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BRENDA support

Literature summary for 3.2.1.1 extracted from

  • Bank, R.A.; Hettema, E.H.; Arwert, F.; Nieuw Amerongen, A.V.; Pronk, J.C.
    Electrophoretic characterization of posttranslational modifications of human parotid salivary alpha-amylase (1991), Electrophoresis, 12, 74-79.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Posttranslational Modification

Posttranslational Modification Comment Organism
glycoprotein in saliva, due to posttranslational modifications, a pattern of 5-6 isoenzymes is observed. Band 2 is the primary gene product, band 1 is the glycosylated counterpart with one neutral oligosaccharide present on each molecule, band 3 originates from band 1 by the transialidase-catalyzed incorporation of sialic acid into the biantennary chain, band 4 and 6 originate from band 2 and 4, respectively by deamination, band 5 is the deamination product of amylase with an acidic oligosaccharide Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
saliva
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Homo sapiens
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