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Literature summary for 3.2.1.17 extracted from

  • Moghadam, T.T.; Ranjbar, B.; Khajeh, K.; Etezad, S.M.; Khalifeh, K.; Ganjalikhany, M.R.
    Interaction of lysozyme with gold nanorods: conformation and activity investigations (2011), Int. J. Biol. Macromol., 49, 629-636.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information interaction with gold nanorods slightly decrease the enzyme activity, most at 25 nM, less at 100 nM Gallus gallus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information Michaelis-Menten curve of lysozyme in the presence and absence of gold nanorods Gallus gallus

Organism

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Renatured (Commentary)

Renatured (Comment) Organism
thermodynamic analysis of unfolding in presence of GdnHCl Gallus gallus

Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
-
Gallus gallus
-
egg white
-
Gallus gallus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information interaction between gold nanorods and lysozyme as moddel protein, the enzyme retains a high fraction of its native structure with a slight increase in the helical content at the expense of beta-turns. Comparison of the gold nanorod treated lysozyme with free enzyme reveals higher thermodynamic stability under denaturing condition. The enzyme's integrity gains more conformational stability in the vicinity of gold nanorods while its lytic activity does not show any undesirable change Gallus gallus ?
-
?

Subunits

Subunits Comment Organism
More secondary structure of lysozyme, free and bound to gold nanorods, no significant change in the secondary structure occurs upon binding, overview Gallus gallus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
purified enzyme, pH 6.2, inactivation after 60 min Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2
-
assay at Gallus gallus

General Information

General Information Comment Organism
additional information the active site of lysozyme contains two catalytic residues, Glu35 and Asp52, which lie in a cleft to the vicinity of the largest pocket and harbor the substrate binding site Gallus gallus