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Volumn 6, Issue 3, 2017, Pages 421-427

Polyketide Bioderivatization Using the Promiscuous Acyltransferase KirCII

Author keywords

antibiotic; click chemistry; engineering; kirromycin; polyketide synthase; trans acyltransferase

Indexed keywords

MOCIMYCIN; NEW DRUG; POLYKETIDE; ACYLTRANSFERASE; ANTIINFECTIVE AGENT; BACTERIAL PROTEIN; POLYKETIDE SYNTHASE; PYRIDONE DERIVATIVE;

EID: 85017588486     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.6b00341     Document Type: Article
Times cited : (39)

References (30)
  • 1
    • 69249202590 scopus 로고    scopus 로고
    • The biosynthetic logic of polyketide diversity
    • Hertweck, C. ( 2009 ) The biosynthetic logic of polyketide diversity Angew. Chem., Int. Ed. 48, 4688-4716 10.1002/anie.200806121
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 4688-4716
    • Hertweck, C.1
  • 2
    • 84893089095 scopus 로고    scopus 로고
    • Prospects for new antibiotics: a molecule-centered perspective
    • Walsh, C. T. and Wencewicz, T. A. ( 2014 ) Prospects for new antibiotics: a molecule-centered perspective J. Antibiot. 67, 7-22 10.1038/ja.2013.49
    • (2014) J. Antibiot. , vol.67 , pp. 7-22
    • Walsh, C.T.1    Wencewicz, T.A.2
  • 3
    • 84864348214 scopus 로고    scopus 로고
    • Discrete acyltransferases involved in polyketide biosynthesis
    • Musiol, E. M. and Weber, T. ( 2012 ) Discrete acyltransferases involved in polyketide biosynthesis MedChemComm 3, 871-886 10.1039/c2md20048a
    • (2012) MedChemComm , vol.3 , pp. 871-886
    • Musiol, E.M.1    Weber, T.2
  • 4
    • 84957093801 scopus 로고    scopus 로고
    • Biosynthesis of polyketides by trans-AT polyketide synthases
    • Helfrich, E. J. and Piel, J. ( 2016 ) Biosynthesis of polyketides by trans-AT polyketide synthases Nat. Prod. Rep. 33, 231-316 10.1039/C5NP00125K
    • (2016) Nat. Prod. Rep. , vol.33 , pp. 231-316
    • Helfrich, E.J.1    Piel, J.2
  • 5
    • 79955412459 scopus 로고    scopus 로고
    • Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS
    • Musiol, E. M., Härtner, T., Kulik, A., Moldenhauer, J., Piel, J., Wohlleben, W., and Weber, T. ( 2011 ) Supramolecular templating in kirromycin biosynthesis: the acyltransferase KirCII loads ethylmalonyl-CoA extender onto a specific ACP of the trans-AT PKS Chem. Biol. 18, 438-444 10.1016/j.chembiol.2011.02.007
    • (2011) Chem. Biol. , vol.18 , pp. 438-444
    • Musiol, E.M.1    Härtner, T.2    Kulik, A.3    Moldenhauer, J.4    Piel, J.5    Wohlleben, W.6    Weber, T.7
  • 6
    • 77953799129 scopus 로고    scopus 로고
    • Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an acyltransferase-less type I polyketide synthase that incorporates two distinct extender units
    • Zhao, C., Coughlin, J. M., Ju, J., Zhu, D., Wendt-Pienkowski, E., Zhou, X., Wang, Z., Shen, B., and Deng, Z. ( 2010 ) Oxazolomycin biosynthesis in Streptomyces albus JA3453 featuring an acyltransferase-less type I polyketide synthase that incorporates two distinct extender units J. Biol. Chem. 285, 20097-20108 10.1074/jbc.M109.090092
    • (2010) J. Biol. Chem. , vol.285 , pp. 20097-20108
    • Zhao, C.1    Coughlin, J.M.2    Ju, J.3    Zhu, D.4    Wendt-Pienkowski, E.5    Zhou, X.6    Wang, Z.7    Shen, B.8    Deng, Z.9
  • 7
    • 77956252963 scopus 로고    scopus 로고
    • Analysis of the sorangicin gene cluster reinforces the utility of a combined phylogenetic/retrobiosynthetic analysis for deciphering natural product assembly by trans-AT PKS
    • Irschik, H., Kopp, M., Weissman, K. J., Buntin, K., Piel, J., and Muller, R. ( 2010 ) Analysis of the sorangicin gene cluster reinforces the utility of a combined phylogenetic/retrobiosynthetic analysis for deciphering natural product assembly by trans-AT PKS ChemBioChem 11, 1840-1849 10.1002/cbic.201000313
    • (2010) ChemBioChem , vol.11 , pp. 1840-1849
    • Irschik, H.1    Kopp, M.2    Weissman, K.J.3    Buntin, K.4    Piel, J.5    Muller, R.6
  • 9
    • 85013703075 scopus 로고    scopus 로고
    • Inversion of extender unit selectivity in the erythromycin polyketide synthase by acyltransferase domain engineering
    • Koryakina, I., Kasey, C., McArthur, J. B., Lowell, A. N., Chemler, J. A., Li, S., Hansen, D. A., Sherman, D. H., and Williams, G. J. ( 2017 ) Inversion of extender unit selectivity in the erythromycin polyketide synthase by acyltransferase domain engineering ACS Chem. Biol. 12, 114-123 10.1021/acschembio.6b00732
    • (2017) ACS Chem. Biol. , vol.12 , pp. 114-123
    • Koryakina, I.1    Kasey, C.2    McArthur, J.B.3    Lowell, A.N.4    Chemler, J.A.5    Li, S.6    Hansen, D.A.7    Sherman, D.H.8    Williams, G.J.9
  • 10
    • 84891396350 scopus 로고    scopus 로고
    • Engineering the acyltransferase substrate specificity of assembly line polyketide synthases
    • Dunn, B. J. and Khosla, C. ( 2013 ) Engineering the acyltransferase substrate specificity of assembly line polyketide synthases J. R. Soc., Interface 10, 20130297 10.1098/rsif.2013.0297
    • (2013) J. R. Soc., Interface , vol.10 , pp. 20130297
    • Dunn, B.J.1    Khosla, C.2
  • 11
    • 84874030515 scopus 로고    scopus 로고
    • Enzyme-directed mutasynthesis: a combined experimental and theoretical approach to substrate recognition of a polyketide synthase
    • Sundermann, U., Bravo-Rodriguez, K., Klopries, S., Kushnir, S., Gomez, H., Sanchez-Garcia, E., and Schulz, F. ( 2013 ) Enzyme-directed mutasynthesis: a combined experimental and theoretical approach to substrate recognition of a polyketide synthase ACS Chem. Biol. 8, 443-450 10.1021/cb300505w
    • (2013) ACS Chem. Biol. , vol.8 , pp. 443-450
    • Sundermann, U.1    Bravo-Rodriguez, K.2    Klopries, S.3    Kushnir, S.4    Gomez, H.5    Sanchez-Garcia, E.6    Schulz, F.7
  • 13
    • 39149122159 scopus 로고    scopus 로고
    • Molecular analysis of the kirromycin biosynthetic gene cluster revealed beta-alanine as precursor of the pyridone moiety
    • Weber, T., Laiple, K. J., Pross, E. K., Textor, A., Grond, S., Welzel, K., Pelzer, S., Vente, A., and Wohlleben, W. ( 2008 ) Molecular analysis of the kirromycin biosynthetic gene cluster revealed beta-alanine as precursor of the pyridone moiety Chem. Biol. 15, 175-188 10.1016/j.chembiol.2007.12.009
    • (2008) Chem. Biol. , vol.15 , pp. 175-188
    • Weber, T.1    Laiple, K.J.2    Pross, E.K.3    Textor, A.4    Grond, S.5    Welzel, K.6    Pelzer, S.7    Vente, A.8    Wohlleben, W.9
  • 14
    • 84880575906 scopus 로고    scopus 로고
    • The AT(2) domain of KirCI loads malonyl extender units to the ACPs of the kirromycin PKS
    • Musiol, E. M., Greule, A., Härtner, T., Kulik, A., Wohlleben, W., and Weber, T. ( 2013 ) The AT(2) domain of KirCI loads malonyl extender units to the ACPs of the kirromycin PKS ChemBioChem 14, 1343-1352 10.1002/cbic.201300211
    • (2013) ChemBioChem , vol.14 , pp. 1343-1352
    • Musiol, E.M.1    Greule, A.2    Härtner, T.3    Kulik, A.4    Wohlleben, W.5    Weber, T.6
  • 15
    • 84901390725 scopus 로고    scopus 로고
    • Reprogramming acyl carrier protein interactions of an acyl-CoA promiscuous trans-acyltransferase
    • Ye, Z., Musiol, E. M., Weber, T., and Williams, G. J. ( 2014 ) Reprogramming acyl carrier protein interactions of an acyl-CoA promiscuous trans-acyltransferase Chem. Biol. 21, 636-646 10.1016/j.chembiol.2014.02.019
    • (2014) Chem. Biol. , vol.21 , pp. 636-646
    • Ye, Z.1    Musiol, E.M.2    Weber, T.3    Williams, G.J.4
  • 17
    • 84928059370 scopus 로고    scopus 로고
    • Biosynthesis: A terminal triple bond toolbox
    • Haritos, V. S. ( 2015 ) Biosynthesis: A terminal triple bond toolbox Nat. Chem. Biol. 11, 98-99 10.1038/nchembio.1731
    • (2015) Nat. Chem. Biol. , vol.11 , pp. 98-99
    • Haritos, V.S.1
  • 18
    • 84877835595 scopus 로고    scopus 로고
    • Click chemistry for drug development and diverse chemical-biology applications
    • Thirumurugan, P., Matosiuk, D., and Jozwiak, K. ( 2013 ) Click chemistry for drug development and diverse chemical-biology applications Chem. Rev. 113, 4905-4979 10.1021/cr200409f
    • (2013) Chem. Rev. , vol.113 , pp. 4905-4979
    • Thirumurugan, P.1    Matosiuk, D.2    Jozwiak, K.3
  • 19
    • 80053608537 scopus 로고    scopus 로고
    • Mutant Malonyl-CoA Synthetases with Altered Specificity for Polyketide Synthase Extender Unit Generation
    • Koryakina, I. and Williams, G. J. ( 2011 ) Mutant Malonyl-CoA Synthetases with Altered Specificity for Polyketide Synthase Extender Unit Generation ChemBioChem 12, 2289-2293 10.1002/cbic.201100383
    • (2011) ChemBioChem , vol.12 , pp. 2289-2293
    • Koryakina, I.1    Williams, G.J.2
  • 20
    • 0026502221 scopus 로고
    • Mass spectrometric techniques for structure and novelty determination of kirromycin-like antibiotics
    • Edwards, D. M. F., Selva, E., Stella, S., Zerilli, L. F., and Gallo, G. G. ( 1992 ) Mass spectrometric techniques for structure and novelty determination of kirromycin-like antibiotics Biol. Mass Spectrom. 21, 51-59 10.1002/bms.1200210110
    • (1992) Biol. Mass Spectrom. , vol.21 , pp. 51-59
    • Edwards, D.M.F.1    Selva, E.2    Stella, S.3    Zerilli, L.F.4    Gallo, G.G.5
  • 21
    • 0016361235 scopus 로고
    • Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu
    • Wolf, H., Chinali, G., and Parmeggiani, A. ( 1974 ) Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu Proc. Natl. Acad. Sci. U. S. A. 71, 4910-4914 10.1073/pnas.71.12.4910
    • (1974) Proc. Natl. Acad. Sci. U. S. A. , vol.71 , pp. 4910-4914
    • Wolf, H.1    Chinali, G.2    Parmeggiani, A.3
  • 22
    • 0017360192 scopus 로고
    • Mechanism of the inhibition of protein synthesis by kirromycin. Role of elongation factor Tu and ribosomes
    • Wolf, H., Chinali, G., and Parmeggiani, A. ( 1977 ) Mechanism of the inhibition of protein synthesis by kirromycin. Role of elongation factor Tu and ribosomes Eur. J. Biochem. 75, 67-75 10.1111/j.1432-1033.1977.tb11504.x
    • (1977) Eur. J. Biochem. , vol.75 , pp. 67-75
    • Wolf, H.1    Chinali, G.2    Parmeggiani, A.3
  • 23
    • 50249159403 scopus 로고    scopus 로고
    • Continuous cell-free protein synthesis using glycolytic intermediates as energy sources
    • Kim, H. C., Kim, T. W., Park, C. G., Oh, I. S., Park, K., and Kim, D. M. ( 2008 ) Continuous cell-free protein synthesis using glycolytic intermediates as energy sources J. Microbiol. Biotechnol. 18, 885-888
    • (2008) J. Microbiol. Biotechnol. , vol.18 , pp. 885-888
    • Kim, H.C.1    Kim, T.W.2    Park, C.G.3    Oh, I.S.4    Park, K.5    Kim, D.M.6
  • 24
    • 34347371434 scopus 로고    scopus 로고
    • An economical and highly productive cell-free protein synthesis system utilizing fructose-1,6-bisphosphate as an energy source
    • Kim, T. W., Keum, J. W., Oh, I. S., Choi, C. Y., Kim, H. C., and Kim, D. M. ( 2007 ) An economical and highly productive cell-free protein synthesis system utilizing fructose-1,6-bisphosphate as an energy source J. Biotechnol. 130, 389-393 10.1016/j.jbiotec.2007.05.002
    • (2007) J. Biotechnol. , vol.130 , pp. 389-393
    • Kim, T.W.1    Keum, J.W.2    Oh, I.S.3    Choi, C.Y.4    Kim, H.C.5    Kim, D.M.6
  • 25
    • 0035907234 scopus 로고    scopus 로고
    • Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox
    • Vogeley, L., Palm, G. J., Mesters, J. R., and Hilgenfeld, R. ( 2001 ) Conformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodox J. Biol. Chem. 276, 17149-17155 10.1074/jbc.M100017200
    • (2001) J. Biol. Chem. , vol.276 , pp. 17149-17155
    • Vogeley, L.1    Palm, G.J.2    Mesters, J.R.3    Hilgenfeld, R.4
  • 26
    • 34247580876 scopus 로고    scopus 로고
    • Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus is resistant to three classes of EF-Tu-specific inhibitors
    • Olsthoorn-Tieleman, L. N., Palstra, R. J., van Wezel, G. P., Bibb, M. J., and Pleij, C. W. ( 2007 ) Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus is resistant to three classes of EF-Tu-specific inhibitors J. Bacteriol. 189, 3581-3590 10.1128/JB.01810-06
    • (2007) J. Bacteriol. , vol.189 , pp. 3581-3590
    • Olsthoorn-Tieleman, L.N.1    Palstra, R.J.2    Van Wezel, G.P.3    Bibb, M.J.4    Pleij, C.W.5
  • 27
    • 23244440886 scopus 로고    scopus 로고
    • An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates
    • Calhoun, K. A. and Swartz, J. R. ( 2005 ) An economical method for cell-free protein synthesis using glucose and nucleoside monophosphates Biotechnol. Prog. 21, 1146-1153 10.1021/bp050052y
    • (2005) Biotechnol. Prog. , vol.21 , pp. 1146-1153
    • Calhoun, K.A.1    Swartz, J.R.2
  • 28
    • 35348861374 scopus 로고    scopus 로고
    • The ABC transporter Tba of Amycolatopsis balhimycina is required for efficient export of the glycopeptide antibiotic balhimycin
    • Menges, R., Muth, G., Wohlleben, W., and Stegmann, E. ( 2007 ) The ABC transporter Tba of Amycolatopsis balhimycina is required for efficient export of the glycopeptide antibiotic balhimycin Appl. Microbiol. Biotechnol. 77, 125-134 10.1007/s00253-007-1139-x
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 125-134
    • Menges, R.1    Muth, G.2    Wohlleben, W.3    Stegmann, E.4
  • 29
    • 33750283167 scopus 로고    scopus 로고
    • Simple procedures for the construction of a robust and cost-effective cell-free protein synthesis system
    • Kim, T. W., Keum, J. W., Oh, I. S., Choi, C. Y., Park, C. G., and Kim, D. M. ( 2006 ) Simple procedures for the construction of a robust and cost-effective cell-free protein synthesis system J. Biotechnol. 126, 554-561 10.1016/j.jbiotec.2006.05.014
    • (2006) J. Biotechnol. , vol.126 , pp. 554-561
    • Kim, T.W.1    Keum, J.W.2    Oh, I.S.3    Choi, C.Y.4    Park, C.G.5    Kim, D.M.6
  • 30
    • 0034681011 scopus 로고    scopus 로고
    • Expression-independent consumption of substrates in cell-free expression system from Escherichia coli
    • Kim, R. G. and Choi, C. Y. ( 2001 ) Expression-independent consumption of substrates in cell-free expression system from Escherichia coli J. Biotechnol. 84, 27-32 10.1016/S0168-1656(00)00326-6
    • (2001) J. Biotechnol. , vol.84 , pp. 27-32
    • Kim, R.G.1    Choi, C.Y.2


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