Structure-based protein engineering enables prenyl donor switching of a fungal aromatic prenyltransferase
Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few...
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| Published in | Organic & biomolecular chemistry Vol. 16; no. 40; pp. 7461 - 7469 |
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| Main Authors | , , , |
| Format | Journal Article |
| Language | English |
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Royal Soc Chemistry
17.10.2018
Royal Society of Chemistry |
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| Abstract | Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from
Aspergillus fumigatus
led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind. |
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| AbstractList | Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from
Aspergillus fumigatus
led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind. Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from Aspergillus fumigatus led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind.Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from Aspergillus fumigatus led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind. Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific prenylation reactions that are of significant pharmaceutical interest. While the majority of PTs accepts dimethylallyl diphosphate (DMAPP), very few such enzymes can use geranyl diphosphate (GPP) or farnesyl diphosphate (FPP) as donors. This catalytic gap prohibits the wide application of PTs for structural diversification. Structure-guided molecular modelling and site-directed mutagenesis of FgaPT2 from Aspergillus fumigatus led to the identification of the gatekeeping residue Met328 responsible for the prenyl selectivity and sets the basis for creation of GPP- and FPP-accepting enzymes. Site-saturation mutagenesis of the gatekeeping residue at position 328 in FgaPT2 revealed that the size of this side chain is the determining factor for prenyl selectivity, while its hydrophobicity is crucial for allowing DMAPP and GPP to bind. |
| Author | Zocher, Georg Stehle, Thilo Li, Shu-Ming Mai, Peter |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/30270371$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1038/nature03668 10.1007/s00253-015-6811-y 10.1073/pnas.0904897106 10.1038/ncomms10849 10.1002/cbic.200700107 10.1093/nar/gki387 10.1021/ja3028636 10.1038/nchembio.1070 10.1099/mic.0.27759-0 10.1038/ja.2012.54 10.1021/ja106817c 10.1039/C4NP00073K 10.15227/orgsyn.066.0211 10.1093/nar/gnh110 10.1007/s00253-014-5509-x 10.1016/j.febslet.2011.12.012 10.1038/nchembio.2263 10.1093/nar/gki408 10.1038/nchembio709 10.1002/jcc.21334 10.1073/pnas.0501980102 10.1039/C4RA00337C 10.1038/nrm.2015.11 10.1128/microbiolspec.FUNK-0009-2016 10.1021/acs.jnatprod.5b01055 10.1039/B909987P 10.1074/jbc.M111.317982 10.1186/1472-6750-8-91 10.1016/j.jmb.2012.05.033 10.1016/j.chembiol.2013.10.007 10.1021/ja909118a 10.1007/s00253-012-4130-0 10.1107/S0907444910007493 10.1002/jcc.20529 10.1038/NCHEMBIO.1070 10.1038/NCHEMBIO.2263 10.1039/b909987p 10.1039/c4ra00337c 10.1039/c4np00073k 10.1038/ja.2012.27 |
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| References | Schymkowitz (C8OB02037J-(cit31)/*[position()=1]) 2005; 33 Okada (C8OB02037J-(cit8)/*[position()=1]) 2005; 1 Chen (C8OB02037J-(cit15)/*[position()=1]) 2017; 13 Jost (C8OB02037J-(cit20)/*[position()=1]) 2010; 132 Yin (C8OB02037J-(cit25)/*[position()=1]) 2013; 97 Steffan (C8OB02037J-(cit27)/*[position()=1]) 2007; 8 Emsley (C8OB02037J-(cit32)/*[position()=1]) 2010; 66 Newman (C8OB02037J-(cit2)/*[position()=1]) 2016; 79 Trott (C8OB02037J-(cit33)/*[position()=1]) 2010; 31 Bérdy (C8OB02037J-(cit3)/*[position()=1]) 2012; 65 Tarcz (C8OB02037J-(cit18)/*[position()=1]) 2014; 4 Liu (C8OB02037J-(cit28)/*[position()=1]) 2008; 8 Walsh (C8OB02037J-(cit4)/*[position()=1]) 2010; 132 Zheng (C8OB02037J-(cit29)/*[position()=1]) 2004; 32 Bills (C8OB02037J-(cit1)/*[position()=1]) 2016; 4 Dumelin (C8OB02037J-(cit9)/*[position()=1]) 2012; 8 Woodside (C8OB02037J-(cit23)/*[position()=1]) 1988; 66 Xu (C8OB02037J-(cit10)/*[position()=1]) 2014; 31 Tsuji (C8OB02037J-(cit7)/*[position()=1]) 2012; 586 Yu (C8OB02037J-(cit22)/*[position()=1]) 2013; 20 Chooi (C8OB02037J-(cit14)/*[position()=1]) 2012; 134 Söding (C8OB02037J-(cit26)/*[position()=1]) 2005; 33 Wang (C8OB02037J-(cit6)/*[position()=1]) 2016; 17 Winkelblech (C8OB02037J-(cit5)/*[position()=1]) 2015; 99 Schuller (C8OB02037J-(cit21)/*[position()=1]) 2012; 422 Metzger (C8OB02037J-(cit13)/*[position()=1]) 2009; 106 Li (C8OB02037J-(cit11)/*[position()=1]) 2010; 27 Mori (C8OB02037J-(cit16)/*[position()=1]) 2016; 7 Yu (C8OB02037J-(cit24)/*[position()=1]) 2012; 287 Schymkowitz (C8OB02037J-(cit30)/*[position()=1]) 2005; 102 Pockrandt (C8OB02037J-(cit17)/*[position()=1]) 2014; 98 Kuzuyama (C8OB02037J-(cit12)/*[position()=1]) 2005; 435 Unsöld (C8OB02037J-(cit19)/*[position()=1]) 2005; 151 Walsh, CT (WOS:000275117900001) 2010; 132 Li, SM (WOS:000272880100004) 2010; 27 Okada, M (WOS:000232621100007) 2005; 1 Winkelblech, J (WOS:000360087900001) 2015; 99 Yu, X (WOS:000299170300051) 2012; 287 Schymkowitz, JWH (WOS:000230665800030) 2005; 102 Mori, T (WOS:000371723700001) 2016; 7 Wang, M (WOS:000369152200010) 2016; 17 Unsold, IA (WOS:000229272100019) 2005; 151 Truhlar, DG (WOS:000243171300008) 2007; 28 Xu, W (WOS:000342179200017) 2014; 31 Schuller, JM (WOS:000308267700008) 2012; 422 Yu, X (WOS:000329270300008) 2013; 20 Liu, HT (WOS:000262697700001) 2008; 8 Jost, M (WOS:000285429800037) 2010; 132 Metzger, U (WOS:000269295100028) 2009; 106 Chooi, YH (WOS:000304837800068) 2012; 134 Chen, RD (WOS:000393533000019) 2017; 13 Berdy, J (WOS:000308278500001) 2012; 65 Bills, GF (WOS:000392208200002) 2016; 4 Pockrandt, D (WOS:000336268900018) 2014; 98 WOODSIDE, AB (WOS:A1988AN23700027) 1988; 66 Schymkowitz, J (WOS:000230271400077) 2005; 33 Newman, DJ (WOS:000373031200024) 2016; 79 Soding, J (WOS:000230271400046) 2005; 33 Yin, SQ (WOS:000314407300022) 2013; 97 Tsuji, F (WOS:000299541200013) 2012; 586 Kuzuyama, T (WOS:000229799700055) 2005; 435 Zheng, L (WOS:000223909300037) 2004; 32 Tarcz, S (WOS:000335228700003) 2014; 4 Steffan, N (WOS:000248443800014) 2007; 8 Emsley, P (WOS:000275941300018) 2010; 66 Dumelin, CE (WOS:000310052100010) 2012; 8 |
| References_xml | – volume: 435 start-page: 983 year: 2005 ident: C8OB02037J-(cit12)/*[position()=1] publication-title: Nature doi: 10.1038/nature03668 – volume: 99 start-page: 7379 year: 2015 ident: C8OB02037J-(cit5)/*[position()=1] publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-015-6811-y – volume: 106 start-page: 14309 year: 2009 ident: C8OB02037J-(cit13)/*[position()=1] publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0904897106 – volume: 7 start-page: 10849 year: 2016 ident: C8OB02037J-(cit16)/*[position()=1] publication-title: Nat. Commun. doi: 10.1038/ncomms10849 – volume: 8 start-page: 1298 year: 2007 ident: C8OB02037J-(cit27)/*[position()=1] publication-title: ChemBioChem doi: 10.1002/cbic.200700107 – volume: 33 start-page: W382 year: 2005 ident: C8OB02037J-(cit31)/*[position()=1] publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki387 – volume: 134 start-page: 9428 year: 2012 ident: C8OB02037J-(cit14)/*[position()=1] publication-title: J. Am. Chem. Soc. doi: 10.1021/ja3028636 – volume: 8 start-page: 913 year: 2012 ident: C8OB02037J-(cit9)/*[position()=1] publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.1070 – volume: 151 start-page: 1499 year: 2005 ident: C8OB02037J-(cit19)/*[position()=1] publication-title: Microbiology doi: 10.1099/mic.0.27759-0 – volume: 65 start-page: 441 year: 2012 ident: C8OB02037J-(cit3)/*[position()=1] publication-title: J. Antibiot. doi: 10.1038/ja.2012.54 – volume: 132 start-page: 17849 year: 2010 ident: C8OB02037J-(cit20)/*[position()=1] publication-title: J. Am. Chem. Soc. doi: 10.1021/ja106817c – volume: 31 start-page: 1474 year: 2014 ident: C8OB02037J-(cit10)/*[position()=1] publication-title: Nat. Prod. Rep. doi: 10.1039/C4NP00073K – volume: 66 start-page: 211 year: 1988 ident: C8OB02037J-(cit23)/*[position()=1] publication-title: Org. Synth. doi: 10.15227/orgsyn.066.0211 – volume: 32 start-page: e115 year: 2004 ident: C8OB02037J-(cit29)/*[position()=1] publication-title: Nucleic Acids Res. doi: 10.1093/nar/gnh110 – volume: 98 start-page: 4987 year: 2014 ident: C8OB02037J-(cit17)/*[position()=1] publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-014-5509-x – volume: 586 start-page: 174 year: 2012 ident: C8OB02037J-(cit7)/*[position()=1] publication-title: FEBS Lett. doi: 10.1016/j.febslet.2011.12.012 – volume: 13 start-page: 226 year: 2017 ident: C8OB02037J-(cit15)/*[position()=1] publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio.2263 – volume: 33 start-page: W244 year: 2005 ident: C8OB02037J-(cit26)/*[position()=1] publication-title: Nucleic Acids Res. doi: 10.1093/nar/gki408 – volume: 1 start-page: 23 year: 2005 ident: C8OB02037J-(cit8)/*[position()=1] publication-title: Nat. Chem. Biol. doi: 10.1038/nchembio709 – volume: 31 start-page: 455 year: 2010 ident: C8OB02037J-(cit33)/*[position()=1] publication-title: J. Comput. Chem. doi: 10.1002/jcc.21334 – volume: 102 start-page: 10147 year: 2005 ident: C8OB02037J-(cit30)/*[position()=1] publication-title: Proc. Natl. Acad. Sci. U. S. A. doi: 10.1073/pnas.0501980102 – volume: 4 start-page: 17986 year: 2014 ident: C8OB02037J-(cit18)/*[position()=1] publication-title: RSC Adv. doi: 10.1039/C4RA00337C – volume: 17 start-page: 110 year: 2016 ident: C8OB02037J-(cit6)/*[position()=1] publication-title: Nat. Rev. Mol. Cell Biol. doi: 10.1038/nrm.2015.11 – volume: 4 start-page: 1 year: 2016 ident: C8OB02037J-(cit1)/*[position()=1] publication-title: Microbiol. Spectrum. doi: 10.1128/microbiolspec.FUNK-0009-2016 – volume: 79 start-page: 629 year: 2016 ident: C8OB02037J-(cit2)/*[position()=1] publication-title: J. Nat. Prod. doi: 10.1021/acs.jnatprod.5b01055 – volume: 27 start-page: 57 year: 2010 ident: C8OB02037J-(cit11)/*[position()=1] publication-title: Nat. Prod. Rep. doi: 10.1039/B909987P – volume: 287 start-page: 1371 year: 2012 ident: C8OB02037J-(cit24)/*[position()=1] publication-title: J. Biol. Chem. doi: 10.1074/jbc.M111.317982 – volume: 8 start-page: 91 year: 2008 ident: C8OB02037J-(cit28)/*[position()=1] publication-title: BMC Biotechnol. doi: 10.1186/1472-6750-8-91 – volume: 422 start-page: 87 year: 2012 ident: C8OB02037J-(cit21)/*[position()=1] publication-title: J. Mol. Biol. doi: 10.1016/j.jmb.2012.05.033 – volume: 20 start-page: 1492 year: 2013 ident: C8OB02037J-(cit22)/*[position()=1] publication-title: Chem. Biol. doi: 10.1016/j.chembiol.2013.10.007 – volume: 132 start-page: 2469 year: 2010 ident: C8OB02037J-(cit4)/*[position()=1] publication-title: J. Am. Chem. Soc. doi: 10.1021/ja909118a – volume: 97 start-page: 1649 year: 2013 ident: C8OB02037J-(cit25)/*[position()=1] publication-title: Appl. Microbiol. Biotechnol. doi: 10.1007/s00253-012-4130-0 – volume: 66 start-page: 486 year: 2010 ident: C8OB02037J-(cit32)/*[position()=1] publication-title: Acta Crystallogr., Sect. D: Biol. Crystallogr. doi: 10.1107/S0907444910007493 – volume: 8 start-page: 1298 year: 2007 ident: WOS:000248443800014 article-title: Chemoenzymatic synthesis of prenylated indole derivatives by using a 4-dimethylallyltryptophan synthase from Aspergillus fumigatus publication-title: CHEMBIOCHEM doi: 10.1002/cbic.200700107 – volume: 4 start-page: ARTN FUNK-0009-2016 year: 2016 ident: WOS:000392208200002 article-title: Biologically Active Secondary Metabolites from the Fungi publication-title: MICROBIOLOGY SPECTRUM doi: 10.1128/microbiolspec.FUNK-0009-2016 – volume: 586 start-page: 174 year: 2012 ident: WOS:000299541200013 article-title: Geranyl modification on the tryptophan residue of ComX(RO-E-2) pheromone by a cell-free system publication-title: FEBS LETTERS doi: 10.1016/j.febslet.2011.12.012 – volume: 28 start-page: 73 year: 2007 ident: WOS:000243171300008 article-title: Valence bond theory for chemical dynamics publication-title: JOURNAL OF COMPUTATIONAL CHEMISTRY doi: 10.1002/jcc.20529 – volume: 106 start-page: 14309 year: 2009 ident: WOS:000269295100028 article-title: The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria publication-title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA doi: 10.1073/pnas.0904897106 – volume: 422 start-page: 87 year: 2012 ident: WOS:000308267700008 article-title: Structure and Catalytic Mechanism of a Cyclic Dipeptide Prenyltransferase with Broad Substrate Promiscuity publication-title: JOURNAL OF MOLECULAR BIOLOGY doi: 10.1016/j.jmb.2012.05.033 – volume: 66 start-page: 211 year: 1988 ident: WOS:A1988AN23700027 article-title: TRISAMMONIUM GERANYL DIPHOSPHATE publication-title: ORGANIC SYNTHESES – volume: 17 start-page: 110 year: 2016 ident: WOS:000369152200010 article-title: Protein prenylation: unique fats make their mark on biology publication-title: NATURE REVIEWS MOLECULAR CELL BIOLOGY doi: 10.1038/nrm.2015.11 – volume: 8 start-page: 913 year: 2012 ident: WOS:000310052100010 article-title: Discovery and biological characterization of geranylated RNA in bacteria publication-title: NATURE CHEMICAL BIOLOGY doi: 10.1038/NCHEMBIO.1070 – volume: 151 start-page: 1499 year: 2005 ident: WOS:000229272100019 article-title: Overproduction, purification and characterization of FgaPT2, a dimethylallyltryptophan synthase from Aspergillus fumigatus publication-title: MICROBIOLOGY-SGM doi: 10.1099/mic.0.27759-0 – volume: 13 start-page: 226 year: 2017 ident: WOS:000393533000019 article-title: Molecular insights into the enzyme promiscuity of an aromatic prenyltransferase publication-title: NATURE CHEMICAL BIOLOGY doi: 10.1038/NCHEMBIO.2263 – volume: 1 start-page: 23 year: 2005 ident: WOS:000232621100007 article-title: Structure of the Bacillus subtilis quorum-sensing peptide pheromone ComX publication-title: NATURE CHEMICAL BIOLOGY doi: 10.1038/nchembio709 – volume: 97 start-page: 1649 year: 2013 ident: WOS:000314407300022 article-title: Identification of a brevianamide F reverse prenyltransferase BrePT from Aspergillus versicolor with a broad substrate specificity towards tryptophan-containing cyclic dipeptides publication-title: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY doi: 10.1007/s00253-012-4130-0 – volume: 66 start-page: 486 year: 2010 ident: WOS:000275941300018 article-title: Features and development of Coot publication-title: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY doi: 10.1107/S0907444910007493 – volume: 7 start-page: ARTN 10849 year: 2016 ident: WOS:000371723700001 article-title: Manipulation of prenylation reactions by structure-based engineering of bacterial indolactam prenyltransferases publication-title: NATURE COMMUNICATIONS doi: 10.1038/ncomms10849 – volume: 8 start-page: ARTN 91 year: 2008 ident: WOS:000262697700001 article-title: An efficient one-step site-directed deletion, insertion, single and multiple-site plasmid mutagenesis protocol publication-title: BMC BIOTECHNOLOGY doi: 10.1186/1472-6750-8-91 – volume: 27 start-page: 57 year: 2010 ident: WOS:000272880100004 article-title: Prenylated indole derivatives from fungi: structure diversity, biological activities, biosynthesis and chemoenzymatic synthesis publication-title: NATURAL PRODUCT REPORTS doi: 10.1039/b909987p – volume: 33 start-page: W382 year: 2005 ident: WOS:000230271400077 article-title: The FoldX web server: an online force field publication-title: NUCLEIC ACIDS RESEARCH doi: 10.1093/nar/gki387 – volume: 32 start-page: ARTN e115 year: 2004 ident: WOS:000223909300037 article-title: An efficient one-step site-directed and site-saturation mutagenesis protocol publication-title: NUCLEIC ACIDS RESEARCH doi: 10.1093/nar/gnh110 – volume: 287 start-page: 1371 year: 2012 ident: WOS:000299170300051 article-title: Biochemical Characterization of Indole Prenyltransferases FILLING THE LAST GAP OF PRENYLATION POSITIONS BY A 5-DIMETHYLALLYLTRYPTOPHAN SYNTHASE FROM ASPERGILLUS CLAVATUS publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY doi: 10.1074/jbc.M111.317982 – volume: 134 start-page: 9428 year: 2012 ident: WOS:000304837800068 article-title: Discovery and Characterization of a Group of Fungal Polycyclic Polyketide Prenyltransferases publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja3028636 – volume: 435 start-page: 983 year: 2005 ident: WOS:000229799700055 article-title: Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products publication-title: NATURE doi: 10.1038/nature03668 – volume: 132 start-page: 2469 year: 2010 ident: WOS:000275117900001 article-title: Natural Products Version 2.0: Connecting Genes to Molecules publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja909118a – volume: 4 start-page: 17986 year: 2014 ident: WOS:000335228700003 article-title: Substrate and catalytic promiscuity of secondary metabolite enzymes: O-prenylation of hydroxyxanthones with different prenyl donors by a bisindolyl benzoquinone C- and N-prenyltransferase publication-title: RSC ADVANCES doi: 10.1039/c4ra00337c – volume: 31 start-page: 1474 year: 2014 ident: WOS:000342179200017 article-title: Biosynthesis of fungal indole alkaloids publication-title: NATURAL PRODUCT REPORTS doi: 10.1039/c4np00073k – volume: 99 start-page: 7379 year: 2015 ident: WOS:000360087900001 article-title: Prenyltransferases as key enzymes in primary and secondary metabolism publication-title: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY doi: 10.1007/s00253-015-6811-y – volume: 20 start-page: 1492 year: 2013 ident: WOS:000329270300008 article-title: Catalytic Mechanism of Stereospecific Formation of cis-Configured Prenylated Pyrroloindoline Diketopiperazines by lndole Prenyltransferases publication-title: CHEMISTRY & BIOLOGY doi: 10.1016/j.chembiol.2013.10.007 – volume: 79 start-page: 629 year: 2016 ident: WOS:000373031200024 article-title: Natural Products as Sources of New Drugs from 1981 to 2014 publication-title: JOURNAL OF NATURAL PRODUCTS doi: 10.1021/acs.jnatprod.5b01055 – volume: 98 start-page: 4987 year: 2014 ident: WOS:000336268900018 article-title: A promiscuous prenyltransferase from Aspergillus oryzae catalyses C-prenylations of hydroxynaphthalenes in the presence of different prenyl donors publication-title: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY doi: 10.1007/s00253-014-5509-x – volume: 65 start-page: 385 year: 2012 ident: WOS:000308278500001 article-title: Thoughts and facts about antibiotics: Where we are now and where we are heading publication-title: JOURNAL OF ANTIBIOTICS doi: 10.1038/ja.2012.27 – volume: 33 start-page: W244 year: 2005 ident: WOS:000230271400046 article-title: The HHpred interactive server for protein homology detection and structure prediction publication-title: NUCLEIC ACIDS RESEARCH doi: 10.1093/nar/gki408 – volume: 132 start-page: 17849 year: 2010 ident: WOS:000285429800037 article-title: Structure-Function Analysis of an Enzymatic Prenyl Transfer Reaction Identifies a Reaction Chamber with Modifiable Specificity publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY doi: 10.1021/ja106817c – volume: 102 start-page: 10147 year: 2005 ident: WOS:000230665800030 article-title: Prediction of water and metal binding sites and their affinities by using the Fold-X force field publication-title: PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA doi: 10.1073/pnas.0501980102 |
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| Snippet | Microorganisms provide valuable enzyme machinery to assemble complex molecules. Fungal prenyltransferases (PTs) typically catalyse highly regiospecific... |
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| SubjectTerms | Catalysis Chemistry Chemistry, Organic Data processing Donors (electronic) Enzymes Fungi Hydrophobicity Microorganisms Molecular modelling Molecular structure Mutagenesis NMR Nuclear magnetic resonance Physical Sciences Prenyltransferases Primers Protein engineering Protein structure Proteins Saturation mutagenesis Science & Technology Selectivity Site-directed mutagenesis |
| Title | Structure-based protein engineering enables prenyl donor switching of a fungal aromatic prenyltransferase |
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