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Literature summary for 3.2.2.22 extracted from

  • De-la-Pena, C.; Badri, D.V.; Vivanco, J.M.
    Novel role for pectin methylesterase in Arabidopsis: A new function showing ribosome-inactivating protein (RIP) activity (2008), Biochim. Biophys. Acta, 1780, 773-783.
    View publication on PubMed

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34600
-
1 * 35000, SDS-PAGE, 1 * 34600, calculated for mature protein, 1 * 62000, calculated for full-length protein including N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2 Arabidopsis thaliana
35000
-
gel filtration Arabidopsis thaliana
62000
-
1 * 35000, SDS-PAGE, 1 * 34600, calculated for mature protein, 1 * 62000, calculated for full-length protein including N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2 Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
pectin methylesterase has ribosome inactivating protein activity
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification full-length sequence contains N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2 Arabidopsis thaliana

Subunits

Subunits Comment Organism
monomer 1 * 35000, SDS-PAGE, 1 * 34600, calculated for mature protein, 1 * 62000, calculated for full-length protein including N-terminal leader sequence, pectin methylesterase inhibitor domain, pectin esterase domain and pectin esterase signature sequences 1 and 2 Arabidopsis thaliana

pH Stability

pH Stability pH Stability Maximum Comment Organism
9
-
no residual activity Arabidopsis thaliana