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Volumn 106, Issue 34, 2009, Pages 14309-14314

The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria

Author keywords

ABBA prenyltransferase; EC 2.5.1.34; Ergot alkaloids; PT barrel

Indexed keywords

BACTERIAL ENZYME; DIMETHYLALLYLTRANSFERASE; DIMETHYLALLYLTRYPTOPHAN SYNTHASE; ERGOT ALKALOID; INDOLE; MAGNESIUM; TRYPTOPHAN DERIVATIVE; UNCLASSIFIED DRUG;

EID: 70149099367     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0904897106     Document Type: Article
Times cited : (161)

References (39)
  • 3
    • 0342688061 scopus 로고
    • Lechler M, ed (Frankfurt am Main, Germany)
    • Lonicer A (1582) Kreuterbuch, Lechler M, ed (Frankfurt am Main, Germany).
    • (1582) Kreuterbuch
    • Lonicer, A.1
  • 4
    • 0031737322 scopus 로고    scopus 로고
    • Ergot alkaloids. Current status and review of clinical pharmacology and therapeutic use compared with other oxytocics in obstetrics and gynaecology
    • de Groot AN, van Dongen PW, Vree TB, Hekster YA, van Roosmalen J (1998) Ergot alkaloids. Current status and review of clinical pharmacology and therapeutic use compared with other oxytocics in obstetrics and gynaecology. Drugs 56:523-535.
    • (1998) Drugs , vol.56 , pp. 523-535
    • De Groot, A.N.1    Van Dongen, P.W.2    Vree, T.B.3    Hekster, Y.A.4    Van Roosmalen, J.5
  • 5
    • 77956679296 scopus 로고    scopus 로고
    • Biochemistry of ergot alkaloids - Achievements and challenges
    • Gröger D, Floss HG (1998) Biochemistry of ergot alkaloids - Achievements and challenges. Alkaloids Chem Biol 50:171-218.
    • (1998) Alkaloids Chem Biol , vol.50 , pp. 171-218
    • Gröger, D.1    Floss, H.G.2
  • 6
    • 4344613110 scopus 로고
    • Die optisch aktiven Hydrazide der Lysergsäure und der Isolysergsäure. (4. Mitteilung über Mutterkornalkaloide)
    • Stoll A, Hofmann A (1943) Die optisch aktiven Hydrazide der Lysergsäure und der Isolysergsäure. (4. Mitteilung über Mutterkornalkaloide). Helv Chim Acta 26:922-928.
    • (1943) Helv Chim Acta , vol.26 , pp. 922-928
    • Stoll, A.1    Hofmann, A.2
  • 7
    • 33645302916 scopus 로고    scopus 로고
    • Current approaches to diagnosis and treatment of invasive aspergillosis
    • Segal BH, Walsh TJ (2006) Current approaches to diagnosis and treatment of invasive aspergillosis. Am J Respir Crit Care Med 173:707-717.
    • (2006) Am J Respir Crit Care Med , vol.173 , pp. 707-717
    • Segal, B.H.1    Walsh, T.J.2
  • 8
    • 0015116740 scopus 로고
    • Isolation of dimethylallylpyrophosphate: Tryptophan dimethylallyl transferase from the ergot fungus (Claviceps spec.)
    • Heinstein PF, Lee SI, Floss HG (1971) Isolation of dimethylallylpyrophosphate: Tryptophan dimethylallyl transferase from the ergot fungus (Claviceps spec.). Biochem Biophys Res Commun 44:1244-1251.
    • (1971) Biochem Biophys Res Commun , vol.44 , pp. 1244-1251
    • Heinstein, P.F.1    Lee, S.I.2    Floss, H.G.3
  • 9
    • 0017176386 scopus 로고
    • Purification and properties of dimethylallylpyrophosphate: Tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps. sp. SD 58
    • Lee SL, Floss HG, Heinstein P (1976) Purification and properties of dimethylallylpyrophosphate: tryptophan dimethylallyl transferase, the first enzyme of ergot alkaloid biosynthesis in Claviceps. sp. SD 58. Arch Biochem Biophys 177:84-94.
    • (1976) Arch Biochem Biophys , vol.177 , pp. 84-94
    • Lee, S.L.1    Floss, H.G.2    Heinstein, P.3
  • 10
    • 0026751389 scopus 로고
    • Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea
    • Gebler JC, Poulter CD (1992) Purification and characterization of dimethylallyl tryptophan synthase from Claviceps purpurea. Arch Biochem Biophys 296:308-313.
    • (1992) Arch Biochem Biophys , vol.296 , pp. 308-313
    • Gebler, J.C.1    Poulter, C.D.2
  • 11
    • 33746326801 scopus 로고    scopus 로고
    • Farnesyl diphosphate synthase. A paradigm for understanding structure and function relationships in E-polyprenyl diphosphate synthases
    • Poulter CD (2006) Farnesyl diphosphate synthase. A paradigm for understanding structure and function relationships in E-polyprenyl diphosphate synthases. Phytochem Rev 5:17-26.
    • (2006) Phytochem Rev , vol.5 , pp. 17-26
    • Poulter, C.D.1
  • 12
    • 0036375597 scopus 로고    scopus 로고
    • Structure, mechanism and function of prenyltransferases
    • Liang PH, Ko TP, Wang AH (2002) Structure, mechanism and function of prenyltransferases. Eur J Biochem 269:3339-3354.
    • (2002) Eur J Biochem , vol.269 , pp. 3339-3354
    • Liang, P.H.1    Ko, T.P.2    Wang, A.H.3
  • 13
    • 0028858379 scopus 로고
    • The Claviceps purpurea gene encoding dimethylallyltryptophan synthase, the committed step for ergot alkaloid biosynthesis
    • Tsai HF, Wang H, Gebler JC, Poulter CD, Schardl CL (1995) The Claviceps purpurea gene encoding dimethylallyltryptophan synthase, the committed step for ergot alkaloid biosynthesis. Biochem Biophys Res Commun 216:119-125.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 119-125
    • Tsai, H.F.1    Wang, H.2    Gebler, J.C.3    Poulter, C.D.4    Schardl, C.L.5
  • 14
    • 19044365898 scopus 로고    scopus 로고
    • Overproduction, purification and characterization of FgaPT2, a dimethylallyltryptophan synthase from Aspergillus fumigatus
    • DOI 10.1099/mic.0.27759-0
    • Unsöld IA, Li SM (2005) Overproduction, purification and characterization of FgaPT2, a dimethylallyltryptophan synthase from Aspergillus fumigatus. Microbiology 151:1499-1505. (Pubitemid 40711797)
    • (2005) Microbiology , vol.151 , Issue.5 , pp. 1499-1505
    • Unsold, I.A.1    Li, S.-M.2
  • 15
    • 47049111183 scopus 로고    scopus 로고
    • Molecular analysis of a 4-dimethylallyltryptophan synthase from Malbranchea aurantiaca
    • Ding Y, Williams RM, Sherman DH (2008) Molecular analysis of a 4-dimethylallyltryptophan synthase from Malbranchea aurantiaca. J Biol Chem 283:16068-16076.
    • (2008) J Biol Chem , vol.283 , pp. 16068-16076
    • Ding, Y.1    Williams, R.M.2    Sherman, D.H.3
  • 16
    • 62349088498 scopus 로고    scopus 로고
    • Indole prenyltransferases from fungi: A new enzyme group with high potential for the production of prenylated indole derivatives
    • Steffan N, Grundmann A, Yin WB, Kremer A, Li S-M (2009) Indole prenyltransferases from fungi: A new enzyme group with high potential for the production of prenylated indole derivatives. Curr Med Chem 16:218-231.
    • (2009) Curr Med Chem , vol.16 , pp. 218-231
    • Steffan, N.1    Grundmann, A.2    Yin, W.B.3    Kremer, A.4    Li, S.-M.5
  • 17
    • 0000644470 scopus 로고    scopus 로고
    • Biosynthesis of prenylated alkaloids derived from tryptophan
    • Williams RM, Stocking EM, Sanz-Cervera JF (2000) Biosynthesis of prenylated alkaloids derived from tryptophan. Top Curr Chem 209:97-173.
    • (2000) Top Curr Chem , vol.209 , pp. 97-173
    • Williams, R.M.1    Stocking, E.M.2    Sanz-Cervera, J.F.3
  • 18
    • 0019877603 scopus 로고
    • Crystallization and partial characterization of dimethylallyl pyrophosphate: L-tryptophan dimethylallyltransferase from Claviceps sp. SD58
    • Cress WA, Chayet LT, Rilling HC (1981) Crystallization and partial characterization of dimethylallyl pyrophosphate: L-tryptophan dimethylallyltransferase from Claviceps sp. SD58. J Biol Chem 256:10917-10923.
    • (1981) J Biol Chem , vol.256 , pp. 10917-10923
    • Cress, W.A.1    Chayet, L.T.2    Rilling, H.C.3
  • 19
    • 20544457539 scopus 로고    scopus 로고
    • Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products
    • DOI 10.1038/nature03668
    • Kuzuyama T, Noel JP, Richard SB (2005) Structural basis for the promiscuous biosynthetic prenylation of aromatic natural products. Nature 435:983-987. (Pubitemid 40896327)
    • (2005) Nature , vol.435 , Issue.7044 , pp. 983-987
    • Kuzuyama, T.1    Noel, J.P.2    Richard, S.B.3
  • 20
    • 44449087804 scopus 로고    scopus 로고
    • The ABBA family of aromatic prenyltransferases: Broadening natural product diversity
    • Tello M, Kuzuyama T, Heide L, Noel JP, Richard SB (2008) The ABBA family of aromatic prenyltransferases: Broadening natural product diversity. Cell Mol Life Sci 65:1459-1463.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 1459-1463
    • Tello, M.1    Kuzuyama, T.2    Heide, L.3    Noel, J.P.4    Richard, S.B.5
  • 21
    • 65349101892 scopus 로고    scopus 로고
    • Prenyl transfer to aromatic substrates: Genetics and enzymology
    • Heide L (2009) Prenyl transfer to aromatic substrates: Genetics and enzymology. Curr Opin Chem Biol 13:171-179.
    • (2009) Curr Opin Chem Biol , vol.13 , pp. 171-179
    • Heide, L.1
  • 22
    • 56649103902 scopus 로고    scopus 로고
    • Searching protein structure databases with DaliLite v.3
    • DOI 10.1093/bioinformatics/btn507
    • Holm L, Kaariainen S, Rosenstrom P, Schenkel A (2008) Searching protein structure databases with DaliLite v.3. Bioinformatics 24:2780-2781. (Pubitemid 352722625)
    • (2008) Bioinformatics , vol.24 , Issue.23 , pp. 2780-2781
    • Holm, L.1    Kaariainen, S.2    Rosenstrom, P.3    Schenkel, A.4
  • 23
    • 0001620284 scopus 로고
    • Dimethylallyltryptophan synthase. An enzyme-catalyzed electrophilic aromatic substitution
    • Gebler JC, Woodside AB, Poulter CD (1992) Dimethylallyltryptophan synthase. An enzyme-catalyzed electrophilic aromatic substitution. J Am Chem Soc 114:7354-7360.
    • (1992) J Am Chem Soc , vol.114 , pp. 7354-7360
    • Gebler, J.C.1    Woodside, A.B.2    Poulter, C.D.3
  • 25
    • 34547450158 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of prenylated indole derivatives by using a 4-dimethylallyltryptophan synthase from Aspergillus fumigatus
    • DOI 10.1002/cbic.200700107
    • Steffan N, Unsöld IA, Li SM (2007) Chemoenzymatic synthesis of prenylated indole derivatives by using a 4-dimethylallyltryptophan synthase from Aspergillus fumigatus. ChemBioChem 8:1298-1307. (Pubitemid 47171997)
    • (2007) ChemBioChem , vol.8 , Issue.11 , pp. 1298-1307
    • Steffan, N.1    Unsold, I.A.2    Li, S.-M.3
  • 27
    • 58649098990 scopus 로고    scopus 로고
    • Acetylaszonalenin biosynthesis in Neosartorya fischeri: Identification of the biosynthetic gene cluster by genomic mining and functional proof of the genes by biochemical investigation
    • Yin WB, Grundmann A, Cheng J, Li SM (2009) Acetylaszonalenin biosynthesis in Neosartorya fischeri: Identification of the biosynthetic gene cluster by genomic mining and functional proof of the genes by biochemical investigation. J Biol Chem 284:100-109.
    • (2009) J Biol Chem , vol.284 , pp. 100-109
    • Yin, W.B.1    Grundmann, A.2    Cheng, J.3    Li, S.M.4
  • 28
    • 35448932356 scopus 로고    scopus 로고
    • A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: Overproduction, purification and biochemical characterization
    • DOI 10.1099/mic.0.2007/009019-0
    • Kremer A, Westrich L, Li SM (2007) A 7-dimethylallyltryptophan synthase from Aspergillus fumigatus: Overproduction, purification and biochemical characterization. Microbiology 153:3409-3416. (Pubitemid 47629546)
    • (2007) Microbiology , vol.153 , Issue.10 , pp. 3409-3416
    • Kremer, A.1    Westrich, L.2    Li, S.-M.3
  • 29
    • 50349085806 scopus 로고    scopus 로고
    • Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities
    • Kumano T, Richard SB, Noel JP, Nishiyama M, Kuzuyama T (2008) Chemoenzymatic syntheses of prenylated aromatic small molecules using Streptomyces prenyltransferases with relaxed substrate specificities. Bioorg Med Chem 16:8117-8126.
    • (2008) Bioorg Med Chem , vol.16 , pp. 8117-8126
    • Kumano, T.1    Richard, S.B.2    Noel, J.P.3    Nishiyama, M.4    Kuzuyama, T.5
  • 30
    • 50649097975 scopus 로고    scopus 로고
    • Biosynthesis and accumulation of ergoline alkaloids in a mutualistic association between Ipomoea asarifolia (Convolvulaceae) and a clavicipitalean fungus
    • DOI 10.1104/pp.108.116699
    • Markert A, et al. (2008) Biosynthesis and accumulation of ergoline alkaloids in a mutualistic association between Ipomoea asarifolia (Convolvulaceae) and a clavicipitalean fungus. Plant Physiol 147:296-305. (Pubitemid 352844368)
    • (2008) Plant Physiology , vol.147 , Issue.1 , pp. 296-305
    • Markert, A.1    Steffan, N.2    Ploss, K.3    Hellwig, S.4    Steiner, U.5    Drewke, C.6    Li, S.-M.7    Boland, W.8    Leistner, E.9
  • 32
    • 54349115932 scopus 로고    scopus 로고
    • Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi
    • Stec E, et al. (2008) Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi. ChemBioChem 9:2055-2058.
    • (2008) ChemBioChem , vol.9 , pp. 2055-2058
    • Stec, E.1
  • 33
    • 46849099981 scopus 로고    scopus 로고
    • Tryptophan Aminopeptidase Activity of Several Indole Prenyltransferases from Aspergillus fumigatus
    • DOI 10.1016/j.chembiol.2008.05.019, PII S1074552108002354
    • Kremer A, Li SM (2008) Tryptophan aminopeptidase activity of several indole prenyltransferases from Aspergillus fumigatus. Chem Biol 15:729-738. (Pubitemid 351957910)
    • (2008) Chemistry and Biology , vol.15 , Issue.7 , pp. 729-738
    • Kremer, A.1    Li, S.-M.2
  • 35
    • 34250208085 scopus 로고    scopus 로고
    • A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates
    • DOI 10.1016/j.febslet.2007.05.031, PII S0014579307005595
    • Haagen Y, et al. (2007)Asoluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates. FEBS Lett 581:2889-2893. (Pubitemid 46899029)
    • (2007) FEBS Letters , vol.581 , Issue.16 , pp. 2889-2893
    • Haagen, Y.1    Unsold, I.2    Westrich, L.3    Gust, B.4    Richard, S.B.5    Noel, J.P.6    Heide, L.7
  • 36
    • 67649816707 scopus 로고    scopus 로고
    • Aromatic prenylation in phenazine biosynthesis: Dihydrophenazine-1- carboxylate dimethylallyltransferase from Streptomyces anulatus
    • Saleh O, Gust B, Boll B, Fiedler HP, Heide L (2009) Aromatic prenylation in phenazine biosynthesis: Dihydrophenazine-1-carboxylate dimethylallyltransferase from Streptomyces anulatus. J Biol Chem 284:14439-14447.
    • (2009) J Biol Chem , vol.284 , pp. 14439-14447
    • Saleh, O.1    Gust, B.2    Boll, B.3    Fiedler, H.P.4    Heide, L.5
  • 37
    • 20144382151 scopus 로고    scopus 로고
    • Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: Roles of the metal ion and conserved residues in catalysis
    • Guo RT, et al. (2005) Crystal structures of undecaprenyl pyrophosphate synthase in complex with magnesium, isopentenyl pyrophosphate, and farnesyl thiopyrophosphate: Roles of the metal ion and conserved residues in catalysis. J Biol Chem 280:20762-20774.
    • (2005) J Biol Chem , vol.280 , pp. 20762-20774
    • Guo, R.T.1
  • 38
    • 44049105743 scopus 로고    scopus 로고
    • A structural model of the membrane-bound aromatic prenyltransferase UbiA from E. coli
    • Bräuer L, Brandt W, Schulze D, Zakharova S, Wessjohann L (2008) A structural model of the membrane-bound aromatic prenyltransferase UbiA from E. coli. ChemBioChem 9:982-992.
    • (2008) ChemBioChem , vol.9 , pp. 982-992
    • Bräuer, L.1    Brandt, W.2    Schulze, D.3    Zakharova, S.4    Wessjohann, L.5
  • 39
    • 67650898865 scopus 로고    scopus 로고
    • Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of phydroxybenzoic acid
    • Ohara K, Muroya A, Fukushima N, Yazaki K (2009) Functional characterization of LePGT1, a membrane-bound prenyltransferase involved in the geranylation of phydroxybenzoic acid. Biochem J 421:231-241.
    • (2009) Biochem J , vol.421 , pp. 231-241
    • Ohara, K.1    Muroya, A.2    Fukushima, N.3    Yazaki, K.4


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