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Literature summary for 3.1.1.11 extracted from

  • Mareck, A.; Lamour, R.; Schaumann, A.; Chan, P.; Driouich, A.; Pelloux, J.; Lerouge, P.
    Analysis of LuPME3, a pectin methylesterase from Linum usitatissimum, revealed a variability in PME proteolytic maturation (2012), Plant Signal. Behav., 7, 59-61.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
34000
-
x * 34000, SDS-PAGE Linum usitatissimum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pectin + H2O Linum usitatissimum
-
methanol + pectate
-
?

Organism

Organism UniProt Comment Textmining
Linum usitatissimum Q9FVF9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
root
-
Linum usitatissimum
-
vascular tissue
-
Linum usitatissimum
-

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 34000, SDS-PAGE Linum usitatissimum

Synonyms

Synonyms Comment Organism
pectin methylesterase
-
Linum usitatissimum
PME3
-
Linum usitatissimum

pI Value

Organism Comment pI Value Maximum pI Value
Linum usitatissimum isoelectric focusing
-
9.8

General Information

General Information Comment Organism
physiological function the enzyme catalyzes the de-methylesterification of pectin in plant cell walls during cell elongation Linum usitatissimum