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Literature summary extracted from

  • Kumar, S.; Ravi, V.K.; Swaminathan, R.
    Suppression of lysozyme aggregation at alkaline pH by tri-N-acetylchitotriose (2009), Biochim. Biophys. Acta, 1794, 913-920.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.17 N,N',N''-triacetylchitotriose competitive. Preincubation at neutral pH impairs aggregation of lysozyme and fibrillogenesis at pH 12.2. Lysozyme-chitotriose complex at pH 12.2 displays reduced thioflavin T and 8-anilino-1-naphthalene sulfonic acid fluorescence, small oligomers but no amyloid fibrils, absence of large aggregates, marginally more helical content, and more than 70% of enzymatic activity after 24 h Gallus gallus

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.17 Gallus gallus P00698
-
-

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.17 12.2
-
lysozyme sponaneously forms soluble oligomers, which are later stabilized by intermolecular disulfide bonds Gallus gallus