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Volumn 138, Issue 21, 2016, Pages 6746-6753

Regulation of the P450 oxygenation cascade involved in glycopeptide antibiotic biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBIOTICS; ASSOCIATION REACTIONS; BIOCHEMISTRY; BIOSYNTHESIS; CATALYSIS; CATALYST ACTIVITY; CYCLIZATION; ENZYMES; REACTION KINETICS;

EID: 84973301114     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/jacs.6b00307     Document Type: Article
Times cited : (46)

References (52)
  • 1
    • 0033516914 scopus 로고    scopus 로고
    • Chemistry, Biology, and Medicine of the Glycopeptide Antibiotics
    • Nicolaou, K. C.; Boddy, C. N. C.; Bräse, S.; Winssinger, N. Chemistry, Biology, and Medicine of the Glycopeptide Antibiotics Angew. Chem., Int. Ed. 1999, 38, 2096-2152 10.1002/(SICI)1521-3773(19990802)38:15<2096::AID-ANIE2096>3.0.CO;2-F
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 2096-2152
    • Nicolaou, K.C.1    Boddy, C.N.C.2    Bräse, S.3    Winssinger, N.4
  • 3
    • 73349085562 scopus 로고    scopus 로고
    • Working outside the protein-synthesis rules: Insights into non-ribosomal peptide synthesis
    • Marahiel, M. A. Working outside the protein-synthesis rules: Insights into non-ribosomal peptide synthesis J. Pept. Sci. 2009, 15, 799-807 10.1002/psc.1183
    • (2009) J. Pept. Sci. , vol.15 , pp. 799-807
    • Marahiel, M.A.1
  • 4
    • 84870062242 scopus 로고    scopus 로고
    • Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology
    • Hur, G. H.; Vickery, C. R.; Burkart, M. D. Explorations of catalytic domains in non-ribosomal peptide synthetase enzymology Nat. Prod. Rep. 2012, 29, 1074-1098 10.1039/c2np20025b
    • (2012) Nat. Prod. Rep. , vol.29 , pp. 1074-1098
    • Hur, G.H.1    Vickery, C.R.2    Burkart, M.D.3
  • 5
    • 0036905773 scopus 로고    scopus 로고
    • Ways of assembling complex natural products on modular nonribosomal peptide synthetases
    • Mootz, H. D.; Schwarzer, D.; Marahiel, M. a. Ways of assembling complex natural products on modular nonribosomal peptide synthetases ChemBioChem 2002, 3, 490-504 10.1002/1439-7633(20020603)3:6<490::AID-CBIC490>3.0.CO;2-N
    • (2002) ChemBioChem , vol.3 , pp. 490-504
    • Mootz, H.D.1    Schwarzer, D.2    Marahiel, M.3
  • 6
    • 84863615074 scopus 로고    scopus 로고
    • Synthetic Biology of secondary metabolite biosynthesis in actinomycetes: Engineering precursor supply as a way to optimize antibiotic production
    • Wohlleben, W.; Mast, Y.; Muth, G.; Röttgen, M.; Stegmann, E.; Weber, T. Synthetic Biology of secondary metabolite biosynthesis in actinomycetes: Engineering precursor supply as a way to optimize antibiotic production FEBS Lett. 2012, 586, 2171-2176 10.1016/j.febslet.2012.04.025
    • (2012) FEBS Lett. , vol.586 , pp. 2171-2176
    • Wohlleben, W.1    Mast, Y.2    Muth, G.3    Röttgen, M.4    Stegmann, E.5    Weber, T.6
  • 7
    • 84937677289 scopus 로고    scopus 로고
    • Structural aspects of phenylglycines, their biosynthesis and occurrence in peptide natural products
    • Al Toma, R. S.; Brieke, C.; Cryle, M. J.; Süssmuth, R. D. Structural aspects of phenylglycines, their biosynthesis and occurrence in peptide natural products Nat. Prod. Rep. 2015, 32, 1207-1235 10.1039/C5NP00025D
    • (2015) Nat. Prod. Rep. , vol.32 , pp. 1207-1235
    • Al Toma, R.S.1    Brieke, C.2    Cryle, M.J.3    Süssmuth, R.D.4
  • 8
    • 42149190531 scopus 로고    scopus 로고
    • How to tailor non-ribosomal peptide products - New clues about the structures and mechanisms of modifying enzymes
    • Samel, S. A.; Marahiel, M. A.; Essen, L.-O. How to tailor non-ribosomal peptide products-new clues about the structures and mechanisms of modifying enzymes Mol. BioSyst. 2008, 4, 387-393 10.1039/b717538h
    • (2008) Mol. BioSyst. , vol.4 , pp. 387-393
    • Samel, S.A.1    Marahiel, M.A.2    Essen, L.-O.3
  • 9
    • 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, R. M.; Onishi, M.; Linne, U.; Marahiel, M. A.; Walsh, C. T. Timing of epimerization and condensation reactions in nonribosomal peptide assembly lines: kinetic analysis of phenylalanine activating elongation modules of tyrocidine synthetase B Biochemistry 2002, 41, 9184-9196 10.1021/bi026047+
    • (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
  • 10
    • 84928911386 scopus 로고    scopus 로고
    • Interrupted adenylation domains: Unique bifunctional enzymes involved in nonribosomal peptide biosynthesis
    • Labby, K. J.; Watsula, S. G.; Garneau-Tsodikova, S. Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis Nat. Prod. Rep. 2015, 32, 641-653 10.1039/C4NP00120F
    • (2015) Nat. Prod. Rep. , vol.32 , pp. 641-653
    • Labby, K.J.1    Watsula, S.G.2    Garneau-Tsodikova, S.3
  • 11
    • 84957046982 scopus 로고    scopus 로고
    • Cyclization of polyketides and non-ribosomal peptides on and off their assembly lines
    • Pang, B.; Wang, M.; Liu, W. Cyclization of polyketides and non-ribosomal peptides on and off their assembly lines Nat. Prod. Rep. 2016, 33, 162-173 10.1039/C5NP00095E
    • (2016) Nat. Prod. Rep. , vol.33 , pp. 162-173
    • Pang, B.1    Wang, M.2    Liu, W.3
  • 12
    • 84957104073 scopus 로고    scopus 로고
    • Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: Logic gate or a victim of fate?
    • Horsman, M. E.; Hari, T. P. A.; Boddy, C. N. Polyketide synthase and non-ribosomal peptide synthetase thioesterase selectivity: logic gate or a victim of fate? Nat. Prod. Rep. 2016, 33, 183-202 10.1039/C4NP00148F
    • (2016) Nat. Prod. Rep. , vol.33 , pp. 183-202
    • Horsman, M.E.1    Hari, T.P.A.2    Boddy, C.N.3
  • 13
    • 84893142381 scopus 로고    scopus 로고
    • Glycopeptide antibiotic biosynthesis
    • Yim, G.; Thaker, M. N.; Koteva, K.; Wright, G. Glycopeptide antibiotic biosynthesis J. Antibiot. 2014, 67, 31-41 10.1038/ja.2013.117
    • (2014) J. Antibiot. , vol.67 , pp. 31-41
    • Yim, G.1    Thaker, M.N.2    Koteva, K.3    Wright, G.4
  • 15
    • 77957784833 scopus 로고    scopus 로고
    • Glycopeptide biosynthesis in the context of basic cellular functions
    • Stegmann, E.; Frasch, H. J.; Wohlleben, W. Glycopeptide biosynthesis in the context of basic cellular functions Curr. Opin. Microbiol. 2010, 13, 595-602 10.1016/j.mib.2010.08.011
    • (2010) Curr. Opin. Microbiol. , vol.13 , pp. 595-602
    • Stegmann, E.1    Frasch, H.J.2    Wohlleben, W.3
  • 17
    • 34548647327 scopus 로고    scopus 로고
    • The Biosynthesis of Teicoplanin-Type Glycopeptide Antibiotics: Assignment of P450 Mono-Oxygenases to Side Chain Cyclizations of Glycopeptide A47934
    • Hadatsch, B.; Butz, D.; Schmiederer, T.; Steudle, J.; Wohlleben, W.; Süssmuth, R. D.; Stegmann, E. The Biosynthesis of Teicoplanin-Type Glycopeptide Antibiotics: Assignment of P450 Mono-Oxygenases to Side Chain Cyclizations of Glycopeptide A47934 Chem. Biol. 2007, 14, 1078-1089 10.1016/j.chembiol.2007.08.014
    • (2007) Chem. Biol. , vol.14 , pp. 1078-1089
    • Hadatsch, B.1    Butz, D.2    Schmiederer, T.3    Steudle, J.4    Wohlleben, W.5    Süssmuth, R.D.6    Stegmann, E.7
  • 18
    • 21144439895 scopus 로고    scopus 로고
    • The biosynthesis of vancomycin-type glycopeptide antibiotics - A model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases
    • Bischoff, D.; Bister, B.; Bertazzo, M.; Pfeifer, V.; Stegmann, E.; Nicholson, G. J.; Keller, S.; Pelzer, S.; Wohlleben, W.; Süssmuth, R. D. The biosynthesis of vancomycin-type glycopeptide antibiotics-A model for oxidative side-chain cross-linking by oxygenases coupled to the action of peptide synthetases ChemBioChem 2005, 6, 267-272 10.1002/cbic.200400328
    • (2005) ChemBioChem , vol.6 , pp. 267-272
    • Bischoff, D.1    Bister, B.2    Bertazzo, M.3    Pfeifer, V.4    Stegmann, E.5    Nicholson, G.J.6    Keller, S.7    Pelzer, S.8    Wohlleben, W.9    Süssmuth, R.D.10
  • 20
    • 10944269741 scopus 로고    scopus 로고
    • An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism
    • Zerbe, K.; Woithe, K.; Li, D. B.; Vitali, F.; Bigler, L.; Robinson, J. A. An oxidative phenol coupling reaction catalyzed by OxyB, a cytochrome P450 from the vancomycin-producing microorganism Angew. Chem., Int. Ed. 2004, 43, 6709-6713 10.1002/anie.200461278
    • (2004) Angew. Chem., Int. Ed. , vol.43 , pp. 6709-6713
    • Zerbe, K.1    Woithe, K.2    Li, D.B.3    Vitali, F.4    Bigler, L.5    Robinson, J.A.6
  • 21
    • 34249780359 scopus 로고    scopus 로고
    • Oxidative phenol coupling reactions catalyzed by OxyB: A cytochrome P450 from the vancomycin producing organism. Implications for vancomycin biosynthesis
    • Woithe, K.; Geib, N.; Zerbe, K.; Dong, B. L.; Heck, M.; Fournier-Rousset, S.; Meyer, O.; Vitali, F.; Matoba, N.; Abou-Hadeed, K.; Robinson, J. A. Oxidative phenol coupling reactions catalyzed by OxyB: A cytochrome P450 from the vancomycin producing organism. Implications for vancomycin biosynthesis J. Am. Chem. Soc. 2007, 129, 6887-6895 10.1021/ja071038f
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 6887-6895
    • Woithe, K.1    Geib, N.2    Zerbe, K.3    Dong, B.L.4    Heck, M.5    Fournier-Rousset, S.6    Meyer, O.7    Vitali, F.8    Matoba, N.9    Abou-Hadeed, K.10    Robinson, J.A.11
  • 22
    • 84929077444 scopus 로고    scopus 로고
    • X-domain of peptide synthetases recruits oxygenases crucial for glycopeptide biosynthesis
    • Haslinger, K.; Peschke, M.; Brieke, C.; Maximowitsch, E.; Cryle, M. J. X-domain of peptide synthetases recruits oxygenases crucial for glycopeptide biosynthesis Nature 2015, 521, 105-109 10.1038/nature14141
    • (2015) Nature , vol.521 , pp. 105-109
    • Haslinger, K.1    Peschke, M.2    Brieke, C.3    Maximowitsch, E.4    Cryle, M.J.5
  • 23
    • 84955389304 scopus 로고    scopus 로고
    • Sequential in Vitro Cyclization by Cytochrome P450 Enzymes of Glycopeptide Antibiotic Precursors Bearing the X-Domain from Nonribosomal Peptide Biosynthesis
    • Brieke, C.; Peschke, M.; Haslinger, K.; Cryle, M. J. Sequential In Vitro Cyclization by Cytochrome P450 Enzymes of Glycopeptide Antibiotic Precursors Bearing the X-Domain from Nonribosomal Peptide Biosynthesis Angew. Chem., Int. Ed. 2015, 54, 15715-15719 10.1002/anie.201507533
    • (2015) Angew. Chem., Int. Ed. , vol.54 , pp. 15715-15719
    • Brieke, C.1    Peschke, M.2    Haslinger, K.3    Cryle, M.J.4
  • 24
    • 62649111637 scopus 로고    scopus 로고
    • Catalytic Turnover-Based Phage Selection for Engineering the Substrate Specificity of Sfp Phosphopantetheinyl Transferase
    • Sunbul, M.; Marshall, N. J.; Zou, Y.; Zhang, K.; Yin, J. Catalytic Turnover-Based Phage Selection for Engineering the Substrate Specificity of Sfp Phosphopantetheinyl Transferase J. Mol. Biol. 2009, 387, 883-898 10.1016/j.jmb.2009.02.010
    • (2009) J. Mol. Biol. , vol.387 , pp. 883-898
    • Sunbul, M.1    Marshall, N.J.2    Zou, Y.3    Zhang, K.4    Yin, J.5
  • 25
    • 84922648459 scopus 로고    scopus 로고
    • Rapid access to glycopeptide antibiotic precursor peptides coupled with cytochrome P450-mediated catalysis: Towards a biomimetic synthesis of glycopeptide antibiotics
    • Brieke, C.; Kratzig, V.; Haslinger, K.; Winkler, A.; Cryle, M. J. Rapid access to glycopeptide antibiotic precursor peptides coupled with cytochrome P450-mediated catalysis: towards a biomimetic synthesis of glycopeptide antibiotics Org. Biomol. Chem. 2015, 13, 2012-2021 10.1039/C4OB02452D
    • (2015) Org. Biomol. Chem. , vol.13 , pp. 2012-2021
    • Brieke, C.1    Kratzig, V.2    Haslinger, K.3    Winkler, A.4    Cryle, M.J.5
  • 27
    • 49149096698 scopus 로고    scopus 로고
    • Exploring the substrate specificity of OxyB, a phenol coupling P450 enzyme involved in vancomycin biosynthesis
    • Woithe, K.; Geib, N.; Meyer, O.; Wörtz, T.; Zerbe, K.; Robinson, J. A. Exploring the substrate specificity of OxyB, a phenol coupling P450 enzyme involved in vancomycin biosynthesis Org. Biomol. Chem. 2008, 6, 2861-2867 10.1039/b805956j
    • (2008) Org. Biomol. Chem. , vol.6 , pp. 2861-2867
    • Woithe, K.1    Geib, N.2    Meyer, O.3    Wörtz, T.4    Zerbe, K.5    Robinson, J.A.6
  • 29
    • 0035805265 scopus 로고    scopus 로고
    • The biosynthesis of vancomycin-type glycopeptide antibiotics - New insights into the cyclization steps
    • Bischoff, D.; Pelzer, S.; Holtzel, A.; Nicholson, G. J.; Stockert, S.; Wohlleben, W.; Jung, G.; Süssmuth, R. D. The biosynthesis of vancomycin-type glycopeptide antibiotics-New insights into the cyclization steps Angew. Chem., Int. Ed. 2001, 40, 1693-1696 10.1002/1521-3773(20010504)40:9<1693::AID-ANIE16930>3.0.CO;2-8
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 1693-1696
    • Bischoff, D.1    Pelzer, S.2    Holtzel, A.3    Nicholson, G.J.4    Stockert, S.5    Wohlleben, W.6    Jung, G.7    Süssmuth, R.D.8
  • 30
    • 0242491431 scopus 로고    scopus 로고
    • New advances in the biosynthesis of glycopeptide antibiotics of the vancomycin type from Amycolatopsis mediterranei
    • Süssmuth, R. D.; Pelzer, S.; Nicholson, G.; Walk, T.; Wohlleben, W.; Jung, G. New advances in the biosynthesis of glycopeptide antibiotics of the vancomycin type from Amycolatopsis mediterranei Angew. Chem., Int. Ed. 1999, 38, 1976-1979 10.1002/(SICI)1521-3773(19990712)38:13/14<1976::AID-ANIE1976>3.0.CO;2-3
    • (1999) Angew. Chem., Int. Ed. , vol.38 , pp. 1976-1979
    • Süssmuth, R.D.1    Pelzer, S.2    Nicholson, G.3    Walk, T.4    Wohlleben, W.5    Jung, G.6
  • 31
    • 84887958896 scopus 로고    scopus 로고
    • Cytochrome P450sky interacts directly with the nonribosomal peptide synthetase to generate three amino acid precursors in skyllamycin biosynthesis
    • Uhlmann, S.; Süssmuth, R. D.; Cryle, M. J. Cytochrome P450sky interacts directly with the nonribosomal peptide synthetase to generate three amino acid precursors in skyllamycin biosynthesis ACS Chem. Biol. 2013, 8, 2586-2596 10.1021/cb400555e
    • (2013) ACS Chem. Biol. , vol.8 , pp. 2586-2596
    • Uhlmann, S.1    Süssmuth, R.D.2    Cryle, M.J.3
  • 32
    • 84905443941 scopus 로고    scopus 로고
    • The structure of a transient complex of a nonribosomal peptide synthetase and a cytochromep450 monooxygenase
    • Haslinger, K.; Brieke, C.; Uhlmann, S.; Sieverling, L.; Süssmuth, R. D.; Cryle, M. J. The structure of a transient complex of a nonribosomal peptide synthetase and a cytochromep450 monooxygenase Angew. Chem., Int. Ed. 2014, 53, 8518-8522 10.1002/anie.201404977
    • (2014) Angew. Chem., Int. Ed. , vol.53 , pp. 8518-8522
    • Haslinger, K.1    Brieke, C.2    Uhlmann, S.3    Sieverling, L.4    Süssmuth, R.D.5    Cryle, M.J.6
  • 33
    • 77955284586 scopus 로고    scopus 로고
    • Structural characterization of OxyD, a cytochrome P450 involved in β-hydroxytyrosine formation in vancomycin biosynthesis
    • Cryle, M. J.; Meinhart, A.; Schlichting, I. Structural characterization of OxyD, a cytochrome P450 involved in β-hydroxytyrosine formation in vancomycin biosynthesis J. Biol. Chem. 2010, 285, 24562-24574 10.1074/jbc.M110.131904
    • (2010) J. Biol. Chem. , vol.285 , pp. 24562-24574
    • Cryle, M.J.1    Meinhart, A.2    Schlichting, I.3
  • 34
    • 0035036477 scopus 로고    scopus 로고
    • Coumarin formation in novobiocin biosynthesis: β-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI
    • Chen, H.; Walsh, C. T. Coumarin formation in novobiocin biosynthesis: β-hydroxylation of the aminoacyl enzyme tyrosyl-S-NovH by a cytochrome P450 NovI Chem. Biol. 2001, 8, 301-312 10.1016/S1074-5521(01)00009-6
    • (2001) Chem. Biol. , vol.8 , pp. 301-312
    • Chen, H.1    Walsh, C.T.2
  • 35
    • 57449096570 scopus 로고    scopus 로고
    • Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI)/ACP complex
    • Cryle, M. J.; Schlichting, I. Structural insights from a P450 Carrier Protein complex reveal how specificity is achieved in the P450(BioI)/ACP complex Proc. Natl. Acad. Sci. U. S. A. 2008, 105, 15696-15701 10.1073/pnas.0805983105
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 15696-15701
    • Cryle, M.J.1    Schlichting, I.2
  • 36
    • 0036008124 scopus 로고    scopus 로고
    • Formation of β-Hydroxy Histidine in the Biosynthesis of Nikkomycin Antibiotics
    • Chen, H.; Hubbard, B. K.; O'Connor, S. E.; Walsh, C. T. Formation of β-Hydroxy Histidine in the Biosynthesis of Nikkomycin Antibiotics Chem. Biol. 2002, 9, 103-112 10.1016/S1074-5521(02)00090-X
    • (2002) Chem. Biol. , vol.9 , pp. 103-112
    • Chen, H.1    Hubbard, B.K.2    O'Connor, S.E.3    Walsh, C.T.4
  • 37
    • 0029902679 scopus 로고    scopus 로고
    • Program DYNAFIT for the analysis of enzyme kinetic data: Application to HIV proteinase
    • Kuzmic, P. Program DYNAFIT for the analysis of enzyme kinetic data: application to HIV proteinase Anal. Biochem. 1996, 237, 260-273 10.1006/abio.1996.0238
    • (1996) Anal. Biochem. , vol.237 , pp. 260-273
    • Kuzmic, P.1
  • 38
    • 0013074994 scopus 로고    scopus 로고
    • The basic equations of enzyme kinetics
    • In, 2 nd ed. W H Freeman: New York
    • Fersht, A. The basic equations of enzyme kinetics. In Structure and Mechanism in Protein Science, 2 nd ed.; W H Freeman: New York, 1999; pp 103-131.
    • (1999) Structure and Mechanism in Protein Science , pp. 103-131
    • Fersht, A.1
  • 40
    • 0030612534 scopus 로고    scopus 로고
    • Aflatoxin B1 8,9-epoxide hydrolysis in the presence of rat and human epoxide hydrolase
    • Johnson, W. W.; Yamazaki, H.; Shimada, T.; Ueng, Y. F.; Guengerich, F. P. Aflatoxin B1 8,9-epoxide hydrolysis in the presence of rat and human epoxide hydrolase Chem. Res. Toxicol. 1997, 10, 672-676 10.1021/tx960209j
    • (1997) Chem. Res. Toxicol. , vol.10 , pp. 672-676
    • Johnson, W.W.1    Yamazaki, H.2    Shimada, T.3    Ueng, Y.F.4    Guengerich, F.P.5
  • 41
    • 33747462891 scopus 로고    scopus 로고
    • A New Paradigm for DNA Polymerase Specificity
    • Tsai, Y.-C.; Johnson, K. A. A New Paradigm for DNA Polymerase Specificity Biochemistry 2006, 45, 9675-9687 10.1021/bi060993z
    • (2006) Biochemistry , vol.45 , pp. 9675-9687
    • Tsai, Y.-C.1    Johnson, K.A.2
  • 42
    • 77949570420 scopus 로고    scopus 로고
    • The kinetic and chemical mechanism of high-fidelity DNA polymerases
    • Johnson, K. A. The kinetic and chemical mechanism of high-fidelity DNA polymerases Biochim. Biophys. Acta, Proteins Proteomics 2010, 1804, 1041-1048 10.1016/j.bbapap.2010.01.006
    • (2010) Biochim. Biophys. Acta, Proteins Proteomics , vol.1804 , pp. 1041-1048
    • Johnson, K.A.1
  • 44
    • 84963491164 scopus 로고    scopus 로고
    • Online pyrophosphate assay for analyzing adenylation domains of non-ribosomal peptide synthetases
    • Kittilä, T.; Schoppet, M.; Cryle, M. J. Online pyrophosphate assay for analyzing adenylation domains of non-ribosomal peptide synthetases ChemBioChem 2016, 17, 576-584 10.1002/cbic.201500555
    • (2016) ChemBioChem , vol.17 , pp. 576-584
    • Kittilä, T.1    Schoppet, M.2    Cryle, M.J.3
  • 45
    • 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 2001, 40, 9023-9031 10.1021/bi010519n
    • (2001) Biochemistry , vol.40 , pp. 9023-9031
    • Patel, H.M.1    Walsh, C.T.2
  • 47
    • 84887669505 scopus 로고    scopus 로고
    • In vitro reconstitution and analysis of the 6-deoxyerythronolide B synthase
    • Lowry, B.; Robbins, T.; Weng, C.-H.; O'Brien, R. V.; Cane, D. E.; Khosla, C. In vitro reconstitution and analysis of the 6-deoxyerythronolide B synthase J. Am. Chem. Soc. 2013, 135, 16809-16812 10.1021/ja409048k
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 16809-16812
    • Lowry, B.1    Robbins, T.2    Weng, C.-H.3    O'Brien, R.V.4    Cane, D.E.5    Khosla, C.6
  • 48
    • 84897028113 scopus 로고    scopus 로고
    • Epimerization and substrate gating by a TE domain in β-lactam antibiotic biosynthesis
    • Gaudelli, N. M.; Townsend, C. A. Epimerization and substrate gating by a TE domain in β-lactam antibiotic biosynthesis Nat. Chem. Biol. 2014, 10, 251-258 10.1038/nchembio.1456
    • (2014) Nat. Chem. Biol. , vol.10 , pp. 251-258
    • Gaudelli, N.M.1    Townsend, C.A.2
  • 49
    • 84899832023 scopus 로고    scopus 로고
    • A facile Fmoc solid phase synthesis strategy to access epimerization-prone biosynthetic intermediates of glycopeptide antibiotics
    • Brieke, C.; Cryle, M. J. A facile Fmoc solid phase synthesis strategy to access epimerization-prone biosynthetic intermediates of glycopeptide antibiotics Org. Lett. 2014, 16, 2454-2457 10.1021/ol500840f
    • (2014) Org. Lett. , vol.16 , pp. 2454-2457
    • Brieke, C.1    Cryle, M.J.2
  • 50
    • 84915809650 scopus 로고    scopus 로고
    • Cytochrome P450 OxyBtei Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis
    • Haslinger, K.; Maximowitsch, E.; Brieke, C.; Koch, A.; Cryle, M. J. Cytochrome P450 OxyBtei Catalyzes the First Phenolic Coupling Step in Teicoplanin Biosynthesis ChemBioChem 2014, 15, 2719-2728 10.1002/cbic.201402441
    • (2014) ChemBioChem , vol.15 , pp. 2719-2728
    • Haslinger, K.1    Maximowitsch, E.2    Brieke, C.3    Koch, A.4    Cryle, M.J.5
  • 51
    • 77949263023 scopus 로고    scopus 로고
    • Protein recognition in ferredoxin-P450 electron transfer in the class i CYP199A2 system from Rhodopseudomonas palustris
    • Bell, S. G.; Xu, F.; Johnson, E. O. D.; Forward, I. M.; Bartlam, M.; Rao, Z.; Wong, L. L. Protein recognition in ferredoxin-P450 electron transfer in the class I CYP199A2 system from Rhodopseudomonas palustris JBIC, J. Biol. Inorg. Chem. 2010, 15, 315-328 10.1007/s00775-009-0604-7
    • (2010) JBIC, J. Biol. Inorg. Chem. , vol.15 , pp. 315-328
    • Bell, S.G.1    Xu, F.2    Johnson, E.O.D.3    Forward, I.M.4    Bartlam, M.5    Rao, Z.6    Wong, L.L.7
  • 52
    • 0015813630 scopus 로고
    • Spectrophotometric determination of protein concentration in cell extracts containing tRNAs and rRNAs
    • Ehresmann, B.; Imbault, P.; Well, J. H. Spectrophotometric determination of protein concentration in cell extracts containing tRNAs and rRNAs Anal. Biochem. 1973, 54, 454-463 10.1016/0003-2697(73)90374-6
    • (1973) Anal. Biochem. , vol.54 , pp. 454-463
    • Ehresmann, B.1    Imbault, P.2    Well, J.H.3


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