메뉴 건너뛰기




Volumn 81, Issue 12, 2015, Pages 4216-4223

Structure and mechanism of ferulic acid decarboxylase (FDC1) from saccharomyces cerevisiae

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; BIOCHEMISTRY; BIOSYNTHESIS; CARBOXYLATION; ENZYMES; HYDROPHOBICITY; METABOLIC ENGINEERING; YEAST;

EID: 84929932912     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.00762-15     Document Type: Article
Times cited : (29)

References (44)
  • 1
    • 0034606729 scopus 로고    scopus 로고
    • Dehydrogenation of ethylbenzene to styrene over Fe2O3/Al2O3 catalysts in the presence of carbon dioxide
    • Mimura N, Saito M. 2000. Dehydrogenation of ethylbenzene to styrene over Fe2O3/Al2O3 catalysts in the presence of carbon dioxide. Catal Today 55:173-178. http://dx.doi.org/10.1016/S0920-5861(99)00236-9.
    • (2000) Catal Today , vol.55 , pp. 173-178
    • Mimura, N.1    Saito, M.2
  • 2
    • 43549122822 scopus 로고    scopus 로고
    • Nature's assembly line: biosynthesis of simple phenylpropanoids and plant polyketides
    • Yu O, Jez JM. 2008. Nature's assembly line: biosynthesis of simple phenylpropanoids and plant polyketides. Plant J 54:750-762. http://dx.doi.org/10.1111/j.1365-313X.2008.03436.x
    • (2008) Plant J , vol.54 , pp. 750-762
    • Yu, O.1    Jez, J.M.2
  • 3
    • 42049116334 scopus 로고    scopus 로고
    • Contributions of conserved serine and tyrosine residues to catalysis, ligand binding, and cofactor processing in the active site of tyrosine ammonia lyase
    • Schroeder AC, Kumaran S, Hicks LM, Cahoon RE, Halls C, Yu O, Jez JM. 2008. Contributions of conserved serine and tyrosine residues to catalysis, ligand binding, and cofactor processing in the active site of tyrosine ammonia lyase. Phytochemistry 69:1496-1506. http://dx.doi.org/10.1016/j.phytochem.2008.02.007.
    • (2008) Phytochemistry , vol.69 , pp. 1496-1506
    • Schroeder, A.C.1    Kumaran, S.2    Hicks, L.M.3    Cahoon, R.E.4    Halls, C.5    Yu, O.6    Jez, J.M.7
  • 4
    • 0032877705 scopus 로고    scopus 로고
    • Characterization of a vanillic acid non-oxidative decarboxylation gene cluster from Streptomyces sp
    • Chow KT, Pope MK, Davies J. 1999. Characterization of a vanillic acid non-oxidative decarboxylation gene cluster from Streptomyces sp. D7. Microbiology 145:2393-2403.
    • (1999) D7. Microbiology , vol.145 , pp. 2393-2403
    • Chow, K.T.1    Pope, M.K.2    Davies, J.3
  • 5
    • 85027943031 scopus 로고    scopus 로고
    • A coenzyme-independent decarboxylase/oxygenase cascade for the efficient synthesis of vanillin
    • Furuya T, Miura M, Kino K. 2014. A coenzyme-independent decarboxylase/oxygenase cascade for the efficient synthesis of vanillin. Chembiochem 15:2248-2254. http://dx.doi.org/10.1002/cbic.201402215.
    • (2014) Chembiochem , vol.15 , pp. 2248-2254
    • Furuya, T.1    Miura, M.2    Kino, K.3
  • 6
    • 0027488894 scopus 로고
    • Mechanisms of ferulic acid conversions to vanillic acid and guaiacol by Rhodotorula rubra
    • Huang Z, Dostal L, Rosazza JP. 1993. Mechanisms of ferulic acid conversions to vanillic acid and guaiacol by Rhodotorula rubra. J Biol Chem 268:23954-23958.
    • (1993) J Biol Chem , vol.268 , pp. 23954-23958
    • Huang, Z.1    Dostal, L.2    Rosazza, J.P.3
  • 7
    • 0042562046 scopus 로고    scopus 로고
    • Enhancing volatile phenol concentrations in wine by expressing various phenolic acid decarboxylase genes in Saccharomyces cerevisiae
    • Smit A, Cordero Otero RR, Lambrechts MG, Pretorius IS, Van Rensburg P. 2003. Enhancing volatile phenol concentrations in wine by expressing various phenolic acid decarboxylase genes in Saccharomyces cerevisiae. J Agric Food Chem 51:4909-4915. http://dx.doi.org/10.1021/jf026224d.
    • (2003) J Agric Food Chem , vol.51 , pp. 4909-4915
    • Smit, A.1    Cordero Otero, R.R.2    Lambrechts, M.G.3    Pretorius, I.S.4    Van Rensburg, P.5
  • 8
    • 0028867596 scopus 로고
    • Biocatalytic syntheses of aromatics from D-glucose: renewable microbial sources of aromatic compounds
    • Frost JW, Draths KM. 1995. Biocatalytic syntheses of aromatics from D-glucose: renewable microbial sources of aromatic compounds. Annu Rev Microbiol 49:557-579. http://dx.doi.org/10.1146/annurev.mi.49.100195.003013.
    • (1995) Annu Rev Microbiol , vol.49 , pp. 557-579
    • Frost, J.W.1    Draths, K.M.2
  • 9
    • 80052027792 scopus 로고    scopus 로고
    • Styrene biosynthesis from glucose by engineered E coli.
    • McKenna R, Nielsen DR. 2011. Styrene biosynthesis from glucose by engineered E. coli. Metab Eng 13:544-554. http://dx.doi.org/10.1016/j.ymben.2011.06.005.
    • (2011) Metab Eng , vol.13 , pp. 544-554
    • McKenna, R.1    Nielsen, D.R.2
  • 10
    • 84919787681 scopus 로고    scopus 로고
    • Rational and combinatorial approaches to engineering styrene production by Saccharomyces cerevisiae
    • McKenna R, Thompson B, Pugh S, Nielsen DR. 2014. Rational and combinatorial approaches to engineering styrene production by Saccharomyces cerevisiae. Microb Cell Fact 13:123. http://dx.doi.org/10.1186/s12934-014-0123-2.
    • (2014) Microb Cell Fact , vol.13 , pp. 123
    • McKenna, R.1    Thompson, B.2    Pugh, S.3    Nielsen, D.R.4
  • 12
    • 0027939914 scopus 로고
    • Purification and characterization of a ferulic acid decarboxylase from Pseudomonas fluorescens
    • Huang Z, Dostal L, Rosazza JP. 1994. Purification and characterization of a ferulic acid decarboxylase from Pseudomonas fluorescens. J Bacteriol 176:5912-5918.
    • (1994) J Bacteriol , vol.176 , pp. 5912-5918
    • Huang, Z.1    Dostal, L.2    Rosazza, J.P.3
  • 13
    • 0028226498 scopus 로고
    • PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae
    • Clausen M, Lamb CJ, Megnet R, Doerner PW. 1994. PAD1 encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid in Saccharomyces cerevisiae. Gene 142:107-112. http://dx.doi.org/10.1016/0378-1119(94)90363-8.
    • (1994) Gene , vol.142 , pp. 107-112
    • Clausen, M.1    Lamb, C.J.2    Megnet, R.3    Doerner, P.W.4
  • 14
    • 0028808722 scopus 로고
    • Cloning, sequencing, and expression in Escherichia coli of the Bacillus pumilus gene for ferulic acid decarboxylase
    • Zago A, Degrassi G, Bruschi CV. 1995. Cloning, sequencing, and expression in Escherichia coli of the Bacillus pumilus gene for ferulic acid decarboxylase. Appl Environ Microbiol 61:4484-4486.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4484-4486
    • Zago, A.1    Degrassi, G.2    Bruschi, C.V.3
  • 15
    • 0028890051 scopus 로고
    • Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus
    • Degrassi G, DeLaureto PP, Bruschi CV. 1995. Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus. Appl Environ Microbiol 61:326-332.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 326-332
    • Degrassi, G.1    DeLaureto, P.P.2    Bruschi, C.V.3
  • 16
    • 0031957895 scopus 로고    scopus 로고
    • Gene cloning, transcriptional analysis, purification, and characterization of phenolic acid decarboxylase from Bacillus subtilis
    • Cavin JF, Dartois V, Diviès C. 1998. Gene cloning, transcriptional analysis, purification, and characterization of phenolic acid decarboxylase from Bacillus subtilis. Appl Environ Microbiol 64:1466-1471.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1466-1471
    • Cavin, J.F.1    Dartois, V.2    Diviès, C.3
  • 17
    • 0032533669 scopus 로고    scopus 로고
    • Stereochemically specific proton transfer in decarboxylation of 4-hydroxycinnamic acids by 4-hydroxycinnamate decarboxylase from Klebsiella oxytoca
    • Hashidoko Y, Tahara S. 1998. Stereochemically specific proton transfer in decarboxylation of 4-hydroxycinnamic acids by 4-hydroxycinnamate decarboxylase from Klebsiella oxytoca. Arch Biochem Biophys 359:225-233. http://dx.doi.org/10.1006/abbi.1998.0911.
    • (1998) Arch Biochem Biophys , vol.359 , pp. 225-233
    • Hashidoko, Y.1    Tahara, S.2
  • 19
  • 20
    • 77954689364 scopus 로고    scopus 로고
    • Gene cloning, expression, and characterization of phenolic acid decarboxylase from Lactobacillus brevis RM84
    • Landete JM, Rodríguez H, Curiel JA, de las Rivas B, Mancheño JM, Muñoz R. 2010. Gene cloning, expression, and characterization of phenolic acid decarboxylase from Lactobacillus brevis RM84. J Ind Microbiol Biotechnol 37:617-624. http://dx.doi.org/10.1007/s10295-010-0709-6.
    • (2010) J Ind Microbiol Biotechnol , vol.37 , pp. 617-624
    • Landete, J.M.1    Rodríguez, H.2    Curiel, J.A.3    de las Rivas, B.4    Mancheño, J.M.5    Muñoz, R.6
  • 21
    • 77952110668 scopus 로고    scopus 로고
    • PAD1 and FDC1 are essential for the decarboxylation of phenylacrylic acids in Saccharomyces cerevisiae
    • Mukai N, Masaki K, Fujii T, Kawamukai M, Iefuji H. 2010. PAD1 and FDC1 are essential for the decarboxylation of phenylacrylic acids in Saccharomyces cerevisiae. J Biosci Bioeng 109:564-569. http://dx.doi.org/10.1016/j.jbiosc.2009.11.011.
    • (2010) J Biosci Bioeng , vol.109 , pp. 564-569
    • Mukai, N.1    Masaki, K.2    Fujii, T.3    Kawamukai, M.4    Iefuji, H.5
  • 23
    • 7244244199 scopus 로고    scopus 로고
    • Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157:H7
    • Rangarajan ES, Li Y, Iannuzzi P, Tocilj A, Hung LW, Matte A, Cygler M. 2004. Crystal structure of a dodecameric FMN-dependent UbiX-like decarboxylase (Pad1) from Escherichia coli O157:H7. Protein Sci 13:3006-3016. http://dx.doi.org/10.1110/ps.04953004.
    • (2004) Protein Sci , vol.13 , pp. 3006-3016
    • Rangarajan, E.S.1    Li, Y.2    Iannuzzi, P.3    Tocilj, A.4    Hung, L.W.5    Matte, A.6    Cygler, M.7
  • 24
    • 80955135674 scopus 로고    scopus 로고
    • Structure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa
    • Kopec J, Schnell R, Schneider G. 2011. Structure of PA4019, a putative aromatic acid decarboxylase from Pseudomonas aeruginosa. Acta Crystallogr Sect F Struct Biol Cryst Commun 67:1184-1188. http://dx.doi.org/10.1107/S174430911102923X.
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 1184-1188
    • Kopec, J.1    Schnell, R.2    Schneider, G.3
  • 26
    • 0033815884 scopus 로고    scopus 로고
    • New advances in coenzymeQbiosynthesis
    • Clarke CE. 2000. New advances in coenzymeQbiosynthesis. Protoplasma 213:134-147. http://dx.doi.org/10.1007/BF01282151.
    • (2000) Protoplasma , vol.213 , pp. 134-147
    • Clarke, C.E.1
  • 27
    • 77951242130 scopus 로고    scopus 로고
    • p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism
    • Rodríguez H, Angulo I, de Las Rivas B, Campillo N, Páez JA, Muñoz R, Mancheño JM. 2010. p-Coumaric acid decarboxylase from Lactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism. Proteins 78:1662-1676. http://dx.doi.org/10.1002/prot.22684.
    • (2010) Proteins , vol.78 , pp. 1662-1676
    • Rodríguez, H.1    Angulo, I.2    de Las Rivas, B.3    Campillo, N.4    Páez, J.A.5    Muñoz, R.6    Mancheño, J.M.7
  • 28
  • 29
    • 79251633326 scopus 로고    scopus 로고
    • Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp
    • Gu W, Yang J, Lou Z, Liang L, Sun Y, Huang J, Li X, Cao Y, Meng Z, Zhang KQ. 2011. Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4. PLoS One 6:e16262. http://dx.doi.org/10.1371/journal.pone.0016262.
    • (2011) Px6-4. PLoS One , vol.6
    • Gu, W.1    Yang, J.2    Lou, Z.3    Liang, L.4    Sun, Y.5    Huang, J.6    Li, X.7    Cao, Y.8    Meng, Z.9    Zhang, K.Q.10
  • 30
    • 84877317598 scopus 로고    scopus 로고
    • Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa
    • Jacewicz A, Izumi A, Brunner K, Schnell R, Schneider G. 2013. Structural insights into the UbiD protein family from the crystal structure of PA0254 from Pseudomonas aeruginosa. PLoS One 8:e63161. http://dx.doi.org/10.1371/journal.pone.0063161.
    • (2013) PLoS One , vol.8
    • Jacewicz, A.1    Izumi, A.2    Brunner, K.3    Schnell, R.4    Schneider, G.5
  • 31
    • 0033759208 scopus 로고    scopus 로고
    • Identification of the ubiD gene on the Escherichia coli chromosome
    • Zhang H, Javor GT. 2000. Identification of the ubiD gene on the Escherichia coli chromosome. J Bacteriol 182:6243-6246. http://dx.doi.org/10.1128/JB.182.21.6243-6246.2000.
    • (2000) J Bacteriol , vol.182 , pp. 6243-6246
    • Zhang, H.1    Javor, G.T.2
  • 32
    • 23244446480 scopus 로고    scopus 로고
    • Distribution of genes encoding the microbial non-oxidative reversible hydroxyarylic acid decarboxylases/phenol decarboxylases
    • Lupa B, Lyon D, Gibbs MD, Reeves RA, Wiegel J. 2005. Distribution of genes encoding the microbial non-oxidative reversible hydroxyarylic acid decarboxylases/phenol decarboxylases. Genomics 86:342-351. http://dx.doi.org/10.1016/j.ygeno.2005.05.002.
    • (2005) Genomics , vol.86 , pp. 342-351
    • Lupa, B.1    Lyon, D.2    Gibbs, M.D.3    Reeves, R.A.4    Wiegel, J.5
  • 33
    • 3042661951 scopus 로고    scopus 로고
    • Rapid isolation of yeast genomic DNA: bust n' grab
    • Harju S, Fedosyuk H, Peterson KR. 2004. Rapid isolation of yeast genomic DNA: bust n' grab. BMC Biotechnol 4:8. http://dx.doi.org/10.1186/1472-6750-4-8.
    • (2004) BMC Biotechnol , vol.4 , pp. 8
    • Harju, S.1    Fedosyuk, H.2    Peterson, K.R.3
  • 34
    • 33745933955 scopus 로고    scopus 로고
    • HKL- 3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes
    • Minor W, Cymborowski M, Otwinowski Z, Chruszcz M. 2006. HKL- 3000: the integration of data reduction and structure solution-from diffraction images to an initial model in minutes. Acta Crystallogr SectDBiol Crystallogr 62:859-866. http://dx.doi.org/10.1107/S0907444906019949.
    • (2006) Acta Crystallogr SectDBiol Crystallogr , vol.62 , pp. 859-866
    • Minor, W.1    Cymborowski, M.2    Otwinowski, Z.3    Chruszcz, M.4
  • 36
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukurai A, Zhang Y. 2010. I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5:725-738. http://dx.doi.org/10.1038/nprot.2010.5.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukurai, A.2    Zhang, Y.3
  • 39
    • 76149120388 scopus 로고    scopus 로고
    • AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading
    • Trott O, Olson AJ. 2010. AutoDock Vina: improving the speed and accuracy of docking with a new scoring function, efficient optimization, and multithreading. J Comp Chem 31:455-461. http://dx.doi.org/10.1002/jcc.21334.
    • (2010) J Comp Chem , vol.31 , pp. 455-461
    • Trott, O.1    Olson, A.J.2
  • 40
    • 84874601304 scopus 로고    scopus 로고
    • Structural characterization of amorfrutins bound to the peroxisome proliferator-activated receptor γ
    • de Groot JC, Weidner C, Krausze J, Kawamoto K, Schroeder FC, Sauer S, Büssow K. 2013. Structural characterization of amorfrutins bound to the peroxisome proliferator-activated receptor γ. J Med Chem 56:1535-1543. http://dx.doi.org/10.1021/jm3013272.
    • (2013) J Med Chem , vol.56 , pp. 1535-1543
    • de Groot, J.C.1    Weidner, C.2    Krausze, J.3    Kawamoto, K.4    Schroeder, F.C.5    Sauer, S.6    Büssow, K.7
  • 41
    • 77954288774 scopus 로고    scopus 로고
    • Dali server: conservation mapping in 3D
    • Holm L, Rosenström P. 2010. Dali server: conservation mapping in 3D. Nucleic Acids Res 38:W545-W549. http://dx.doi.org/10.1093/nar/gkq366.
    • (2010) Nucleic Acids Res , vol.38 , pp. W545-W549
    • Holm, L.1    Rosenström, P.2
  • 42
    • 84887624536 scopus 로고    scopus 로고
    • Pathway and protein engineering approaches to produce novel and commodity small molecules
    • Bhan N, Xu P, Koffas MA. 2013. Pathway and protein engineering approaches to produce novel and commodity small molecules. Curr Opin Biotechnol 24:1137-1143. http://dx.doi.org/10.1016/j.copbio.2013.02.019.
    • (2013) Curr Opin Biotechnol , vol.24 , pp. 1137-1143
    • Bhan, N.1    Xu, P.2    Koffas, M.A.3
  • 43
    • 84891871419 scopus 로고    scopus 로고
    • Molecular engineering of industrial enzymes: recent advances and future prospects
    • Yang H, Li J, Shin HD, Du G, Liu L, Chen J. 2014. Molecular engineering of industrial enzymes: recent advances and future prospects. Appl Microbiol Biotechnol 98:23-29. http://dx.doi.org/10.1007/s00253-013-5370-3.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 23-29
    • Yang, H.1    Li, J.2    Shin, H.D.3    Du, G.4    Liu, L.5    Chen, J.6
  • 44
    • 0035293855 scopus 로고    scopus 로고
    • Expression in Escherichia coli of native and chimeric phenolic acid decarboxylases with modified enzymatic activities and method for screening recombinant E coli strains expressing these enzymes.
    • Barthelmebs L, Diviès C, Cavin JF. 2001. Expression in Escherichia coli of native and chimeric phenolic acid decarboxylases with modified enzymatic activities and method for screening recombinant E. coli strains expressing these enzymes. Appl Environ Microbiol 67:1063-1069. http://dx.doi.org/10.1128/AEM.67.3.1063-1069.2001.
    • (2001) Appl Environ Microbiol , vol.67 , pp. 1063-1069
    • Barthelmebs, L.1    Diviès, C.2    Cavin, J.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.