The peculiar structural features of kiwi fruit pectin methylesterase: amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor.

@article{Ciardiello2008ThePS,
  title={The peculiar structural features of kiwi fruit pectin methylesterase: amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor.},
  author={Maria Antonietta Ciardiello and Rossana D'avino and Angela Amoresano and Lisa Tuppo and Andrea Carpentieri and Vito Carratore and Maurizio Tamburrini and Alfonso Giovane and Piero Pucci and Laura Camardella},
  journal={Proteins},
  year={2008},
  volume={71 1},
  pages={
          195-206
        }
}
Pectin methylesterase (PME) from kiwi fruit (Actinidia deliciosa) is a glycoprotein, showing an apparent molecular mass of 50 kDa upon size exclusion chromatography and SDS-PAGE. The primary structure, elucidated by direct sequencing of the protein, comprises 321 amino acid residues providing a molecular mass of 35 kDa. The protein has an acetylated Thr residue at the amino terminus and five N-glycosylation consensus sequences, four of which are actually glycosylated. A careful investigation of… CONTINUE READING

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