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 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 | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Renatured (Comment) | Organism |
---|---|
thermodynamic analysis of unfolding in presence of GdnHCl | Gallus gallus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Gallus gallus | - |
egg white | - |
Gallus gallus | - |
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 | 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 Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
85 | - |
purified enzyme, pH 6.2, inactivation after 60 min | Gallus gallus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.2 | - |
assay at | Gallus gallus |
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 |