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Volumn 271, Issue 8, 2004, Pages 1536-1545

Mutational analysis of a type II thioesterase associated with nonribosomal peptide synthesis

Author keywords

Catalytic triad; Fatty acid synthases; Nonribosomal peptide synthesis; Peptide synthetases; Type II thioesterase polyketide synthases

Indexed keywords

ALANINE; ALIPHATIC COMPOUND; ASPARAGINE; CYSTEINE; HYDROLASE; LIPOPEPTIDE; RIBOSOME PROTEIN; SERINE; SURFACTIN; THIOL ESTER HYDROLASE;

EID: 2142710129     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.2004.04063.x     Document Type: Article
Times cited : (31)

References (50)
  • 1
    • 0037088538 scopus 로고    scopus 로고
    • Cloning and characterization of an S-formylglutathione hydrolase from Arabidopsis thaliana
    • Kordic, S., Cummins, I. & Edwards, R. (2002) Cloning and characterization of an S-formylglutathione hydrolase from Arabidopsis thaliana. Arch. Biochem. Biophys. 399, 232-238.
    • (2002) Arch. Biochem. Biophys. , vol.399 , pp. 232-238
    • Kordic, S.1    Cummins, I.2    Edwards, R.3
  • 2
    • 0035875063 scopus 로고    scopus 로고
    • Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis
    • Das, A.K., Lu, J.Y. & Hofmann, S.L. (2001) Biochemical analysis of mutations in palmitoyl-protein thioesterase causing infantile and late-onset forms of neuronal ceroid lipofuscinosis. Hum. Mol. Genet. 10, 1431-1439.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1431-1439
    • Das, A.K.1    Lu, J.Y.2    Hofmann, S.L.3
  • 3
    • 0035023450 scopus 로고    scopus 로고
    • Multimodular biocatalysts for natural product assembly
    • Schwarzer, D. & Marahiel, M.A. (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
  • 4
    • 0033485280 scopus 로고    scopus 로고
    • The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases
    • Cane, D.E. & Walsh, C.T. (1999) The parallel and convergent universes of polyketide synthases and nonribosomal peptide synthetases. Chem. Biol. 6, R319-R325.
    • (1999) Chem. Biol. , vol.6
    • Cane, D.E.1    Walsh, C.T.2
  • 6
    • 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, M.R., Marahiel, M.A. & Ficner, R. (1999) Crystal structure of the surfactin synthetase-activating enzyme Sfp: a prototype of the 4′-phosphopantetheinyl-transferase superfamily. EMBO J. 18, 6823-6831.
    • (1999) EMBO J. , vol.18 , pp. 6823-6831
    • Reuter, K.1    Mofid, M.R.2    Marahiel, M.A.3    Ficner, R.4
  • 7
    • 0348087044 scopus 로고    scopus 로고
    • Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore synthesis in Pseudomonas aeruginosa
    • Finking, R., Solsbacher, J., Konz, D., Schobert, M., Schafer, A., Jahn, D. & Marahiel, M.A. (2002) Characterization of a new type of phosphopantetheinyl transferase for fatty acid and siderophore synthesis in Pseudomonas aeruginosa. J. Biol. Chem. 277, 50293-50302.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50293-50302
    • Finking, R.1    Solsbacher, J.2    Konz, D.3    Schobert, M.4    Schafer, A.5    Jahn, D.6    Marahiel, M.A.7
  • 8
    • 0035813125 scopus 로고    scopus 로고
    • 4′-Phosphopantetheine transfer in primary and secondary metabolism of Bacillus subtilis
    • Mootz, H.D., Finking, R. & Marahiel, M.A. (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
  • 9
    • 0034648798 scopus 로고    scopus 로고
    • Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase
    • Trauger, J., Kohli, R., Mootz, H., Marahiel, M. & Walsh, C. (2000) Peptide cyclization catalysed by the thioesterase domain of tyrocidine synthetase. Nature (London) 407, 215-218.
    • (2000) Nature (London) , vol.407 , pp. 215-218
    • Trauger, J.1    Kohli, R.2    Mootz, H.3    Marahiel, M.4    Walsh, C.5
  • 10
    • 0035912883 scopus 로고    scopus 로고
    • Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases
    • Kohli, R.M., Trauger, J.W., Schwarzer, D., Marahiel, M.A. & Walsh, C.T. (2001) Generality of peptide cyclization catalyzed by isolated thioesterase domains of nonribosomal peptide synthetases. Biochemistry 40, 7099-7108.
    • (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
  • 11
    • 0037069317 scopus 로고    scopus 로고
    • Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase
    • Tseng, C.C., Bruner, S.D., Kohli, R.M., Marahiel, M.A., Walsh, C.T. & Sieber, S.A. (2002) Characterization of the surfactin synthetase C-terminal thioesterase domain as a cyclic depsipeptide synthase. Biochemistry 41, 13350-13359.
    • (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
  • 12
    • 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, M.A. (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, 404-410.
    • (1998) Arch. Microbiol. , vol.169 , pp. 404-410
    • Schneider, A.1    Marahiel, M.A.2
  • 13
    • 0033942260 scopus 로고    scopus 로고
    • Yersinia pestis YbtU and YbtT are involved in synthesis of the siderophore yersiniabactin but have different effects on regulation
    • Geoffroy, V.A., Fetherston, J.D. & Perry, R.D. (2000) Yersinia pestis YbtU and YbtT are involved in synthesis of the siderophore yersiniabactin but have different effects on regulation. Infect Immun. 68, 4452-4461.
    • (2000) Infect Immun. , vol.68 , pp. 4452-4461
    • Geoffroy, V.A.1    Fetherston, J.D.2    Perry, R.D.3
  • 14
    • 0033133991 scopus 로고    scopus 로고
    • Impact of thioesterase activity on tylosin biosynthesis in Streptomyces fradiae
    • Butler, A.R., Bate, N. & Cundliffe, E. (1999) Impact of thioesterase activity on tylosin biosynthesis in Streptomyces fradiae. Chem. Biol. 6, 287-292.
    • (1999) Chem. Biol. , vol.6 , pp. 287-292
    • Butler, A.R.1    Bate, N.2    Cundliffe, E.3
  • 15
    • 0035068571 scopus 로고    scopus 로고
    • Role of type II thioesterases: Evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units
    • Heathcote, M.L., Staunton, J. & Leadlay, P.F. (2001) Role of type II thioesterases: evidence for removal of short acyl chains produced by aberrant decarboxylation of chain extender units. Chem. Biol. 8, 207-220.
    • (2001) Chem. Biol. , vol.8 , pp. 207-220
    • Heathcote, M.L.1    Staunton, J.2    Leadlay, P.F.3
  • 16
    • 0037073685 scopus 로고    scopus 로고
    • Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin
    • Kim, B.S., Cropp, T.A., Beck, B.J., Sherman, D.H. & Reynolds, K.A. (2002) Biochemical evidence for an editing role of thioesterase II in the biosynthesis of the polyketide pikromycin. J. Biol. Chem. 277, 48028-48034.
    • (2002) J. Biol. Chem. , vol.277 , pp. 48028-48034
    • Kim, B.S.1    Cropp, T.A.2    Beck, B.J.3    Sherman, D.H.4    Reynolds, K.A.5
  • 17
    • 0037195068 scopus 로고    scopus 로고
    • Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases
    • Schwarzer, D., Mootz, H.D., Linne, U. & Marahiel, M.A. (2002) Regeneration of misprimed nonribosomal peptide synthetases by type II thioesterases. Proc. Natl Acad. Sci. USA 99, 14083-14088.
    • (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
  • 18
    • 0023664065 scopus 로고
    • Regulation of pantothenate kinase by coenzyme A and its thioesters
    • Vallari, D.S., Jackowski, S. & Rock, C.O. (1987) Regulation of pantothenate kinase by coenzyme A and its thioesters. J. Biol. Chem. 262, 2468-2471.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2468-2471
    • Vallari, D.S.1    Jackowski, S.2    Rock, C.O.3
  • 19
    • 0023096434 scopus 로고
    • Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thioester hydrolase from rat mammary gland
    • Randhawa, Z.I. & Smith, S. (1987) Complete amino acid sequence of the medium-chain S-acyl fatty acid synthetase thioester hydrolase from rat mammary gland. Biochemistry 26, 1365-1373.
    • (1987) Biochemistry , vol.26 , pp. 1365-1373
    • Randhawa, Z.I.1    Smith, S.2
  • 20
    • 0023187912 scopus 로고
    • Cloning and sequencing of the medium-chain S-acyl fatty acid synthetase thioester hydrolase cDNA from rat mammary gland
    • Naggert, J., Williams, B., Cashman, D.P. & Smith, S. (1987) Cloning and sequencing of the medium-chain S-acyl fatty acid synthetase thioester hydrolase cDNA from rat mammary gland. Biochem. J. 243, 597-601.
    • (1987) Biochem. J. , vol.243 , pp. 597-601
    • Naggert, J.1    Williams, B.2    Cashman, D.P.3    Smith, S.4
  • 21
    • 0027340323 scopus 로고
    • Roles of Ser101, Asp236, and His237 in catalysis of thioesterase II and of the C-terminal region of the enzyme in its interaction with fatty acid synthase
    • Tai, M.H., Chirala, S.S. & Wakil, S.J. (1993) Roles of Ser101, Asp236, and His237 in catalysis of thioesterase II and of the C-terminal region of the enzyme in its interaction with fatty acid synthase. Proc. Natl Acad. Sci. USA 90, 1852-1856.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1852-1856
    • Tai, M.H.1    Chirala, S.S.2    Wakil, S.J.3
  • 22
    • 0026661647 scopus 로고
    • Utilization of an active serine 101-cysteine mutant to demonstrate the proximity of the catalytic serine 101 and histidine 237 residues in thioesterase H
    • Witkowski, A., Naggert, J., Witkowska, H.E., Randhawa, Z.I. & Smith, S. (1992) Utilization of an active serine 101-cysteine mutant to demonstrate the proximity of the catalytic serine 101 and histidine 237 residues in thioesterase H. J. Biol. Chem. 267, 18488-18492.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18488-18492
    • Witkowski, A.1    Naggert, J.2    Witkowska, H.E.3    Randhawa, Z.I.4    Smith, S.5
  • 23
    • 0025954263 scopus 로고
    • A catalytic role for histidine 237 in rat mammary gland thioesterase II
    • Witkowski, A., Naggert, J., Wessa, B. & Smith, S. (1991) A catalytic role for histidine 237 in rat mammary gland thioesterase II. J. Biol. Chem. 266, 18514-18519.
    • (1991) J. Biol. Chem. , vol.266 , pp. 18514-18519
    • Witkowski, A.1    Naggert, J.2    Wessa, B.3    Smith, S.4
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of the bacteriophage T4
    • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227, 491-493.
    • (1970) Nature (London) , vol.227 , pp. 491-493
    • Laemmli, U.K.1
  • 26
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, C.T. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-269
    • Yang, C.T.1
  • 27
    • 0033852319 scopus 로고    scopus 로고
    • Biosynthesis of the anti-parasitic agent megalomicin: Transformation of erythromycin to megalomicin in Saccharopolyspora erythraea
    • Volchegursky, Y., Hu, Z., Katz, L. & McDaniel, R. (2000) Biosynthesis of the anti-parasitic agent megalomicin: transformation of erythromycin to megalomicin in Saccharopolyspora erythraea. Mol. Microbiol. 37, 752-762.
    • (2000) Mol. Microbiol. , vol.37 , pp. 752-762
    • Volchegursky, Y.1    Hu, Z.2    Katz, L.3    McDaniel, R.4
  • 28
    • 0030669091 scopus 로고    scopus 로고
    • The tyrocidine biosynthesis operon of Bacillus brevis: Complete nucleotide sequence and biochemical characterization of functional internal adenylation domains
    • Mootz, H.D. & Marahiel, M.A. (1997) The tyrocidine biosynthesis operon of Bacillus brevis: complete nucleotide sequence and biochemical characterization of functional internal adenylation domains. J. Bacteriol. 179, 6843-6850.
    • (1997) J. Bacteriol. , vol.179 , pp. 6843-6850
    • Mootz, H.D.1    Marahiel, M.A.2
  • 29
    • 0032955583 scopus 로고    scopus 로고
    • Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin
    • Konz, D., Doekel, S. & Marahiel, M.A. (1999) Molecular and biochemical characterization of the protein template controlling biosynthesis of the lipopeptide lichenysin. J. Bacteriol. 181, 133-140.
    • (1999) J. Bacteriol. , vol.181 , pp. 133-140
    • Konz, D.1    Doekel, S.2    Marahiel, M.A.3
  • 31
    • 0036120595 scopus 로고    scopus 로고
    • Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE
    • Bruner, S.D., Weber, T., Kohli, R.M., Schwarzer, D., Marahiel, M.A., Walsh, C.T. & Stubbs, M.T. (2002) Structural basis for the cyclization of the lipopeptide antibiotic surfactin by the thioesterase domain SrfTE. Structure (Camb). 10, 301-310.
    • (2002) Structure (Camb). , vol.10 , pp. 301-310
    • Bruner, S.D.1    Weber, T.2    Kohli, R.M.3    Schwarzer, D.4    Marahiel, M.A.5    Walsh, C.T.6    Stubbs, M.T.7
  • 32
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson, G. & Wlodawer, A. (1998) Catalytic triads and their relatives. Trends Biochem. Sci. 23, 347-352.
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 33
    • 0022342164 scopus 로고
    • Inhibition of the functional interaction between fatty acid synthetase and thioesterase II by modification of a single cysteine thiol on the thioesterase
    • Witkowski, A. & Smith, S. (1985) Inhibition of the functional interaction between fatty acid synthetase and thioesterase II by modification of a single cysteine thiol on the thioesterase. Arch. Biochem. Biophys. 243, 420-426.
    • (1985) Arch. Biochem. Biophys. , vol.243 , pp. 420-426
    • Witkowski, A.1    Smith, S.2
  • 35
    • 0029049768 scopus 로고
    • Crystallization and preliminary diffraction studies of thioesterase II from rat mammary gland
    • Buchbinder, J.L., Witkowski, A., Smith, S. & Fletterick, R.J. (1995) Crystallization and preliminary diffraction studies of thioesterase II from rat mammary gland. Proteins 22, 73-75.
    • (1995) Proteins , vol.22 , pp. 73-75
    • Buchbinder, J.L.1    Witkowski, A.2    Smith, S.3    Fletterick, R.J.4
  • 36
    • 0028040231 scopus 로고
    • Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase
    • Witkowski, A., Witkowska, H.E. & Smith, S. (1994) Reengineering the specificity of a serine active-site enzyme. Two active-site mutations convert a hydrolase to a transferase. J. Biol. Chem. 269, 379-383.
    • (1994) J. Biol. Chem. , vol.269 , pp. 379-383
    • Witkowski, A.1    Witkowska, H.E.2    Smith, S.3
  • 38
    • 0035909913 scopus 로고    scopus 로고
    • Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: Versatility from a unique substrate channel
    • Tsai, S.C., Miercke, L.J., Krucinski, J., Gokhale, R., Chen, J.C., Foster, P.G., Cane, D.E., Khosla, C. & Stroud, R.M. (2001) Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel. Proc. Natl Acad. Sci. USA 98, 14808-14813.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14808-14813
    • Tsai, S.C.1    Miercke, L.J.2    Krucinski, J.3    Gokhale, R.4    Chen, J.C.5    Foster, P.G.6    Cane, D.E.7    Khosla, C.8    Stroud, R.M.9
  • 39
    • 0031459595 scopus 로고    scopus 로고
    • The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: Molecular characterization of three multi-modular peptide synthetases
    • Konz, D., Klens, A., Schorgendorfer, K. & Marahiel, M.A. (1997) The bacitracin biosynthesis operon of Bacillus licheniformis ATCC 10716: molecular characterization of three multi-modular peptide synthetases. Chem. Biol. 4, 927-937.
    • (1997) Chem. Biol. , vol.4 , pp. 927-937
    • Konz, D.1    Klens, A.2    Schorgendorfer, K.3    Marahiel, M.A.4
  • 40
  • 41
    • 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, M.A. (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, 5422-5429.
    • (1989) J. Bacteriol. , vol.171 , pp. 5422-5429
    • Kratzschmar, J.1    Krause, M.2    Marahiel, M.A.3
  • 43
    • 2142743387 scopus 로고    scopus 로고
    • Proteus mirabilis NrpS (nrpS) gene, partial cds, NrpU (nrpU), NrpT (nrpT), NrpA (nrpA), NrpB (nrpB), NrpG (nrpG) and IrpP (irpP) genes, complete cds
    • accession number U46488
    • Gaisser, S. & Hughes, C. (1996) Proteus mirabilis NrpS (nrpS) gene, partial cds, NrpU (nrpU), NrpT (nrpT), NrpA (nrpA), NrpB (nrpB), NrpG (nrpG) and IrpP (irpP) genes, complete cds. NCBI Nucleotide Databank, accession number U46488. http:// www.ncbi.nlm.nih.gov.
    • (1996) NCBI Nucleotide Databank
    • Gaisser, S.1    Hughes, C.2
  • 44
    • 0034047123 scopus 로고    scopus 로고
    • Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: Analysis of the gene cluster and deduction of the biosynthetic pathway
    • Brautaset, T., Sekurova, O.N., Sletta, H., Ellingsen, T.E., StrLm, A.R., Valla, S. & Zotchev, S.B. (2000) Biosynthesis of the polyene antifungal antibiotic nystatin in Streptomyces noursei ATCC 11455: analysis of the gene cluster and deduction of the biosynthetic pathway. Chem. Biol. 7, 395-403.
    • (2000) Chem. Biol. , vol.7 , pp. 395-403
    • Brautaset, T.1    Sekurova, O.N.2    Sletta, H.3    Ellingsen, T.E.4    StrLm, A.R.5    Valla, S.6    Zotchev, S.B.7
  • 45
    • 0031020825 scopus 로고    scopus 로고
    • Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron- regulated pchDCBA operon in Pseudomonas aeruginosa
    • Serino, L., Reimmann, C., Visca, P., Beyeler, M., Chiesa, V.D. & Haas, D. (1997) Biosynthesis of pyochelin and dihydroaeruginoic acid requires the iron- regulated pchDCBA operon in Pseudomonas aeruginosa. J. Bacteriol. 179, 248-257.
    • (1997) J. Bacteriol. , vol.179 , pp. 248-257
    • Serino, L.1    Reimmann, C.2    Visca, P.3    Beyeler, M.4    Chiesa, V.D.5    Haas, D.6
  • 46
    • 0032514668 scopus 로고    scopus 로고
    • A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: Architecture of metabolic diversity
    • Xue, Y., Zhao, L., Liu, H.W. & Sherman, D.H. (1998) A gene cluster for macrolide antibiotic biosynthesis in Streptomyces venezuelae: architecture of metabolic diversity. Proc. Natl Acad. Sci. USA 95, 12111-12116.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 12111-12116
    • Xue, Y.1    Zhao, L.2    Liu, H.W.3    Sherman, D.H.4
  • 47
    • 0033763409 scopus 로고    scopus 로고
    • A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis
    • Aparicio, J.F., Fouces, R., Mendes, M.V., Olivera, N. & Martin, J.F. (2000) A complex multienzyme system encoded by five polyketide synthase genes is involved in the biosynthesis of the 26-membered polyene macrolide pimaricin in Streptomyces natalensis. Chem. Biol. 7, 895-905.
    • (2000) Chem. Biol. , vol.7 , pp. 895-905
    • Aparicio, J.F.1    Fouces, R.2    Mendes, M.V.3    Olivera, N.4    Martin, J.F.5
  • 48
    • 13144258781 scopus 로고    scopus 로고
    • Biosynthesis of the ansamycin antibiotic rifamycin: Deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699
    • August, P.R., Tang, L. et al. e. (1998) Biosynthesis of the ansamycin antibiotic rifamycin: deductions from the molecular analysis of the rif biosynthetic gene cluster of Amycolatopsis mediterranei S699. Chem. Biol. 5, 69-79.
    • (1998) Chem. Biol. , vol.5 , pp. 69-79
    • August, P.R.1    Tang, L.2
  • 49
    • 0030895052 scopus 로고    scopus 로고
    • Genetic organization of the yersiniabactin biosynthetic region and construction of avirulent mutants in Yersinia pestis
    • Bearden, S.W., Fetherston, J.D. & Perry, R.D. (1997) Genetic organization of the yersiniabactin biosynthetic region and construction of avirulent mutants in Yersinia pestis. Infect. Immun. 65, 1659-1668.
    • (1997) Infect. Immun. , vol.65 , pp. 1659-1668
    • Bearden, S.W.1    Fetherston, J.D.2    Perry, R.D.3
  • 50
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: The family keeps growing
    • Nardini, M. & Dijkstra, B.W. (1999) Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9, 732-737.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijkstra, B.W.2


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