptide synthetase condensation domains. Biochemistry 39:15513-21
    • (2000) Biochemistry , vol.39 , pp. 15513-15521
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3
  • 78
    • 0036295033 scopus 로고    scopus 로고
    • The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains
    • Keating TA, Marshall CG, Walsh CT, Keating AE. 2002. The structure of VibH represents nonribosomal peptide synthetase condensation, cyclization and epimerization domains. Nat. Struct. Biol. 9:522-26
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 522-526
    • Keating, T.A.1    Marshall, C.G.2    Walsh, C.T.3    Keating, A.E.4
  • 79
    • 0034712679 scopus 로고    scopus 로고
    • Expression, purification, and characterization of HMWP2, a 229 kDa, six domain protein subunit of yersiniabactin synthetase
    • Keating TA, Miller DA, Walsh CT. 2000. Expression, purification, and characterization of HMWP2, a 229 kDa, six domain protein subunit of yersiniabactin synthetase. Biochemistry 39:4729-39
    • (2000) Biochemistry , vol.39 , pp. 4729-4739
    • Keating, T.A.1    Miller, D.A.2    Walsh, C.T.3
  • 80
    • 0032829915 scopus 로고    scopus 로고
    • Initiation, elongation, and termination strategies in polyketide and polypeptide antibiotic biosynthesis
    • Keating TA, Walsh CT. 1999. Initiation, elongation, and termination strategies in polyketide and polypeptide antibiotic biosynthesis. Curr. Opin. Chem. Biol. 3:598-606
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 598-606
    • Keating, T.A.1    Walsh, C.T.2
  • 81
    • 1542350231 scopus 로고    scopus 로고
    • The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains
    • Kessler N, Schuhmann H, Morneweg S, Linne U, Marahiel MA. 2004. The linear pentadecapeptide gramicidin is assembled by four multimodular nonribosomal peptide synthetases that comprise 16 modules with 56 catalytic domains. J. Biol. Chem. 279:7413-19
    • (2004) J. Biol. Chem. , vol.279 , pp. 7413-7419
    • Kessler, N.1    Schuhmann, H.2    Morneweg, S.3    Linne, U.4    Marahiel, M.A.5
  • 82
    • 0038112130 scopus 로고    scopus 로고
    • The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans
    • Keszenman-Pereyra D, Lawrence S, Twfieg ME, Price J, Turner G. 2003. The npgA/cfwA gene encodes a putative 4′-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans. Curr. Genet. 43:186-90
    • (2003) Curr. Genet. , vol.43 , pp. 186-190
    • Keszenman-Pereyra, D.1    Lawrence, S.2    Twfieg, M.E.3    Price, J.4    Turner, G.5
  • 83
    • 0035912883 scopus 로고    scopus 로고
    • Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases
    • Kohli RM, Trauger JW, Schwarzer D, Marahiel MA, Walsh CT. 2001. Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases. Biochemistry 40:7099-108
    • (2001) Biochemistry , vol.40 , pp. 7099-7108
    • Kohli, R.M.1    Trauger, J.W.2    Schwarzer, D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 84
    • 0024437776 scopus 로고
    • Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases
    • Kratzschmar J, Krause M, Marahiel MA. 1989. Gramicidin S biosynthesis operon containing the structural genes grsA and grsB has an open reading frame encoding a protein homologous to fatty acid thioesterases. J. Bacteriol. 171:5422-29
    • (1989) J. Bacteriol. , vol.171 , pp. 5422-5429
    • Kratzschmar, J.1    Krause, M.2    Marahiel, M.A.3
  • 86
    • 0028882690 scopus 로고
    • Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase
    • Lambalot RH, Walsh CT. 1995. Cloning, overproduction, and characterization of the Escherichia coli holo-acyl carrier protein synthase. J. Biol. Chem. 270:24658-61
    • (1995) J. Biol. Chem. , vol.270 , pp. 24658-24661
    • Lambalot, R.H.1    Walsh, C.T.2
  • 87
    • 0031419005 scopus 로고    scopus 로고
    • Holo-[acyl-carrier-protein] synthase of Escherichia coli
    • Lambalot RH, Walsh CT 1997. Holo-[acyl-carrier-protein] synthase of Escherichia coli. Methods Enzymol. 279:254-62
    • (1997) Methods Enzymol. , vol.279 , pp. 254-262
    • Lambalot, R.H.1    Walsh, C.T.2
  • 88
    • 0037472114 scopus 로고    scopus 로고
    • Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein
    • Li Q, Khosla C, Puglisi JD, Liu CW. 2003. Solution structure and backbone dynamics of the holo form of the frenolicin acyl carrier protein. Biochemistry 42:4648-57
    • (2003) Biochemistry , vol.42 , pp. 4648-4657
    • Li, Q.1    Khosla, C.2    Puglisi, J.D.3    Liu, C.W.4
  • 89
    • 0035951102 scopus 로고    scopus 로고
    • Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases
    • Linne U, Doekel S, Marahiel MA. 2001. Portability of epimerization domain and role of peptidyl carrier protein on epimerization activity in nonribosomal peptide synthetases. Biochemistry 40:15824-34
    • (2001) Biochemistry , vol.40 , pp. 15824-15834
    • Linne, U.1    Doekel, S.2    Marahiel, M.A.3
  • 90
    • 0034730091 scopus 로고    scopus 로고
    • Control of directionality in nonribosomal peptide synthesis: Role of the condensation domain in preventing misinitiation and timing of epimerization
    • Linne U, Marahiel MA. 2000. Control of directionality in nonribosomal peptide synthesis: role of the condensation domain in preventing misinitiation and timing of epimerization. Biochemistry 39:10439-47
    • (2000) Biochemistry , vol.39 , pp. 10439-10447
    • Linne, U.1    Marahiel, M.A.2
  • 91
    • 0037995374 scopus 로고    scopus 로고
    • Systematic and quantitative analysis of protein-protein recognition between nonribosomal peptide synthetases investigated in the tyrocidine biosynthetic template
    • Linne U, Stein DB, Mootz HD, Marahiel MA. 2003. Systematic and quantitative analysis of protein-protein recognition between nonribosomal peptide synthetases investigated in the tyrocidine biosynthetic template. Biochemistry 42:5114-24
    • (2003) Biochemistry , vol.42 , pp. 5114-5124
    • Linne, U.1    Stein, D.B.2    Mootz, H.D.3    Marahiel, M.A.4
  • 92
    • 0037162408 scopus 로고    scopus 로고
    • Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: Kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B
    • Luo L, Kohli RM, Onishi M, Linne U, Marahiel MA, Walsh CT. 2002. Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B. Biochemistry 41:9184-96
    • (2002) Biochemistry , vol.41 , pp. 9184-9196
    • Luo, L.1    Kohli, R.M.2    Onishi, M.3    Linne, U.4    Marahiel, M.A.5    Walsh, C.T.6
  • 93
    • 0031215148 scopus 로고    scopus 로고
    • Protein templates for the biosynthesis of peptide antibiotics
    • Marahiel MA. 1997. Protein templates for the biosynthesis of peptide antibiotics. Chem. Biol. 4:561-67
    • (1997) Chem. Biol. , vol.4 , pp. 561-567
    • Marahiel, M.A.1
  • 94
    • 9444278428 scopus 로고    scopus 로고
    • Modular peptide synthetases involved in nonribosomal peptide synthesis
    • Marahiel MA, Stachelhaus T, Mootz HD. 1997. Modular peptide synthetases involved in nonribosomal peptide synthesis. Chem. Rev. 97:2651-74
    • (1997) Chem. Rev. , vol.97 , pp. 2651-2674
    • Marahiel, M.A.1    Stachelhaus, T.2    Mootz, H.D.3
  • 95
    • 0028863835 scopus 로고
    • The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase of fatty acid synthesis
    • Marini P, Li S-J, Gardiol D, Cronan JE Jr, de Mendoza D. 1995. The genes encoding the biotin carboxyl carrier protein and biotin carboxylase subunits of Bacillus subtilis acetyl coenzyme A carboxylase of fatty acid synthesis. J. Bacteriol. 177:7003-6
    • (1995) J. Bacteriol. , vol.177 , pp. 7003-7006
    • Marini, P.1    Li, S.-J.2    Gardiol, D.3    Cronan Jr., J.E.4    De Mendoza, D.5
  • 96
    • 0036863098 scopus 로고    scopus 로고
    • Mechanistic diversity and regulation of type II fatty acid synthesis
    • Marrakchi H, Zhang Y-M, Rock CO. 2002. Mechanistic diversity and regulation of type II fatty acid synthesis. Biochem. Soc. Trans. 30:1050-55
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 1050-1055
    • Marrakchi, H.1    Zhang, Y.-M.2    Rock, C.O.3
  • 97
    • 0037039287 scopus 로고    scopus 로고
    • Catalytic mapping of the vibriobactin biosynthetic enzyme VibF
    • Marshall CG, Hillson NJ, Walsh CT. 2002. Catalytic mapping of the vibriobactin biosynthetic enzyme VibF. Biochemistry 41:244-50
    • (2002) Biochemistry , vol.41 , pp. 244-250
    • Marshall, C.G.1    Hillson, N.J.2    Walsh, C.T.3
  • 98
    • 0037126024 scopus 로고    scopus 로고
    • Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases
    • May JJ, Keßler N, Marahiel MA, Stubbs MT. 2002. Crystal structure of DhbE, an archetype for aryl acid activating domains of modular nonribosomal peptide synthetases. Proc. Natl. Acad. Sci. USA 99:12120-25
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12120-12125
    • May, J.J.1    Keßler, N.2    Marahiel, M.A.3    Stubbs, M.T.4
  • 99
    • 0035831486 scopus 로고    scopus 로고
    • The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin
    • May JJ, Wendrich TM, Marahiel MA. 2001. The dhb operon of Bacillus subtilis encodes the biosynthetic template for the catecholic siderophore 2,3-dihydroxybenzoate-glycine-threonine trimeric ester bacillibactin. J. Biol. Chem. 276:7209-17
    • (2001) J. Biol. Chem. , vol.276 , pp. 7209-7217
    • May, J.J.1    Wendrich, T.M.2    Marahiel, M.A.3
  • 100
    • 0034613261 scopus 로고    scopus 로고
    • Biochemical and molecular analyses of the Streptococcus pneumoniae acyl carrier protein synthase, an enzyme essential for fatty acid biosynthesis
    • McAllister KA, Peery RB, Meier TI, Fischl AS, Zhao G. 2000. Biochemical and molecular analyses of the Streptococcus pneumoniae acyl carrier protein synthase, an enzyme essential for fatty acid biosynthesis. J. Biol. Chem. 275:30864-72
    • (2000) J. Biol. Chem. , vol.275 , pp. 30864-30872
    • McAllister, K.A.1    Peery, R.B.2    Meier, T.I.3    Fischl, A.S.4    Zhao, G.5
  • 101
    • 0036009334 scopus 로고    scopus 로고
    • Yersiniabactin synthetase. A four-protein assembly line producing the nonribosomal peptide/polyketide hybrid siderophore of Yersinia pestis
    • Miller DA, Luo L, Hillson N, Keating TA, Walsh CT. 2002. Yersiniabactin synthetase. A four-protein assembly line producing the nonribosomal peptide/polyketide hybrid siderophore of Yersinia pestis. Chem. Biol. 9:333-44
    • (2002) Chem. Biol. , vol.9 , pp. 333-344
    • Miller, D.A.1    Luo, L.2    Hillson, N.3    Keating, T.A.4    Walsh, C.T.5
  • 102
    • 0035339908 scopus 로고    scopus 로고
    • Yersiniabactin synthetase: Probing the recognition of carrier protein domains by the catalytic heterocyclization domains, Cy1 and Cy2, in the chain-initiating HWMP2 subunit
    • Miller DA, Walsh CT. 2001. Yersiniabactin synthetase: probing the recognition of carrier protein domains by the catalytic heterocyclization domains, Cy1 and Cy2, in the chain-initiating HWMP2 subunit. Biochemistry 40:5313-21
    • (2001) Biochemistry , vol.40 , pp. 5313-5321
    • Miller, D.A.1    Walsh, C.T.2
  • 104
    • 0037053388 scopus 로고    scopus 로고
    • Recognition of hybrid peptidyl carrier proteins/acyl carrier proteins in nonribosomal peptide synthetase modules by the 4′-phosphopantetheinyl transferases AcpS and Sfp
    • Mofid MR, Finking R, Marahiel MA. 2002. Recognition of hybrid peptidyl carrier proteins/acyl carrier proteins in nonribosomal peptide synthetase modules by the 4′-phosphopantetheinyl transferases AcpS and Sfp. J. Biol. Chem. 277:17023-31
    • (2002) J. Biol. Chem. , vol.277 , pp. 17023-17031
    • Mofid, M.R.1    Finking, R.2    Marahiel, M.A.3
  • 105
    • 1842531416 scopus 로고    scopus 로고
    • Structure-based mutational analysis of the 4′-phosphopantetheinyl transferases Sfp from Bacillus subtilis: Carrier protein recognition and reaction mechanism
    • Mofid MR, Finking R, Marahiel MA. 2004. Structure-based mutational analysis of the 4′-phosphopantetheinyl transferases Sfp from Bacillus subtilis: carrier protein recognition and reaction mechanism. Biochemistry 43:4128-36
    • (2004) Biochemistry , vol.43 , pp. 4128-4136
    • Mofid, M.R.1    Finking, R.2    Marahiel, M.A.3
  • 106
    • 0033135983 scopus 로고    scopus 로고
    • Crystallization and preliminary crystallographic studies of Sfp: A phosphopantetheinyl transferase of modular peptide synthetases
    • Mofid MR, Marahiel MA, Ficner R, Reuter K. 1999. Crystallization and preliminary crystallographic studies of Sfp: a phosphopantetheinyl transferase of modular peptide synthetases. Acta. Crystallogr. D 55:1098-100
    • (1999) Acta. Crystallogr. D , vol.55 , pp. 1098-1100
    • Mofid, M.R.1    Marahiel, M.A.2    Ficner, R.3    Reuter, K.4
  • 107
    • 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. 276:37289-98
    • (2001) J. Biol. Chem. , vol.276 , pp. 37289-37298
    • Mootz, H.D.1    Finking, R.2    Marahiel, M.A.3
  • 108
    • 0037130634 scopus 로고    scopus 로고
    • Decreasing the ring-size of a nonribosomal peptide antibiotic by in frame module deletion in the biosynthetic genes
    • Mootz HD, Kessler N, Linne U, Eppelmann K, Schwarzer D, Marahiel MA. 2002. Decreasing the ring-size of a nonribosomal peptide antibiotic by in frame module deletion in the biosynthetic genes. J. Am. Chem. Soc. 124:10980-81
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 10980-10981
    • Mootz, H.D.1    Kessler, N.2    Linne, U.3    Eppelmann, K.4    Schwarzer, D.5    Marahiel, M.A.6
  • 109
    • 0030669091 scopus 로고    scopus 로고
    • The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains
    • Mootz HD, Marahiel MA. 1997. The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179:6843-50
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 110
    • 0037118621 scopus 로고    scopus 로고
    • Functional characterization of 4′-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae Lys5
    • Mootz HD, Schörgendorfer K, Marahiel MA. 2002. Functional characterization of 4′-phosphopantetheinyl transferase genes of bacterial and fungal origin by complementation of Saccharomyces cerevisiae Lys5. FEMS Microbiol. Lett. 213:51-57
    • (2002) FEMS Microbiol. Lett. , vol.213 , pp. 51-57
    • Mootz, H.D.1    Schörgendorfer, K.2    Marahiel, M.A.3
  • 111
    • 0034705130 scopus 로고    scopus 로고
    • Construction of hybrid peptide synthetases by module and domain fusions
    • Mootz HD, Schwarzer D, Marahiel MA. 2000. Construction of hybrid peptide synthetases by module and domain fusions. Proc. Natl. Acad. Sci. USA 97:5848-53
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 5848-5853
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 112
    • 0036905773 scopus 로고    scopus 로고
    • Ways of assembling complex natural products on modular nonribosomal peptide synthetases
    • Mootz HD, Schwarzer D, Marahiel MA. 2002. Ways of assembling complex natural products on modular nonribosomal peptide synthetases. ChemBioChem. 3:490-504
    • (2002) ChemBioChem. , vol.3 , pp. 490-504
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.A.3
  • 113
    • 0026520361 scopus 로고
    • Isolation and characterization of sfp: A gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis
    • Nakano MM, Corbell N, Besson J, Zuber P. 1992. Isolation and characterization of sfp: a gene that functions in the production of the lipopeptide biosurfactant, surfactin, in Bacillus subtilis. Mol. Gen. Genet. 232:313-21
    • (1992) Mol. Gen. Genet. , vol.232 , pp. 313-321
    • Nakano, M.M.1    Corbell, N.2    Besson, J.3    Zuber, P.4
  • 114
    • 0034614460 scopus 로고    scopus 로고
    • Expression and assay of an N-methyltransferase involved in the biosynthesis of a vancomycin group antibiotic
    • O'Brien DP, Kirkpatrick PN, O'Brien WW, Staroske T, Richardson TI, et al. 2000. Expression and assay of an N-methyltransferase involved in the biosynthesis of a vancomycin group antibiotic. Chem. Com. 103-4.
    • (2000) Chem. Com. , pp. 103-104
    • O'Brien, D.P.1    Kirkpatrick, P.N.2    O'Brien, W.W.3    Staroske, T.4    Richardson, T.I.5
  • 115
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • Ogle JM, Carter AP, Ramakrishnan V. 2003. Insights into the decoding mechanism from recent ribosome structures. Trends Biochem. Sci. 28:259-66
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 259-266
    • Ogle, J.M.1    Carter, A.P.2    Ramakrishnan, V.3
  • 116
    • 0034662753 scopus 로고    scopus 로고
    • Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites
    • Parris KD, Lin L, Tam A, Mathew R, Hixon J, et al. 2000. Crystal structures of substrate binding to Bacillus subtilis holo-(acyl carrier protein) synthase reveal a novel trimeric arrangement of molecules resulting in three active sites. Struct. Fold. Des. 8:883-95
    • (2000) Struct. Fold. Des. , vol.8 , pp. 883-895
    • Parris, K.D.1    Lin, L.2    Tam, A.3    Mathew, R.4    Hixon, J.5
  • 117
    • 0042318441 scopus 로고    scopus 로고
    • Epimerization of an L-cysteinyl to a D-cysteinyl residue during thiazoline ring formation in siderophore chain elongation by pyochelin synthetase from Pseudomonas aeruginosa
    • Patel HM, Tao J, Walsh CT. 2003. Epimerization of an L-cysteinyl to a D-cysteinyl residue during thiazoline ring formation in siderophore chain elongation by pyochelin synthetase from Pseudomonas aeruginosa. Biochemistry 42:10514-27
    • (2003) Biochemistry , vol.42 , pp. 10514-10527
    • Patel, H.M.1    Tao, J.2    Walsh, C.T.3
  • 118
    • 0035979338 scopus 로고    scopus 로고
    • In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: Characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities
    • Patel HM, Walsh CT. 2001. In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities. Biochemistry 40:9023-31
    • (2001) Biochemistry , vol.40 , pp. 9023-9031
    • Patel, H.M.1    Walsh, C.T.2
  • 120
    • 0019416792 scopus 로고
    • A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein]
    • Polacco ML, Cronan JE Jr. 1981. A mutant of Escherichia coli conditionally defective in the synthesis of holo-[acyl carrier protein]. J. Biol. Chem. 256:5750-54
    • (1981) J. Biol. Chem. , vol.256 , pp. 5750-5754
    • Polacco, M.L.1    Cronan Jr., J.E.2
  • 121
    • 0035716604 scopus 로고    scopus 로고
    • Identification of the α-aminoadipic semialdehyde dehydrogenase-phosphopantetheinyl transferase gene, the human ortholog of the yeast LysS gene
    • Praphanphoj V, Sacksteder KA, Gould SJ, Thomas GH, Geraghty MT. 2001. Identification of the α-aminoadipic semialdehyde dehydrogenase- phosphopantetheinyl transferase gene, the human ortholog of the yeast LysS gene. Mol. Gen. Metab. 72:336-42
    • (2001) Mol. Gen. Metab. , vol.72 , pp. 336-342
    • Praphanphoj, V.1    Sacksteder, K.A.2    Gould, S.J.3    Thomas, G.H.4    Geraghty, M.T.5
  • 122
    • 0033539471 scopus 로고    scopus 로고
    • Assembly of the Pseudomonasaeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF
    • Quadri LE, Keating TA, Patel HM, Walsh CT. 1999. Assembly of the Pseudomonasaeruginosa nonribosomal peptide siderophore pyochelin: in vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF. Biochemistry 38:14941-54
    • (1999) Biochemistry , vol.38 , pp. 14941-14954
    • Quadri, L.E.1    Keating, T.A.2    Patel, H.M.3    Walsh, C.T.4
  • 123
    • 0032501971 scopus 로고    scopus 로고
    • Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases
    • Quadri LE, Weinreb PH, Lei M, Nakano MM, Zuber P, Walsh CT. 1998. Characterization of Sfp, a Bacillus subtilis phosphopantetheinyl transferase for peptidyl carrier protein domains in peptide synthetases. Biochemistry 37:1585-95
    • (1998) Biochemistry , vol.37 , pp. 1585-1595
    • Quadri, L.E.1    Weinreb, P.H.2    Lei, M.3    Nakano, M.M.4    Zuber, P.5    Walsh, C.T.6
  • 124
    • 0035845638 scopus 로고    scopus 로고
    • Mapping of the functional topology of the animal fatty acid synthase by mutant complementation in vitro
    • Rangan VS, Joshi AK, Smith S. 2001. Mapping of the functional topology of the animal fatty acid synthase by mutant complementation in vitro. Biochemistry 40:10792-99
    • (2001) Biochemistry , vol.40 , pp. 10792-10799
    • Rangan, V.S.1    Joshi, A.K.2    Smith, S.3
  • 125
    • 0030911617 scopus 로고    scopus 로고
    • Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA: acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue
    • Rangan VS, Smith S. 1997. Alteration of the substrate specificity of the malonyl-CoA/acetyl-CoA:acyl carrier protein S-acyltransferase domain of the multifunctional fatty acid synthase by mutation of a single arginine residue. J. Biol. Chem. 272:11975-78
    • (1997) J. Biol. Chem. , vol.272 , pp. 11975-11978
    • Rangan, V.S.1    Smith, S.2
  • 126
    • 0035151726 scopus 로고    scopus 로고
    • Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa
    • Reimmann C,Patel HM, Serino L, Barone M, Walsh CT, Haas D. 2001. Essential PchG-dependent reduction in pyochelin biosynthesis of Pseudomonas aeruginosa. J. Bacteriol. 183:813-20
    • (2001) J. Bacteriol. , vol.183 , pp. 813-820
    • Reimmann, C.1    Patel, H.M.2    Serino, L.3    Barone, M.4    Walsh, C.T.5    Haas, D.6
  • 127
    • 0033485259 scopus 로고    scopus 로고
    • Crystal structure of the surfactin synthetase-activating enzyme Sfp: A prototype of the 4′-phosphopantetheinyl transferase superfamily
    • Reuter K, Mofid MR, Marahiel MA, Ficner R. 1999. Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4′-phosphopantetheinyl transferase superfamily. EMBO J. 18:6823-31
    • (1999) EMBO J. , vol.18 , pp. 6823-6831
    • Reuter, K.1    Mofid, M.R.2    Marahiel, M.A.3    Ficner, R.4
  • 128
    • 0142071737 scopus 로고    scopus 로고
    • Ebony: A novel nonribosomal peptide synthetase for β-alanine conjugation with biogenic amines in Drosophila
    • Richardt A, Kemme T, Wagner S, Schwarzer D, Marahiel MA, Hovemann BT. 2003. Ebony: a novel nonribosomal peptide synthetase for β-alanine conjugation with biogenic amines in Drosophila. J. Biol. Chem. 278:41160-66
    • (2003) J. Biol. Chem. , vol.278 , pp. 41160-41166
    • Richardt, A.1    Kemme, T.2    Wagner, S.3    Schwarzer, D.4    Marahiel, M.A.5    Hovemann, B.T.6
  • 129
    • 0030581109 scopus 로고    scopus 로고
    • Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis
    • Rock CO, Cronan JE. 1996. Escherichia coli as a model for the regulation of dissociable (type II) fatty acid biosynthesis. Biochim. Biophys. Acta 1302:1-16
    • (1996) Biochim. Biophys. Acta , vol.1302 , pp. 1-16
    • Rock, C.O.1    Cronan, J.E.2
  • 130
    • 0033926435 scopus 로고    scopus 로고
    • Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90
    • Rouhiainen L, Paulin L, Suomalainen S, Hyytiainen H, Buikema W, et al. 2000. Genes encoding synthetases of cyclic depsipeptides, anabaenopeptilides, in Anabaena strain 90. Mol. Microblol. 37:156-67
    • (2000) Mol. Microblol. , vol.37 , pp. 156-167
    • Rouhiainen, L.1    Paulin, L.2    Suomalainen, S.3    Hyytiainen, H.4    Buikema, W.5
  • 131
    • 0028049440 scopus 로고
    • Entire nucleotide sequence for Bacillus brevis Nagano Grs2 gene encoding gramicidin S synthetase 2: A multifunctional peptide synthetase
    • Saito F, Hori K, Kanda M, Kurotsu T, Saito Y. 1994. Entire nucleotide sequence for Bacillus brevis Nagano Grs2 gene encoding gramicidin S synthetase 2: a multifunctional peptide synthetase. J. Biochem. 116:357-67
    • (1994) J. Biochem. , vol.116 , pp. 357-367
    • Saito, F.1    Hori, K.2    Kanda, M.3    Kurotsu, T.4    Saito, Y.5
  • 134
    • 0026766758 scopus 로고
    • Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases
    • Schmidt B, Riesner D, Lawen A, Kleinkauf H. 1992. Cyclosporin synthetase is a 1.4 MDa multienzyme polypeptide. Re-evaluation of the molecular mass of various peptide synthetases. FEBS Lett. 307:355-60
    • (1992) FEBS Lett. , vol.307 , pp. 355-360
    • Schmidt, B.1    Riesner, D.2    Lawen, A.3    Kleinkauf, H.4
  • 135
    • 1642496906 scopus 로고    scopus 로고
    • The challenge of multidrug resistance: Actual strategies in the development of novel antibacterials
    • Schmidt FR. 2004. The challenge of multidrug resistance: actual strategies in the development of novel antibacterials. Appl. Microbiol. Biotechnol. 63(4):335-43
    • (2004) Appl. Microbiol. Biotechnol. , vol.63 , Issue.4 , pp. 335-343
    • Schmidt, F.R.1
  • 136
    • 0031943369 scopus 로고    scopus 로고
    • Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis
    • Schneider A, Marahiel MA. 1998. Genetic evidence for a role of thioesterase domains, integrated in or associated with peptide synthetases, in non-ribosomal peptide biosynthesis in Bacillus subtilis. Arch. Microbiol. 169:404-10
    • (1998) Arch. Microbiol. , vol.169 , pp. 404-410
    • Schneider, A.1    Marahiel, M.A.2
  • 137
    • 0042242569 scopus 로고    scopus 로고
    • Oxidase domains in epothilone and bleomycin biosynthesis: Thiazoline to thiazole oxidation during chain elongation
    • Schneider TL, Shen B, Walsh CT. 2003. Oxidase domains in epothilone and bleomycin biosynthesis: thiazoline to thiazole oxidation during chain elongation. Biochemistry 42:9722-30
    • (2003) Biochemistry , vol.42 , pp. 9722-9730
    • Schneider, T.L.1    Shen, B.2    Walsh, C.T.3
  • 139
    • 0035023450 scopus 로고    scopus 로고
    • Multimodular biocatalysts for natural product assembly
    • Schwarzer D, Marahiel MA. 2001. Multimodular biocatalysts for natural product assembly. Naturwissenschaften 88:93-101
    • (2001) Naturwissenschaften , vol.88 , pp. 93-101
    • Schwarzer, D.1    Marahiel, M.A.2
  • 140
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer D, Mootz HD, Linne U, Marahiel MA. 2002. Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl. Acad. Sci. USA 99:14083-88
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 14083-14088
    • Schwarzer, D.1    Mootz, H.D.2    Linne, U.3    Marahiel, M.A.4
  • 141
    • 0033150199 scopus 로고    scopus 로고
    • Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization
    • Shaw-Reid CA, Kelleher NL, Losey HC, Gehring AM, Berg C, Walsh CT. 1999. Assembly line enzymology by multimodular nonribosomal peptide synthetases: The thioesterase domain of E. coli EntF catalyzes both elongation and cyclolactonization. Chem. Biol 6:385-400
    • (1999) Chem. Biol. , vol.6 , pp. 385-400
    • Shaw-Reid, C.A.1    Kelleher, N.L.2    Losey, H.C.3    Gehring, A.M.4    Berg, C.5    Walsh, C.T.6
  • 143
    • 0345097576 scopus 로고    scopus 로고
    • Learning from nature's drug factories: Nonribosomal synthesis of macrocyclic peptides
    • Sieber SA, Marahiel MA. 2003. Learning from nature's drug factories: nonribosomal synthesis of macrocyclic peptides. J. Bacteriol. 185:7036-43
    • (2003) J. Bacteriol. , vol.185 , pp. 7036-7043
    • Sieber, S.A.1    Marahiel, M.A.2
  • 144
    • 0842285878 scopus 로고    scopus 로고
    • Peptidyl thiophenols as substrates for nonribosomal peptide cyclases
    • Sieber SA, Tao J, Walsh CT, Marahiel MA. 2004. Peptidyl thiophenols as substrates for nonribosomal peptide cyclases. Angew. Chem. 43:493-98
    • (2004) Angew. Chem. , vol.43 , pp. 493-498
    • Sieber, S.A.1    Tao, J.2    Walsh, C.T.3    Marahiel, M.A.4
  • 145
    • 0042233828 scopus 로고    scopus 로고
    • Loading peptidyl-coenzyme A onto peptidyl carrier proteins: A novel approach in characterizing macrocyclization by thioesterase domains
    • Sieber SA, Walsh CT, Marahiel MA. 2003. Loading peptidyl-coenzyme A onto peptidyl carrier proteins: a novel approach in characterizing macrocyclization by thioesterase domains. J. Am. Chem. Soc. 125:10862-66
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10862-10866
    • Sieber, S.A.1    Walsh, C.T.2    Marahiel, M.A.3
  • 146
    • 0033762192 scopus 로고    scopus 로고
    • The myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sga15
    • Silakowski B, Kunze B, Nordsiek G, Blocker H, Hofle G, Muller R. 2000. The myxochelin iron transport regulon of the myxobacterium Stigmatella aurantiaca Sga15. Eur. J. Biochem. 267:6476-85
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6476-6485
    • Silakowski, B.1    Kunze, B.2    Nordsiek, G.3    Blocker, H.4    Hofle, G.5    Muller, R.6
  • 147
    • 0033601178 scopus 로고    scopus 로고
    • New lessons for combinatorial biosynthesis from myxobacteria. The myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1
    • Silakowski B, Schairer HU, Ehret H, Kunze B, Weinig S, et al. 1999. New lessons for combinatorial biosynthesis from myxobacteria. The myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1. J. Biol. Chem. 274:37391-99
    • (1999) J. Biol. Chem. , vol.274 , pp. 37391-37399
    • Silakowski, B.1    Schairer, H.U.2    Ehret, H.3    Kunze, B.4    Weinig, S.5
  • 148
    • 0030292865 scopus 로고    scopus 로고
    • Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases
    • Stachelhaus T, Hüser A, Marahiel MA. 1996. Biochemical characterization of peptidyl carrier protein (PCP), the thiolation domain of multifunctional peptide synthetases. Chem. Biol. 3:913-21
    • (1996) Chem. Biol. , vol.3 , pp. 913-921
    • Stachelhaus, T.1    Hüser, A.2    Marahiel, M.A.3
  • 149
    • 0028908601 scopus 로고
    • Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA
    • Stachelhaus T, Marahiel MA. 1995. Modular structure of peptide synthetases revealed by dissection of the multifunctional enzyme GrsA. J. Biol. Chem. 270:6163-69
    • (1995) J. Biol. Chem. , vol.270 , pp. 6163-6169
    • Stachelhaus, T.1    Marahiel, M.A.2
  • 150
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain
    • Stachelhaus T, Mootz HD, Bergendahl V, Marahiel MA. 1998. Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain. J. Biol. Chem. 273:22773-81
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 151
    • 0033179468 scopus 로고    scopus 로고
    • The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases
    • Stachelhaus T, Mootz HD, Marahiel MA. 1999. The specificity-conferring code of adenylation domains in nonribosomal peptide synthetases. Chem. Biol. 6:493-505
    • (1999) Chem. Biol. , vol.6 , pp. 493-505
    • Stachelhaus, T.1    Mootz, H.D.2    Marahiel, M.A.3
  • 152
    • 0029034197 scopus 로고
    • Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains
    • Stachelhaus T, Schneider A, Marahiel MA. 1995. Rational design of peptide antibiotics by targeted replacement of bacterial and fungal domains. Science 269:69-72
    • (1995) Science , vol.269 , pp. 69-72
    • Stachelhaus, T.1    Schneider, A.2    Marahiel, M.A.3
  • 153
    • 0034673983 scopus 로고    scopus 로고
    • Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase
    • Stachelhaus T, Walsh CT. 2000. Mutational analysis of the epimerization domain in the initiation module PheATE of gramicidin S synthetase. Biochemistry 39:5775-87
    • (2000) Biochemistry , vol.39 , pp. 5775-5787
    • Stachelhaus, T.1    Walsh, C.T.2
  • 155
    • 0029978534 scopus 로고    scopus 로고
    • The multiple carrier model of nonribosomal peptide biosynthesis at modular multienzymatic templates
    • Stein T, Vater J, Kruft V, Otto A, Wittmann-Liebold B, et al. 1996. The multiple carrier model of nonribosomal peptide biosynthesis at modular multienzymatic templates. J. Biol. Chem. 271:15428-35
    • (1996) J. Biol. Chem. , vol.271 , pp. 15428-15435
    • Stein, T.1    Vater, J.2    Kruft, V.3    Otto, A.4    Wittmann-Liebold, B.5
  • 156
    • 0033976983 scopus 로고    scopus 로고
    • Purification of the fengycin synthetase multienzyme system from Bacillus subtilis b213
    • Steller S, Vater J. 2000. Purification of the fengycin synthetase multienzyme system from Bacillus subtilis b213. J. Chromatogr. B Biomed. Sci. Appl. 737:267-75
    • (2000) J. Chromatogr. B Biomed. Sci. Appl. , vol.737 , pp. 267-275
    • Steller, S.1    Vater, J.2
  • 157
    • 0019888073 scopus 로고
    • Animal fatty acid synthetase. A novel arrangement of the β-ketoacyl synthetase sites comprising domains of the two subunits
    • Stoops JK, Wakil SJ. 1981. Animal fatty acid synthetase. A novel arrangement of the β-ketoacyl synthetase sites comprising domains of the two subunits. J. Biol. Chem. 256:5128-33
    • (1981) J. Biol. Chem. , vol.256 , pp. 5128-5133
    • Stoops, J.K.1    Wakil, S.J.2
  • 158
    • 0020490493 scopus 로고
    • Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the β-ketoacyl synthetase site and their role in its cold inactivation
    • Stoops JK, Wakil SJ. 1982. Animal fatty acid synthetase. Identification of the residues comprising the novel arrangement of the β-ketoacyl synthetase site and their role in its cold inactivation. J. Biol. Chem. 257:3230-35
    • (1982) J. Biol. Chem. , vol.257 , pp. 3230-3235
    • Stoops, J.K.1    Wakil, S.J.2
  • 159
    • 9244228715 scopus 로고
    • ed. G Stoll, B Pfeiffer, J Guglielmi. Heidelberg/Berlin/New York: Spektrum Akad
    • Stryer L. 1995. Biochemie, vierte Auflage, der Fettstoffwechsel, ed. G Stoll, B Pfeiffer, J Guglielmi, pp. 635-37. Heidelberg/Berlin/New York: Spektrum Akad.
    • (1995) Biochemie, Vierte Auflage, der Fettstoffwechsel , pp. 635-637
    • Stryer, L.1
  • 160
    • 0030885954 scopus 로고    scopus 로고
    • Identification, isolation and biochemical characterization of a phosphopantetheine:protein transferase that activates the two type-I fatty acid synthases of Brevibacterium ammoniagenes
    • Stuible H-P, Meier S, Schweizer E. 1997. Identification, isolation and biochemical characterization of a phosphopantetheine:protein transferase that activates the two type-I fatty acid synthases of Brevibacterium ammoniagenes. Eur. J. Biochem. 248:481-87
    • (1997) Eur. J. Biochem. , vol.248 , pp. 481-487
    • Stuible, H.-P.1    Meier, S.2    Schweizer, E.3
  • 161
    • 0032575508 scopus 로고    scopus 로고
    • A novel phosphopantetheine:protein transferase activating yeast mitochondrial acyl carrier protein
    • Stuible H-P, Meier S, Wagner C, Hannappel W, Schweizer E. 1996. A novel phosphopantetheine:protein transferase activating yeast mitochondrial acyl carrier protein. J. Biol. Chem. 273:22334-39
    • (1996) J. Biol. Chem. , vol.273 , pp. 22334-22339
    • Stuible, H.-P.1    Meier, S.2    Wagner, C.3    Hannappel, W.4    Schweizer, E.5
  • 162
    • 0035793081 scopus 로고    scopus 로고
    • Purification, priming, and catalytic acylation of carrier protein domains in the polyketide synthase and nonribosomal peptidyl synthetase modules of the HMWP1 subunit of yersiniabactin synthetase
    • Suo Z, Tseng CC, Walsh CT. 2001. Purification, priming, and catalytic acylation of carrier protein domains in the polyketide synthase and nonribosomal peptidyl synthetase modules of the HMWP1 subunit of yersiniabactin synthetase. Proc. Natl. Acad. Sci. USA 98:99-104
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 99-104
    • Suo, Z.1    Tseng, C.C.2    Walsh, C.T.3
  • 163
    • 0344761973 scopus 로고    scopus 로고
    • Tandem heterocyclization activity of the multidomain 230 kDa HMWP2 subunit of Yersinia pestis yersiniabactin synthetase: Interaction of the 1-1382 and 1383-2035 fragments
    • Suo Z, Walsh CT, Miller DA. 1999. Tandem heterocyclization activity of the multidomain 230 kDa HMWP2 subunit of Yersinia pestis yersiniabactin synthetase: interaction of the 1-1382 and 1383-2035 fragments. Biochemistry 38:14023-35
    • (1999) Biochemistry , vol.38 , pp. 14023-14035
    • Suo, Z.1    Walsh, C.T.2    Miller, D.A.3
  • 164
    • 0026509083 scopus 로고
    • Locating essential Escherichia coli genes by using mini-Tn10 transposons: The pdxJ operon
    • Takiff HE, Baker T, Copeland T, Chen SM, Court DL. 1992. Locating essential Escherichia coli genes by using mini-Tn10 transposons: the pdxJ operon. J. Bacteriol. 174:1544-53
    • (1992) J. Bacteriol. , vol.174 , pp. 1544-1553
    • Takiff, H.E.1    Baker, T.2    Copeland, T.3    Chen, S.M.4    Court, D.L.5
  • 165
    • 0034648798 scopus 로고    scopus 로고
    • Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase
    • Trauger JW, Kohli RM, Mootz HD, Marahiel MA, Walsh CT. 2000. Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase. Nature 407:215-18
    • (2000) Nature , vol.407 , pp. 215-218
    • Trauger, J.W.1    Kohli, R.M.2    Mootz, H.D.3    Marahiel, M.A.4    Walsh, C.T.5
  • 166
    • 0035912930 scopus 로고    scopus 로고
    • Cyclization of backbone-substituted peptides catalyzed by the thioesterase domain from the tyrocidine nonribosomal peptide synthetase
    • Trauger JW, Kohli RM, Walsh CT. 2001. Cyclization of backbone-substituted peptides catalyzed by the thioesterase domain from the tyrocidine nonribosomal peptide synthetase. Biochemistry 40:7092-98
    • (2001) Biochemistry , vol.40 , pp. 7092-7098
    • Trauger, J.W.1    Kohli, R.M.2    Walsh, C.T.3
  • 167
    • 0037069317 scopus 로고    scopus 로고
    • Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase
    • Tseng CC, Bruner SD, Kohli RM, Marahiel MA, Walsh CT, Sieber SA. 2002. Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase. Biochemistry 41:13350-59
    • (2002) Biochemistry , vol.41 , pp. 13350-13359
    • Tseng, C.C.1    Bruner, S.D.2    Kohli, R.M.3    Marahiel, M.A.4    Walsh, C.T.5    Sieber, S.A.6
  • 169
    • 0026926521 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 MA. 1992. Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Mol. Microbiol. 6:529-46
    • (1992) Mol. Microbiol. , vol.6 , pp. 529-546
    • Turgay, K.1    Krause, M.2    Marahiel, M.A.3
  • 172
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • Walsh C. 2000. Molecular mechanisms that confer antibacterial drug resistance. Nature 406:775-81
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.1
  • 173
    • 0035478654 scopus 로고    scopus 로고
    • Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines
    • Walsh CT, Chen H, Keating TA, Hubbard BK, Losey HC, et al. 2001. Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines. Curr. Opin. Chem. Biol. 5:525-34
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 525-534
    • Walsh, C.T.1    Chen, H.2    Keating, T.A.3    Hubbard, B.K.4    Losey, H.C.5
  • 175
    • 0028284699 scopus 로고
    • The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame
    • Weber G, Schorgendorfer K, Schneider-Scherzer E, Leitner E. 1994. The peptide synthetase catalyzing cyclosporine production in Tolypocladium niveum is encoded by a giant 45.8-kilobase open reading frame. Curr. Genet. 26:120-25
    • (1994) Curr. Genet. , vol.26 , pp. 120-125
    • Weber, G.1    Schorgendorfer, K.2    Schneider-Scherzer, E.3    Leitner, E.4
  • 176
    • 0034656331 scopus 로고    scopus 로고
    • Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases
    • Weber T, Baumgartner R, Renner C, Marahiel MA, Holak TA. 2000. Solution structure of PCP, a prototype for the peptidyl carrier domains of modular peptide synthetases. Struct. Fold. Des. 8:407-18
    • (2000) Struct. Fold. Des. , vol.8 , pp. 407-418
    • Weber, T.1    Baumgartner, R.2    Renner, C.3    Marahiel, M.A.4    Holak, T.A.5
  • 177
    • 0035156443 scopus 로고    scopus 로고
    • Exploring the domain structure of modular nonribosomal peptide synthetases
    • Weber T, Marahiel MA. 2001. Exploring the domain structure of modular nonribosomal peptide synthetases. Structure 9:3-9
    • (2001) Structure , vol.9 , pp. 3-9
    • Weber, T.1    Marahiel, M.A.2
  • 178
    • 0142167587 scopus 로고    scopus 로고
    • Melithiazol biosynthesis: Further insights into myxobacterial PKS/NRPS systems and evidence for a new subclass of methyl transferases
    • Weinig S, Hecht H-J, Mahmud T, Müller R. 2003. Melithiazol biosynthesis: further insights into myxobacterial PKS/NRPS systems and evidence for a new subclass of methyl transferases. Chem. Biol. 10:939-52
    • (2003) Chem. Biol. , vol.10 , pp. 939-952
    • Weinig, S.1    Hecht, H.-J.2    Mahmud, T.3    Müller, R.4
  • 179
    • 0029816829 scopus 로고    scopus 로고
    • Fatty acid synthase: In vitro complementation of inactive mutants
    • Witkowski A, Joshi A, Smith S. 1996. Fatty acid synthase: in vitro complementation of inactive mutants. Biochemistry 40:10569-75
    • (1996) Biochemistry , vol.40 , pp. 10569-10575
    • Witkowski, A.1    Joshi, A.2    Smith, S.3
  • 180
    • 0037013187 scopus 로고    scopus 로고
    • The solution structure of acyl carrier protein from Mycobacterium tuberculosis
    • Wong HC, Liu G, Zhang Y-M, Rock CO, Zheng J. 2002. The solution structure of acyl carrier protein from Mycobacterium tuberculosis. J. Biol. Chem. 277:15874-80
    • (2002) J. Biol. Chem. , vol.277 , pp. 15874-15880
    • Wong, H.C.1    Liu, G.2    Zhang, Y.-M.3    Rock, C.O.4    Zheng, J.5
  • 181
    • 0037117747 scopus 로고    scopus 로고
    • Quantitative analysis of the relative contributions of donor acyl carrier proteins, acceptor ketosynthases, and linker regions to intermodular transfer of intermediates in hybrid polyketide synthases
    • Wu N, Cane DE, Khosla C. 2002. Quantitative analysis of the relative contributions of donor acyl carrier proteins, acceptor ketosynthases, and linker regions to intermodular transfer of intermediates in hybrid polyketide synthases. Biochemistry 41:5056-66
    • (2002) Biochemistry , vol.41 , pp. 5056-5066
    • Wu, N.1    Cane, D.E.2    Khosla, C.3
  • 182
    • 0030729715 scopus 로고    scopus 로고
    • Cloning of a Vibrio cholerae vibriobactin gene cluster: Identification of genes required for early steps in siderophore biosynthesis
    • Wyckoff EE, Stoebner JA, Reed KE, Payne SM. 1997. Cloning of a Vibrio cholerae vibriobactin gene cluster: identification of genes required for early steps in siderophore biosynthesis. J. Bacteriol. 179:7055-62
    • (1997) J. Bacteriol. , vol.179 , pp. 7055-7062
    • Wyckoff, E.E.1    Stoebner, J.A.2    Reed, K.E.3    Payne, S.M.4
  • 184
    • 0035896547 scopus 로고    scopus 로고
    • Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III
    • Zhang YM, Rao MS, Heath RJ, Price AC, Olson AJ, et al. 2001. Identification and analysis of the acyl carrier protein (ACP) docking site on β-ketoacyl-ACP synthase III. J. Biol. Chem. 276:8231-38
    • (2001) J. Biol. Chem. , vol.276 , pp. 8231-8238
    • Zhang, Y.M.1    Rao, M.S.2    Heath, R.J.3    Price, A.C.4    Olson, A.J.5


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