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Literature summary for 4.2.2.5 extracted from

  • Zamfir, A.D.; Flangea, C.; Sisu, E.; Seidler, D.G.; Peter-Katalinic J.
    Combining size-exclusion chromatography and fully automated chip-based nanoelectrospray quadrupole time-of-flight tandem mass spectrometry for structural analysis of chondroitin/dermatan sulfate in human decorin (2011), Electrophoresis, 32, 1639-1646.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Homo sapiens
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Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information chondroitin/dermatan sulfate chain of decorin, with a high complexity due to the large variety of glycoforms, from human skin fibroblasts is released by reductive beta-elimination reaction and digested with chondroitin AC I lyase. Mass spectrometric substrate and product analysis, e.g. tetrasulfated octasaccharide, decasaccharides, a trisulfated, a hexasulfated [4,5-D-GlcAGalNAc(IdoAGalNAc)4], and [4,5-D-GlcAGalNAc(IdoAGalNAc)3], and disaccharides, overview Homo sapiens ?
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Synonyms

Synonyms Comment Organism
chondroitin AC I lyase
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Homo sapiens

General Information

General Information Comment Organism
physiological function chondroitin AC I lyase, an enzyme belonging to the class of lyases, which due to its endolytic activity cleaves the glycosidic bonds between GalNAc and D-GlcA for depolymerization of chondroitin sulfate and dermatan sulfate Homo sapiens