Literature summary for 3.2.1.17 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.

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Inhibitors

Inhibitors	Comment	Organism	Structure
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

Organism	UniProt	Comment	Textmining
Gallus gallus	P00698	-	-

pH Stability

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

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Release 2023.1 (January 2023)