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Volumn 34, Issue C, 2000, Pages 285-315

Chapter Nine Evolution of acyltransferase genes: Origin and diversification fo the BAHD superfamily of acyltransferases involved in secondary metabolism

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EID: 77957043732     PISSN: 00799920     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S0079-9920(00)80010-6     Document Type: Chapter
Times cited : (237)

References (86)
  • 1
    • 0032575862 scopus 로고    scopus 로고
    • Gallotannin biosynthesis-purification of β-glucogallin-1,2,3,4,6-pentagalloyl-β-D-glucose galloyltransferase from Sumac leaves
    • Niemetz R., and Gross G.G. Gallotannin biosynthesis-purification of β-glucogallin-1,2,3,4,6-pentagalloyl-β-D-glucose galloyltransferase from Sumac leaves. Phytochemistry 49 (1998) 327-332
    • (1998) Phytochemistry , vol.49 , pp. 327-332
    • Niemetz, R.1    Gross, G.G.2
  • 2
    • 0033212918 scopus 로고    scopus 로고
    • Glucose polyester biosynthesis. Purification and characterization of a glucose acyltransferase
    • Li A.X., Eannetta N., Changas G.S., and Steffens J. Glucose polyester biosynthesis. Purification and characterization of a glucose acyltransferase. Plant Physiol. 121 (1999) 453-460
    • (1999) Plant Physiol. , vol.121 , pp. 453-460
    • Li, A.X.1    Eannetta, N.2    Changas, G.S.3    Steffens, J.4
  • 3
    • 0025697934 scopus 로고
    • Partial purification and characterization of indol-3-ylacetylglucose: myo-inositol indol-3-ylacetyltransferase (indoleacetic acid-inositol synthase)
    • Kesy J.M., and Bandurski R.S. Partial purification and characterization of indol-3-ylacetylglucose: myo-inositol indol-3-ylacetyltransferase (indoleacetic acid-inositol synthase). Plant Physiol. 94 (1990) 1598-1604
    • (1990) Plant Physiol. , vol.94 , pp. 1598-1604
    • Kesy, J.M.1    Bandurski, R.S.2
  • 4
    • 0344973933 scopus 로고
    • Purification and properties of 1-(hydroxycinnamoyl)-glucose: 1-(hydroxycinnamoyl)-glucose hydroxycinnamoyl-transferase from radish seedlings
    • Dahlbender B., and Strack D. Purification and properties of 1-(hydroxycinnamoyl)-glucose: 1-(hydroxycinnamoyl)-glucose hydroxycinnamoyl-transferase from radish seedlings. Phytochemistry 25 (1986) 1043-1046
    • (1986) Phytochemistry , vol.25 , pp. 1043-1046
    • Dahlbender, B.1    Strack, D.2
  • 5
    • 0038316666 scopus 로고
    • II. Secondary plant substances. Special topics in phenylpropanoid metabolism
    • Schütte H.R. II. Secondary plant substances. Special topics in phenylpropanoid metabolism. Prog. Bot. 53 (1992) 78-98
    • (1992) Prog. Bot. , vol.53 , pp. 78-98
    • Schütte, H.R.1
  • 6
    • 0344542979 scopus 로고
    • Purification and characterization of chlorogenic acid: chlorogenate caffeoyl transferase in sweet potato roots
    • Villegas R.J.A., Shimokawa T., Okuyama H., and Kojima M. Purification and characterization of chlorogenic acid: chlorogenate caffeoyl transferase in sweet potato roots. Phytochemistry 26 (1987) 1577-1581
    • (1987) Phytochemistry , vol.26 , pp. 1577-1581
    • Villegas, R.J.A.1    Shimokawa, T.2    Okuyama, H.3    Kojima, M.4
  • 7
    • 0346856289 scopus 로고
    • Properties and activity changes of chlorogenic acid: glucaric acid caffeoyltransferase from tomato (Lycopersicon esculentum)
    • Strack D., and Gross W. Properties and activity changes of chlorogenic acid: glucaric acid caffeoyltransferase from tomato (Lycopersicon esculentum). Plant Physiol. 92 (1990) 41-47
    • (1990) Plant Physiol. , vol.92 , pp. 41-47
    • Strack, D.1    Gross, W.2
  • 8
    • 0028273219 scopus 로고
    • Choline acetyltransferase: celebrating its fiftieth year
    • Wu D., and Hersh L.B. Choline acetyltransferase: celebrating its fiftieth year. J. Neurochem. 62 (1994) 1653-1663
    • (1994) J. Neurochem. , vol.62 , pp. 1653-1663
    • Wu, D.1    Hersh, L.B.2
  • 9
    • 0030859046 scopus 로고    scopus 로고
    • Molecular aspects of intracellular sterol esterification: The acyl coenzyme A: cholesterol acyltransferase reaction
    • Sturley S.L. Molecular aspects of intracellular sterol esterification: The acyl coenzyme A: cholesterol acyltransferase reaction. Curr. Opin. Lipidol. 8 (1997) 167-173
    • (1997) Curr. Opin. Lipidol. , vol.8 , pp. 167-173
    • Sturley, S.L.1
  • 11
    • 0032235209 scopus 로고    scopus 로고
    • Polymorphisms of N-acetyltransferases, glutathione S-transferases, microsomal epoxide hydrolase and sulfotransferases: influence on cancer susceptibility
    • Hengstler J.G., Arand M., Herrero M.E., and Oesch F. Polymorphisms of N-acetyltransferases, glutathione S-transferases, microsomal epoxide hydrolase and sulfotransferases: influence on cancer susceptibility. Rec. Res. Cancer Res. 154 (1998) 47-85
    • (1998) Rec. Res. Cancer Res. , vol.154 , pp. 47-85
    • Hengstler, J.G.1    Arand, M.2    Herrero, M.E.3    Oesch, F.4
  • 12
    • 0032142918 scopus 로고    scopus 로고
    • Roles of histone acetyltransferases and deacetylases in gene regulation
    • Kuo M.H., and Allis C.D. Roles of histone acetyltransferases and deacetylases in gene regulation. Bioessays 20 (1998) 615-626
    • (1998) Bioessays , vol.20 , pp. 615-626
    • Kuo, M.H.1    Allis, C.D.2
  • 13
    • 23444440823 scopus 로고
    • Inactivation of antibiotics and the dissemination of resistance genes
    • Davies J. Inactivation of antibiotics and the dissemination of resistance genes. Science 264 (1994) 375-382
    • (1994) Science , vol.264 , pp. 375-382
    • Davies, J.1
  • 14
    • 0031028172 scopus 로고    scopus 로고
    • O-Acetyltransferases for chloramphenicol and other natural products
    • Murray I.A., and Shaw W.V. O-Acetyltransferases for chloramphenicol and other natural products. Antimicrob. Agents Chemother 41 (1997) 1-6
    • (1997) Antimicrob. Agents Chemother , vol.41 , pp. 1-6
    • Murray, I.A.1    Shaw, W.V.2
  • 15
    • 0028237942 scopus 로고
    • A novel O-tigloyltransferase for alkaloid biosynthesis in plants. Purification, characterization, and distribution in Lupinus plants
    • Suzuki H., Murakoshi I., and Saito K. A novel O-tigloyltransferase for alkaloid biosynthesis in plants. Purification, characterization, and distribution in Lupinus plants. J. Biol. Chem. 269 (1994) 15853-15860
    • (1994) J. Biol. Chem. , vol.269 , pp. 15853-15860
    • Suzuki, H.1    Murakoshi, I.2    Saito, K.3
  • 16
    • 0029559296 scopus 로고
    • Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis
    • Lenz R., and Zenk M.H. Acetyl coenzyme A: salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis. J. Biol. Chem. 270 (1995) 31091-31096
    • (1995) J. Biol. Chem. , vol.270 , pp. 31091-31096
    • Lenz, R.1    Zenk, M.H.2
  • 17
    • 0011623122 scopus 로고
    • Acetyl coenzyme A: deacetylvindoline O-acetyltransferase, a novel enzyme from Catharanthus
    • De Luca V., Balsevich J., and Kurz W.G.W. Acetyl coenzyme A: deacetylvindoline O-acetyltransferase, a novel enzyme from Catharanthus. Plant Physiol. 121 (1985) 417-428
    • (1985) Plant Physiol. , vol.121 , pp. 417-428
    • De Luca, V.1    Balsevich, J.2    Kurz, W.G.W.3
  • 18
    • 0029138109 scopus 로고
    • Tigloyl-Coa: pseudotropine acyl transferase-an enzyme of tropane alkaloid biosynthesis
    • Rabot S., Peerless A.C.J., and Robins R.J. Tigloyl-Coa: pseudotropine acyl transferase-an enzyme of tropane alkaloid biosynthesis. Phytochemistry 39 (1995) 315-322
    • (1995) Phytochemistry , vol.39 , pp. 315-322
    • Rabot, S.1    Peerless, A.C.J.2    Robins, R.J.3
  • 19
    • 0031444524 scopus 로고    scopus 로고
    • Characterization and heterologous expression of hydroxycinnamoyl/benzoyl-CoA: anthranilate N-hydroxycinnamoyl/benzoyltransferase from elicited cell cultures of carnation, Dianthus caryophyllus L.
    • Yang Q., Reinhard K., Schiltz E., and Matern U. Characterization and heterologous expression of hydroxycinnamoyl/benzoyl-CoA: anthranilate N-hydroxycinnamoyl/benzoyltransferase from elicited cell cultures of carnation, Dianthus caryophyllus L. Plant Mol. Biol. 35 (1997) 777-789
    • (1997) Plant Mol. Biol. , vol.35 , pp. 777-789
    • Yang, Q.1    Reinhard, K.2    Schiltz, E.3    Matern, U.4
  • 21
    • 0001248666 scopus 로고
    • Metabolism of monoterpenes. Acetylation of (-)-menthol by a soluble enzyme preparation from peppermint (Mentha piperita) leaves
    • Croteau R., and Hooper C.L. Metabolism of monoterpenes. Acetylation of (-)-menthol by a soluble enzyme preparation from peppermint (Mentha piperita) leaves. Plant Physiol. 61 (1978) 737-742
    • (1978) Plant Physiol. , vol.61 , pp. 737-742
    • Croteau, R.1    Hooper, C.L.2
  • 22
    • 0033560575 scopus 로고    scopus 로고
    • Partial purification and characterization of acetyl coenzyme A: taxa-4(20), 11(12)-dien-5 alpha-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis
    • Walker K., Ketchum R.E.B., Hezari M., Gatfield D., Goleniowski M., Barthol A., and Croteau R. Partial purification and characterization of acetyl coenzyme A: taxa-4(20), 11(12)-dien-5 alpha-ol O-acetyl transferase that catalyzes the first acylation step of taxol biosynthesis. Arch. Biochem. Biophys. 364 (1999) 273-279
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 273-279
    • Walker, K.1    Ketchum, R.E.B.2    Hezari, M.3    Gatfield, D.4    Goleniowski, M.5    Barthol, A.6    Croteau, R.7
  • 23
    • 0031835383 scopus 로고    scopus 로고
    • Acetyl-CoA-benzylalcohol acetyltransferase-an enzyme involved in floral scent production in Clarkia breweri
    • Dudareva N., Dauria J.C., Nam K.H., Raguso R.A., and Pichersky E. Acetyl-CoA-benzylalcohol acetyltransferase-an enzyme involved in floral scent production in Clarkia breweri. Plant J. 14 (1998) 297-304
    • (1998) Plant J. , vol.14 , pp. 297-304
    • Dudareva, N.1    Dauria, J.C.2    Nam, K.H.3    Raguso, R.A.4    Pichersky, E.5
  • 24
    • 0032534050 scopus 로고    scopus 로고
    • Two crystal structures of N-acetyltransferases reveal a new fold for coA-dependent enzymes
    • Modis Y., and Wierenga R. Two crystal structures of N-acetyltransferases reveal a new fold for coA-dependent enzymes. Structure 6 (1998) 1345-1350
    • (1998) Structure , vol.6 , pp. 1345-1350
    • Modis, Y.1    Wierenga, R.2
  • 25
    • 0030444352 scopus 로고    scopus 로고
    • The diverse world of coenzyme A binding proteins
    • Engel C., and Wierenga R. The diverse world of coenzyme A binding proteins. Curr. Opin. Struct. Biol. 6 (1996) 790-797
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 790-797
    • Engel, C.1    Wierenga, R.2
  • 26
    • 0012287659 scopus 로고
    • Purification and properties of hydroxycinnamoyl CoA quinate hydroxycinnamoyl transferase from potatoes
    • Rhodes M.J.C., Wooltorton L.S.C., and Lourenço E.J. Purification and properties of hydroxycinnamoyl CoA quinate hydroxycinnamoyl transferase from potatoes. Phystochemistry 18 (1979)
    • (1979) Phystochemistry , vol.18
    • Rhodes, M.J.C.1    Wooltorton, L.S.C.2    Lourenço, E.J.3
  • 27
    • 0001613641 scopus 로고    scopus 로고
    • Purification of hydroxycinnamoyltransferase-CoA-tyramine hydroxycinnamoyltransferase from cell-suspension cultures of Solanum tuberosum L cv Datura
    • Hohlfeld H., Scheel D., and Strack D. Purification of hydroxycinnamoyltransferase-CoA-tyramine hydroxycinnamoyltransferase from cell-suspension cultures of Solanum tuberosum L cv Datura. Planta 199 (1996) 166-168
    • (1996) Planta , vol.199 , pp. 166-168
    • Hohlfeld, H.1    Scheel, D.2    Strack, D.3
  • 28
    • 0030740715 scopus 로고    scopus 로고
    • Purification, characterization and partial amino acid sequencing of hydroxycinnamoyl-CoA-tyramine N-(hydroxycinnamoyl)transferase from tobacco cell-suspension cultures
    • Negrel J., and Javelle F. Purification, characterization and partial amino acid sequencing of hydroxycinnamoyl-CoA-tyramine N-(hydroxycinnamoyl)transferase from tobacco cell-suspension cultures. Eur. J. Biochem. 247 (1997) 1127-1135
    • (1997) Eur. J. Biochem. , vol.247 , pp. 1127-1135
    • Negrel, J.1    Javelle, F.2
  • 29
    • 0032125745 scopus 로고    scopus 로고
    • Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants-structural and kinetic properties of the free and bound enzymes
    • Droux M., Ruffet M.L., Douce R., and Job D. Interactions between serine acetyltransferase and O-acetylserine (thiol) lyase in higher plants-structural and kinetic properties of the free and bound enzymes. Eur. J. Biochem. 255 (1998) 235-245
    • (1998) Eur. J. Biochem. , vol.255 , pp. 235-245
    • Droux, M.1    Ruffet, M.L.2    Douce, R.3    Job, D.4
  • 30
    • 0028858945 scopus 로고
    • Purification and characterization of 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from tomato fruit
    • Martin M.N., and Saftner R.A. Purification and characterization of 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from tomato fruit. Plant Physiol. 108 (1995) 1241-1249
    • (1995) Plant Physiol. , vol.108 , pp. 1241-1249
    • Martin, M.N.1    Saftner, R.A.2
  • 31
    • 1842411894 scopus 로고    scopus 로고
    • Immunopurification and characterization of a 40-kD 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from Mung bean seedling hypocotyls
    • Chick W.S.H., and Leung P.C. Immunopurification and characterization of a 40-kD 1-aminocyclopropane-1-carboxylic acid N-malonyltransferase from Mung bean seedling hypocotyls. Plant Physiol. 113 (1997) 119-126
    • (1997) Plant Physiol. , vol.113 , pp. 119-126
    • Chick, W.S.H.1    Leung, P.C.2
  • 32
    • 0033105111 scopus 로고    scopus 로고
    • Purification and characterization of acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis
    • Menhard B., and Zenk M.H. Purification and characterization of acetyl coenzyme A: 10-hydroxytaxane O-acetyltransferase from cell suspension cultures of Taxus chinensis. Phytochemistry 50 (1999) 763-774
    • (1999) Phytochemistry , vol.50 , pp. 763-774
    • Menhard, B.1    Zenk, M.H.2
  • 33
    • 0032104554 scopus 로고    scopus 로고
    • The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer
    • ST-Pierre B., Laflamme P., Alarco A.M., and De luca V. The terminal O-acetyltransferase involved in vindoline biosynthesis defines a new class of proteins responsible for coenzyme A-dependent acyl transfer. Plant J. 14 (1998) 703-713
    • (1998) Plant J. , vol.14 , pp. 703-713
    • ST-Pierre, B.1    Laflamme, P.2    Alarco, A.M.3    De luca, V.4
  • 34
    • 0000095437 scopus 로고
    • Purification and some properties of alcohol acetyltransferase from banana fruit
    • Harada M., Ueda Y., and Iwata T. Purification and some properties of alcohol acetyltransferase from banana fruit. Plant Cell Physiol. 26 (1985) 1067-1074
    • (1985) Plant Cell Physiol. , vol.26 , pp. 1067-1074
    • Harada, M.1    Ueda, Y.2    Iwata, T.3
  • 35
    • 0029760896 scopus 로고    scopus 로고
    • Pyrification and characterization of hydroxycinnamoyl-Coenzyme A: ω-hydroxypalmitic acid O-hydroxycinnamoyltranferase from tobacco (Nicotiana tabacum L.) cell-suspension cultures
    • Lotfy S., Javelle F., and Negrel J. Pyrification and characterization of hydroxycinnamoyl-Coenzyme A: ω-hydroxypalmitic acid O-hydroxycinnamoyltranferase from tobacco (Nicotiana tabacum L.) cell-suspension cultures. Planta 199 (1996) 475-480
    • (1996) Planta , vol.199 , pp. 475-480
    • Lotfy, S.1    Javelle, F.2    Negrel, J.3
  • 36
    • 0029820448 scopus 로고    scopus 로고
    • Hydroxycinnamoyltransferases involved in the accumulation of caffeic acid esters in gametophytes and sporophytes of Equisetum arvense
    • Hohlfeld M., Veit M., and Strack D. Hydroxycinnamoyltransferases involved in the accumulation of caffeic acid esters in gametophytes and sporophytes of Equisetum arvense. Plant Physiol. 111 (1996) 1153-1159
    • (1996) Plant Physiol. , vol.111 , pp. 1153-1159
    • Hohlfeld, M.1    Veit, M.2    Strack, D.3
  • 37
    • 0032560951 scopus 로고    scopus 로고
    • Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens
    • Fujiwara H., Tanaka Y., Fukui Y., Ashikari T., Yamaguchi M., and Kusumi T. Purification and characterization of anthocyanin 3-aromatic acyltransferase from Perilla frutescens. Plant Sci. 137 (1998) 87-94
    • (1998) Plant Sci. , vol.137 , pp. 87-94
    • Fujiwara, H.1    Tanaka, Y.2    Fukui, Y.3    Ashikari, T.4    Yamaguchi, M.5    Kusumi, T.6
  • 38
    • 0030862686 scopus 로고    scopus 로고
    • Anthocyanin 5-aromatic acyltransferase from Gentiana triflora-Purification, characterization and Its role in anthocyanin biosynthesis
    • Fujiwara H., Tanaka Y., Fukui Y., Nakao M., Ashikari T., and Kusumi T. Anthocyanin 5-aromatic acyltransferase from Gentiana triflora-Purification, characterization and Its role in anthocyanin biosynthesis. Eur. J. Biochem. 249 (1997) 45-51
    • (1997) Eur. J. Biochem. , vol.249 , pp. 45-51
    • Fujiwara, H.1    Tanaka, Y.2    Fukui, Y.3    Nakao, M.4    Ashikari, T.5    Kusumi, T.6
  • 39
    • 0343899497 scopus 로고
    • Purification and characterization of 1-aminocyclopropane-1-carboxylate N-malonyltranferase from etiolated mung bean hypocotyls
    • Guo L., Arteca R., and Philips A.Y.L. Purification and characterization of 1-aminocyclopropane-1-carboxylate N-malonyltranferase from etiolated mung bean hypocotyls. Plant Physiol. 100 (1992) 2041-2045
    • (1992) Plant Physiol. , vol.100 , pp. 2041-2045
    • Guo, L.1    Arteca, R.2    Philips, A.Y.L.3
  • 41
    • 0020842093 scopus 로고
    • Further characterization and regulation of malonyl-coenzyme A flavonoid glucoside malonyltransferases from parsley cell suspension cultures (Petroselinum hortense)
    • Matern U., Feser C., and Hammer D. Further characterization and regulation of malonyl-coenzyme A flavonoid glucoside malonyltransferases from parsley cell suspension cultures (Petroselinum hortense). Arch. Biochem. Biophys. 226 (1983) 206-217
    • (1983) Arch. Biochem. Biophys. , vol.226 , pp. 206-217
    • Matern, U.1    Feser, C.2    Hammer, D.3
  • 42
    • 0025333983 scopus 로고
    • Purification and characterization of acetylcoenzyme A: deacetylvindoline 4-O-acetyltransferase from Catharanthus roseus
    • Power R., Kurz W.G.W., and De Luca V. Purification and characterization of acetylcoenzyme A: deacetylvindoline 4-O-acetyltransferase from Catharanthus roseus. Arch. Biochem. Biophys. 279 (1990) 370-376
    • (1990) Arch. Biochem. Biophys. , vol.279 , pp. 370-376
    • Power, R.1    Kurz, W.G.W.2    De Luca, V.3
  • 43
    • 0028877640 scopus 로고
    • Inactivation and kinetic characterization of hydroxycinnamoyl-Coa-hydroaromatic acid O-hydroxycinnamoyltransferases from Cichroium endivia and Phoenix dactylfiera
    • Lotfy S. Inactivation and kinetic characterization of hydroxycinnamoyl-Coa-hydroaromatic acid O-hydroxycinnamoyltransferases from Cichroium endivia and Phoenix dactylfiera. Plant Physiol. Biochem. 33 (1995) 423-431
    • (1995) Plant Physiol. Biochem. , vol.33 , pp. 423-431
    • Lotfy, S.1
  • 44
    • 12644251376 scopus 로고
    • Enzymatic synthesis of quinolizidine alkaloid esters: a tigloyl-CoA: 13-hydroxylupanine O-tigloltransferase from Lupinus albus L
    • Wink M., and Hartmann T. Enzymatic synthesis of quinolizidine alkaloid esters: a tigloyl-CoA: 13-hydroxylupanine O-tigloltransferase from Lupinus albus L. Planta 156 (1982) 560-565
    • (1982) Planta , vol.156 , pp. 560-565
    • Wink, M.1    Hartmann, T.2
  • 45
    • 0001524443 scopus 로고
    • Late enzymes in vindoline biosynthesis. Acetyl-CoA: 17-O-acetyltransferase
    • Fahn W., Grundlach H., Deur-Neumann B., and Stockigt J. Late enzymes in vindoline biosynthesis. Acetyl-CoA: 17-O-acetyltransferase. Plant Cell Rep. 4 (1985) 333-336
    • (1985) Plant Cell Rep. , vol.4 , pp. 333-336
    • Fahn, W.1    Grundlach, H.2    Deur-Neumann, B.3    Stockigt, J.4
  • 47
    • 0031915374 scopus 로고    scopus 로고
    • Trichothecene 3-O-acetyltransferase protects both the producing organism and transformed yeast from related mycotoxins-cloning and characterization of Tri101
    • Kimura M., Kaneko I., Komiyama M., Takatsuki A., Koshino H., Yoneyama K., and Yamaguchi I. Trichothecene 3-O-acetyltransferase protects both the producing organism and transformed yeast from related mycotoxins-cloning and characterization of Tri101. J. Biol. Chem. 273 (1998) 1654-1661
    • (1998) J. Biol. Chem. , vol.273 , pp. 1654-1661
    • Kimura, M.1    Kaneko, I.2    Komiyama, M.3    Takatsuki, A.4    Koshino, H.5    Yoneyama, K.6    Yamaguchi, I.7
  • 48
    • 0030061746 scopus 로고    scopus 로고
    • Isolation and characterization of Tri3, a gene encoding 15-O-acetyltransferase from Fusarium sporotrichioides
    • Mccormick S.P., Hohn T.M., and Desjardins A.E. Isolation and characterization of Tri3, a gene encoding 15-O-acetyltransferase from Fusarium sporotrichioides. Appl. Environ. Microbiol. 62 (1996) 353-359
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 353-359
    • Mccormick, S.P.1    Hohn, T.M.2    Desjardins, A.E.3
  • 49
    • 0028015972 scopus 로고
    • Molecular cloning, sequence analysis, and expression of the yeast alcohol acetyltransferase gene
    • Fujii T., Nagasawa N., Iwamatsu A., Bogaki T., Tamai W., and Hamachi M. Molecular cloning, sequence analysis, and expression of the yeast alcohol acetyltransferase gene. Appl. Environ. Microbiol 60 (1994) 2786-2792
    • (1994) Appl. Environ. Microbiol , vol.60 , pp. 2786-2792
    • Fujii, T.1    Nagasawa, N.2    Iwamatsu, A.3    Bogaki, T.4    Tamai, W.5    Hamachi, M.6
  • 50
    • 0030087885 scopus 로고    scopus 로고
    • Molecular cloning and characterization of the CER2 gene of Arabidopsis thaliana
    • Negruk V., Yang P., Subramanian M., Mcnevin J.P., and Lemieux B. Molecular cloning and characterization of the CER2 gene of Arabidopsis thaliana. Plant J. 9 (1996) 137-145
    • (1996) Plant J. , vol.9 , pp. 137-145
    • Negruk, V.1    Yang, P.2    Subramanian, M.3    Mcnevin, J.P.4    Lemieux, B.5
  • 52
    • 0030221855 scopus 로고    scopus 로고
    • Cloning and characterization of CER2, an Arabidopsis gene that affects cuticular wax accumulation
    • Xia Y., Nikolau B.J., and Schnable P.S. Cloning and characterization of CER2, an Arabidopsis gene that affects cuticular wax accumulation. Plant Cell 8 (1996) 1291-1304
    • (1996) Plant Cell , vol.8 , pp. 1291-1304
    • Xia, Y.1    Nikolau, B.J.2    Schnable, P.S.3
  • 53
    • 0029257170 scopus 로고
    • Directed tagging of the Arabidopsis FATTY ACID ELONGATIONI (FAE1) gene with the maize transposon activator
    • James D.W.J., Lim E., Keller J., Plooy I., Ralston E., and Dooner H.K. Directed tagging of the Arabidopsis FATTY ACID ELONGATIONI (FAE1) gene with the maize transposon activator. Plant Cell 7 (1995) 309-319
    • (1995) Plant Cell , vol.7 , pp. 309-319
    • James, D.W.J.1    Lim, E.2    Keller, J.3    Plooy, I.4    Ralston, E.5    Dooner, H.K.6
  • 54
    • 0025756456 scopus 로고
    • Acyl-CoA elongase from a higher plant (Lunaria annua): Metabolic intermediates of very-long-chain acyl-CoA products and substrate specificity
    • Fehling E., and Mukherjee K.D. Acyl-CoA elongase from a higher plant (Lunaria annua): Metabolic intermediates of very-long-chain acyl-CoA products and substrate specificity. Biochim. Biophys. Acta 1082 (1991) 239-246
    • (1991) Biochim. Biophys. Acta , vol.1082 , pp. 239-246
    • Fehling, E.1    Mukherjee, K.D.2
  • 55
    • 0026645148 scopus 로고
    • Solubilization and partial purification of constituents of acyl-CoA elongase from Lunaria annua
    • Fehling E., Lessire R., Cassagne C., and Mukherjee K.D. Solubilization and partial purification of constituents of acyl-CoA elongase from Lunaria annua. Biochim. Biophys. Acta 1126 (1992) 88-94
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 88-94
    • Fehling, E.1    Lessire, R.2    Cassagne, C.3    Mukherjee, K.D.4
  • 56
    • 0030997975 scopus 로고    scopus 로고
    • Characterization of two cDNA clones for mRNAs expressed during ripening of melon (Cucumis melo L.) fruits
    • Aggelis A., John I., Karvouni Z., and Grierson D. Characterization of two cDNA clones for mRNAs expressed during ripening of melon (Cucumis melo L.) fruits. Plant Mol. Biol. 33 (1997) 313-322
    • (1997) Plant Mol. Biol. , vol.33 , pp. 313-322
    • Aggelis, A.1    John, I.2    Karvouni, Z.3    Grierson, D.4
  • 57
    • 0001638937 scopus 로고
    • Isolation and characterization of cDNA clones for tomato polygalacturonase and other ripening-relatd proteins
    • Slater A., Maunders M.J., Edwads K., Schuch W., and Grierson D. Isolation and characterization of cDNA clones for tomato polygalacturonase and other ripening-relatd proteins. Plant Mol. Biol. 5 (1985) 137-147
    • (1985) Plant Mol. Biol. , vol.5 , pp. 137-147
    • Slater, A.1    Maunders, M.J.2    Edwads, K.3    Schuch, W.4    Grierson, D.5
  • 59
    • 0025977185 scopus 로고
    • Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme
    • Russell G.C., and Guest J.R. Sequence similarities within the family of dihydrolipoamide acyltransferases and discovery of a previously unidentified fungal enzyme. Biochim. Biophys. Acta 1076 (1991) 225-232
    • (1991) Biochim. Biophys. Acta , vol.1076 , pp. 225-232
    • Russell, G.C.1    Guest, J.R.2
  • 60
    • 0028304469 scopus 로고
    • Catalytically important domains of rat carnitine palmitoyltransferase II as determined by site-directed mutagenesis and chemical modification. Evidence for a critical histidine residue
    • Brown N.F., Anderson R.C., Caplan S.L., Foster D.W., and Mcgarry J.D. Catalytically important domains of rat carnitine palmitoyltransferase II as determined by site-directed mutagenesis and chemical modification. Evidence for a critical histidine residue. J. Biol. Chem. 269 (1994) 19157-19162
    • (1994) J. Biol. Chem. , vol.269 , pp. 19157-19162
    • Brown, N.F.1    Anderson, R.C.2    Caplan, S.L.3    Foster, D.W.4    Mcgarry, J.D.5
  • 61
    • 0027156457 scopus 로고
    • Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis
    • Carbini L.A., and Hersh L.B. Functional analysis of conserved histidines in choline acetyltransferase by site-directed mutagenesis. J. Neurochem. 61 (1993) 247-253
    • (1993) J. Neurochem. , vol.61 , pp. 247-253
    • Carbini, L.A.1    Hersh, L.B.2
  • 62
    • 0028807689 scopus 로고
    • Multienzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation
    • De Crécy-Lagard V., Marlière P., and Saurin W. Multienzymatic non ribosomal peptide biosynthesis: identification of the functional domains catalysing peptide elongation and epimerisation. C. R. Acad. Sci. III 318 (1995) 927-936
    • (1995) C. R. Acad. Sci. III , vol.318 , pp. 927-936
    • De Crécy-Lagard, V.1    Marlière, P.2    Saurin, W.3
  • 63
    • 0033548080 scopus 로고    scopus 로고
    • Cloning and expression of a potato cDNA encoding hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase
    • Schmidt A., Grimm R., Schmidt J., Scheel D., Strack D., and Rosahl S. Cloning and expression of a potato cDNA encoding hydroxycinnamoyl-CoA:tyramine N-(hydroxycinnamoyl)transferase. J. Biol. Chem. 274 (1999) 4273-4280
    • (1999) J. Biol. Chem. , vol.274 , pp. 4273-4280
    • Schmidt, A.1    Grimm, R.2    Schmidt, J.3    Scheel, D.4    Strack, D.5    Rosahl, S.6
  • 64
    • 0033083406 scopus 로고    scopus 로고
    • Molecular characterization of the Acremonium chrysogenum cefGgene product: the native deacetylcephalosporin C acetyltransferase is not processed into subunits
    • Velasco J., Guttierrez S., Campoy S., and Martin J.F. Molecular characterization of the Acremonium chrysogenum cefGgene product: the native deacetylcephalosporin C acetyltransferase is not processed into subunits. Biochem. J. 337 (1999) 379-385
    • (1999) Biochem. J. , vol.337 , pp. 379-385
    • Velasco, J.1    Guttierrez, S.2    Campoy, S.3    Martin, J.F.4
  • 65
    • 0032575648 scopus 로고    scopus 로고
    • Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain
    • Stachelhaus T., Mootz H.D., Bergendahl V., and Marahiel M.A. Peptide bond formation in nonribosomal peptide biosynthesis. Catalytic role of the condensation domain. J. Biol. Chem. 273 (1998) 22773-22781
    • (1998) J. Biol. Chem. , vol.273 , pp. 22773-22781
    • Stachelhaus, T.1    Mootz, H.D.2    Bergendahl, V.3    Marahiel, M.A.4
  • 67
    • 0032563138 scopus 로고    scopus 로고
    • Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
    • Knapp J.E., Mitchell D.T., Yazdi M.A., Ernst S.R., Reed L.J., and Hackert M.L. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280 (1998) 655-668
    • (1998) J. Mol. Biol. , vol.280 , pp. 655-668
    • Knapp, J.E.1    Mitchell, D.T.2    Yazdi, M.A.3    Ernst, S.R.4    Reed, L.J.5    Hackert, M.L.6
  • 69
    • 0025335792 scopus 로고
    • Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75resolution
    • Leslie A.G. Refined crystal structure of type III chloramphenicol acetyltransferase at 1.75resolution. J. Mol. Biol. 213 (1990) 167-186
    • (1990) J. Mol. Biol. , vol.213 , pp. 167-186
    • Leslie, A.G.1
  • 70
    • 0028300363 scopus 로고
    • Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate
    • Lewendon A., Murray I.A., Shaw W.V., Gibbs M.R., and Leslie A.G. Replacement of catalytic histidine-195 of chloramphenicol acetyltransferase: evidence for a general base role for glutamate. Biochemistry 33 (1994) 1944-1950
    • (1994) Biochemistry , vol.33 , pp. 1944-1950
    • Lewendon, A.1    Murray, I.A.2    Shaw, W.V.3    Gibbs, M.R.4    Leslie, A.G.5
  • 71
    • 0025280447 scopus 로고
    • Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue
    • Russell G.C., and Guest J.R. Overexpression of restructured pyruvate dehydrogenase complexes and site-directed mutagenesis of a potential active-site histidine residue. Biochem. J. 269 (1990) 443-450
    • (1990) Biochem. J. , vol.269 , pp. 443-450
    • Russell, G.C.1    Guest, J.R.2
  • 72
    • 0027940510 scopus 로고
    • Site-directed mutagenesis and functional analysis of the active-site residues of the E2 component of bovine branched-chain alpha-keto acid dehydrogenase complex
    • Meng M.H., and Chuang D.T. Site-directed mutagenesis and functional analysis of the active-site residues of the E2 component of bovine branched-chain alpha-keto acid dehydrogenase complex. Biochemistry 33 (1994) 12879-12885
    • (1994) Biochemistry , vol.33 , pp. 12879-12885
    • Meng, M.H.1    Chuang, D.T.2
  • 73
    • 0031941001 scopus 로고    scopus 로고
    • A conserved histidine is essential for glycerolipid acyltransferase catalysis
    • Heath R.J., and Rock C.O. A conserved histidine is essential for glycerolipid acyltransferase catalysis. J. Bacteriol. 180 (1998) 1425-1430
    • (1998) J. Bacteriol. , vol.180 , pp. 1425-1430
    • Heath, R.J.1    Rock, C.O.2
  • 74
    • 0027010625 scopus 로고
    • Chemical anatomy of antibiotic resistance: chloramphenicol acetyltransferase
    • Shaw W.V. Chemical anatomy of antibiotic resistance: chloramphenicol acetyltransferase. Sci. Progr. 76 (1992) 565-580
    • (1992) Sci. Progr. , vol.76 , pp. 565-580
    • Shaw, W.V.1
  • 76
    • 0026730661 scopus 로고
    • Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
    • Terecero J.C., Riles L.E., and Wickner R.B. Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae. J. Biol. Chem. 267 (1992) 20270-20276
    • (1992) J. Biol. Chem. , vol.267 , pp. 20270-20276
    • Terecero, J.C.1    Riles, L.E.2    Wickner, R.B.3
  • 77
    • 0026730661 scopus 로고
    • Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae
    • Tercero J.C., Riles L.E., and Wickner R.B. Localized mutagenesis and evidence for post-transcriptional regulation of MAK3. A putative N-acetyltransferase required for double-stranded RNA virus propagation in Saccharomyces cerevisiae. J. Biol. Chem. 267 (1992) 20270-20276
    • (1992) J. Biol. Chem. , vol.267 , pp. 20270-20276
    • Tercero, J.C.1    Riles, L.E.2    Wickner, R.B.3
  • 78
    • 0027253353 scopus 로고
    • Yeast MAK3 N-acetyltransferase recognizes the N-terminal four amino acids of the major coat protein (gag) of the L-A double-stranded RNA virus
    • Tercero J.C., Dinman J.D., and Wickner R.B. Yeast MAK3 N-acetyltransferase recognizes the N-terminal four amino acids of the major coat protein (gag) of the L-A double-stranded RNA virus. J. Bacteriol. 175 (1993) 3192-3194
    • (1993) J. Bacteriol. , vol.175 , pp. 3192-3194
    • Tercero, J.C.1    Dinman, J.D.2    Wickner, R.B.3
  • 79
    • 0032435715 scopus 로고    scopus 로고
    • Anthranilate N-hydroxycinnamoyl/benzoyltransferase gene from carnation: rapid elicitation of transcription and promoter analysis
    • Yang Q., Grimmig B., and Matern U. Anthranilate N-hydroxycinnamoyl/benzoyltransferase gene from carnation: rapid elicitation of transcription and promoter analysis. Plant Mol. Biol. 38 (1998) 1201-1214
    • (1998) Plant Mol. Biol. , vol.38 , pp. 1201-1214
    • Yang, Q.1    Grimmig, B.2    Matern, U.3
  • 80
    • 0030152183 scopus 로고    scopus 로고
    • Characteization of hsr201 and hsr515, two tobacco genes preferentially expressed during the hypersensitive reaction provoked by phytopathogenic bacteria
    • Czernic P., Huang H.C., and Marco Y. Characteization of hsr201 and hsr515, two tobacco genes preferentially expressed during the hypersensitive reaction provoked by phytopathogenic bacteria. Plant Mol. Biol. 31 (1996) 255-265
    • (1996) Plant Mol. Biol. , vol.31 , pp. 255-265
    • Czernic, P.1    Huang, H.C.2    Marco, Y.3
  • 81
    • 0032544435 scopus 로고    scopus 로고
    • The mystery of the trichothecene 3-O-acetyltransferase gene-Analysis of the region around Tri101 and characterization of its homologue from Fusarium sporotrichioides
    • Kimura M., Matsumoto G., Shingu Y., Yoneyama K., and Yamaguchi I. The mystery of the trichothecene 3-O-acetyltransferase gene-Analysis of the region around Tri101 and characterization of its homologue from Fusarium sporotrichioides. FEBS Lett. 435 (1998) 163-168
    • (1998) FEBS Lett. , vol.435 , pp. 163-168
    • Kimura, M.1    Matsumoto, G.2    Shingu, Y.3    Yoneyama, K.4    Yamaguchi, I.5
  • 82
  • 83
    • 0032004228 scopus 로고    scopus 로고
    • The DWF4 gene of Arabidopsis encodes a cytochrome P450 that mediates multiple 22alpha-hydroxylation steps in brassinosteroid biosynthesis
    • Choe S., Dilkes B.P., Fujioka S., Takatsuto S., Sakurai A., and Feldmann K.A. The DWF4 gene of Arabidopsis encodes a cytochrome P450 that mediates multiple 22alpha-hydroxylation steps in brassinosteroid biosynthesis. Plant Cell 10 (1998) 231-243
    • (1998) Plant Cell , vol.10 , pp. 231-243
    • Choe, S.1    Dilkes, B.P.2    Fujioka, S.3    Takatsuto, S.4    Sakurai, A.5    Feldmann, K.A.6
  • 84
    • 0029347160 scopus 로고
    • The maize Dwarf3 gene encodes a cytochrome P450-mediated early step in Gibberellin biosynthesis
    • Winkler R.G., and Helentjaris T. The maize Dwarf3 gene encodes a cytochrome P450-mediated early step in Gibberellin biosynthesis. Plant Cell 7 (1995) 1307-1317
    • (1995) Plant Cell , vol.7 , pp. 1307-1317
    • Winkler, R.G.1    Helentjaris, T.2
  • 85
    • 0030175185 scopus 로고    scopus 로고
    • The tomato Dwarf gene isolated by heterologous transposon tagging encodes the first member of a new cytochrome P450 family
    • Bishop G.J., Harrison K., and Jones J.D. The tomato Dwarf gene isolated by heterologous transposon tagging encodes the first member of a new cytochrome P450 family. Plant Cell 8 (1996) 959-969
    • (1996) Plant Cell , vol.8 , pp. 959-969
    • Bishop, G.J.1    Harrison, K.2    Jones, J.D.3
  • 86
    • 0031079973 scopus 로고    scopus 로고
    • Metabolic pathway gene clusters in filamentous fungi
    • Keller N.P., and Hohn T.M. Metabolic pathway gene clusters in filamentous fungi. Fungal Genet. Biol. 21 (1997) 17-29
    • (1997) Fungal Genet. Biol. , vol.21 , pp. 17-29
    • Keller, N.P.1    Hohn, T.M.2


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