메뉴 건너뛰기




Volumn 1749, Issue 1, 2005, Pages 53-64

Action pattern of Fusarium moniliforme endopolygalacturonase towards pectin fragments: Comprehension and prediction

Author keywords

Action pattern; Endopolygalacturonase; Homogalacturonan; Molecular modeling; Subsite binding

Indexed keywords

AMINO ACID; OLIGOMER; PECTIN; POLYGALACTURONASE;

EID: 17444386303     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.02.008     Document Type: Article
Times cited : (14)

References (33)
  • 1
  • 3
    • 0027818642 scopus 로고
    • Pectin, pectinase and protopectinase: Production, properties and applications
    • T. Sakai, T. Sakamoto, J. Hallaert, and E.J. Vandamme Pectin, pectinase and protopectinase: production, properties and applications Adv. Appl. Microbiol. 39 1993 213 294
    • (1993) Adv. Appl. Microbiol. , vol.39 , pp. 213-294
    • Sakai, T.1    Sakamoto, T.2    Hallaert, J.3    Vandamme, E.J.4
  • 4
    • 0034011112 scopus 로고    scopus 로고
    • Perspectives in the biological function and the technological application of polygalacturonases
    • C. Lang, and H. Dönenburg Perspectives in the biological function and the technological application of polygalacturonases Appl. Microbiol. Biotechnol. 53 2000 366 375
    • (2000) Appl. Microbiol. Biotechnol. , vol.53 , pp. 366-375
    • Lang, C.1    Dönenburg, H.2
  • 5
    • 0030733350 scopus 로고    scopus 로고
    • Structural and sequence-based classification of glycoside hydrolases
    • B. Henrissat, and G.J. Davies Structural and sequence-based classification of glycoside hydrolases Curr. Opin. Struct. Biol. 7 1997 637 644
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 637-644
    • Henrissat, B.1    Davies, G.J.2
  • 6
    • 0032059448 scopus 로고    scopus 로고
    • Enzymology of cell-wall degradation
    • B. Henrissat Enzymology of cell-wall degradation Biochem. Soc. Trans. 26 1998 153 156
    • (1998) Biochem. Soc. Trans. , vol.26 , pp. 153-156
    • Henrissat, B.1
  • 7
    • 0030078980 scopus 로고    scopus 로고
    • Nature of sites hydrolyzable by endopolygalacturonase in partially-esterified homogalacturonans
    • E.M.W. Chen, and A.J. Mort Nature of sites hydrolyzable by endopolygalacturonase in partially-esterified homogalacturonans Carbohydr. Polym. 29 1996 129 136
    • (1996) Carbohydr. Polym. , vol.29 , pp. 129-136
    • Chen, E.M.W.1    Mort, A.J.2
  • 8
    • 0033083712 scopus 로고    scopus 로고
    • Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I, II and C
    • J.A.E. Benen, H.C.M. Kester, and J. Visser Kinetic characterization of Aspergillus niger N400 endopolygalacturonases I, II and C Eur. J. Biochem. 259 1999 577 585
    • (1999) Eur. J. Biochem. , vol.259 , pp. 577-585
    • Benen, J.A.E.1    Kester, H.C.M.2    Visser, J.3
  • 9
    • 0034142291 scopus 로고    scopus 로고
    • EndoPGaA and endoPGaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger
    • L. Parenicova, J.A.E. Benen, H. Kester, and J. Visser endoPGaA and endoPGaB encode two constitutively expressed endopolygalacturonases of Aspergillus niger Biochem. J. 345 2000 637 644
    • (2000) Biochem. J. , vol.345 , pp. 637-644
    • Parenicova, L.1    Benen, J.A.E.2    Kester, H.3    Visser, J.4
  • 10
    • 0343114331 scopus 로고    scopus 로고
    • Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties
    • L. Parenicova, H.C.M. Kester, J.A.E. Benen, and J. Visser Characterization of a novel endopolygalacturonase from Aspergillus niger with unique kinetic properties FEBS Lett. 467 2000 333 336
    • (2000) FEBS Lett. , vol.467 , pp. 333-336
    • Parenicova, L.1    Kester, H.C.M.2    Benen, J.A.E.3    Visser, J.4
  • 11
    • 0003048644 scopus 로고
    • Damage, symptoms and crop loss caused by vascular pathogens
    • R.K.A. Wood G.J. Jellis Blackwell Scientific Publications Oxford
    • P.W. Talboys Damage, symptoms and crop loss caused by vascular pathogens R.K.A. Wood G.J. Jellis Plant Diseases: Infection, Damage and Loss 1984 Blackwell Scientific Publications Oxford 171 187
    • (1984) Plant Diseases: Infection, Damage and Loss , pp. 171-187
    • Talboys, P.W.1
  • 12
    • 0032954512 scopus 로고    scopus 로고
    • Purification and characterization of an endo-polygalacturonase from Verticillium albo-atrum
    • L.-K. Huang, and R.R. Mahoney Purification and characterization of an endo-polygalacturonase from Verticillium albo-atrum J. Appl. Microbiol. 86 1999 145 156
    • (1999) J. Appl. Microbiol. , vol.86 , pp. 145-156
    • Huang, L.-K.1    Mahoney, R.R.2
  • 14
    • 0036538722 scopus 로고    scopus 로고
    • Hydrolysis of pectins with different degrees and patterns of methylation by the endopolygalacturonase of Fusarium moniliforme
    • E. Bonnin, A. Le Goff, R. Körner, J. Vigouroux, P. Roepstorff, and J.-F. Thibault Hydrolysis of pectins with different degrees and patterns of methylation by the endopolygalacturonase of Fusarium moniliforme Biochim. Biophys. Acta 1596 2002 83 94
    • (2002) Biochim. Biophys. Acta , vol.1596 , pp. 83-94
    • Bonnin, E.1    Le Goff, A.2    Körner, R.3    Vigouroux, J.4    Roepstorff, P.5    Thibault, J.-F.6
  • 15
    • 0035943418 scopus 로고    scopus 로고
    • The X-ray structure of Aspergillus aculeatus Polygalacturonase and a modeled structure of the polygalacturonase-octagalacturonate complex
    • S.W. Cho, S. Lee, and W. Shin The X-ray structure of Aspergillus aculeatus Polygalacturonase and a modeled structure of the polygalacturonase- octagalacturonate complex J. Mol. Biol. 314 2001 863 878
    • (2001) J. Mol. Biol. , vol.314 , pp. 863-878
    • Cho, S.W.1    Lee, S.2    Shin, W.3
  • 16
    • 1442349119 scopus 로고    scopus 로고
    • Computer modeling of the rhamnogalacturonase-"hairy" pectin complex, proteins
    • J.K. Choi, B.H. Lee, C.H. Chae, and W. Shin Computer modeling of the rhamnogalacturonase-"hairy" pectin complex, proteins Struct. Funct. Bioinformatics 55 2004 22 33
    • (2004) Struct. Funct. Bioinformatics , vol.55 , pp. 22-33
    • Choi, J.K.1    Lee, B.H.2    Chae, C.H.3    Shin, W.4
  • 17
    • 0032908195 scopus 로고    scopus 로고
    • Amylose chain behavior in an interacting context II-molecular modelling of a maltopentaose fragment in the barley α-amylase catalytic site
    • G. André, A. Buléon, M. Juy, N. Aghajari, R. Haser, and V. Tran Amylose chain behavior in an interacting context II-molecular modelling of a maltopentaose fragment in the barley α-amylase catalytic site Biopolymers 49 1999 107 119
    • (1999) Biopolymers , vol.49 , pp. 107-119
    • André, G.1    Buléon, A.2    Juy, M.3    Aghajari, N.4    Haser, R.5    Tran, V.6
  • 18
    • 0345580183 scopus 로고    scopus 로고
    • Amylose chain behaviour in an interacting context III-complete occupancy of the AMY2 barley α-amylase cleft and comparison with biochemical data
    • G. André, A. Buléon, R. Haser, and V. Tran Amylose chain behaviour in an interacting context III-complete occupancy of the AMY2 barley α-amylase cleft and comparison with biochemical data Biopolymers 50 1999 751 762
    • (1999) Biopolymers , vol.50 , pp. 751-762
    • André, G.1    Buléon, A.2    Haser, R.3    Tran, V.4
  • 20
    • 0031841279 scopus 로고    scopus 로고
    • The HSSP database of protein structure-sequence alignments and family profiles
    • C. Dodge, R. Schneider, and C. Sander The HSSP database of protein structure-sequence alignments and family profiles Nucleic Acids Res. 26 1998 313 315
    • (1998) Nucleic Acids Res. , vol.26 , pp. 313-315
    • Dodge, C.1    Schneider, R.2    Sander, C.3
  • 22
    • 3242878412 scopus 로고    scopus 로고
    • 3DCoffee: A web server for mixing sequences and structures into multiple sequence alignments
    • O. Poirot, K. Suhre, C. Abergel, E. O'Toole, and C. Notredame 3DCoffee: a web server for mixing sequences and structures into multiple sequence alignments Nucleic Acids Res. 32 2004 37 40
    • (2004) Nucleic Acids Res. , vol.32 , pp. 37-40
    • Poirot, O.1    Suhre, K.2    Abergel, C.3    O'Toole, E.4    Notredame, C.5
  • 23
    • 0029159799 scopus 로고
    • Finding flexible patterns in unaligned protein sequences
    • I. Jonassen, J.-F. Collins, and D. Higgins Finding flexible patterns in unaligned protein sequences Protein Sci. 4 1995 1587 1595
    • (1995) Protein Sci. , vol.4 , pp. 1587-1595
    • Jonassen, I.1    Collins, J.-F.2    Higgins, D.3
  • 24
    • 0028414130 scopus 로고
    • Solution conformation of a pectic acid fragment by 1H-NMR and molecular dynamics
    • A. Di Nola, G. Fabrizi, D. Lamba, and L. Segre Solution conformation of a pectic acid fragment by 1H-NMR and molecular dynamics Biopolymers 34 1994 457 462
    • (1994) Biopolymers , vol.34 , pp. 457-462
    • Di Nola, A.1    Fabrizi, G.2    Lamba, D.3    Segre, L.4
  • 25
    • 0019888723 scopus 로고
    • Conformations and interactions of pectins-I X-ray diffraction analyses of sodium pectate in neutral and acidified forms
    • M.D. Walknishaw, and S. Arnott Conformations and interactions of pectins-I X-ray diffraction analyses of sodium pectate in neutral and acidified forms J. Mol. Biol. 153 1981 1055 1073
    • (1981) J. Mol. Biol. , vol.153 , pp. 1055-1073
    • Walknishaw, M.D.1    Arnott, S.2
  • 26
    • 0027080068 scopus 로고
    • Solution conformation of a pectin fragment disaccharide using molecular modelling and nuclear magnetic resonance
    • S. Cros, C. Hervé du Penhoat, N. Bouchemal, H. Ohassan, A. Imberty, and S. Pérez Solution conformation of a pectin fragment disaccharide using molecular modelling and nuclear magnetic resonance Int. J. Biol. Macromol. 14 1992 313 320
    • (1992) Int. J. Biol. Macromol. , vol.14 , pp. 313-320
    • Cros, S.1    Hervé Du Penhoat, C.2    Bouchemal, N.3    Ohassan, H.4    Imberty, A.5    Pérez, S.6
  • 27
    • 0037188358 scopus 로고    scopus 로고
    • Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution
    • T. Shimizu, T. Nakatsu, K. Miyairi, T. Okuno, and H. Kato Active-site architecture of endopolygalacturonase I from Stereum purpureum revealed by crystal structures in native and ligand-bound forms at atomic resolution Biochemistry 41 2002 6651 6659
    • (2002) Biochemistry , vol.41 , pp. 6651-6659
    • Shimizu, T.1    Nakatsu, T.2    Miyairi, K.3    Okuno, T.4    Kato, H.5
  • 28
    • 0032589464 scopus 로고    scopus 로고
    • 1.68 a crystal structure of endopolygalacturonase II from Aspergillus Niger and identification of active site residues by site-directed mutagenesis
    • Y. Van Santen, J.A.E. Benen, K.-H. Schroter, K.H. Kalk, S. Armand, J. Visser, and B.W. Dijkstra 1.68 a crystal structure of endopolygalacturonase II from Aspergillus Niger and identification of active site residues by site-directed mutagenesis J. Biol. Chem. 274 1999 30474 30480
    • (1999) J. Biol. Chem. , vol.274 , pp. 30474-30480
    • Van Santen, Y.1    Benen, J.A.E.2    Schroter, K.-H.3    Kalk, K.H.4    Armand, S.5    Visser, J.6    Dijkstra, B.W.7
  • 31
    • 0031570284 scopus 로고    scopus 로고
    • Two crystal structures of pectin lyase a from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases
    • O. Mayans, M. Scott, I. Connerton, T. Gravesen, J. Benen, J. Visser, R. Pickersgill, and J. Jenkins Two crystal structures of pectin lyase A from Aspergillus reveal a pH driven conformational change and striking divergence in the substrate-binding clefts of pectin and pectate lyases Structure 5 1997 677 689
    • (1997) Structure , vol.5 , pp. 677-689
    • Mayans, O.1    Scott, M.2    Connerton, I.3    Gravesen, T.4    Benen, J.5    Visser, J.6    Pickersgill, R.7    Jenkins, J.8
  • 32
    • 0035951291 scopus 로고    scopus 로고
    • Three-dimensional structure of Erwinia chrysantemi pectin methylesterase reveals a novel esterase active site
    • J. Jenkins, O. Mayans, D. Smith, K. Worboys, and R.W. Pickersgill Three-dimensional structure of Erwinia chrysantemi pectin methylesterase reveals a novel esterase active site J. Mol. Biol. 305 2001 951 960
    • (2001) J. Mol. Biol. , vol.305 , pp. 951-960
    • Jenkins, J.1    Mayans, O.2    Smith, D.3    Worboys, K.4    Pickersgill, R.W.5
  • 33


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.