PROSITE documentation PDOC00413 [for PROSITE entry PS00800]

Pectinesterase signatures




Description

Pectinesterase (EC 3.1.1.11) (pectin methylesterase) catalyzes the hydrolysis of pectin into pectate and methanol. In plants, it plays an important role in cell wall metabolism during fruit ripening, cell wall extension and during pollen germination. 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.

Prokaryotic and eukaryotic pectinesterases share a few regions of sequence similarity [1,2,3]. We selected two of these regions as signature patterns. The first is based on a region in the N-terminal section of these enzymes; it contains a conserved tyrosine which may play a role in the catalytic mechanism [3]. The second pattern corresponds to the conserved sequence around an active site aspartate [4], an octapeptide located in the central part of these enzymes.

Last update:

June 2002 / Text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PECTINESTERASE_1, PS00800; Pectinesterase signature 1  (PATTERN)

PECTINESTERASE_2, PS00503; Pectinesterase signature 2  (PATTERN)


References

1AuthorsRay J., Knapp J., Grierson D., Bird C., Schuch W.
TitleIdentification and sequence determination of a cDNA clone for tomato pectin esterase.
SourceEur. J. Biochem. 174:119-124(1988).
PubMed ID3371355

2AuthorsPlastow G.S.
TitleMolecular cloning and nucleotide sequence of the pectin methyl esterase gene of Erwinia chrysanthemi B374.
SourceMol. Microbiol. 2:247-254(1988).
PubMed ID2837615

3AuthorsMarkovic O., Joernvall H.
TitleDisulfide bridges in tomato pectinesterase: variations from pectinesterases of other species; conservation of possible active site segments.
SourceProtein Sci. 1:1288-1292(1992).
PubMed ID1303747

4AuthorsMarkovic O., Cederlund E., Griffiths W.J., Lipka T., Joernvall H.
TitleCharacterization of carrot pectin methylesterase.
SourceCell. Mol. Life Sci. 59:513-518(2002).
PubMed ID11964128



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