메뉴 건너뛰기




Volumn 2, Issue 1, 2012, Pages 1-10

An endogenous factor enhances ferulic acid decarboxylation catalyzed by phenolic acid decarboxylase from Candida guilliermondii

Author keywords

activator; Candida guilliermondii; ferulic acid decarboxylase; p coumaric acid decarboxylase; phenolic acid decarboxylase

Indexed keywords

AMINO ACID; CARBOXYLYASE; CELL EXTRACT; FERULIC ACID; FUNGAL ENZYME; FUNGAL PROTEIN; PARA COUMARIC ACID; PHENOLIC ACID DECARBOXYLASE; THIOL; UNCLASSIFIED DRUG;

EID: 84863125606     PISSN: None     EISSN: 21910855     Source Type: Journal    
DOI: 10.1186/2191-0855-2-4     Document Type: Article
Times cited : (16)

References (43)
  • 1
    • 84985273059 scopus 로고
    • Inhibition of Saccharomyces cerevisiae by naturally occurring hydroxycinnamates
    • Baranowski JD, Davidson PM, Nagel CW, Branen AL: Inhibition ofSaccharomyces cerevisiaeby naturally occurring hydroxycinnamates. J Food Sci 1980, 45: 592-594.
    • (1980) J Food Sci , vol.45 , pp. 592-594
    • Baranowski, J.D.1    Davidson, P.M.2    Nagel, C.W.3    Branen, A.L.4
  • 2
    • 0034461483 scopus 로고    scopus 로고
    • Inducible metabolism of phenolic acids in Pediococcus pentosaceus is encoded by an autoregulated operon which involves a new class of negative transcriptional regulator
    • Barthelmebs L, Lecomte B, Diviès C, Cavin JF: Inducible metabolism of phenolic acids inPediococcus pentosaceusis encoded by an autoregulated operon which involves a new class of negative transcriptional regulator. J Bacteriol 2000, 182: 6724-6731.
    • (2000) J Bacteriol , vol.182 , pp. 6724-6731
    • Barthelmebs, L.1    Lecomte, B.2    Diviès, C.3    Cavin, J.F.4
  • 3
    • 33646809781 scopus 로고    scopus 로고
    • The sulfur-containing amino acids: an overview
    • Brosnan JT, Brosnan ME: The sulfur-containing amino acids: an overview. J Nutr 2006, 136: 1636S-1640S.
    • (2006) J Nutr , vol.136
    • Brosnan, J.T.1    Brosnan, M.E.2
  • 4
    • 0030902352 scopus 로고    scopus 로고
    • Molecular characterization of an inducible p-coumaric acid decarboxylase from Lactobacillus plantarum: gene cloning, transcriptional analysis, overexpression in Escherichia coli, purification and characterization
    • Cavin JF, Barthelmebs L, Diviès C: Molecular characterization of an induciblep-coumaric acid decarboxylase fromLactobacillus plantarum: gene cloning, transcriptional analysis, overexpression inEscherichia coli, purification and characterization. Appl Environ Microbiol 1997a, 63: 1939-1944.
    • (1997) Appl Environ Microbiol , vol.63 , pp. 1939-1944
    • Cavin, J.F.1    Barthelmebs, L.2    Diviès, C.3
  • 6
    • 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: Gene cloning, transcriptional analysis, purification, and characterization of phenolic acid decarboxylase fromBacillus subtilis. Appl Environ Microbiol 1998, 64: 1466-1471.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 1466-1471
    • Cavin, J.F.1    Dartois, V.2    Diviès, C.3
  • 7
    • 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: PAD1encodes phenylacrylic acid decarboxylase which confers resistance to cinnamic acid inSaccharomyces cerevisiae. Gene 1994, 142: 107-112.
    • (1994) Gene , vol.142 , pp. 107-112
    • Clausen, M.1    Lamb, C.J.2    Megnet, R.3    Doerner, P.W.4
  • 8
    • 0842327894 scopus 로고    scopus 로고
    • Ferulic acid release and 4-vinylguaiacol formation during brewing and fermentation: indications for feruloyl esterase activity in Saccharomyces cerevisiae
    • Coghe S, Benoot K, Delvaux F, Vanderhaegen B, Delvaux FR: Ferulic acid release and 4-vinylguaiacol formation during brewing and fermentation: indications for feruloyl esterase activity inSaccharomyces cerevisiae. J Agric Food Chem 2004, 52: 602-608.
    • (2004) J Agric Food Chem , vol.52 , pp. 602-608
    • Coghe, S.1    Benoot, K.2    Delvaux, F.3    Vanderhaegen, B.4    Delvaux, F.R.5
  • 9
    • 0028890051 scopus 로고
    • Purification and characterization of ferulate and p-coumarate decarboxylase from Bacillus pumilus
    • Degrassi G, Polverino de Laureto P, Bruschi CV: Purification and characterization of ferulate andp-coumarate decarboxylase fromBacillus pumilus. Appl Environ Microbiol 1995, 61: 326-332.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 326-332
    • Degrassi, G.1    Polverino de Laureto, P.2    Bruschi, C.V.3
  • 10
    • 0032030542 scopus 로고    scopus 로고
    • Purification and characterization of hydroxycinnamate decarboxylase from Brettanomyces anomalus
    • Edlin DAN, Narbad A, Gasson MJ, Dickinson JR, Lloyd D: Purification and characterization of hydroxycinnamate decarboxylase fromBrettanomyces anomalus. Enzyme Microb Technol 1998, 22: 232-239.
    • (1998) Enzyme Microb Technol , vol.22 , pp. 232-239
    • Edlin, D.A.N.1    Narbad, A.2    Gasson, M.J.3    Dickinson, J.R.4    Lloyd, D.5
  • 11
    • 0021830125 scopus 로고
    • Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation
    • Estell DA, Graycar TP, Wells JA: Engineering an enzyme by site-directed mutagenesis to be resistant to chemical oxidation. J Biol Chem 1985, 260: 6518-6521.
    • (1985) J Biol Chem , vol.260 , pp. 6518-6521
    • Estell, D.A.1    Graycar, T.P.2    Wells, J.A.3
  • 12
    • 50949122613 scopus 로고    scopus 로고
    • Purification and characterization of a p-coumarate decarboxylase and a vinylphenol reductase from Brettanomyces bruxellensis
    • Godoy L, Martínez C, Carrasco N, Ganga MA: Purification and characterization of ap-coumarate decarboxylase and a vinylphenol reductase fromBrettanomyces bruxellensis. Int J Food Microbiol 2008, 127: 6-11.
    • (2008) Int J Food Microbiol , vol.127 , pp. 6-11
    • Godoy, L.1    Martínez, C.2    Carrasco, N.3    Ganga, M.A.4
  • 13
    • 0020466394 scopus 로고
    • Genetic and biochemical analysis of the ability of Saccharomyces cerevisiae to decarboxylate cinnamic acids
    • Goodey AR, Tubb RS: Genetic and biochemical analysis of the ability ofSaccharomyces cerevisiaeto decarboxylate cinnamic acids. J Gen Microbiol 1982, 128: 2615-2620.
    • (1982) J Gen Microbiol , vol.128 , pp. 2615-2620
    • Goodey, A.R.1    Tubb, R.S.2
  • 14
    • 79952574595 scopus 로고    scopus 로고
    • Cloning, sequencing, and overexpression in Escherichia coli of the Enterobacter sp. Px6-4 gene for ferulic acid decarboxylase
    • Gu W, Li X, Huang J, Duan Y, Meng Z, Zhang KQ, Yang J: Cloning, sequencing, and overexpression inEscherichia coliof theEnterobactersp. Px6-4 gene for ferulic acid decarboxylase. Appl Microbiol Biotechnol 2011a, 89: 1797-1805.
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1797-1805
    • Gu, W.1    Li, X.2    Huang, J.3    Duan, Y.4    Meng, Z.5    Zhang, K.Q.6    Yang, J.7
  • 15
    • 79251633326 scopus 로고    scopus 로고
    • Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) from Enterobacter sp. Px6-4
    • Gu W, Yang J, Lou Z, Liang L, Sun Y, Huang J, Li X, Cao Y, Meng Z, Zhang KQ: Structural basis of enzymatic activity for the ferulic acid decarboxylase (FADase) fromEnterobactersp. Px6-4. PLoS ONE 2011b, 6(1): e16262.
    • (2011) PLoS ONE , vol.6 , Issue.1
    • 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
  • 16
    • 68549101804 scopus 로고    scopus 로고
    • Inactivation of PadR, the repressor of the phenolic acid stress response, by molecular interaction with Usp1, a universal stress protein from Lactobacillus plantarum, in Escherichia coli
    • Gury J, Seraut H, Tran NP, Barthelmebs L, Weidmann S, Gervais P, Cavin JF: Inactivation of PadR, the repressor of the phenolic acid stress response, by molecular interaction with Usp1, a universal stress protein fromLactobacillus plantarum, inEscherichia coli. Appl Environ Microbiol 2009, 75: 5273-5283.
    • (2009) Appl Environ Microbiol , vol.75 , pp. 5273-5283
    • Gury, J.1    Seraut, H.2    Tran, N.P.3    Barthelmebs, L.4    Weidmann, S.5    Gervais, P.6    Cavin, J.F.7
  • 17
    • 33846262073 scopus 로고    scopus 로고
    • Oxidative stabilization of an alkaliphilic Bacillus α-amylase by replacing single specific methionine residue by site-directed mutagenesis
    • Hagihara H, Hatada Y, Ozawa T, Igarashi K, Araki H, Ozaki K, Kobayashi T, Kawai S, Ito S: Oxidative stabilization of an alkaliphilicBacillusα-amylase by replacing single specific methionine residue by site-directed mutagenesis. J Appl Glycosci 2003, 50: 367-372.
    • (2003) J Appl Glycosci , vol.50 , pp. 367-372
    • Hagihara, H.1    Hatada, Y.2    Ozawa, T.3    Igarashi, K.4    Araki, H.5    Ozaki, K.6    Kobayashi, T.7    Kawai, S.8    Ito, S.9
  • 18
    • 0034836495 scopus 로고    scopus 로고
    • Deduced amino-acid sequence of a calcium-free α-amylase from a strain of Bacillus. Implications from molecular modeling of high oxidation stability and chelator resistance of the enzyme
    • Hagihara H, Hayashi Y, Endo K, Igarashi K, Ozawa T, Kawai S, Ozaki K, Ito S: Deduced amino-acid sequence of a calcium-free α-amylase from a strain ofBacillus. Implications from molecular modeling of high oxidation stability and chelator resistance of the enzyme. Eur J Biochem 2001, 268: 3974-3982.
    • (2001) Eur J Biochem , vol.268 , pp. 3974-3982
    • Hagihara, H.1    Hayashi, Y.2    Endo, K.3    Igarashi, K.4    Ozawa, T.5    Kawai, S.6    Ozaki, K.7    Ito, S.8
  • 19
    • 84857626532 scopus 로고    scopus 로고
    • Purification and properties of phenolic acid decarboxylase from Candida guilliermondii
    • doi:10.1007/s10295-011-0998-4
    • Huang HK, Tokashiki M, Maeno S, Onaga S, Taira T, Ito S: Purification and properties of phenolic acid decarboxylase fromCandida guilliermondii. J Ind Microbiol Biotechnol 2011. doi: 10. 1007/s10295-011-0998-4.
    • (2011) J Ind Microbiol Biotechnol
    • Huang, H.K.1    Tokashiki, M.2    Maeno, S.3    Onaga, S.4    Taira, T.5    Ito, S.6
  • 20
    • 0027939914 scopus 로고
    • Purification and characterization of a ferulic acid decarboxylase from Pseudomonas fluorescens
    • Huang Z, Dostal L, Rosazza JP: Purification and characterization of a ferulic acid decarboxylase fromPseudomonas fluorescens. J Bacteriol 1994, 176: 5912-5918.
    • (1994) J Bacteriol , vol.176 , pp. 5912-5918
    • Huang, Z.1    Dostal, L.2    Rosazza, J.P.3
  • 21
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch W, Sander C: Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 1983, 22: 2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 22
    • 76649127721 scopus 로고    scopus 로고
    • Phylogenetic analysis of ascomycete yeasts that form coenzymeQ-9 and the proposal of the new genera Babjeviella, Meyerozyma, Millerozyma, Priceomyces, and Scheffersomyces
    • Kurtzman CP, Suzuki M: Phylogenetic analysis of ascomycete yeasts that form coenzymeQ-9 and the proposal of the new generaBabjeviella, Meyerozyma, Millerozyma, Priceomyces, andScheffersomyces. Mycoscience 2010, 51: 2-14.
    • (2010) Mycoscience , vol.51 , pp. 2-14
    • Kurtzman, C.P.1    Suzuki, M.2
  • 24
    • 4444320433 scopus 로고    scopus 로고
    • Ferulic acid: an antioxidant found naturally in plant cell walls and feruloyl esterases involved in its release and their applications
    • Mathew S, Abraham TE: Ferulic acid: an antioxidant found naturally in plant cell walls and feruloyl esterases involved in its release and their applications. Crit Rev Biotechnol 2004, 24: 59-83.
    • (2004) Crit Rev Biotechnol , vol.24 , pp. 59-83
    • Mathew, S.1    Abraham, T.E.2
  • 25
    • 33747098188 scopus 로고    scopus 로고
    • Bioconversions of ferulic acid, a hydroxycinnamic acid
    • Mathew S, Abraham TE: Bioconversions of ferulic acid, a hydroxycinnamic acid. Crit Rev Microbiol 2006, 32: 115-125.
    • (2006) Crit Rev Microbiol , vol.32 , pp. 115-125
    • Mathew, S.1    Abraham, T.E.2
  • 26
    • 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: PAD1andFDC1are essential for the decarboxylation of phenylacrylic acids inSaccharomyces cerevisiae. J Biosci Bioeng 2010, 109: 564-569.
    • (2010) J Biosci Bioeng , vol.109 , pp. 564-569
    • Mukai, N.1    Masaki, K.2    Fujii, T.3    Kawamukai, M.4    Iefuji, H.5
  • 27
    • 0042090311 scopus 로고    scopus 로고
    • Crystal structure of calcium-free α-amylase from Bacillus sp. strain KSM-K38 (AmyK38) and its sodium ion binding sites
    • Nonaka T, Fujihashi M, Kita A, Hagihara H, Ozaki K, Ito S, Miki K: Crystal structure of calcium-free α-amylase fromBacillussp. strain KSM-K38 (AmyK38) and its sodium ion binding sites. J Biol Chem 2003, 278: 24818-24824.
    • (2003) J Biol Chem , vol.278 , pp. 24818-24824
    • Nonaka, T.1    Fujihashi, M.2    Kita, A.3    Hagihara, H.4    Ozaki, K.5    Ito, S.6    Miki, K.7
  • 28
    • 8744220594 scopus 로고    scopus 로고
    • The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal β-barrel domain
    • Nonaka T, Fujihashi M, Kita A, Saeki K, Ito S, Horikoshi K, Miki K: The crystal structure of an oxidatively stable subtilisin-like alkaline serine protease, KP-43, with a C-terminal β-barrel domain. J Biol Chem 2004, 279: 47344-47351.
    • (2004) J Biol Chem , vol.279 , pp. 47344-47351
    • Nonaka, T.1    Fujihashi, M.2    Kita, A.3    Saeki, K.4    Ito, S.5    Horikoshi, K.6    Miki, K.7
  • 29
    • 70349865217 scopus 로고    scopus 로고
    • Significance of Brettanomyces and Dekkera during winemaking: a synoptic review
    • Oelofse A, Pretorius IS, du Toit M: Significance ofBrettanomycesandDekkeraduring winemaking: a synoptic review. S Afr J Enol Vitic 2008, 29: 128-144.
    • (2008) S Afr J Enol Vitic , vol.29 , pp. 128-144
    • Oelofse, A.1    Pretorius, I.S.2    Du Toit, M.3
  • 30
    • 78651087662 scopus 로고    scopus 로고
    • Inhibitory action of toxic compounds present in lignocellulosic hydrolysates on xylose to xylitol bioconversion by Candida guilliermondii
    • Pereira RS, Mussatto SI, Roberto IC: Inhibitory action of toxic compounds present in lignocellulosic hydrolysates on xylose to xylitol bioconversion byCandida guilliermondii. J Ind Microbiol Biotechnol 2011, 38: 71-78.
    • (2011) J Ind Microbiol Biotechnol , vol.38 , pp. 71-78
    • Pereira, R.S.1    Mussatto, S.I.2    Roberto, I.C.3
  • 32
    • 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: p-Coumaric acid decarboxylase fromLactobacillus plantarum: structural insights into the active site and decarboxylation catalytic mechanism. Proteins 2010, 78: 1662-1676.
    • (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
  • 33
    • 34447280364 scopus 로고    scopus 로고
    • Detergent alkaline proteases: enzymatic properties, genes, and crystal structures
    • Saeki K, Ozaki K, Kobayashi T, Ito S: Detergent alkaline proteases: enzymatic properties, genes, and crystal structures. J Biosci Bioeng 2007, 103: 501-508.
    • (2007) J Biosci Bioeng , vol.103 , pp. 501-508
    • Saeki, K.1    Ozaki, K.2    Kobayashi, T.3    Ito, S.4
  • 34
    • 77954479044 scopus 로고    scopus 로고
    • Enhanced volatile phenols in wine fermented with Saccharomyces cerevisiae and spoiled with Pichia guilliermondii and Dekkera bruxellensis
    • Sáez JS, Lopes CA, Kirs VC, Sangorrín MP: Enhanced volatile phenols in wine fermented withSaccharomyces cerevisiaeand spoiled withPichia guilliermondiiandDekkera bruxellensis. Lett Appl Microbiol 2010, 51: 170-176.
    • (2010) Lett Appl Microbiol , vol.51 , pp. 170-176
    • Sáez, J.S.1    Lopes, C.A.2    Kirs, V.C.3    Sangorrín, M.P.4
  • 35
    • 0027136282 scopus 로고
    • Comparative protein modeling by satisfaction of spatial restraints
    • Sali A, Blundell TL: Comparative protein modeling by satisfaction of spatial restraints. J Mol Biol 1993, 234: 779-815.
    • (1993) J Mol Biol , vol.234 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 36
    • 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: Enhancing volatile phenol concentrations in wine by expressing various phenolic acid decarboxylase genes inSaccharomyces cerevisiae. J Agric Food Chem 2003, 51: 4909-4915.
    • (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
  • 37
    • 0028937079 scopus 로고
    • The effect of hydroxycinnamic acids and potassium sorbate on the growth of 11 strains of spoilage yeasts
    • Stead D: The effect of hydroxycinnamic acids and potassium sorbate on the growth of 11 strains of spoilage yeasts. J Appl Microbiol 1995, 78: 82-87.
    • (1995) J Appl Microbiol , vol.78 , pp. 82-87
    • Stead, D.1
  • 38
    • 0009704509 scopus 로고
    • Evidence for nonidentical chains in the β-galactosidase of Escherichia coli K12
    • Steers E Jr, Craven GR, Anfinsen CB: Evidence for nonidentical chains in the β-galactosidase ofEscherichia coliK12. J Biol Chem 1965, 240: 2478-2484.
    • (1965) J Biol Chem , vol.240 , pp. 2478-2484
    • Steers Jr., E.1    Craven, G.R.2    Anfinsen, C.B.3
  • 39
    • 0031574072 scopus 로고    scopus 로고
    • The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG: The Clustal_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucl Acids Res 1997, 25: 4876-4882.
    • (1997) Nucl Acids Res , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 40
    • 84979437796 scopus 로고
    • Screening yeast strains for their ability to produce phenolic off-flavours: a simple method for determining phenols in wort and beer
    • Thurston PA, Tubb RS: Screening yeast strains for their ability to produce phenolic off-flavours: a simple method for determining phenols in wort and beer. J Inst Brew 1981, 87: 177-179.
    • (1981) J Inst Brew , vol.87 , pp. 177-179
    • Thurston, P.A.1    Tubb, R.S.2
  • 42
    • 38549120650 scopus 로고    scopus 로고
    • Identification of the 4-hydroxycinnamate decarboxylase (PAD) gene of Klebsiella oxytoca
    • Uchiyama H, Hashidoko Y, Kuriyama Y, Tahara S: Identification of the 4-hydroxycinnamate decarboxylase (PAD) gene ofKlebsiella oxytoca. Biosci Biotechnol Biochem 2008, 72: 116-123.
    • (2008) Biosci Biotechnol Biochem , vol.72 , pp. 116-123
    • Uchiyama, H.1    Hashidoko, Y.2    Kuriyama, Y.3    Tahara, S.4
  • 43
    • 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: Cloning, sequencing, and expression inEscherichia coliof theBacillus pumilusgene for ferulic acid decarboxylase. Appl Environ Microbiol 1995, 61: 4484-4486.
    • (1995) Appl Environ Microbiol , vol.61 , pp. 4484-4486
    • Zago, A.1    Degrassi, G.2    Bruschi, C.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.