Literature summary for 3.2.1.17 extracted from

Maroufi, B.; Ranjbar, B.; Khajeh, K.; Naderi-Manesh, H.; Yaghoubi, H.
Structural studies of hen egg-white lysozyme dimer: comparison with monomer (2008), Biochim. Biophys. Acta, 1784, 1043-1049.

Application

Application	Comment	Organism
analysis	cross-linking method for lysozyme and catalytic activity assay. Catalytic activity of lysozyme dimer is the same as monomer	Gallus gallus

Organism

Organism	UniProt	Comment	Textmining
Gallus gallus	P00698	-	-

Renatured (Commentary)

Renatured (Comment)	Organism
study on guanidinium chloride-induced equilibrium unfolding of monomer and dimer at pH 2.0. Unfolding curves at 222 and 289 nm in lysozyme dimer lack coincidence, while lysozyme monomer shows a single cooperative transition. Kinetic parameters are calculated on basis of a two-state mechanism for monomer and a three-state mechanism for dimer. Zero length cross-linking can stabilize the intermediate	Gallus gallus

Renatured (Comment)

Organism

study on guanidinium chloride-induced equilibrium unfolding of monomer and dimer at pH 2.0. Unfolding curves at 222 and 289 nm in lysozyme dimer lack coincidence, while lysozyme monomer shows a single cooperative transition. Kinetic parameters are calculated on basis of a two-state mechanism for monomer and a three-state mechanism for dimer. Zero length cross-linking can stabilize the intermediate

Gallus gallus

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Release 2023.1 (January 2023)