메뉴 건너뛰기




Volumn 13, Issue 12, 2006, Pages 1327-1338

Structural Determinants and Modulation of Substrate Specificity in Phenylalanine-Tyrosine Ammonia-Lyases

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA LYASE; CAFFEIC ACID; CAFFEIC ACID DERIVATIVE; COUMARIC ACID; L TYROSINE AMMONIA LYASE; L-TYROSINE AMMONIA-LYASE; PHENYLALANINE;

EID: 33845482046     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2006.11.011     Document Type: Article
Times cited : (121)

References (34)
  • 1
    • 20444473471 scopus 로고    scopus 로고
    • Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine
    • Poppe L., and Rétey J. Friedel-Crafts-type mechanism for the enzymatic elimination of ammonia from histidine and phenylalanine. Angew. Chem. Int. Ed. Engl. 44 (2005) 3668-3688
    • (2005) Angew. Chem. Int. Ed. Engl. , vol.44 , pp. 3668-3688
    • Poppe, L.1    Rétey, J.2
  • 2
    • 1842287997 scopus 로고    scopus 로고
    • Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity
    • Rosler J., Krekel F., Amrhein N., and Schmid J. Maize phenylalanine ammonia-lyase has tyrosine ammonia-lyase activity. Plant Physiol. 113 (1997) 175-179
    • (1997) Plant Physiol. , vol.113 , pp. 175-179
    • Rosler, J.1    Krekel, F.2    Amrhein, N.3    Schmid, J.4
  • 3
    • 20444422841 scopus 로고    scopus 로고
    • Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae
    • Jiang H., Wood K.V., and Morgan J.A. Metabolic engineering of the phenylpropanoid pathway in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 71 (2005) 2962-2969
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2962-2969
    • Jiang, H.1    Wood, K.V.2    Morgan, J.A.3
  • 4
    • 20444437973 scopus 로고    scopus 로고
    • Biochemical characterization of a prokaryotic phenylalanine ammonia lyase
    • Xiang L., and Moore B.S. Biochemical characterization of a prokaryotic phenylalanine ammonia lyase. J. Bacteriol. 187 (2005) 4286-4289
    • (2005) J. Bacteriol. , vol.187 , pp. 4286-4289
    • Xiang, L.1    Moore, B.S.2
  • 5
    • 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., Thomas M., and Clarke D.J. The gene stlA encodes a phenylalanine ammonia-lyase that is involved in the production of a stilbene antibiotic in Photorhabdus luminescens TT01. Microbiol. 151 (2005) 2543-2550
    • (2005) Microbiol. , vol.151 , pp. 2543-2550
    • Williams, J.S.1    Thomas, M.2    Clarke, D.J.3
  • 6
    • 33845493213 scopus 로고    scopus 로고
    • Investigation of the early stages in soraphen A biosynthesis
    • Hill A.M., Thompson B.L., Harris J.P., and Segret R. Investigation of the early stages in soraphen A biosynthesis. ChemBioChem 4 (2003) 1358-1359
    • (2003) ChemBioChem , vol.4 , pp. 1358-1359
    • Hill, A.M.1    Thompson, B.L.2    Harris, J.P.3    Segret, R.4
  • 7
    • 0014777998 scopus 로고
    • Partial purification and properties of 1-phenylalanine ammonia lyase from Streptomyces verticillatus
    • Emes A.V., and Vining L.C. Partial purification and properties of 1-phenylalanine ammonia lyase from Streptomyces verticillatus. Can. J. Biochem. 48 (1970) 613-622
    • (1970) Can. J. Biochem. , vol.48 , pp. 613-622
    • Emes, A.V.1    Vining, L.C.2
  • 8
    • 0037070203 scopus 로고    scopus 로고
    • Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein
    • Kyndt J.A., Meyer T.E., Cusanovich M.A., and Van Beeumen J.J. Characterization of a bacterial tyrosine ammonia lyase, a biosynthetic enzyme for the photoactive yellow protein. FEBS Lett. 512 (2002) 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
  • 9
    • 3242737570 scopus 로고    scopus 로고
    • Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli
    • Watts K.T., Lee P.C., and Schmidt-Dannert C. Exploring recombinant flavonoid biosynthesis in metabolically engineered Escherichia coli. ChemBioChem 5 (2004) 500-507
    • (2004) ChemBioChem , vol.5 , pp. 500-507
    • Watts, K.T.1    Lee, P.C.2    Schmidt-Dannert, C.3
  • 10
    • 33645235844 scopus 로고    scopus 로고
    • Genes and enzymes involved in caffeic acid biosynthesis in the actinomycete Saccharothrix espanaensis
    • Berner M., Krug D., Bihlmaier C., Vente A., Müller R., and Bechthold A. Genes and enzymes involved in caffeic acid biosynthesis in the actinomycete Saccharothrix espanaensis. J. Bacteriol. 188 (2006) 2666-2673
    • (2006) J. Bacteriol. , vol.188 , pp. 2666-2673
    • Berner, M.1    Krug, D.2    Bihlmaier, C.3    Vente, A.4    Müller, R.5    Bechthold, A.6
  • 11
    • 0036154018 scopus 로고    scopus 로고
    • Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase
    • Baedeker M., and Schulz G.E. Autocatalytic peptide cyclization during chain folding of histidine ammonia-lyase. Structure 10 (2002) 61-67
    • (2002) Structure , vol.10 , pp. 61-67
    • Baedeker, M.1    Schulz, G.E.2
  • 12
    • 1242341209 scopus 로고    scopus 로고
    • Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group
    • Rétey J. Discovery and role of methylidene imidazolone, a highly electrophilic prosthetic group. Biochim. Biophys. Acta 1647 (2003) 179-184
    • (2003) Biochim. Biophys. Acta , vol.1647 , pp. 179-184
    • Rétey, J.1
  • 13
    • 4444306767 scopus 로고    scopus 로고
    • Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis
    • Calabrese J.C., Jordan D.B., Boodhoo A., Sariaslani S., and Vannelli T. Crystal structure of phenylalanine ammonia lyase: multiple helix dipoles implicated in catalysis. Biochemistry 43 (2004) 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
  • 14
    • 0038288848 scopus 로고    scopus 로고
    • A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis
    • Christenson S.D., Liu W., Toney M.D., and Shen B. A novel 4-methylideneimidazole-5-one-containing tyrosine aminomutase in enediyne antitumor antibiotic C-1027 biosynthesis. J. Am. Chem. Soc. 125 (2003) 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
  • 15
    • 11144225850 scopus 로고    scopus 로고
    • Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in taxol biosynthesis
    • Walker K.D., Klettke K., Akiyama T., and Croteau R. Cloning, heterologous expression, and characterization of a phenylalanine aminomutase involved in taxol biosynthesis. J. Biol. Chem. 279 (2004) 53947-53954
    • (2004) J. Biol. Chem. , vol.279 , pp. 53947-53954
    • Walker, K.D.1    Klettke, K.2    Akiyama, T.3    Croteau, R.4
  • 16
    • 19444380670 scopus 로고    scopus 로고
    • Purification, cloning, and functional expression of phenylalanine aminomutase: the first committed step in Taxol side-chain biosynthesis
    • Steele C.L., Chen Y., Dougherty B.A., Li W., Hofstead S., Lam K.S., Xing Z., and Chiang S.J. Purification, cloning, and functional expression of phenylalanine aminomutase: the first committed step in Taxol side-chain biosynthesis. Arch. Biochem. Biophys. 438 (2005) 1-10
    • (2005) Arch. Biochem. Biophys. , vol.438 , pp. 1-10
    • Steele, C.L.1    Chen, Y.2    Dougherty, B.A.3    Li, W.4    Hofstead, S.5    Lam, K.S.6    Xing, Z.7    Chiang, S.J.8
  • 18
    • 18044364010 scopus 로고    scopus 로고
    • Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase
    • Ritter H., and Schulz G.E. Structural basis for the entrance into the phenylpropanoid metabolism catalyzed by phenylalanine ammonia-lyase. Plant Cell 16 (2004) 3426-3436
    • (2004) Plant Cell , vol.16 , pp. 3426-3436
    • Ritter, H.1    Schulz, G.E.2
  • 19
    • 0041154057 scopus 로고    scopus 로고
    • Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile
    • Schwede T.F., Rétey J., and Schulz G.E. Crystal structure of histidine ammonia-lyase revealing a novel polypeptide modification as the catalytic electrophile. Biochemistry 38 (1999) 5355-5361
    • (1999) Biochemistry , vol.38 , pp. 5355-5361
    • Schwede, T.F.1    Rétey, J.2    Schulz, G.E.3
  • 20
    • 33644943815 scopus 로고    scopus 로고
    • The essential tyrosine-containing loop conformation and the role of the C-terminal multi-helix region in eukaryotic phenylalanine ammonia-lyases
    • Pilbák S., Tomin A., Rétey J., and Poppe L. The essential tyrosine-containing loop conformation and the role of the C-terminal multi-helix region in eukaryotic phenylalanine ammonia-lyases. FEBS J. 273 (2006) 1004-1019
    • (2006) FEBS J. , vol.273 , pp. 1004-1019
    • Pilbák, S.1    Tomin, A.2    Rétey, J.3    Poppe, L.4
  • 21
    • 0036223618 scopus 로고    scopus 로고
    • Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism
    • Baedeker M., and Schulz G.E. Structures of two histidine ammonia-lyase modifications and implications for the catalytic mechanism. Eur. J. Biochem. 269 (2002) 1790-1797
    • (2002) Eur. J. Biochem. , vol.269 , pp. 1790-1797
    • Baedeker, M.1    Schulz, G.E.2
  • 22
    • 0028083417 scopus 로고
    • Structural and catalytic properties of the four phenylalanine ammonia-lyases from parsley (Petroselinum crispum Nym)
    • Appert C., Logemann E., Hahlbrock K., Schmid J., and Amrhein N. Structural and catalytic properties of the four phenylalanine ammonia-lyases from parsley (Petroselinum crispum Nym). Eur. J. Biochem. 225 (1994) 2177-2185
    • (1994) Eur. J. Biochem. , vol.225 , pp. 2177-2185
    • Appert, C.1    Logemann, E.2    Hahlbrock, K.3    Schmid, J.4    Amrhein, N.5
  • 23
    • 12244298867 scopus 로고    scopus 로고
    • Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues
    • Appert C., Zón J., and Amrhein N. Kinetic analysis of the inhibition of phenylalanine ammonia-lyase by 2-aminoindan-2-phosphonic acid and other phenylalanine analogues. Phytochemistry 62 (2003) 415-422
    • (2003) Phytochemistry , vol.62 , pp. 415-422
    • Appert, C.1    Zón, J.2    Amrhein, N.3
  • 24
    • 0035206610 scopus 로고    scopus 로고
    • Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida
    • Rother D., Poppe L., Viergutz S., Langer B., and Rétey J. Characterization of the active site of histidine ammonia-lyase from Pseudomonas putida. Eur. J. Biochem. 268 (2001) 6011-6019
    • (2001) Eur. J. Biochem. , vol.268 , pp. 6011-6019
    • Rother, D.1    Poppe, L.2    Viergutz, S.3    Langer, B.4    Rétey, J.5
  • 25
    • 0036311143 scopus 로고    scopus 로고
    • An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum
    • Rother D., Poppe L., Morlock G., Viergutz S., and Rétey J. An active site homology model of phenylalanine ammonia-lyase from Petroselinum crispum. Eur. J. Biochem. 269 (2002) 3065-3075
    • (2002) Eur. J. Biochem. , vol.269 , pp. 3065-3075
    • Rother, D.1    Poppe, L.2    Morlock, G.3    Viergutz, S.4    Rétey, J.5
  • 26
    • 0034620559 scopus 로고    scopus 로고
    • Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase
    • Jez J.M., Ferrer J.L., Bowman M.E., Dixon R.A., and Noel J.P. Dissection of malonyl-coenzyme A decarboxylation from polyketide formation in the reaction mechanism of a plant polyketide synthase. Biochemistry 39 (2000) 890-902
    • (2000) Biochemistry , vol.39 , pp. 890-902
    • Jez, J.M.1    Ferrer, J.L.2    Bowman, M.E.3    Dixon, R.A.4    Noel, J.P.5
  • 27
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 28
    • 33845509228 scopus 로고    scopus 로고
    • Leslie, A.G.W. (1992). Joint CCP4 + ESF-EAMCB Newsletter on Protein Crystallography, No. 26.
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallog. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallog. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 30
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 31
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • Sali A., and Blundell T.L. Comparative protein modelling by satisfaction of spatial restraints. J. Mol. Biol. 234 (1993) 779-815
    • (1993) J. Mol. Biol. , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 33
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography and NMR system: a new software suite for macromolecular structure determination
    • Brunger A.T., and Warren G.L. Crystallography and NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D Biol. Crystallogr. 54 (1998) 905-921
    • (1998) Acta Crystallogr. D Biol. Crystallogr. , vol.54 , pp. 905-921
    • Brunger, A.T.1    Warren, G.L.2
  • 34
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density
    • McRee D.E. XtalView/Xfit: a versatile program for manipulating atomic coordinates and electron density. J. Struct. Biol. 125 (1999) 156-165
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.