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Volumn 8, Issue 4, 2000, Pages 373-383

Rhamnogalacturonan acetylesterase elucidates the structure and function of a new family of hydrolases

Author keywords

Carbohydrate esterase; Catalytic triad; Pectin; Rhamnogalacturonan; SGNH hydrolase

Indexed keywords

ACETYLESTERASE; CARBOHYDRATE; HYDROLASE; PECTIN; POLYSACCHARIDE;

EID: 0034655985     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00118-0     Document Type: Article
Times cited : (189)

References (44)
  • 1
    • 0031128046 scopus 로고    scopus 로고
    • O-acetylated oligosaccharides from pectins of potato tuber cell walls
    • Tshii T. O-acetylated oligosaccharides from pectins of potato tuber cell walls. Plant Physiol. 113:1997;1265-1272.
    • (1997) Plant Physiol. , vol.113 , pp. 1265-1272
    • Tshii, T.1
  • 3
    • 0028143066 scopus 로고
    • Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus
    • Kofod L., Dalbøge H.et al. Cloning and characterization of two structurally and functionally divergent rhamnogalacturonases from Aspergillus aculeatus. J. Biol. Chem. 269:1994;29182-29189.
    • (1994) J. Biol. Chem. , vol.269 , pp. 29182-29189
    • Kofod, L.1    Dalbøge, H.2
  • 4
    • 0026446384 scopus 로고
    • Rhamnogalacturonan acetylesterase: A novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regions of pectins
    • Searle-van Leeuwen M.J.F., van den Broek L.A.M., Schols H.A., Beldman G., Voragen A.G.J. Rhamnogalacturonan acetylesterase: a novel enzyme from Aspergillus aculeatus, specific for the deacetylation of hairy (ramified) regions of pectins. Appl. Microbiol. Biotechnol. 38:1992;347-349.
    • (1992) Appl. Microbiol. Biotechnol. , vol.38 , pp. 347-349
    • Searle-Van Leeuwen, M.J.F.1    Van Den Broek, L.A.M.2    Schols, H.A.3    Beldman, G.4    Voragen, A.G.J.5
  • 5
    • 0031569829 scopus 로고    scopus 로고
    • The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: A right-handed paralled β helix
    • Petersen T., Kauppinen S., Larsen S. The crystal structure of rhamnogalacturonase A from Aspergillus aculeatus: a right-handed paralled β helix. Structure. 5:1997;533-544.
    • (1997) Structure , vol.5 , pp. 533-544
    • Petersen, T.1    Kauppinen, S.2    Larsen, S.3
  • 6
    • 0028787502 scopus 로고
    • Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus
    • Kauppinen S., Christgau S., Kofod L.V., Halkier T., Dörreich K., Dalbøge H. Molecular cloning and characterization of a rhamnogalacturonan acetylesterase from Aspergillus aculeatus. J. Biol. Chem. 270:1995;27172-27178.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27172-27178
    • Kauppinen, S.1    Christgau, S.2    Kofod, L.V.3    Halkier, T.4    Dörreich, K.5    Dalbøge, H.6
  • 7
    • 0032169323 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus
    • Mølgaard A., Larsen S.et al. Crystallization and preliminary X-ray diffraction studies of the heterogeneously glycosylated enzyme rhamnogalacturonan acetylesterase from Aspergillus aculeatus. Acta Crystallogr. D. 54:1998;1026-1029.
    • (1998) Acta Crystallogr. D , vol.54 , pp. 1026-1029
    • Mølgaard, A.1    Larsen, S.2
  • 8
    • 0030788755 scopus 로고    scopus 로고
    • Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi
    • Shevchik V., Hugouvieux-Cotte-Pattat N. Identification of a bacterial pectin acetyl esterase in Erwinia chrysanthemi. Mol. Microbiol. 24:1997;1285-1301.
    • (1997) Mol. Microbiol. , vol.24 , pp. 1285-1301
    • Shevchik, V.1    Hugouvieux-Cotte-Pattat, N.2
  • 9
    • 0001973467 scopus 로고    scopus 로고
    • Carbohydrate-active enzymes: An integrated database approach
    • Cambridge: The Royal Society of Chemistry
    • Coutinho P., Henrissat B. Carbohydrate-active enzymes: an integrated database approach. Recent Advances in Carbohydrate Bioengineering. 1999;The Royal Society of Chemistry, Cambridge.
    • (1999) Recent Advances in Carbohydrate Bioengineering
    • Coutinho, P.1    Henrissat, B.2
  • 10
    • 0030864850 scopus 로고    scopus 로고
    • Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases
    • Dalrymple B., Lowry J.et al. Three Neocallimastix patriciarum esterases associated with the degradation of complex polysaccharides are members of a new family of hydrolases. Microbiology. 143:1997;2605-2614.
    • (1997) Microbiology , vol.143 , pp. 2605-2614
    • Dalrymple, B.1    Lowry, J.2
  • 12
    • 0031021088 scopus 로고    scopus 로고
    • Brain acetylhydrolase that inactivates platelet-activating factor is a γ-protein-like trimer
    • Ho Y., Derewenda Z.et al. Brain acetylhydrolase that inactivates platelet-activating factor is a γ-protein-like trimer. Nature. 385:1997;89-93.
    • (1997) Nature , vol.385 , pp. 89-93
    • Ho, Y.1    Derewenda, Z.2
  • 13
    • 0026540411 scopus 로고
    • The α/β hydrolase fold
    • Ollis D., Goldman A.et al. The α/β hydrolase fold. Protein Eng. 5:1992;197-211.
    • (1992) Protein Eng. , vol.5 , pp. 197-211
    • Ollis, D.1    Goldman, A.2
  • 14
  • 15
    • 0030039296 scopus 로고    scopus 로고
    • Promotif - A program to identify and analyze structural motifs in proteins
    • Hutchinson E.G., Thornton J.M. Promotif - a program to identify and analyze structural motifs in proteins. Protein Sci. 5:1996;212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 16
    • 0026305078 scopus 로고
    • Relationships among serine hydrolases: Evidence for a common structural motif in triacylglyceride lipases and esterases
    • Derewenda Z., Derewenda U. Relationships among serine hydrolases: evidence for a common structural motif in triacylglyceride lipases and esterases. Biochem. Cell Biol. 69:1991;842-851.
    • (1991) Biochem. Cell Biol. , vol.69 , pp. 842-851
    • Derewenda, Z.1    Derewenda, U.2
  • 17
    • 0030874881 scopus 로고    scopus 로고
    • Lipases and the α/β hydrolase fold
    • Schrag J., Cygler M. Lipases and the α/β hydrolase fold. Methods Enzymol. 284:1997;85-107.
    • (1997) Methods Enzymol. , vol.284 , pp. 85-107
    • Schrag, J.1    Cygler, M.2
  • 18
    • 0029158641 scopus 로고
    • Molecular mechanism of enantiorecognition by esterases
    • Derewenda Z., Wei Y. Molecular mechanism of enantiorecognition by esterases. J. Am. Chem. Soc. 117:1995;2104-2105.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 2104-2105
    • Derewenda, Z.1    Wei, Y.2
  • 19
    • 0027057526 scopus 로고
    • A database of protein structure families with common folding motifs
    • Holm L., Ouzounis C., Sander C., Tuparev G., Vriend G. A database of protein structure families with common folding motifs. Protein Sci. 1:1992;1691-1698.
    • (1992) Protein Sci. , vol.1 , pp. 1691-1698
    • Holm, L.1    Ouzounis, C.2    Sander, C.3    Tuparev, G.4    Vriend, G.5
  • 20
    • 0027991446 scopus 로고
    • The fssp database of structurally aligned protein fold families
    • Holm L., Sander C. The fssp database of structurally aligned protein fold families. Nucleic Acids Res. 22:1994;3600-3609.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 3600-3609
    • Holm, L.1    Sander, C.2
  • 21
    • 0029007122 scopus 로고
    • A new family of lipolytic enzymes?
    • Upton C., Buckley J. A new family of lipolytic enzymes? Trends Biochem. Sci. 20:1995;178-179.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 178-179
    • Upton, C.1    Buckley, J.2
  • 22
    • 0032578355 scopus 로고    scopus 로고
    • The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin
    • Kuhn P., Knapp M., Soltis M., Ganshaw G., Thoene M., Bott R. The 0.78 Å structure of a serine protease: Bacillus lentus subtilisin. Biochemistry. 37:1998;13446-13452.
    • (1998) Biochemistry , vol.37 , pp. 13446-13452
    • Kuhn, P.1    Knapp, M.2    Soltis, M.3    Ganshaw, G.4    Thoene, M.5    Bott, R.6
  • 23
    • 0032859479 scopus 로고    scopus 로고
    • Probing the substrate specificity of the intracellular brain platelet-activating factor acetylhydrolase
    • Ho Y.S., Derewenda Z.S.et al. Probing the substrate specificity of the intracellular brain platelet-activating factor acetylhydrolase. Protein Eng. 12:1999;693-700.
    • (1999) Protein Eng. , vol.12 , pp. 693-700
    • Ho, Y.S.1    Derewenda, Z.S.2
  • 24
    • 0017709445 scopus 로고
    • β-Turns in proteins
    • Chou P., Fasman G. β-Turns in proteins. J. Mol. Biol. 115:1977;135-175.
    • (1977) J. Mol. Biol. , vol.115 , pp. 135-175
    • Chou, P.1    Fasman, G.2
  • 25
    • 0029925587 scopus 로고    scopus 로고
    • Identification of the catalytic triad of the lipase/acyltransferase from Aeromonas hydrophila
    • Brumlik M., Buckley J. Identification of the catalytic triad of the lipase/acyltransferase from Aeromonas hydrophila. J. Bacteriol. 178:1996;2060-2064.
    • (1996) J. Bacteriol. , vol.178 , pp. 2060-2064
    • Brumlik, M.1    Buckley, J.2
  • 26
    • 0027351945 scopus 로고
    • Structural models of primary cell walls in flowering plants: Consistency of molecular structure with the physical properties of the walls during growth
    • Carpita N.C., Gibeaut D.M. Structural models of primary cell walls in flowering plants: consistency of molecular structure with the physical properties of the walls during growth. Plant J. 3:1993;1-30.
    • (1993) Plant J. , vol.3 , pp. 1-30
    • Carpita, N.C.1    Gibeaut, D.M.2
  • 29
    • 0000497441 scopus 로고
    • Structural features of hairy regions of pectins isolated from apple juice produced by the liquefaction process
    • Schols H.A., Posthumus M.A., Voragen A.G.J. Structural features of hairy regions of pectins isolated from apple juice produced by the liquefaction process. Carbohydr. Res. 206:1990;117-129.
    • (1990) Carbohydr. Res. , vol.206 , pp. 117-129
    • Schols, H.A.1    Posthumus, M.A.2    Voragen, A.G.J.3
  • 30
    • 0030063641 scopus 로고    scopus 로고
    • Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan cda-L-rhamnopyranosyl-(1-4)-α-D-galactopyranosyluronide lyase
    • Mutter M., Colquhoun I.J., Schols H.A., Beldman G., Voragen A.G. Rhamnogalacturonase B from Aspergillus aculeatus is a rhamnogalacturonan cda-L-rhamnopyranosyl-(1-4)-α-D-galactopyranosyluronide lyase. Plant Physiol. 110:1996;73-79.
    • (1996) Plant Physiol. , vol.110 , pp. 73-79
    • Mutter, M.1    Colquhoun, I.J.2    Schols, H.A.3    Beldman, G.4    Voragen, A.G.5
  • 31
    • 0029793554 scopus 로고    scopus 로고
    • A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease
    • Tong L., Qian C., Massariol M.-J., Bonneau P., Cordingley M., Lagace L. A new serine-protease fold revealed by the crystal structure of human cytomegalovirus protease. Nature. 383:1996;272-275.
    • (1996) Nature , vol.383 , pp. 272-275
    • Tong, L.1    Qian, C.2    Massariol, M.-J.3    Bonneau, P.4    Cordingley, M.5    Lagace, L.6
  • 33
    • 0028103275 scopus 로고
    • The ccp4 suite: Programs for protein crystallography
    • The ccp4 suite: programs for protein crystallography. Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 34
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and location of the errors in these models
    • Jones T., Zou J.-Y., Cowan S., Kjeldgaard M. Improved methods for building protein models in electron-density maps and location of the errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 110-119
    • Jones, T.1    Zou, J.-Y.2    Cowan, S.3    Kjeldgaard, M.4
  • 35
    • 0026597444 scopus 로고
    • The free R value: A novel statistical quantity for assessing the accuracy of crystal structures
    • Brünger A. The free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992;472-474.
    • (1992) Nature , vol.355 , pp. 472-474
    • Brünger, A.1
  • 36
    • 0003769049 scopus 로고
    • A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT
    • Brünger, A.T. (1992). X-PLOR Version 3.1. A System for X-ray Crystallography and NMR. Yale University Press, New Haven, CT.
    • (1992) X-PLOR Version 3.1
    • Brünger, A.T.1
  • 37
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction: Solvation properties of penicillopepsion and neuraminidase crystal structures
    • Jiang J.-S., Brünger A. Protein hydration observed by X-ray diffraction: solvation properties of penicillopepsion and neuraminidase crystal structures. J. Mol. Biol. 243:1994;100-115.
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.-S.1    Brünger, A.2
  • 38
    • 0023518540 scopus 로고
    • A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons
    • Barton G.J., Sternberg M.J.E. A strategy for the rapid multiple alignment of protein sequences. Confidence levels from tertiary structure comparisons. J. Mol. Biol. 198:1987;327-337.
    • (1987) J. Mol. Biol. , vol.198 , pp. 327-337
    • Barton, G.J.1    Sternberg, M.J.E.2
  • 39
    • 0025303764 scopus 로고
    • Protein multiple sequence alignment and flexible pattern matching
    • Barton G. Protein multiple sequence alignment and flexible pattern matching. Methods Enzymol. 183:1990;403-428.
    • (1990) Methods Enzymol. , vol.183 , pp. 403-428
    • Barton, G.1
  • 40
    • 0027412196 scopus 로고
    • Alscript a tool to format multiple sequence alignments
    • Barton G.J. Alscript a tool to format multiple sequence alignments. Protein Eng. 6:1993;37-40.
    • (1993) Protein Eng. , vol.6 , pp. 37-40
    • Barton, G.J.1
  • 41
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of molscript that includes greatly enhanced coloring capacities
    • Esnouf R. An extensively modified version of molscript that includes greatly enhanced coloring capacities. J. Mol. Graph. 15:1997;132-134.
    • (1997) J. Mol. Graph. , vol.15 , pp. 132-134
    • Esnouf, R.1
  • 42
    • 0026244229 scopus 로고
    • Molscript: A program to produce detailed and schematic plots of protein structures
    • Kraulis P. Molscript: a program to produce detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:1991;946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 43
    • 0025160881 scopus 로고
    • Refined structure of dienelactone hydrolase at 1.8 Å
    • Pathak D., Ollis D. Refined structure of dienelactone hydrolase at 1.8 Å J. Mol. Biol. 214:1990;497-525.
    • (1990) J. Mol. Biol. , vol.214 , pp. 497-525
    • Pathak, D.1    Ollis, D.2


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