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Volumn 67, Issue 1, 2014, Pages 59-64

KtzJ-dependent serine activation and O-methylation by KtzH for kutznerides biosynthesis

Author keywords

Antifungal; Antimicrobial; Interrupted adenylation domain; MbtH like protein; Methyltransferase; Nonribosomal peptide; Protein production and activation

Indexed keywords

ANTIFUNGAL AGENT; KUTZNERIDE DERIVATIVE; METHYLTRANSFERASE; NONRIBOSOMAL PEPTIDE SYNTHETASE; PROTEIN KTZH; PROTEIN KTZJ; UNCLASSIFIED DRUG;

EID: 84893080339     PISSN: 00218820     EISSN: 18811469     Source Type: Journal    
DOI: 10.1038/ja.2013.98     Document Type: Article
Times cited : (25)

References (33)
  • 1
    • 32644436910 scopus 로고    scopus 로고
    • Kutznerides 1-4 depsipeptides from the actinomycete kutzneria sp 744 inhabiting mycorrhizal roots of picea abies seedlings
    • Broberg, A., Menkis, A. & Vasiliauskas, R. Kutznerides 1-4, depsipeptides from the actinomycete Kutzneria sp. 744 inhabiting mycorrhizal roots of Picea abies seedlings. J. Nat. Prod. 69, 97-102 (2006
    • (2006) J. Nat. Prod , vol.69 , pp. 97-102
    • Broberg, A.1    Menkis, A.2    Vasiliauskas, R.3
  • 2
    • 33846443967 scopus 로고    scopus 로고
    • Low-Abundance kutznerides from kutzneria sp 744
    • Pohanka, A., Menkis, A., Levenfors, J. & Broberg, A. Low-Abundance kutznerides from Kutzneria sp. 744. J. Nat. Prod. 69, 1776-1781 (2006
    • (2006) J. Nat. Prod , vol.69 , pp. 1776-1781
    • Pohanka, A.1    Menkis, A.2    Levenfors, J.3    Broberg, A.4
  • 3
    • 36749099421 scopus 로고    scopus 로고
    • Cloning and characterization of the biosynthetic gene cluster for kutznerides
    • Fujimori, D. G. et al. Cloning and characterization of the biosynthetic gene cluster for kutznerides. Proc. Natl Acad. Sci. USA 104, 16498-16503 (2007
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 16498-16503
    • Fujimori, D.G.1
  • 4
    • 84860255172 scopus 로고    scopus 로고
    • Biosynthesis of piperazic acid via N5-hydroxy-ornithine in Kutzneria spp 744
    • Neumann, C. S. et al. Biosynthesis of piperazic acid via N5-hydroxy-ornithine in Kutzneria spp. 744. Chembiochem 13, 972-976 (2012
    • (2012) Chembiochem , vol.13 , pp. 972-976
    • Neumann, C.S.1
  • 5
    • 79959966890 scopus 로고    scopus 로고
    • Biosynthetic chlorination of the piperazate residue in kutzneride biosynthesis by KthP
    • Jiang, W. et al. Biosynthetic chlorination of the piperazate residue in kutzneride biosynthesis by KthP. Biochemistry 50, 6063-6072 (2011
    • (2011) Biochemistry , vol.50 , pp. 6063-6072
    • Jiang, W.1
  • 6
    • 70349394353 scopus 로고    scopus 로고
    • Stereospecific synthesis of threo- and erythro-beta-hydroxyglutamic acid during kutzneride biosynthesis
    • Strieker, M., Nolan, E. M., Walsh, C. T. & Marahiel, M. A. Stereospecific synthesis of threo- And erythro-beta-hydroxyglutamic acid during kutzneride biosynthesis. J. Am. Chem. Soc. 131, 13523-13530 (2009
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 13523-13530
    • Strieker, M.1    Nolan, E.M.2    Walsh, C.T.3    Marahiel, M.A.4
  • 7
    • 54849415919 scopus 로고    scopus 로고
    • Tandem action of the O2- and FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly
    • Heemstra, J. R. Jr. & Walsh, C. T. Tandem action of the O2- And FADH2-dependent halogenases KtzQ and KtzR produce 6,7-dichlorotryptophan for kutzneride assembly. J. Am. Chem. Soc. 130, 14024-14025 (2008
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 14024-14025
    • Heemstra Jr., J.R.1    Walsh, C.T.2
  • 8
    • 54849427485 scopus 로고    scopus 로고
    • Biosynthesis of (II)-(1S,2R)-Allocoronamic acyl thioester by an Fe(II)-dependent halogenase and a cyclopropane-forming flavoprotein
    • Neumann, C. S. & Walsh, C. T. Biosynthesis of (II)-(1S,2R)- Allocoronamic acyl thioester by an Fe(II)-dependent halogenase and a cyclopropane-forming flavoprotein. J. Am. Chem. Soc. 130, 14022-14023 (2008
    • (2008) J. Am. Chem. Soc , vol.130 , pp. 14022-14023
    • Neumann, C.S.1    Walsh, C.T.2
  • 9
    • 59749101384 scopus 로고    scopus 로고
    • A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis
    • McQuade, T. J. et al. A nonradioactive high-throughput assay for screening and characterization of adenylation domains for nonribosomal peptide combinatorial biosynthesis. Anal. Biochem. 386, 244-250 (2009
    • (2009) Anal. Biochem , vol.386 , pp. 244-250
    • McQuade, T.J.1
  • 10
    • 33749512427 scopus 로고    scopus 로고
    • Protein assembly line components in prodigiosin biosyn thesis: Characterization of PigA,G,H,I,J
    • Garneau-Tsodikova, S., Dorrestein, P. C., Kelleher, N. L. & Walsh, C. T. Protein assembly line components in prodigiosin biosynthesis: Characterization of PigA,G,H,I,J. J. Am. Chem. Soc. 128, 12600-12601 (2006
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12600-12601
    • Garneau-Tsodikova, S.1    Dorrestein, P.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 11
    • 14344261742 scopus 로고    scopus 로고
    • Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis
    • Garneau, S., Dorrestein, P. C., Kelleher, N. L. & Walsh, C. T. Characterization of the formation of the pyrrole moiety during clorobiocin and coumermycin A1 biosynthesis. Biochemistry 44, 2770-2780 (2005
    • (2005) Biochemistry , vol.44 , pp. 2770-2780
    • Garneau, S.1    Dorrestein, P.C.2    Kelleher, N.L.3    Walsh, C.T.4
  • 12
    • 77957920621 scopus 로고    scopus 로고
    • MbtH-like proteins as integral components of bacterial nonribosomal peptide synthetases
    • Felnagle, E. A. et al. MbtH-like proteins as integral components of bacterial nonribosomal peptide synthetases. Biochemistry 49, 8815-8817 (2010
    • (2010) Biochemistry , vol.49 , pp. 8815-8817
    • Felnagle, E.A.1
  • 13
    • 78649307586 scopus 로고    scopus 로고
    • Activation of the pacidamycin PacL adenylation domain by MbtH-like proteins
    • Zhang, W., Heemstra, J. R. Jr., Walsh, C. T. & Imker, H. J. Activation of the pacidamycin PacL adenylation domain by MbtH-like proteins. Biochemistry 49, 9946-9947 (2010
    • (2010) Biochemistry , vol.49 , pp. 9946-9947
    • Zhang, W.1    Heemstra Jr., J.R.2    Walsh, C.T.3    Imker, H.J.4
  • 14
    • 84864340102 scopus 로고    scopus 로고
    • Importance of the MbtH-like protein TioT in production and activation of the thiocoraline adenylation domain of TioK
    • Zolova, O. E. & Garneau-Tsodikova, S. Importance of the MbtH-like protein TioT in production and activation of the thiocoraline adenylation domain of TioK. Med. Chem. Comm. 3, 950-955 (2012
    • (2012) Med. Chem. Comm , vol.3 , pp. 950-955
    • Zolova, O.E.1    Garneau-Tsodikova, S.2
  • 15
    • 84874321692 scopus 로고    scopus 로고
    • In vitro characterization of echinomycin biosynthesis: Formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) beta-hydroxytryptophan
    • Zhang, C. et al. In vitro characterization of echinomycin biosynthesis: Formation and hydroxylation of L-tryptophanyl-S-enzyme and oxidation of (2S,3S) beta-hydroxytryptophan. PLoS One 8, e56772 (2013
    • (2013) PLoS One , vol.8
    • Zhang, C.1
  • 16
    • 80054691286 scopus 로고    scopus 로고
    • Role of MbtH-like proteins in the adenylation of tyrosine during aminocoumarin and vancomycin biosynthesis
    • Boll, B., Taubitz, T. & Heide, L. Role of MbtH-like proteins in the adenylation of tyrosine during aminocoumarin and vancomycin biosynthesis. J. Biol. Chem. 286, 36281-36290 (2011
    • (2011) J. Biol. Chem , vol.286 , pp. 36281-36290
    • Boll, B.1    Taubitz, T.2    Heide, L.3
  • 17
    • 84873336552 scopus 로고    scopus 로고
    • Non-ribosomal propeptide precursor in nocardicin A biosynthesis predicted from adenylation domain specificity dependent on the MbtH family protein NocI
    • Davidsen, J. M., Bartley, D. M. & Townsend, C. A. Non-ribosomal propeptide precursor in nocardicin A biosynthesis predicted from adenylation domain specificity dependent on the MbtH family protein NocI. J. Am. Chem. Soc. 135, 1749-1759 (2013
    • (2013) J. Am. Chem. Soc , vol.135 , pp. 1749-1759
    • Davidsen, J.M.1    Bartley, D.M.2    Townsend, C.A.3
  • 18
    • 84863993933 scopus 로고    scopus 로고
    • Analyses of mbtb mbte and mbtf suggest revisions to the mycobactin biosynthesis pathway in mycobacterium tuberculosis
    • McMahon, M. D., Rush, J. S. & Thomas, M. G. Analyses of MbtB, MbtE, and MbtF suggest revisions to the mycobactin biosynthesis pathway in Mycobacterium tuberculosis. J. Bacteriol. 194, 2809-2818 (2012
    • (2012) J. Bacteriol , vol.194 , pp. 2809-2818
    • McMahon, M.D.1    Rush, J.S.2    Thomas, M.G.3
  • 19
    • 78049413334 scopus 로고    scopus 로고
    • N-Acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF
    • Imker, H. J., Krahn, D., Clerc, J., Kaiser, M. & Walsh, C. T. N-Acylation during glidobactin biosynthesis by the tridomain nonribosomal peptide synthetase module GlbF. Chem. Biol. 17, 1077-1083 (2010
    • (2010) Chem. Biol , vol.17 , pp. 1077-1083
    • Imker, H.J.1    Krahn, D.2    Clerc, J.3    Kaiser, M.4    Walsh, C.T.5
  • 20
    • 84872734321 scopus 로고    scopus 로고
    • Structural basis of the interaction of MbtH-like proteins, putative regulators of nonribosomal peptide biosyn thesis, with adenylating enzymes
    • Herbst, D. A., Boll, B., Zocher, G., Stehle, T. & Heide, L. Structural basis of the interaction of MbtH-like proteins, putative regulators of nonribosomal peptide biosynthesis, with adenylating enzymes. J. Biol. Chem. 288, 1991-2003 (2013
    • (2013) J. Biol. Chem , vol.288 , pp. 1991-2003
    • Herbst, D.A.1    Boll, B.2    Zocher, G.3    Stehle, T.4    Heide, L.5
  • 21
    • 79956150138 scopus 로고    scopus 로고
    • Characterization of TioQ, a type II thioesterase from the thiocoraline biosynthetic cluster
    • Mady, A. S. et al. Characterization of TioQ, a type II thioesterase from the thiocoraline biosynthetic cluster. Mol. Biosyst. 7, 1999-2011 (2011
    • (2011) Mol. Biosyst , vol.7 , pp. 1999-2011
    • Mady, A.S.1
  • 22
    • 80855147553 scopus 로고    scopus 로고
    • Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery
    • Baltz, R. H. Function of MbtH homologs in nonribosomal peptide biosynthesis and applications in secondary metabolite discovery. J. Ind. Microbiol. Biotechnol. 38, 1747-1760 (2011
    • (2011) J. Ind. Microbiol. Biotechnol , vol.38 , pp. 1747-1760
    • Baltz, R.H.1
  • 23
    • 34249004256 scopus 로고    scopus 로고
    • Effects of deletions of mbtH-like genes on clorobiocin biosynthesis in Streptomyces coelicolor
    • Wolpert, M., Gust, B., Kammerer, B. & Heide, L. Effects of deletions of mbtH-like genes on clorobiocin biosynthesis in Streptomyces coelicolor. Microbiology 153 (Pt 5), 1413-1423 (2007
    • (2007) Microbiology , vol.153 , Issue.PART 5 , pp. 1413-1423
    • Wolpert, M.1    Gust, B.2    Kammerer, B.3    Heide, L.4
  • 24
    • 34249053161 scopus 로고    scopus 로고
    • MbtH-like proteinmediated cross-talk between non-ribosomal peptide antibiotic and siderophore biosynthetic pathways in Streptomyces coelicolor M145
    • Lautru, S., Oves-Costales, D., Pernodet, J L. & Challis, G. L. MbtH-like proteinmediated cross-talk between non-ribosomal peptide antibiotic and siderophore biosynthetic pathways in Streptomyces coelicolor M145. Microbiology 153 (Pt 5), 1405-1412 (2007
    • (2007) Microbiology , vol.153 , Issue.PART 5 , pp. 1405-1412
    • Lautru, S.1    Oves-Costales, D.2    Pernodet, J.L.3    Challis, G.L.4
  • 25
    • 34547116228 scopus 로고    scopus 로고
    • The 1.8 A crystal structure of PA2412, an MbtH-like protein from the pyoverdine cluster of Pseudomonas aeruginosa
    • Drake, E. J. et al. The 1.8 A crystal structure of PA2412, an MbtH-like protein from the pyoverdine cluster of Pseudomonas aeruginosa. J. Biol. Chem. 282, 20425-20434 (2007
    • (2007) J. Biol. Chem , vol.282 , pp. 20425-20434
    • Drake, E.J.1
  • 26
    • 77955713027 scopus 로고    scopus 로고
    • Solution structure of Rv2377cfounding member of the MbtH-like protein family
    • Buchko, G. W., Kim, C. Y., Terwilliger, T. C. & Myler, P. J. Solution structure of Rv2377cfounding member of the MbtH-like protein family. Tuberculosis 90, 245-251 (2010
    • (2010) Tuberculosis , vol.90 , pp. 245-251
    • Buchko, G.W.1    Kim, C.Y.2    Terwilliger, T.C.3    Myler, P.J.4
  • 27
    • 70350140439 scopus 로고    scopus 로고
    • Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase
    • Gulick, A. M. Conformational dynamics in the Acyl-CoA synthetases, adenylation domains of non-ribosomal peptide synthetases, and firefly luciferase. ACS. Chem. Biol. 4, 811-827 (2009
    • (2009) ACS. Chem. Biol , vol.4 , pp. 811-827
    • Gulick, A.M.1
  • 28
    • 77954653156 scopus 로고    scopus 로고
    • Recent developments in bisintercalator natural products
    • Zolova, O. E., Mady, A. S. & Garneau-Tsodikova, S. Recent developments in bisintercalator natural products. Biopolymers 93, 777-790 (2010
    • (2010) Biopolymers , vol.93 , pp. 777-790
    • Zolova, O.E.1    Mady, A.S.2    Garneau-Tsodikova, S.3
  • 29
    • 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, H. M. & Walsh, C. T. In vitro reconstitution of the Pseudomonas aeruginosa nonribosomal peptide synthesis of pyochelin: Characterization of backbone tailoring thiazoline reductase and N-methyltransferase activities. Biochemistry 40, 9023-9031 (2001
    • (2001) Biochemistry , vol.40 , pp. 9023-9031
    • Patel, H.M.1    Walsh, C.T.2
  • 30
    • 4344669553 scopus 로고    scopus 로고
    • Identification and analysis of the core biosynthetic machinery of tubulysin, a potent cytotoxin with potential anticancer activity
    • Sandmann, A., Sasse, F. & Muller, R. Identification and analysis of the core biosynthetic machinery of tubulysin, a potent cytotoxin with potential anticancer activity. Chem. Biol. 11, 1071-1079 (2004
    • (2004) Chem. Biol , vol.11 , pp. 1071-1079
    • Sandmann, A.1    Sasse, F.2    Muller, R.3
  • 31
    • 33747799012 scopus 로고    scopus 로고
    • Characterization of the cereulide NRPS alpha-hydroxy acid specifying modules: Activation of alpha-keto acids and chiral reduction on the assembly line
    • Magarvey, N. A., Ehling-Schulz, M. & Walsh, C. T. Characterization of the cereulide NRPS alpha-hydroxy acid specifying modules: Activation of alpha-keto acids and chiral reduction on the assembly line. J. Am. Chem. Soc. 128, 10698-10699 (2006
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 10698-10699
    • Magarvey, N.A.1    Ehling-Schulz, M.2    Walsh, C.T.3
  • 32
    • 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. et al. New lessons for combinatorial biosynthesis from myxobacteria. The myxothiazol biosynthetic gene cluster of Stigmatella aurantiaca DW4/3-1. J. Biol. Chem. 274, 37391-37399 (1999
    • (1999) J. Biol. Chem , vol.274 , pp. 37391-37399
    • Silakowski, B.1
  • 33
    • 0142167587 scopus 로고    scopus 로고
    • Melithiazol biosyn thesis: Further insights into myxobacterial PKS/NRPS systems and evidence for a new subclass of methyl transferases
    • Weinig, S., Hecht, H. J., Mahmud, T. & Muller, R. Melithiazol biosynthesis: Further insights into myxobacterial PKS/NRPS systems and evidence for a new subclass of methyl transferases. Chem. Biol. 10, 939-952 (2003
    • (2003) Chem. Biol , vol.10 , pp. 939-952
    • Weinig, S.1    Hecht, H.J.2    Mahmud, T.3    Muller, R.4


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