메뉴 건너뛰기




Volumn 338, Issue 3, 2004, Pages 495-506

The crystal structure of feruloyl esterase A from Aspergillus niger suggests evolutive functional convergence in feruloyl esterase family

Author keywords

AnFaeA, feruloyl esterase A from Aspergillus niger; Aspergillus niger; Crystal structure; Feruloyl esterase; MCA, methyl ester of caffeic acid; MFA, methyl ester of ferulic acid; MpCA, methyl ester of p coumaric acid; Plant cell degradation

Indexed keywords

ARABINOXYLAN; FERULIC ACID; FERULOYL ESTERASE A; FUNGAL ENZYME; HYDROLASE; TRIACYLGLYCEROL LIPASE; UNCLASSIFIED DRUG;

EID: 1842686201     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.003     Document Type: Article
Times cited : (109)

References (57)
  • 1
    • 0035141873 scopus 로고    scopus 로고
    • Wall structure and wall loosening. A look backwards and forwards
    • Cosgrove D.J. Wall structure and wall loosening. A look backwards and forwards. Plant Physiol. 125:2001;131-134.
    • (2001) Plant Physiol. , vol.125 , pp. 131-134
    • Cosgrove, D.J.1
  • 2
    • 0033214507 scopus 로고    scopus 로고
    • A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex
    • Fillingham I.J., Kroon P.A., Williamson G., Gilbert H.J., Hazlewood G.P. A modular cinnamoyl ester hydrolase from the anaerobic fungus Piromyces equi acts synergistically with xylanase and is part of a multiprotein cellulose-binding cellulase-hemicellulase complex. Biochem. J. 343:1999;215-224.
    • (1999) Biochem. J. , vol.343 , pp. 215-224
    • Fillingham, I.J.1    Kroon, P.A.2    Williamson, G.3    Gilbert, H.J.4    Hazlewood, G.P.5
  • 3
    • 0033983751 scopus 로고    scopus 로고
    • Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ
    • Blum D.L., Kataeva I.A., Li X.-L., Ljungdahl L.G. Feruloyl esterase activity of the Clostridium thermocellum cellulosome can be attributed to previously unknown domains of XynY and XynZ. J. Bacteriol. 182:2000;1346-1351.
    • (2000) J. Bacteriol. , vol.182 , pp. 1346-1351
    • Blum, D.L.1    Kataeva, I.A.2    Li, X.-L.3    Ljungdahl, L.G.4
  • 4
    • 0035199524 scopus 로고    scopus 로고
    • Aspergillus enzymes involved in degradation of plant cell wall polysaccharides
    • de Vries R.P., Visser J. Aspergillus enzymes involved in degradation of plant cell wall polysaccharides. Microb. Mol. Biol. Rev. 65:2001;497-522.
    • (2001) Microb. Mol. Biol. Rev. , vol.65 , pp. 497-522
    • De Vries, R.P.1    Visser, J.2
  • 6
    • 0017228954 scopus 로고
    • Detection of bound ferulic acid in cell walls of the Gramineae by ultraviolet fluorescence microscopy
    • Harris P.J., Hartley R.D. Detection of bound ferulic acid in cell walls of the Gramineae by ultraviolet fluorescence microscopy. Nature. 259:1977;508-510.
    • (1977) Nature , vol.259 , pp. 508-510
    • Harris, P.J.1    Hartley, R.D.2
  • 7
    • 46149133474 scopus 로고
    • Feruloylated pectic substances from sugar-beet pulp
    • Rombouts F.M., Thibault J.-F. Feruloylated pectic substances from sugar-beet pulp. Carbohydr. Res. 154:1986;177-187.
    • (1986) Carbohydr. Res. , vol.154 , pp. 177-187
    • Rombouts, F.M.1    Thibault, J.-F.2
  • 8
    • 0020134357 scopus 로고
    • Phenolic components of the primary cell wall
    • Fry S.C. Phenolic components of the primary cell wall. Biochem. J. 203:1982;493-504.
    • (1982) Biochem. J. , vol.203 , pp. 493-504
    • Fry, S.C.1
  • 9
    • 0025068644 scopus 로고
    • Feruloylated xyloglucan and p-coumaroyl arabinoxylan oligosaccharides from bamboo shoot cell-walls
    • Ishii T., Hiroi T., Thomas J.R. Feruloylated xyloglucan and p-coumaroyl arabinoxylan oligosaccharides from bamboo shoot cell-walls. Phytochemistry. 29:1990;1999-2003.
    • (1990) Phytochemistry , vol.29 , pp. 1999-2003
    • Ishii, T.1    Hiroi, T.2    Thomas, J.R.3
  • 10
    • 0029854451 scopus 로고    scopus 로고
    • The wall-bound phenolics of Chinese water chestnut (Eleocharis dulcis)
    • Parr A.J., Waldron K.W., Ng A., Parker M.J. The wall-bound phenolics of Chinese water chestnut (Eleocharis dulcis). J. Sci. Fd Agric. 71:1996;501-507.
    • (1996) J. Sci. Fd Agric. , vol.71 , pp. 501-507
    • Parr, A.J.1    Waldron, K.W.2    Ng, A.3    Parker, M.J.4
  • 11
    • 0028935268 scopus 로고
    • Hydroxycinnamic-acid polymers constitute the polyaromatic domain of suberin
    • Bernards M.A., Lopez M.L., Zajicek J., Lewis N.G. Hydroxycinnamic-acid polymers constitute the polyaromatic domain of suberin. J. Biol. Chem. 270:1995;7382-7386.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7382-7386
    • Bernards, M.A.1    Lopez, M.L.2    Zajicek, J.3    Lewis, N.G.4
  • 12
    • 0028518951 scopus 로고
    • Structure identification of feruloylated oligosaccharides from sugar-beet pulp by NMR spectroscopy
    • Colquhoun I.J., Ralet M.-C., Thibault J.-F., Faulds C.B., Williamson G. Structure identification of feruloylated oligosaccharides from sugar-beet pulp by NMR spectroscopy. Carbohydr. Res. 263:1994;243-256.
    • (1994) Carbohydr. Res. , vol.263 , pp. 243-256
    • Colquhoun, I.J.1    Ralet, M.-C.2    Thibault, J.-F.3    Faulds, C.B.4    Williamson, G.5
  • 13
    • 0035873049 scopus 로고    scopus 로고
    • Diferulates as structural components in soluble and insoluble cereal dietary fibre
    • Bunzel M., Ralph J., Marita J.M., Hatfield R.D., Steinhart H. Diferulates as structural components in soluble and insoluble cereal dietary fibre. J. Sci. Fd Agric. 81:2001;653-660.
    • (2001) J. Sci. Fd Agric. , vol.81 , pp. 653-660
    • Bunzel, M.1    Ralph, J.2    Marita, J.M.3    Hatfield, R.D.4    Steinhart, H.5
  • 14
    • 0027611199 scopus 로고
    • Esterases of xylan-degradating microorganisms: Production, properties, and significance
    • Christov L.P., Prior B.A. Esterases of xylan-degradating microorganisms: production, properties, and significance. Enzyme Microb. Technol. 15:1993;460-475.
    • (1993) Enzyme Microb. Technol. , vol.15 , pp. 460-475
    • Christov, L.P.1    Prior, B.A.2
  • 15
    • 0028218853 scopus 로고
    • Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: Specificity for the phenolic moiety and binding to micro-crystalline cellulose
    • Faulds C.B., Williamson G. Purification and characterization of a ferulic acid esterase (FAE-III) from Aspergillus niger: specificity for the phenolic moiety and binding to micro-crystalline cellulose. Microbiology. 140:1994;779-787.
    • (1994) Microbiology , vol.140 , pp. 779-787
    • Faulds, C.B.1    Williamson, G.2
  • 17
    • 0025954878 scopus 로고
    • The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes
    • Faulds C.B., Williamson G. The purification and characterization of 4-hydroxy-3-methoxycinnamic (ferulic) acid esterase from Streptomyces olivochromogenes. J. Gen. Microbiol. 137:1991;2339-2345.
    • (1991) J. Gen. Microbiol. , vol.137 , pp. 2339-2345
    • Faulds, C.B.1    Williamson, G.2
  • 19
    • 0035181636 scopus 로고    scopus 로고
    • Esterase activity able to hydrolyze dietary antioxidant hydroxycinnamates is distributed along the intestine of mammals
    • Andreasen M.F., Kroon P.A., Williamson G., Garcia-Conesa M.T. Esterase activity able to hydrolyze dietary antioxidant hydroxycinnamates is distributed along the intestine of mammals. J. Agric. Fd Chem. 49:2001;5679-5684.
    • (2001) J. Agric. Fd Chem. , vol.49 , pp. 5679-5684
    • Andreasen, M.F.1    Kroon, P.A.2    Williamson, G.3    Garcia-Conesa, M.T.4
  • 20
    • 0030847038 scopus 로고    scopus 로고
    • Methyl phenylalkanoates as substrates to probe the active site of esterases
    • Kroon P.A., Faulds C.B., Brezillon C., Williamson G. Methyl phenylalkanoates as substrates to probe the active site of esterases. Eur. J. Biochem. 248:1997;245-251.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 245-251
    • Kroon, P.A.1    Faulds, C.B.2    Brezillon, C.3    Williamson, G.4
  • 22
    • 0028892406 scopus 로고
    • Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger
    • Faulds C.B., Williamson G. Release of ferulic acid from wheat bran by a ferulic acid esterase (FAE-III) from Aspergillus niger. Appl. Microbiol. Biotechnol. 43:1995;1082-1087.
    • (1995) Appl. Microbiol. Biotechnol. , vol.43 , pp. 1082-1087
    • Faulds, C.B.1    Williamson, G.2
  • 23
    • 0029888799 scopus 로고    scopus 로고
    • Purification and characterization of a novel ferulic acid esterase induced by growth of Aspergillus niger on sugarbeet pulp
    • Kroon P.A., Faulds C.B., Williamson G. Purification and characterization of a novel ferulic acid esterase induced by growth of Aspergillus niger on sugarbeet pulp. Biotechnol. Appl. Biochem. 23:1996;255-262.
    • (1996) Biotechnol. Appl. Biochem. , vol.23 , pp. 255-262
    • Kroon, P.A.1    Faulds, C.B.2    Williamson, G.3
  • 24
    • 0035666321 scopus 로고    scopus 로고
    • The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition
    • Prates J.A.M., Tarbouriech N., Charnock S.J., Fontes C.M.G.A., Ferreira L.M.A., Davies G.J. The structure of the feruloyl esterase module of xylanase 10B from Clostridium thermocellum provides insights into substrate recognition. Structure. 9:2001;1183-1190.
    • (2001) Structure , vol.9 , pp. 1183-1190
    • Prates, J.A.M.1    Tarbouriech, N.2    Charnock, S.J.3    Fontes, C.M.G.A.4    Ferreira, L.M.A.5    Davies, G.J.6
  • 25
    • 0035940512 scopus 로고    scopus 로고
    • Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum
    • Schubot F.D., Kataeva I.A., Blum D.L., Shah A.C., Ljungdahl L.G., Rose J.P., Wang B.-C. Structural basis for the substrate specificity of the feruloyl esterase domain of the cellulosomal xylanase Z from Clostridium thermocellum. Biochemistry. 40:2001;12524-12532.
    • (2001) Biochemistry , vol.40 , pp. 12524-12532
    • Schubot, F.D.1    Kataeva, I.A.2    Blum, D.L.3    Shah, A.C.4    Ljungdahl, L.G.5    Rose, J.P.6    Wang, B.-C.7
  • 27
    • 0031033383 scopus 로고    scopus 로고
    • An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (XylD) release a 5,5′ ferulic acid dehydrodimers (diferulic acid) from barley and wheat cell walls
    • Bartolomé B., Faulds C.B., Kroon P.A., Waldron K.W., Gilbert H.J., Hazlewood G.P., Williamson G. An Aspergillus niger esterase (ferulic acid esterase III) and a recombinant Pseudomonas fluorescens subsp. cellulosa esterase (XylD) release a 5,5′ ferulic acid dehydrodimers (diferulic acid) from barley and wheat cell walls. Appl. Environ. Microbiol. 63:1997;208-212.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 208-212
    • Bartolomé, B.1    Faulds, C.B.2    Kroon, P.A.3    Waldron, K.W.4    Gilbert, H.J.5    Hazlewood, G.P.6    Williamson, G.7
  • 29
    • 0037090961 scopus 로고    scopus 로고
    • The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds
    • de Vries R.P., van Kuyk P.A., Kester H.C.M., Visser J. The Aspergillus niger faeB gene encodes a second feruloyl esterase involved in pectin and xylan degradation and is specifically induced in the presence of aromatic compounds. Biochem. J. 363:2002;377-386.
    • (2002) Biochem. J. , vol.363 , pp. 377-386
    • De Vries, R.P.1    Van Kuyk, P.A.2    Kester, H.C.M.3    Visser, J.4
  • 31
    • 0033679102 scopus 로고    scopus 로고
    • A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module
    • Kroon P.A., Williamson G., Fish N.M., Archer D.B., Belshaw N.J. A modular esterase from Penicillium funiculosum which releases ferulic acid from plant cell walls and binds crystalline cellulose contains a carbohydrate binding module. Eur. J. Biochem. 267:2000;6740-6752.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 6740-6752
    • Kroon, P.A.1    Williamson, G.2    Fish, N.M.3    Archer, D.B.4    Belshaw, N.J.5
  • 33
    • 0032784276 scopus 로고    scopus 로고
    • Alpha/beta hydrolase fold enzymes: The family keeps growing
    • Nardini M., Dijsktra B.W. Alpha/beta hydrolase fold enzymes: the family keeps growing. Curr. Opin. Struct. Biol. 9:1999;732-737.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 732-737
    • Nardini, M.1    Dijsktra, B.W.2
  • 35
    • 0033153557 scopus 로고    scopus 로고
    • Of barn owls and bankers: A lush variety of alpha/beta hydrolases
    • Heikinheimo P., Goldman A., Jeffries C., Ollis D.L. Of barn owls and bankers: a lush variety of alpha/beta hydrolases. Structure. 7:1999;R141-R146.
    • (1999) Structure , vol.7
    • Heikinheimo, P.1    Goldman, A.2    Jeffries, C.3    Ollis, D.L.4
  • 36
    • 0020020315 scopus 로고
    • Crystallographic and NMR studies of the serine proteases
    • Steitz T.A., Shulman R.G. Crystallographic and NMR studies of the serine proteases. Annu. Rev. Biophys. Bioeng. 11:1982;419-444.
    • (1982) Annu. Rev. Biophys. Bioeng. , vol.11 , pp. 419-444
    • Steitz, T.A.1    Shulman, R.G.2
  • 39
  • 40
    • 0028295251 scopus 로고
    • Conformational lability of lipases observed in the absence of an oil-water interface - Crystallographic studies of enzymes from the fungi Humicola lanuginose and Rhizopus delemar
    • Derewenda U., Swenson L., Wei Y.Y., Green R., Kobos P.M., Joerger R., Haas M.J., Derewenda Z.S. Conformational lability of lipases observed in the absence of an oil-water interface - crystallographic studies of enzymes from the fungi Humicola lanuginose and Rhizopus delemar. J. Lipid Res. 35:1994;524-534.
    • (1994) J. Lipid Res. , vol.35 , pp. 524-534
    • Derewenda, U.1    Swenson, L.2    Wei, Y.Y.3    Green, R.4    Kobos, P.M.5    Joerger, R.6    Haas, M.J.7    Derewenda, Z.S.8
  • 42
  • 44
    • 0035735155 scopus 로고    scopus 로고
    • High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris
    • Juge N., Williamson G., Puigserver A., Cummings N.J., Connerton I.F., Faulds C.B. High-level production of recombinant Aspergillus niger cinnamoyl esterase (FAEA) in the methylotrophic yeast Pichia pastoris. FEMS Yeast Res. 1:2001;127-132.
    • (2001) FEMS Yeast Res. , vol.1 , pp. 127-132
    • Juge, N.1    Williamson, G.2    Puigserver, A.3    Cummings, N.J.4    Connerton, I.F.5    Faulds, C.B.6
  • 45
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallog. sect. D. 50:1994;760-763.
    • (1994) Acta Crystallog. Sect. D , vol.50 , pp. 760-763
  • 46
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecular replacement
    • Navaza J. AMoRe: an automated package for molecular replacement. Acta Crystallog. sect. A. 50:1994;157-163.
    • (1994) Acta Crystallog. Sect. a , vol.50 , pp. 157-163
    • Navaza, J.1
  • 47
    • 0035788101 scopus 로고    scopus 로고
    • Implementation of molecular replacement in AMoRe
    • Navaza J. Implementation of molecular replacement in AMoRe. Acta Crystallog. sect. D. 57:2001;1367-1372.
    • (2001) Acta Crystallog. Sect. D , vol.57 , pp. 1367-1372
    • Navaza, J.1
  • 48
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
    • (1991) Acta Crystallog. Sect. a , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 52
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis P. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 53
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: A photorealistic molecular graphics
    • Merritt E., Bacon D. Raster3D: a photorealistic molecular graphics. Methods Enzymol. 277:1997;505-524.
    • (1997) Methods Enzymol. , vol.277 , pp. 505-524
    • Merritt, E.1    Bacon, D.2
  • 54
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296.
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 55
    • 0027169343 scopus 로고
    • A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain
    • Ferreira L.M.A., Wood T.M., Williamson G., Faulds C., Hazlewood G.P., Black G.W., Gilbert H.J. A modular esterase from Pseudomonas fluorescens subsp. cellulosa contains a non-catalytic cellulose-binding domain. Biochem. J. 294:1993;349-355.
    • (1993) Biochem. J. , vol.294 , pp. 349-355
    • Ferreira, L.M.A.1    Wood, T.M.2    Williamson, G.3    Faulds, C.4    Hazlewood, G.P.5    Black, G.W.6    Gilbert, H.J.7
  • 56
    • 1542314901 scopus 로고    scopus 로고
    • The feruloyl esterase system of Talaromyces stipitatus: Production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity
    • Garcia-Conesa M.-T., Crepin V.F., Goldson A.J., Williamson G., Cummings N.J., Connerton I.F., Faulds C.B., Kroon P.A. The feruloyl esterase system of Talaromyces stipitatus: production of three discrete feruloyl esterases, including a novel enzyme, TsFaeC, with a broad substrate specificity. J. Biotechnol. 108:2004;227-241.
    • (2004) J. Biotechnol. , vol.108 , pp. 227-241
    • Garcia-Conesa, M.-T.1    Crepin, V.F.2    Goldson, A.J.3    Williamson, G.4    Cummings, N.J.5    Connerton, I.F.6    Faulds, C.B.7    Kroon, P.A.8
  • 57
    • 0242417646 scopus 로고    scopus 로고
    • A non-modular type-B feruloyl esterase from Neurospora crassa exhibits concentration dependent substrate inhibition
    • Crepin V.F., Faulds C.B., Connerton I.F. A non-modular type-B feruloyl esterase from Neurospora crassa exhibits concentration dependent substrate inhibition. Biochem. J. 370:2003;417-427.
    • (2003) Biochem. J. , vol.370 , pp. 417-427
    • Crepin, V.F.1    Faulds, C.B.2    Connerton, I.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.