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Literature summary extracted from

  • Ciardiello, M.A.; DAvino, R.; Amoresano, A.; Tuppo, L.; Carpentieri, A.; Carratore, V.; Tamburrini, M.; Giovane, A.; Pucci, P.; Camardella, L.
    The peculiar structural features of kiwi fruit pectin methylesterase: amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor (2008), Proteins Struct. Funct. Bioinform., 71, 195-206.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.1.1.11 pectin methylesterase inhibitor PMEI Actinidia deliciosa

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
3.1.1.11 cell wall
-
 Actinidia deliciosa 5618
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.1.11 35400
-
 calculated from amino acid sequence Actinidia deliciosa
3.1.1.11 50000
-
 purified enzyme, SDS-PAGE Actinidia deliciosa

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.11 Actinidia deliciosa P85076
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
3.1.1.11 glycoprotein
-
 Actinidia deliciosa

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.11 DE52 column chromatography, SP-Sepharose column chromatography, Mono-S column chromatography, and Superdex 75 gel filtration Actinidia deliciosa

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.1.11 fruit
-
 Actinidia deliciosa
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.11 pectin + H2O
-
 Actinidia deliciosa methanol + pectate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.11 pectin methylesterase
-
 Actinidia deliciosa
3.1.1.11 PME
-
 Actinidia deliciosa