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InterPro: IPR018040 Pectinesterase, active site
Protein matches
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UniProtKB Matches: 780 proteins |
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Accession
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IPR018040 Pectinesterase_AS |
Type
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Active_site |
Signatures
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InterPro Relationships
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Found in
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IPR000070 Pectinesterase, catalytic
IPR011050 Pectin lyase fold/virulence factor
IPR012334 Pectin lyase fold
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Pectinesterase EC:3.1.1.11 (pectin methylesterase) catalyses the de-esterification of pectin into pectate and methanol. Pectin is one of the main components of the plant cell wall. In plants, pectinesterase plays an important role in cell wall metabolism during fruit ripening. In plant bacterial pathogens such as Erwinia carotovora and in fungal pathogens such as Aspergillus niger, pectinesterase is involved in maceration and soft-rotting of plant tissue. Plant pectinesterases are regulated by pectinesterase inhibitors, which are ineffective against microbial enzymes [1].
Prokaryotic and eukaryotic pectinesterases share a few regions of sequence similarity. The crystal structure of pectinesterase from Erwinia chrysanthemi revealed a beta-helix structure similar to that found in pectinolytic enzymes, though it is different from most structures of esterases [2]. The putative catalytic residues are in a similar location to those of the active site and substrate-binding cleft of pectate lyase.
This entry represents conserved sequence regions found in these proteins, one of which (Pectinesterase signature 2) contains the active site aspartate [3].
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Structural links
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Database links
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Publications
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1.
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Di Matteo A, Giovane A, Raiola A, Camardella L, Bonivento D, De Lorenzo G, Cervone F, Bellincampi D, Tsernoglou D.
Structural basis for the interaction between pectin methylesterase and a specific inhibitor protein.
Plant Cell 17 849-58 2005
[PubMed: 15722470]
http://dx.doi.org/10.1105/tpc.104.028886
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2.
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Jenkins J, Mayans O, Smith D, Worboys K, Pickersgill RW.
Three-dimensional structure of Erwinia chrysanthemi pectin methylesterase reveals a novel esterase active site.
J. Mol. Biol. 305 951-60 2001
[PubMed: 11162105]
http://dx.doi.org/10.1006/jmbi.2000.4324
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3.
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Markovic O, Cederlund E, Griffiths WJ, Lipka T, Jornvall H.
Characterization of carrot pectin methylesterase.
Cell. Mol. Life Sci. 59 513-8 2002
[PubMed: 11964128]
http://dx.doi.org/10.1007/s00018-002-8442-6
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Additional Reading
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Plastow GS.
Molecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374.
Mol. Microbiol. 2 1988 247-54
[PubMed: 2837615]
http://dx.doi.org/10.1111/j.1365-2958.1988.tb00026.x
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Giovane A, Servillo L, Balestrieri C, Raiola A, D'Avino R, Tamburrini M, Ciardiello MA, Camardella L.
Pectin methylesterase inhibitor.
Biochim. Biophys. Acta 1696 2004 245-52
[PubMed: 14871665]
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Johansson K, El-Ahmad M, Friemann R, Jornvall H, Markovic O, Eklund H.
Crystal structure of plant pectin methylesterase.
FEBS Lett. 514 2002 243-9
[PubMed: 11943159]
http://dx.doi.org/10.1016/S0014-5793(02)02372-4
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D'Avino R, Camardella L, Christensen TM, Giovane A, Servillo L.
Tomato pectin methylesterase: modeling, fluorescence, and inhibitor interaction studies-comparison with the bacterial (Erwinia chrysanthemi) enzyme.
Proteins 53 2003 830-9
[PubMed: 14635125]
http://dx.doi.org/10.1002/prot.10487
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Fries M, Ihrig J, Brocklehurst K, Shevchik VE, Pickersgill RW.
Molecular basis of the activity of the phytopathogen pectin methylesterase.
EMBO J. 26 2007 3879-87
[PubMed: 17717531]
http://dx.doi.org/10.1038/sj.emboj.7601816
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Markovic O, Jornvall H.
Disulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments.
Protein Sci. 1 1992 1288-92
[PubMed: 1303747]
http://www.proteinscience.org/cgi/content/abstract/1/10/1288
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Ray J, Knapp J, Grierson D, Bird C, Schuch W.
Identification and sequence determination of a cDNA clone for tomato pectin esterase.
Eur. J. Biochem. 174 1988 119-24
[PubMed: 3371355]
http://dx.doi.org/10.1111/j.1432-1033.1988.tb14070.x
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InterPro 23.1
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