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Volumn 188, Issue 7, 2006, Pages 2666-2673

Genes and enzymes involved in caffeic acid biosynthesis in the actinomycete Saccharothrix espanaensis

Author keywords

[No Author keywords available]

Indexed keywords

4 COUMARATE 3 HYDROXYLASE; AGLYCONE; AMMONIA LYASE; ANTIBIOTIC AGENT; BACTERIAL DNA; CAFFEIC ACID; COUMARIC ACID; HISTIDINE AMMONIALYASE; OLIGOSACCHARIDE; OXYGENASE; PARA COUMARIC ACID; SACCHAROMICIN A; SACCHAROMICIN B; TYROSINE; TYROSINE AMMONIA LYASE; UNCLASSIFIED DRUG;

EID: 33645235844     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.188.7.2666-2673.2006     Document Type: Article
Times cited : (148)

References (31)
  • 1
    • 0028083417 scopus 로고
    • Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley
    • Appert, C., E. Logemann, K. Hahlbrock, J. Schmid, and N. Amrhein. 1994. Structural and catalytic properties of the four phenylalanine ammonia-lyase isoenzymes from parsley. Eur. J. Biochem. 225:491-499.
    • (1994) Eur. J. Biochem. , vol.225 , pp. 491-499
    • Appert, C.1    Logemann, E.2    Hahlbrock, K.3    Schmid, J.4    Amrhein, N.5
  • 2
    • 0002333191 scopus 로고
    • Flavin nucleotide-dependent 3-hydroxylation of 4-hydroxyphenylpropanoid carboxylic acids by particulate preparations from potato-tubers
    • Boniwell, J. M., and V. S. Butt. 1986. Flavin nucleotide-dependent 3-hydroxylation of 4-hydroxyphenylpropanoid carboxylic acids by particulate preparations from potato-tubers. Z. Naturforsch. C 41:56-60.
    • (1986) Z. Naturforsch. C , vol.41 , pp. 56-60
    • Boniwell, J.M.1    Butt, V.S.2
  • 3
    • 0023160460 scopus 로고
    • High-performance liquid-chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans
    • Buck, R. H., and K. Krummen. 1987. High-performance liquid- chromatographic determination of enantiomeric amino acids and amino alcohols after derivatization with o-phthaldialdehyde and various chiral mercaptans. J. Chromatogr. 387:255-265.
    • (1987) J. Chromatogr. , vol.387 , pp. 255-265
    • Buck, R.H.1    Krummen, K.2
  • 4
    • 4444306767 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine ammonia lyase: Multiple helix dipoles implicated in catalysis
    • Calabrese, J. C., D. B. Jordan, A. Boodhoo, S. Sariaslani, and T. Vannelli. 2004. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry 43:11403-11416.
    • (2004) Biochemistry , vol.43 , pp. 11403-11416
    • Calabrese, J.C.1    Jordan, D.B.2    Boodhoo, A.3    Sariaslani, S.4    Vannelli, T.5
  • 5
    • 0038288848 scopus 로고    scopus 로고
    • A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis
    • Christenson, S. D., W. Liu, M. D. Toney, and B. Shen. 2003. A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. J. Am. Chem. Soc. 125:6062-6063.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 6062-6063
    • Christenson, S.D.1    Liu, W.2    Toney, M.D.3    Shen, B.4
  • 6
    • 0242349771 scopus 로고    scopus 로고
    • Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis
    • Christenson, S. D., W. M. Wu, M. A. Spies, B. Shen, and M. D. Toney. 2003. Kinetic analysis of the 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. Biochemistry 42:12708-12718.
    • (2003) Biochemistry , vol.42 , pp. 12708-12718
    • Christenson, S.D.1    Wu, W.M.2    Spies, M.A.3    Shen, B.4    Toney, M.D.5
  • 8
    • 0000333340 scopus 로고    scopus 로고
    • Biosynthesis of flavonoids
    • Sir Derek Barton and Koji Nakanishi (ed.). Elsevier Science Ltd., Oxford, United Kingdom
    • Forkmann, G., and W. Heller. 1999. Biosynthesis of flavonoids, p. 713-748. In Sir Derek Barton and Koji Nakanishi (ed.), Comprehensive natural products chemistry. Elsevier Science Ltd., Oxford, United Kingdom.
    • (1999) Comprehensive Natural Products Chemistry , pp. 713-748
    • Forkmann, G.1    Heller, W.2
  • 9
    • 0036011028 scopus 로고    scopus 로고
    • Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis
    • Franke, R., M. R. Hemm, J. W. Denault, M. O. Ruegger, J. M. Humphreys, and C. Chapple. 2002. Changes in secondary metabolism and deposition of an unusual lignin in the ref8 mutant of Arabidopsis. Plant J. 30:47-59.
    • (2002) Plant J. , vol.30 , pp. 47-59
    • Franke, R.1    Hemm, M.R.2    Denault, J.W.3    Ruegger, M.O.4    Humphreys, J.M.5    Chapple, C.6
  • 11
    • 0022115972 scopus 로고
    • Elicitor induction of a microsomal 5-O-(4-coumaroyl)shikimate 3′-hydroxylase in parsley cell suspension cultures
    • Heller, W., and T. Kühnl. 1985. Elicitor induction of a microsomal 5-O-(4-coumaroyl)shikimate 3′-hydroxylase in parsley cell suspension cultures. Arch. Biochem. Biophys. 241:453-460.
    • (1985) Arch. Biochem. Biophys. , vol.241 , pp. 453-460
    • Heller, W.1    Kühnl, T.2
  • 13
    • 0024632120 scopus 로고
    • 2+-dependent enzymes in cultured plant cells and its activation by an elicitor-induced pH shift
    • 2+-dependent enzymes in cultured plant cells and its activation by an elicitor-induced pH shift. Arch. Biochem. Biophys. 269:455-462.
    • (1989) Arch. Biochem. Biophys. , vol.269 , pp. 455-462
    • Kneusel, R.E.1    Matern, U.2    Nicolay, K.3
  • 14
    • 0024616611 scopus 로고
    • Detection and characterization of p-coumaric acid hydroxylase in mung bean, Vigna mungo, seedlings
    • Kojima, M., and W. Takeuchi. 1989. Detection and characterization of p-coumaric acid hydroxylase in mung bean, Vigna mungo, seedlings. J. Biochem. 105:265-270.
    • (1989) J. Biochem. , vol.105 , pp. 265-270
    • Kojima, M.1    Takeuchi, W.2
  • 16
    • 0023433013 scopus 로고
    • Chlorogenic acid biosynthesis-characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase from carrot (Daucus carota L.) cell suspension cultures
    • Kühnl, T., U. Koch, W. Heller, and E. Wellmann. 1987. Chlorogenic acid biosynthesis-characterization of a light-induced microsomal 5-O-(4-coumaroyl)-D-quinate/shikimate 3′-hydroxylase from carrot (Daucus carota L.) cell suspension cultures. Arch. Biochem. Biophys. 258:226-232.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 226-232
    • Kühnl, T.1    Koch, U.2    Heller, W.3    Wellmann, E.4
  • 17
    • 0037070203 scopus 로고    scopus 로고
    • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein
    • Kyndt, J. A., T. E. Meyer, M. A. Cusanovich, and J. J. Van Beeumen. 2002. Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Lett. 512:240-244.
    • (2002) FEBS Lett. , vol.512 , pp. 240-244
    • Kyndt, J.A.1    Meyer, T.E.2    Cusanovich, M.A.3    Van Beeumen, J.J.4
  • 18
    • 0033960223 scopus 로고    scopus 로고
    • Phylogenetic analysis of Saccharothrix and related taxa: Proposal for Actinosynnemataceae fam. nov.
    • Labeda, D. P., and R. M. Kroppenstedt. 2000. Phylogenetic analysis of Saccharothrix and related taxa: proposal for Actinosynnemataceae fam. nov. Int. J. Syst. Evol. Microbiol. 50:331-336.
    • (2000) Int. J. Syst. Evol. Microbiol. , vol.50 , pp. 331-336
    • Labeda, D.P.1    Kroppenstedt, R.M.2
  • 19
    • 0036742670 scopus 로고    scopus 로고
    • Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast
    • Nair, R. B., Q. Xia, C. J. Kartha, E. Kurylo, R. N. Hirji, R. Datla, and G. Selvaraj. 2002. Arabidopsis CYP98A3 mediating aromatic 3-hydroxylation. Developmental regulation of the gene, and expression in yeast. Plant Physiol. 130:210-220.
    • (2002) Plant Physiol. , vol.130 , pp. 210-220
    • Nair, R.B.1    Xia, Q.2    Kartha, C.J.3    Kurylo, E.4    Hirji, R.N.5    Datla, R.6    Selvaraj, G.7
  • 20
    • 20444473471 scopus 로고    scopus 로고
    • Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine
    • Poppe, L., and J. Retey. 2005. Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine. Angew. Chem. Int. Ed. Engl. 44:3668-3688.
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 3668-3688
    • Poppe, L.1    Retey, J.2
  • 21
    • 0036311143 scopus 로고    scopus 로고
    • An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
    • Röther, D., L. Poppe, G. Morlock, S. Viergutz, and J. Rétey. 2002. An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum. Eur. J. Biochem. 269:3065-3075.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3065-3075
    • Röther, D.1    Poppe, L.2    Morlock, G.3    Viergutz, S.4    Rétey, J.5
  • 22
    • 0035206610 scopus 로고    scopus 로고
    • Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida
    • Röther, R., L. Poppe, S. Viergutz, B. Langer, and J. Rétey. 2001. Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida. Eur. J. Biochem. 268:6011-6019.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6011-6019
    • Röther, R.1    Poppe, L.2    Viergutz, S.3    Langer, B.4    Rétey, J.5
  • 23
    • 0035965253 scopus 로고    scopus 로고
    • CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway
    • Schoch, G., S. Goepfert, M. Morant, A. Hehn, D. Meyer, P. Ullmann, and D. Werck-Reichhart. 2001. CYP98A3 from Arabidopsis thaliana is a 3′-hydroxylase of phenolic esters, a missing link in the phenylpropanoid pathway. J. Biol. Chem. 276:36566-36574.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36566-36574
    • Schoch, G.1    Goepfert, S.2    Morant, M.3    Hehn, A.4    Meyer, D.5    Ullmann, P.6    Werck-Reichhart, D.7
  • 24
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede, T. F., J. Rétey, and G. E. Schulz. 1999. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38:5355-5361.
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Rétey, J.2    Schulz, G.E.3
  • 25
    • 0033931843 scopus 로고    scopus 로고
    • Saccharomicins, novel heptadecaglycoside antibiotics produced by Saccharothrix espanaensis: Antibacterial and mechanistic activities
    • Singh, M. P., P. J. Petersen, W. J. Weiss, F. Kong, and M. Greenstein. 2000. Saccharomicins, novel heptadecaglycoside antibiotics produced by Saccharothrix espanaensis: antibacterial and mechanistic activities. Antimicrob. Agents Chemother. 44:2154-2159.
    • (2000) Antimicrob. Agents Chemother. , vol.44 , pp. 2154-2159
    • Singh, M.P.1    Petersen, P.J.2    Weiss, W.J.3    Kong, F.4    Greenstein, M.5
  • 26
    • 0000773756 scopus 로고
    • 4-Hydroxycinnamic acid hydroxylase and polyphenolase-activities in Sorghum vulgare
    • Stafford, H. A., and S. Dresler. 1972. 4-Hydroxycinnamic acid hydroxylase and polyphenolase-activities in Sorghum vulgare. Plant Physiol. 49:590-595.
    • (1972) Plant Physiol. , vol.49 , pp. 590-595
    • Stafford, H.A.1    Dresler, S.2
  • 27
    • 0026089069 scopus 로고
    • Purification and characterization of p-coumaroyl-D-glucose hydroxylase of sweet potato (Ipomoea batatas) roots
    • Tanaka, M., and M. Kojima. 1991. Purification and characterization of p-coumaroyl-D-glucose hydroxylase of sweet potato (Ipomoea batatas) roots. Arch. Biochem. Biophys. 284:151-157.
    • (1991) Arch. Biochem. Biophys. , vol.284 , pp. 151-157
    • Tanaka, M.1    Kojima, M.2
  • 28
    • 0347753488 scopus 로고    scopus 로고
    • Expression of the landomycin biosynthetic gene cluster in a PKS mutant of Streptomyces fradiae is dependent on the coexpression of a putative transcriptional activator gene
    • von Mulert, U., A. Luzhetskyy, C. Hofmann, A. Mayer, and A. Bechthold. 2004. Expression of the landomycin biosynthetic gene cluster in a PKS mutant of Streptomyces fradiae is dependent on the coexpression of a putative transcriptional activator gene. FEMS Microbiol. Lett. 230:91-97.
    • (2004) FEMS Microbiol. Lett. , vol.230 , pp. 91-97
    • Von Mulert, U.1    Luzhetskyy, A.2    Hofmann, C.3    Mayer, A.4    Bechthold, A.5
  • 29
    • 23844490046 scopus 로고    scopus 로고
    • The gene stlA encodes a phenylalanine ammonia-lyase that is involved in the production of a stilbene antibiotic in Photorhabdus luminescens TT01
    • Williams, J. S., M. Thomas, and D. J. Clarke. 2005. The gene stlA encodes a phenylalanine ammonia-lyase that is involved in the production of a stilbene antibiotic in Photorhabdus luminescens TT01. Microbiology 151:2543-2550.
    • (2005) Microbiology , vol.151 , pp. 2543-2550
    • Williams, J.S.1    Thomas, M.2    Clarke, D.J.3
  • 30
    • 0037031911 scopus 로고    scopus 로고
    • Inactivation, complementation, and heterologous expression of encP, a novel bacterial phenylalanine ammonia-lyase gene
    • Xiang, L. K., and B. S. Moore. 2002. Inactivation, complementation, and heterologous expression of encP, a novel bacterial phenylalanine ammonia-lyase gene. J. Biol. Chem. 277:32505-32509.
    • (2002) J. Biol. Chem. , vol.277 , pp. 32505-32509
    • Xiang, L.K.1    Moore, B.S.2
  • 31
    • 20444437973 scopus 로고    scopus 로고
    • Biochemical characterization of a prokaryotic phenylalanine ammonia lyase
    • Xiang, L. K., and B. S. Moore. 2005. Biochemical characterization of a prokaryotic phenylalanine ammonia lyase. J. Bacteriol. 187:4286-4289.
    • (2005) J. Bacteriol. , vol.187 , pp. 4286-4289
    • Xiang, L.K.1    Moore, B.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.