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Literature summary for 3.2.1.137 extracted from

  • Gomathinayagam, S.; Hamilton, S.
    In vitro enzymatic treatment to remove O-linked mannose from intact glycoproteins (2014), Appl. Microbiol. Biotechnol., 98, 2545-2554 .
    View publication on PubMed
Search for more literature for 3.2.1.137

Organism

Organism UniProt Comment Textmining
Canavalia ensiformis
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-
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Canavalia ensiformis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycoprotein A + H2O
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 Canavalia ensiformis deglycosylated glycoprotein A + alpha-D-mannose
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 ?
glycoprotein B + H2O
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 Canavalia ensiformis deglycosylated glycoprotein B + alpha-D-mannose
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 ?
granulocyte colony-stimulating factor protein + H2O recombinant human rhGCSF expressed in a GFI2.0 glycoengineered Pichia pastoris strain and possessing O-linked glycosylation composed of a single O-linked mannose residue Canavalia ensiformis deglycosylated granulocyte colony-stimulating factor protein + alpha-D-mannose
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 ?
granulocyte/macrophage colony-stimulating factor + H2O i.e. GM-CSF, sargramostim, recombinantly expressed in Pichia pastoris Canavalia ensiformis deglycosylated granulocyte/macrophage colony-stimulating factor + alpha-D-mannose
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 ?
additional information the alpha-1,2/3/6-mannosidase from Jack bean is able to hydrolyze the Man-O-Ser/Thr glycosidic linkage on four individual undenatured intact glycoproteins. Jack bean alpha-1,2/3/6-mannosidase removal of O-linked mannose is not specific for intact glycoproteins produced in Pichia pastoris Canavalia ensiformis ?
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 ?

Synonyms

Synonyms Comment Organism
alpha-1,2/3/6-mannosidase
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 Canavalia ensiformis
JBM
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 Canavalia ensiformis