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Literature summary for 3.1.1.11 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

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain M15, the recombinant PME proteins (full-length and mature) do not show either PME or RIP activity Arabidopsis thaliana

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
35000
-
SDS-PAGE Arabidopsis thaliana

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
ecotype Col-0
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA His-bind resin chromatography, DEAE-Sephadex gel filtration, CM-cellulose column chromatography, and Shephacryl SH-100 gel filtration Arabidopsis thaliana

Source Tissue

Source Tissue Comment Organism Textmining
whole plant
-
Arabidopsis thaliana
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pectin + H2O
-
Arabidopsis thaliana methanol + pectate
-
?

Synonyms

Synonyms Comment Organism
pectin methylesterase
-
Arabidopsis thaliana
PME
-
Arabidopsis thaliana
RIP the RIP purified is identified as a mature form of pectin methylesterase, the purified native protein shows both pectin methylesterase and ribosome-inactivating protein activity Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
Arabidopsis thaliana

pH Stability

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