메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Crystal structure of tyrosine decarboxylase and identification of key residues involved in conformational swing and substrate binding

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; BACTERIAL PROTEIN; PROTEIN BINDING; PYRIDOXAL 5 PHOSPHATE; TYROSINE DECARBOXYLASE;

EID: 84974679370     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27779     Document Type: Article
Times cited : (51)

References (40)
  • 1
    • 0142026250 scopus 로고    scopus 로고
    • Tyramine and octopamine: Antagonistic modulators of behavior and metabolism
    • Roeder, T., Seifert, M., Kahler, C. & Gewecke, M. Tyramine and octopamine: Antagonistic modulators of behavior and metabolism. Arch. Insect Biochem. Physiol. 54, 1-13 (2003).
    • (2003) Arch. Insect Biochem. Physiol. , vol.54 , pp. 1-13
    • Roeder, T.1    Seifert, M.2    Kahler, C.3    Gewecke, M.4
  • 2
    • 0005225952 scopus 로고    scopus 로고
    • Biogenic amines: Their importance in foods
    • Santos, M. H. S. Biogenic amines: Their importance in foods. Int. J. Food Microbiol. 29, 213-231 (1996).
    • (1996) Int. J. Food Microbiol. , vol.29 , pp. 213-231
    • Santos, M.H.S.1
  • 3
    • 33847247838 scopus 로고    scopus 로고
    • Tyramine excites rat subthalamic neurons in vitro by a dopamine-dependent mechanism
    • Zhu, Z. T., Munhall, A. C. & Johnson, S. W. Tyramine excites rat subthalamic neurons in vitro by a dopamine-dependent mechanism. Neuropharmacology 52, 1169-1178 (2007).
    • (2007) Neuropharmacology , vol.52 , pp. 1169-1178
    • Zhu, Z.T.1    Munhall, A.C.2    Johnson, S.W.3
  • 4
    • 23844485491 scopus 로고    scopus 로고
    • Isolation cloning, tissue expression of a putative octopamine/tyramine receptor from locust visceral muscle tissues
    • Molaei, G., Paluzzi, J. P., Bendena, W. G. & Lange, A. B. Isolation, cloning, tissue expression of a putative octopamine/tyramine receptor from locust visceral muscle tissues. Arch. Insect. Biochem. Physiol. 59, 132-149 (2005).
    • (2005) Arch. Insect. Biochem. Physiol. , vol.59 , pp. 132-149
    • Molaei, G.1    Paluzzi, J.P.2    Bendena, W.G.3    Lange, A.B.4
  • 5
    • 55749085263 scopus 로고    scopus 로고
    • Enhanced octopamine synthesis through the ectopic expression of tyrosine decarboxylase in rice plants
    • Lee, K., Kang, K., Park, M., Park, S. & Back, K. Enhanced octopamine synthesis through the ectopic expression of tyrosine decarboxylase in rice plants. Plant Science 176, 46-50 (2009).
    • (2009) Plant Science , vol.176 , pp. 46-50
    • Lee, K.1    Kang, K.2    Park, M.3    Park, S.4    Back, K.5
  • 6
    • 1442265210 scopus 로고    scopus 로고
    • Identification of the gene encoding a putative tyrosine decarboxylase of Carnobacterium divergens 508. Development of molecular tools for the detection of tyramine-producing bacteria
    • Coton, M., Coton, E., Lucas, P. & Lonvaud, A. Identification of the gene encoding a putative tyrosine decarboxylase of Carnobacterium divergens 508. Development of molecular tools for the detection of tyramine-producing bacteria. Food Microbiol. 21, 125-130 (2004).
    • (2004) Food Microbiol. , vol.21 , pp. 125-130
    • Coton, M.1    Coton, E.2    Lucas, P.3    Lonvaud, A.4
  • 9
    • 0028281750 scopus 로고
    • Multiple evolutionary origin of pyridoxal-5?-phosphate-dependent amino-acid decarboxylases
    • Sandmeier, E., Hale, T. I. & Christen, P. Multiple evolutionary origin of pyridoxal-5?-phosphate-dependent amino-acid decarboxylases. Eur. J. Biochem. 221, 997-1002 (1994).
    • (1994) Eur. J. Biochem. , vol.221 , pp. 997-1002
    • Sandmeier, E.1    Hale, T.I.2    Christen, P.3
  • 10
    • 84888347554 scopus 로고    scopus 로고
    • Tyrosine decarboxylase from Lactobacillus brevis: Soluble expression and characterization
    • Zhang, K. & Ni, Y. Tyrosine decarboxylase from Lactobacillus brevis: soluble expression and characterization. Protein Expres. Purif. 94, 33-39 (2014).
    • (2014) Protein Expres. Purif. , vol.94 , pp. 33-39
    • Zhang, K.1    Ni, Y.2
  • 11
    • 0032870009 scopus 로고    scopus 로고
    • Tyrosine decarboxylase activity of Lactobacillus brevis IOEB 9809 isolated from wine and L. brevis ATCC 367
    • Moreno-Arribas, V. & Lonvaud-Funel, A. Tyrosine decarboxylase activity of Lactobacillus brevis IOEB 9809 isolated from wine and L. brevis ATCC 367. FEMS Microbiol. Lett. 180, 55-60 (1999).
    • (1999) FEMS Microbiol. Lett. , vol.180 , pp. 55-60
    • Moreno-Arribas, V.1    Lonvaud-Funel, A.2
  • 12
    • 67349158074 scopus 로고    scopus 로고
    • Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana
    • Lehmann, T. & Pollmann, S. Gene expression and characterization of a stress-induced tyrosine decarboxylase from Arabidopsis thaliana. FEBS Lett. 583, 1895-1900 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 1895-1900
    • Lehmann, T.1    Pollmann, S.2
  • 13
    • 0029257145 scopus 로고
    • Expression in Escherichia coli and partial characterization of two tyrosine-dopa decarboxylases from opium poppy
    • Facchini, P. J. & Deluca, V. Expression in Escherichia coli and partial characterization of two tyrosine-dopa decarboxylases from opium poppy. Phytochemistry 38, 1119-1126 (1995).
    • (1995) Phytochemistry , vol.38 , pp. 1119-1126
    • Facchini, P.J.1    Deluca, V.2
  • 14
    • 17444402206 scopus 로고    scopus 로고
    • Two functional but noncomplementing Drosophila tyrosine decarboxylase genes: Distinct roles for neural tyramine and octopamine in female fertility
    • Cole, S. H. et al. Two functional but noncomplementing Drosophila tyrosine decarboxylase genes: distinct roles for neural tyramine and octopamine in female fertility. J. Biol. Chem. 280, 14948-14955 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 14948-14955
    • Cole, S.H.1
  • 15
    • 84857048031 scopus 로고    scopus 로고
    • Aversive odorant causing appetite decrease downregulates tyrosine decarboxylase gene expression in the olfactory receptor neuron of the blowfly, Phormia regina
    • Ishida, Y. & Ozaki, M. Aversive odorant causing appetite decrease downregulates tyrosine decarboxylase gene expression in the olfactory receptor neuron of the blowfly, Phormia regina. Die Naturwissenschaften 99, 71-75 (2012).
    • (2012) Die Naturwissenschaften , vol.99 , pp. 71-75
    • Ishida, Y.1    Ozaki, M.2
  • 16
    • 0035808975 scopus 로고    scopus 로고
    • Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 isolated from wine
    • Moreno-Arribas, V. & Lonvaud-Funel, A. Purification and characterization of tyrosine decarboxylase of Lactobacillus brevis IOEB 9809 isolated from wine. Fems Microbiology Letters 195, 103-107 (2001).
    • (2001) Fems Microbiology Letters , vol.195 , pp. 103-107
    • Moreno-Arribas, V.1    Lonvaud-Funel, A.2
  • 17
    • 0024968602 scopus 로고
    • Purification and characterisation of tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase
    • Borresen, T., Klausen, N. K., Larsen, L. M. & Sorensen, H. Purification and characterisation of tyrosine decarboxylase and aromatic-L-amino-acid decarboxylase. Biochim. Et Biophy. Acta 993, 108-115 (1989).
    • (1989) Biochim. et Biophy. Acta , vol.993 , pp. 108-115
    • Borresen, T.1    Klausen, N.K.2    Larsen, L.M.3    Sorensen, H.4
  • 18
    • 14544282848 scopus 로고    scopus 로고
    • Identification and characterization of a L-tyrosine decarboxylase in Methanocaldococcus jannaschii
    • Kezmarsky, N. D., Xu, H., Graham, D. E. & White, R. H. Identification and characterization of a L-tyrosine decarboxylase in Methanocaldococcus jannaschii. Biochim. Et Biophy. Acta 1722, 175-182 (2005).
    • (2005) Biochim. et Biophy. Acta , vol.1722 , pp. 175-182
    • Kezmarsky, N.D.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 19
    • 79958100930 scopus 로고    scopus 로고
    • Characterization of the tyramine-producing pathway in Sporolactobacillus sp. P3J
    • Coton, M. et al. Characterization of the tyramine-producing pathway in Sporolactobacillus sp. P3J. Microbiology 157, 1841-1849 (2011).
    • (2011) Microbiology , vol.157 , pp. 1841-1849
    • Coton, M.1
  • 20
    • 63449140809 scopus 로고    scopus 로고
    • Biotransformation of L-tyrosine to tyramine by the growing cells of Lactococcus lactis
    • Thakur, M. & Azmi, W. Biotransformation of L-tyrosine to tyramine by the growing cells of Lactococcus lactis. Acta Microbiol. Imm. H. 56, 101-114 (2009).
    • (2009) Acta Microbiol. Imm. H. , vol.56 , pp. 101-114
    • Thakur, M.1    Azmi, W.2
  • 21
    • 58149387437 scopus 로고    scopus 로고
    • Dual role for the tyrosine decarboxylation pathway in Enterococcus faecium E17: Response to an acid challenge and generation of a proton motive force
    • Pereira, C. I., Matos, D., Romao, M. V. S. & Crespo, M. T. B. Dual role for the tyrosine decarboxylation pathway in Enterococcus faecium E17: response to an acid challenge and generation of a proton motive force. Appl. Environ. Microbiol. 75, 345-352 (2009).
    • (2009) Appl. Environ. Microbiol. , vol.75 , pp. 345-352
    • Pereira, C.I.1    Matos, D.2    Romao, M.V.S.3    Crespo, M.T.B.4
  • 22
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie, S. Preparation of selenomethionyl proteins for phase determination. Methods Enzymol. 276, 523-530 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 523-530
    • Doublie, S.1
  • 23
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 24
    • 66249112826 scopus 로고    scopus 로고
    • Decision-making in structure solution using Bayesian estimates of map quality: The PHENIX AutoSol wizard
    • Terwilliger, T. C. et al. Decision-making in structure solution using Bayesian estimates of map quality: the PHENIX AutoSol wizard. Acta Crystallogr. Sect. D-Biol. Crystallogr. 65, 582-601 (2009).
    • (2009) Acta Crystallogr. Sect. D-Biol. Crystallogr. , vol.65 , pp. 582-601
    • Terwilliger, T.C.1
  • 25
    • 37349103121 scopus 로고    scopus 로고
    • Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard
    • Terwilliger, T. C. et al. Iterative model building, structure refinement and density modification with the PHENIX AutoBuild wizard. Acta Crystallogr. Sect. D-Biol. Crystallogr. 64, 61-69 (2008).
    • (2008) Acta Crystallogr. Sect. D-Biol. Crystallogr. , vol.64 , pp. 61-69
    • Terwilliger, T.C.1
  • 26
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. Sect. D-Biol. Crystallogr. 66, 213-221 (2010).
    • (2010) Acta Crystallogr. Sect. D-Biol. Crystallogr. , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 28
    • 34447508216 scopus 로고    scopus 로고
    • Phaser crystallographic software
    • McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658-674 (2007).
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 658-674
    • McCoy, A.J.1
  • 29
    • 16644397843 scopus 로고    scopus 로고
    • Developments in the CCP4 molecular-graphics project
    • Potterton, L. et al. Developments in the CCP4 molecular-graphics project. Acta Crystallogr. Sect. D-Biol. Crystallogr. 60, 2288-2294 (2004).
    • (2004) Acta Crystallogr. Sect. D-Biol. Crystallogr. , vol.60 , pp. 2288-2294
    • Potterton, L.1
  • 30
    • 84855517335 scopus 로고    scopus 로고
    • Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases
    • G. Giardina. et al. Open conformation of human DOPA decarboxylase reveals the mechanism of PLP addition to Group II decarboxylases. Proc. Natl. Acad. Sci. USA 108, 20514-20519 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20514-20519
    • Giardina, G.1
  • 33
    • 34247249781 scopus 로고    scopus 로고
    • GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop
    • Fenalti, G. et al. GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nature Struc. Mol. Biol. 14, 280-286 (2007).
    • (2007) Nature Struc. Mol. Biol. , vol.14 , pp. 280-286
    • Fenalti, G.1
  • 34
    • 0037184097 scopus 로고    scopus 로고
    • Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase
    • Bertoldi, M., Gonsalvi, M., Contestabile, R. & Voltattorni, C. B. Mutation of tyrosine 332 to phenylalanine converts dopa decarboxylase into a decarboxylation-dependent oxidative deaminase. J. Biol. Chem. 277, 36357-36362 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 36357-36362
    • Bertoldi, M.1    Gonsalvi, M.2    Contestabile, R.3    Voltattorni, C.B.4
  • 35
    • 84865242184 scopus 로고    scopus 로고
    • Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase
    • Komori, H., Nitta, Y., Ueno, H. & Higuchi, Y. Structural study reveals that Ser-354 determines substrate specificity on human histidine decarboxylase. J. Biol. Chem. 287, 29175-29183 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 29175-29183
    • Komori, H.1    Nitta, Y.2    Ueno, H.3    Higuchi, Y.4
  • 36
    • 0029682083 scopus 로고    scopus 로고
    • Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis
    • Ishii, S., Mizuguchi, H., Nishino, J., Hayashi, H. & Kagamiyama, H. Functionally important residues of aromatic L-amino acid decarboxylase probed by sequence alignment and site-directed mutagenesis. J. Biochem. 120, 369-376 (1996).
    • (1996) J. Biochem. , vol.120 , pp. 369-376
    • Ishii, S.1    Mizuguchi, H.2    Nishino, J.3    Hayashi, H.4    Kagamiyama, H.5
  • 37
    • 77952475277 scopus 로고    scopus 로고
    • Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase
    • Han, Q., Ding, H., Robinson, H., Christensen, B. M. & Li, J. Crystal structure and substrate specificity of Drosophila 3,4-dihydroxyphenylalanine decarboxylase. PloS ONE 5, e8826 (2010).
    • (2010) PloS ONE , vol.5 , pp. e8826
    • Han, Q.1    Ding, H.2    Robinson, H.3    Christensen, B.M.4    Li, J.5
  • 38
    • 68549109351 scopus 로고    scopus 로고
    • Multiple roles of the active site lysine of Dopa decarboxylase
    • Bertoldi, M. & Voltattorni, C. B. Multiple roles of the active site lysine of Dopa decarboxylase. Arch. Biochem. Biophys. 488, 130-139 (2009).
    • (2009) Arch. Biochem. Biophys. , vol.488 , pp. 130-139
    • Bertoldi, M.1    Voltattorni, C.B.2
  • 39
    • 0034826435 scopus 로고    scopus 로고
    • Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase
    • Bertoldi, M., Castellani, S. & Voltattorni, C., B. Mutation of residues in the coenzyme binding pocket of Dopa decarboxylase. Eur. J. Biochem. 268, 2975-2981 (2001).
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2975-2981
    • Bertoldi, M.1    Castellani, S.2    Voltattorni, C.B.3
  • 40
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. & Doolittle, R. F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157, 105-132 (1982).
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.