Tryptophan prenyltransferases showing higher catalytic activities for Friedel–Crafts alkylation of o- and m-tyrosines than tyrosine prenyltransferases

Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATS Sv and 7-DMATS catalyse regiospecific C -prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O -prenylation of the phenolic hydroxyl group. In this study, we report the Friedel–Crafts alkylation of l -...

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Published inOrganic & biomolecular chemistry Vol. 13; no. 27; pp. 7551 - 7557
Main Authors Fan, Aili, Xie, Xiulan, Li, Shu-Ming
Format Journal Article
LanguageEnglish
Published CAMBRIDGE Royal Soc Chemistry 21.07.2015
Subjects
Alkylation
Biocatalysis
Carbon-13 Magnetic Resonance Spectroscopy
Chemistry
Chemistry, Organic
Chromatography, High Pressure Liquid
Dimethylallyltranstransferase - metabolism
Kinetics
Physical Sciences
Prenylation
Proton Magnetic Resonance Spectroscopy
Science & Technology
Tryptophan - metabolism
Tyrosine - metabolism
DIMETHYLALLYLTRYPTOPHAN SYNTHASE
ASPERGILLUS-FUMIGATUS
INDOLE PRENYLTRANSFERASES
OVERPRODUCTION
PRENYLATION
ENZYMES
PURIFICATION
BIOCHEMICAL-CHARACTERIZATION
SUPERFAMILY
DERIVATIVES
Online AccessGet full text

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Abstract Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATS Sv and 7-DMATS catalyse regiospecific C -prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O -prenylation of the phenolic hydroxyl group. In this study, we report the Friedel–Crafts alkylation of l - o -tyrosine by these enzymes. Surprisingly, no conversion was detected with SirD and three tryptophan prenyltransferases showed significantly higher activity than another tyrosine prenyltransferase TyrPT. C 5-prenylated l - o -tyrosine was identified as a unique product of these enzymes. Using l - m -tyrosine as the prenylation substrate, product formation was only observed with the tryptophan prenyltransferases FgaPT2 and 7-DMATS. C 4- and C 6-prenylated derivatives were identified in the reaction mixture of FgaPT2. These results provided additional evidence for the similarities and differences between these two subgroups within the DMATS superfamily in their catalytic behaviours.
AbstractList Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATSSv and 7-DMATS catalyse regiospecific C-prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O-prenylation of the phenolic hydroxyl group. In this study, we report the Friedel-Crafts alkylation of L-o-tyrosine by these enzymes. Surprisingly, no conversion was detected with SirD and three tryptophan prenyltransferases showed significantly higher activity than another tyrosine prenyltransferase TyrPT. C5-prenylated L-o-tyrosine was identified as a unique product of these enzymes. Using L-m-tyrosine as the prenylation substrate, product formation was only observed with the tryptophan prenyltransferases FgaPT2 and 7-DMATS. C4- and C6-prenylated derivatives were identified in the reaction mixture of FgaPT2. These results provided additional evidence for the similarities and differences between these two subgroups within the DMATS superfamily in their catalytic behaviours.Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATSSv and 7-DMATS catalyse regiospecific C-prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O-prenylation of the phenolic hydroxyl group. In this study, we report the Friedel-Crafts alkylation of L-o-tyrosine by these enzymes. Surprisingly, no conversion was detected with SirD and three tryptophan prenyltransferases showed significantly higher activity than another tyrosine prenyltransferase TyrPT. C5-prenylated L-o-tyrosine was identified as a unique product of these enzymes. Using L-m-tyrosine as the prenylation substrate, product formation was only observed with the tryptophan prenyltransferases FgaPT2 and 7-DMATS. C4- and C6-prenylated derivatives were identified in the reaction mixture of FgaPT2. These results provided additional evidence for the similarities and differences between these two subgroups within the DMATS superfamily in their catalytic behaviours.
Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATS Sv and 7-DMATS catalyse regiospecific C -prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O -prenylation of the phenolic hydroxyl group. In this study, we report the Friedel–Crafts alkylation of l - o -tyrosine by these enzymes. Surprisingly, no conversion was detected with SirD and three tryptophan prenyltransferases showed significantly higher activity than another tyrosine prenyltransferase TyrPT. C 5-prenylated l - o -tyrosine was identified as a unique product of these enzymes. Using l - m -tyrosine as the prenylation substrate, product formation was only observed with the tryptophan prenyltransferases FgaPT2 and 7-DMATS. C 4- and C 6-prenylated derivatives were identified in the reaction mixture of FgaPT2. These results provided additional evidence for the similarities and differences between these two subgroups within the DMATS superfamily in their catalytic behaviours.
Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATSSv and 7-DMATS catalyse regiospecific C-prenylations on the indole ring, while tyrosine prenyltransferases SirD and TyrPT catalyse the O-prenylation of the phenolic hydroxyl group. In this study, we report the Friedel-Crafts alkylation of L-o-tyrosine by these enzymes. Surprisingly, no conversion was detected with SirD and three tryptophan prenyltransferases showed significantly higher activity than another tyrosine prenyltransferase TyrPT. C5-prenylated L-o-tyrosine was identified as a unique product of these enzymes. Using L-m-tyrosine as the prenylation substrate, product formation was only observed with the tryptophan prenyltransferases FgaPT2 and 7-DMATS. C4- and C6-prenylated derivatives were identified in the reaction mixture of FgaPT2. These results provided additional evidence for the similarities and differences between these two subgroups within the DMATS superfamily in their catalytic behaviours.
Author Li, Shu-Ming
Fan, Aili
Xie, Xiulan
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Cites_doi 10.1039/B909987P
10.1002/cbic.201400046
10.1002/cbic.200800237
10.1007/s00253-009-2128-z
10.1099/mic.0.033886-0
10.1007/s00253-014-5872-7
10.1021/ja106817c
10.1016/j.phytochem.2009.08.023
10.1099/mic.0.27759-0
10.1074/jbc.M111.317982
10.1099/mic.0.2007/009019-0
10.15227/orgsyn.066.0211
10.1074/jbc.M114.623413
10.1080/10715760500307107
10.1021/ja906485u
10.1111/j.1523-1755.2005.00687.x
10.1016/j.bmc.2014.02.031
10.1055/s-2006-947195
10.1073/pnas.0904897106
10.1002/chem.201001451
10.1021/op700093y
10.1002/anie.201309591
10.1016/j.tetlet.2014.07.080
10.1016/j.cbpa.2009.02.020
10.1021/ja311145n
10.1111/j.1365-2958.2004.04215.x
10.1002/anie.200460416
10.1016/B978-0-12-394291-3.00005-8
10.1039/C0NP00060D
10.1039/b909987p
10.1039/c0np00060d
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Issue 27
Keywords DIMETHYLALLYLTRYPTOPHAN SYNTHASE
ASPERGILLUS-FUMIGATUS
INDOLE PRENYLTRANSFERASES
OVERPRODUCTION
PRENYLATION
ENZYMES
PURIFICATION
BIOCHEMICAL-CHARACTERIZATION
SUPERFAMILY
DERIVATIVES
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References Fan (C5OB01040C-(cit17)/*[position()=1]) 2014; 98
Woodside (C5OB01040C-(cit27)/*[position()=1]) 1988; 66
Li (C5OB01040C-(cit1)/*[position()=1]) 2010; 27
Humphrey (C5OB01040C-(cit21)/*[position()=1]) 2007; 11
Li (C5OB01040C-(cit7)/*[position()=1]) 2009; 84
Fan (C5OB01040C-(cit22)/*[position()=1]) 2014; 55
Li (C5OB01040C-(cit13)/*[position()=1]) 2006; 72
Stec (C5OB01040C-(cit26)/*[position()=1]) 2008; 9
Miyamoto (C5OB01040C-(cit9)/*[position()=1]) 2014; 22
Molnar (C5OB01040C-(cit20)/*[position()=1]) 2005; 68
Yin (C5OB01040C-(cit14)/*[position()=1]) 2013; 135
Wallwey (C5OB01040C-(cit3)/*[position()=1]) 2011; 28
Kremer (C5OB01040C-(cit15)/*[position()=1]) 2010; 156
Molnar (C5OB01040C-(cit19)/*[position()=1]) 2005; 39
Gardiner (C5OB01040C-(cit16)/*[position()=1]) 2004; 53
Winkelblech (C5OB01040C-(cit8)/*[position()=1]) 2014; 15
Ruiz-Sanchis (C5OB01040C-(cit2)/*[position()=1]) 2011; 17
Yu (C5OB01040C-(cit11)/*[position()=1]) 2012; 287
Jost (C5OB01040C-(cit24)/*[position()=1]) 2010; 132
Kremer (C5OB01040C-(cit12)/*[position()=1]) 2007; 153
Heide (C5OB01040C-(cit4)/*[position()=1]) 2009; 13
Yazaki (C5OB01040C-(cit5)/*[position()=1]) 2009; 70
Metzger (C5OB01040C-(cit25)/*[position()=1]) 2009; 106
Hohne (C5OB01040C-(cit30)/*[position()=1]) 2014; 53
Luk (C5OB01040C-(cit23)/*[position()=1]) 2009; 131
Unsöld (C5OB01040C-(cit10)/*[position()=1]) 2005; 151
Yu (C5OB01040C-(cit6)/*[position()=1]) 2012; 516
Fan (C5OB01040C-(cit18)/*[position()=1]) 2015; 290
Berger (C5OB01040C-(cit28)/*[position()=1]) 2004
Bornscheuer (C5OB01040C-(cit29)/*[position()=1]) 2004; 43
Kremer, A (WOS:000274368500031) 2010; 156
Li, SM (WOS:000272880100004) 2010; 27
Humphrey, CE (WOS:000251061400022) 2007; 11
Wallwey, C (WOS:000287706000003) 2011; 28
Gardiner, DM (WOS:000223495100003) 2004; 53
Yu, X (WOS:000299170300051) 2012; 287
Unsold, IA (WOS:000229272100019) 2005; 151
Fan, AL (WOS:000345331700017) 2014; 98
Yazaki, K (WOS:000272730000013) 2009; 70
Molnar, GA (WOS:000233430100010) 2005; 39
Berger, S. (000357414400024.1) 2004
Luk, LYP (WOS:000270433900024) 2009; 131
WOODSIDE AB (WOS:000357414400024.26) 1988; 66
Jost, M (WOS:000285429800037) 2010; 132
Yin, WB (WOS:000315080100009) 2013; 135
Metzger, U (WOS:000269295100028) 2009; 106
Kremer, A (WOS:000250279500021) 2007; 153
Li, SM (WOS:000269911000004) 2009; 84
Stec, E (WOS:000259067000005) 2008; 9
Fan, AL (WOS:000341476400021) 2014; 55
Fan, AL (WOS:000348056400006) 2015; 290
Molnar, GA (WOS:000232388800066) 2005; 68
Li, SM (WOS:000241250800004) 2006; 72
Heide, L (WOS:000266345400006) 2009; 13
Hohne, M (WOS:000336504500001) 2014; 53
Winkelblech, J (WOS:000335022800016) 2014; 15
Bornscheuer, UT (WOS:000225445200003) 2004; 43
Yu, X (WOS:000313665100014) 2012; 516
Ruiz-Sanchis, P (WOS:000287555600001) 2011; 17
Miyamoto, K (WOS:000334338000016) 2014; 22
References_xml – volume: 27
  start-page: 57
  year: 2010
  ident: C5OB01040C-(cit1)/*[position()=1]
  publication-title: Nat. Prod. Rep.
  doi: 10.1039/B909987P
– volume: 15
  start-page: 1030
  year: 2014
  ident: C5OB01040C-(cit8)/*[position()=1]
  publication-title: ChemBioChem
  doi: 10.1002/cbic.201400046
– volume: 9
  start-page: 2055
  year: 2008
  ident: C5OB01040C-(cit26)/*[position()=1]
  publication-title: ChemBioChem
  doi: 10.1002/cbic.200800237
– volume: 84
  start-page: 631
  year: 2009
  ident: C5OB01040C-(cit7)/*[position()=1]
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-009-2128-z
– volume: 156
  start-page: 278
  year: 2010
  ident: C5OB01040C-(cit15)/*[position()=1]
  publication-title: Microbiology
  doi: 10.1099/mic.0.033886-0
– volume: 98
  start-page: 10119
  year: 2014
  ident: C5OB01040C-(cit17)/*[position()=1]
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-014-5872-7
– volume: 132
  start-page: 17849
  year: 2010
  ident: C5OB01040C-(cit24)/*[position()=1]
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja106817c
– volume: 70
  start-page: 1739
  year: 2009
  ident: C5OB01040C-(cit5)/*[position()=1]
  publication-title: Phytochemistry
  doi: 10.1016/j.phytochem.2009.08.023
– volume: 151
  start-page: 1499
  year: 2005
  ident: C5OB01040C-(cit10)/*[position()=1]
  publication-title: Microbiology
  doi: 10.1099/mic.0.27759-0
– volume: 287
  start-page: 1371
  year: 2012
  ident: C5OB01040C-(cit11)/*[position()=1]
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M111.317982
– volume: 153
  start-page: 3409
  year: 2007
  ident: C5OB01040C-(cit12)/*[position()=1]
  publication-title: Microbiology
  doi: 10.1099/mic.0.2007/009019-0
– volume: 66
  start-page: 211
  year: 1988
  ident: C5OB01040C-(cit27)/*[position()=1]
  publication-title: Org. Synth.
  doi: 10.15227/orgsyn.066.0211
– volume: 290
  start-page: 1364
  year: 2015
  ident: C5OB01040C-(cit18)/*[position()=1]
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M114.623413
– volume: 39
  start-page: 1359
  year: 2005
  ident: C5OB01040C-(cit19)/*[position()=1]
  publication-title: Free Radical Res.
  doi: 10.1080/10715760500307107
– volume: 131
  start-page: 13932
  year: 2009
  ident: C5OB01040C-(cit23)/*[position()=1]
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja906485u
– volume: 68
  start-page: 2281
  year: 2005
  ident: C5OB01040C-(cit20)/*[position()=1]
  publication-title: Kidney Int.
  doi: 10.1111/j.1523-1755.2005.00687.x
– volume-title: 200 and More NMR Experiments. A Practical Course
  year: 2004
  ident: C5OB01040C-(cit28)/*[position()=1]
– volume: 22
  start-page: 2517
  year: 2014
  ident: C5OB01040C-(cit9)/*[position()=1]
  publication-title: Bioorg. Med. Chem.
  doi: 10.1016/j.bmc.2014.02.031
– volume: 72
  start-page: 1117
  year: 2006
  ident: C5OB01040C-(cit13)/*[position()=1]
  publication-title: Planta Med.
  doi: 10.1055/s-2006-947195
– volume: 106
  start-page: 14309
  year: 2009
  ident: C5OB01040C-(cit25)/*[position()=1]
  publication-title: Proc. Natl. Acad. Sci. U. S. A.
  doi: 10.1073/pnas.0904897106
– volume: 17
  start-page: 1388
  year: 2011
  ident: C5OB01040C-(cit2)/*[position()=1]
  publication-title: Chemistry
  doi: 10.1002/chem.201001451
– volume: 11
  start-page: 1069
  year: 2007
  ident: C5OB01040C-(cit21)/*[position()=1]
  publication-title: Org. Process Res. Dev.
  doi: 10.1021/op700093y
– volume: 53
  start-page: 1200
  year: 2014
  ident: C5OB01040C-(cit30)/*[position()=1]
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.201309591
– volume: 55
  start-page: 5199
  year: 2014
  ident: C5OB01040C-(cit22)/*[position()=1]
  publication-title: Tetrahedron Lett.
  doi: 10.1016/j.tetlet.2014.07.080
– volume: 13
  start-page: 171
  year: 2009
  ident: C5OB01040C-(cit4)/*[position()=1]
  publication-title: Curr. Opin. Chem. Biol.
  doi: 10.1016/j.cbpa.2009.02.020
– volume: 135
  start-page: 2064
  year: 2013
  ident: C5OB01040C-(cit14)/*[position()=1]
  publication-title: J. Am. Chem. Soc.
  doi: 10.1021/ja311145n
– volume: 53
  start-page: 1307
  year: 2004
  ident: C5OB01040C-(cit16)/*[position()=1]
  publication-title: Mol. Microbiol.
  doi: 10.1111/j.1365-2958.2004.04215.x
– volume: 43
  start-page: 6032
  year: 2004
  ident: C5OB01040C-(cit29)/*[position()=1]
  publication-title: Angew. Chem., Int. Ed.
  doi: 10.1002/anie.200460416
– volume: 516
  start-page: 259
  year: 2012
  ident: C5OB01040C-(cit6)/*[position()=1]
  publication-title: Methods Enzymol.
  doi: 10.1016/B978-0-12-394291-3.00005-8
– volume: 28
  start-page: 496
  year: 2011
  ident: C5OB01040C-(cit3)/*[position()=1]
  publication-title: Nat. Prod. Rep.
  doi: 10.1039/C0NP00060D
– year: 2004
  ident: 000357414400024.1
  publication-title: 200 and More NMR Experiments. A Practical Course
– volume: 17
  start-page: 1388
  year: 2011
  ident: WOS:000287555600001
  article-title: Structure, Bioactivity and Synthesis of Natural Products with Hexahydropyrrolo[2,3-b]indole
  publication-title: CHEMISTRY-A EUROPEAN JOURNAL
  doi: 10.1002/chem.201001451
– volume: 68
  start-page: 2281
  year: 2005
  ident: WOS:000232388800066
  article-title: Urinary ortho-tyrosine excretion in diabetes mellitus and renal failure: Evidence for hydroxyl radical production
  publication-title: KIDNEY INTERNATIONAL
– volume: 135
  start-page: 2064
  year: 2013
  ident: WOS:000315080100009
  article-title: A Nonribosomal Peptide Synthetase-Derived Iron(III) Complex from the Pathogenic Fungus Aspergillus fumigatus
  publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
  doi: 10.1021/ja311145n
– volume: 11
  start-page: 1069
  year: 2007
  ident: WOS:000251061400022
  article-title: Optimized synthesis of l-m-tyrosine suitable for chemical scale-up
  publication-title: ORGANIC PROCESS RESEARCH & DEVELOPMENT
  doi: 10.1021/op700093y
– 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: 15
  start-page: 1030
  year: 2014
  ident: WOS:000335022800016
  article-title: Biochemical Investigations of Two 6-DMATS Enzymes from Streptomyces Reveal New Features of l- Tryptophan Prenyltransferases
  publication-title: CHEMBIOCHEM
  doi: 10.1002/cbic.201400046
– volume: 43
  start-page: 6032
  year: 2004
  ident: WOS:000225445200003
  article-title: Catalytic promiscuity in biocatalysis: Using old enzymes to form new bonds and follow new pathways
  publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
  doi: 10.1002/anie.200460416
– volume: 156
  start-page: 278
  year: 2010
  ident: WOS:000274368500031
  article-title: A tyrosine O-prenyltransferase catalyses the first pathway-specific step in the biosynthesis of sirodesmin PL
  publication-title: MICROBIOLOGY-SGM
  doi: 10.1099/mic.0.033886-0
– volume: 131
  start-page: 13932
  year: 2009
  ident: WOS:000270433900024
  article-title: Mechanism of Dimethylallyltryptophan Synthase: Evidence for a Dimethylallyl Cation Intermediate in an Aromatic Prenyltransferase Reaction
  publication-title: JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
  doi: 10.1021/ja906485u
– volume: 55
  start-page: 5199
  year: 2014
  ident: WOS:000341476400021
  article-title: Prenylation of tyrosine and derivatives by a tryptophan C7-prenyltransferase
  publication-title: TETRAHEDRON LETTERS
  doi: 10.1016/j.tetlet.2014.07.080
– 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: 72
  start-page: 1117
  year: 2006
  ident: WOS:000241250800004
  article-title: Post-genome research on the biosynthesis of ergot alkaloids
  publication-title: PLANTA MEDICA
  doi: 10.1055/s-2006-947195
– volume: 290
  start-page: 1364
  year: 2015
  ident: WOS:000348056400006
  article-title: Site-directed Mutagenesis Switching a Dimethylallyl Tryptophan Synthase to a Specific Tyrosine C-3-Prenylating Enzyme
  publication-title: JOURNAL OF BIOLOGICAL CHEMISTRY
  doi: 10.1074/jbc.M114.623413
– volume: 39
  start-page: 1359
  year: 2005
  ident: WOS:000233430100010
  article-title: Accumulation of the hydroxyl free radical markers meta-, ortho-tyrosine and DOPA in cataractous lenses is accompanied by a lower protein and phenylalanine content of the water-soluble phase
  publication-title: FREE RADICAL RESEARCH
  doi: 10.1080/10715760500307107
– volume: 9
  start-page: 2055
  year: 2008
  ident: WOS:000259067000005
  article-title: Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi
  publication-title: CHEMBIOCHEM
  doi: 10.1002/cbic.200800237
– volume: 53
  start-page: 1200
  year: 2014
  ident: WOS:000336504500001
  article-title: Protein Engineering from "Scratch" Is Maturing
  publication-title: ANGEWANDTE CHEMIE-INTERNATIONAL EDITION
  doi: 10.1002/anie.201309591
– volume: 70
  start-page: 1739
  year: 2009
  ident: WOS:000272730000013
  article-title: Prenylation of aromatic compounds, a key diversification of plant secondary metabolites
  publication-title: PHYTOCHEMISTRY
  doi: 10.1016/j.phytochem.2009.08.023
– volume: 516
  start-page: 259
  year: 2012
  ident: WOS:000313665100014
  article-title: Prenyltransferases of the Dimethylallyltryptophan Synthase Superfamily
  publication-title: NATURAL PRODUCT BIOSYNTHESIS BY MICROORGANISMS AND PLANTS, PT B
  doi: 10.1016/B978-0-12-394291-3.00005-8
– volume: 98
  start-page: 10119
  year: 2014
  ident: WOS:000345331700017
  article-title: A new member of the DMATS superfamily from Aspergillus niger catalyzes prenylations of both tyrosine and tryptophan derivatives
  publication-title: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  doi: 10.1007/s00253-014-5872-7
– volume: 84
  start-page: 631
  year: 2009
  ident: WOS:000269911000004
  article-title: Applications of dimethylallyltryptophan synthases and other indole prenyltransferases for structural modification of natural products
  publication-title: APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
  doi: 10.1007/s00253-009-2128-z
– 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: 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: 53
  start-page: 1307
  year: 2004
  ident: WOS:000223495100003
  article-title: The sirodesmin biosynthetic gene cluster of the plant pathogenic fungus Leptosphaeria maculans
  publication-title: MOLECULAR MICROBIOLOGY
  doi: 10.1111/j.1365-2958.2004.04215.x
– volume: 13
  start-page: 171
  year: 2009
  ident: WOS:000266345400006
  article-title: Prenyl transfer to aromatic substrates: genetics and enzymology
  publication-title: CURRENT OPINION IN CHEMICAL BIOLOGY
  doi: 10.1016/j.cbpa.2009.02.020
– volume: 153
  start-page: 3409
  year: 2007
  ident: WOS:000250279500021
  article-title: A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: overproduction, purification and biochemical characterization
  publication-title: MICROBIOLOGY-SGM
  doi: 10.1099/mic.0.2007/009019-0
– volume: 28
  start-page: 496
  year: 2011
  ident: WOS:000287706000003
  article-title: Ergot alkaloids: structure diversity, biosynthetic gene clusters and functional proof of biosynthetic genes
  publication-title: NATURAL PRODUCT REPORTS
  doi: 10.1039/c0np00060d
– 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: 66
  start-page: 211
  year: 1988
  ident: WOS:000357414400024.26
  publication-title: ORG SYNTH
– volume: 22
  start-page: 2517
  year: 2014
  ident: WOS:000334338000016
  article-title: A 7-dimethylallyl tryptophan synthase from a fungal Neosartorya sp.: Biochemical characterization and structural insight into the regioselective prenylation
  publication-title: BIOORGANIC & MEDICINAL CHEMISTRY
  doi: 10.1016/j.bmc.2014.02.031
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Snippet Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATS Sv and 7-DMATS catalyse regiospecific C -prenylations on the indole ring, while tyrosine...
Tryptophan prenyltransferases FgaPT2, 5-DMATS, 6-DMATSSv and 7-DMATS catalyse regiospecific C-prenylations on the indole ring, while tyrosine...
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SubjectTerms Alkylation
Biocatalysis
Carbon-13 Magnetic Resonance Spectroscopy
Chemistry
Chemistry, Organic
Chromatography, High Pressure Liquid
Dimethylallyltranstransferase - metabolism
Kinetics
Physical Sciences
Prenylation
Proton Magnetic Resonance Spectroscopy
Science & Technology
Tryptophan - metabolism
Tyrosine - metabolism
Title Tryptophan prenyltransferases showing higher catalytic activities for Friedel–Crafts alkylation of o- and m-tyrosines than tyrosine prenyltransferases
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https://www.ncbi.nlm.nih.gov/pubmed/26077893
https://www.proquest.com/docview/1693730209
Volume 13
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