Literature summary for 3.2.1.17 extracted from

Yum, S.; Kim, M.J.; Xu, Y.; Jin, X.L.; Yoo, H.Y.; Park, J.W.; Gong, J.H.; Choe, K.M.; Lee, B.L.; Ha, N.C.
Structural basis for the recognition of lysozyme by MliC, a periplasmic lysozyme inhibitor in Gram-negative bacteria (2009), Biochem. Biophys. Res. Commun., 378, 244-248.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
crystallization data in complex with membrane bound lysozyme inhibitor of C-type lysozyme MliC. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues	Gallus gallus

Inhibitors

Inhibitors	Comment	Organism	Structure
MliC	i.e. membrane bound lysozyme inhibitor of C-type lysozyme, crystallization data in complex with chicken egg white lysozyme. The invariant loop of MliC plays a crucial role in the inhibition by its insertion to the active site cleft of the lysozyme, where the loop forms hydrogen and ionic bonds with the catalytic residues	Gallus gallus

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	P00698	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
egg white	-	Gallus gallus	-

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Release 2023.1 (January 2023)