Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Human serum albumin | the catalytic rate constant decreases tenfold when the albumin concentration increases, while the Michaelis constant remains almost constant in the albumin concentration range employed. Theoretical modeling of the structure of the human serum albumin-lysozyme complex shows that the Glu35 and Asp52 residues located in the active site of lysozyme are oriented toward the human serum albumin surface. This conformation will inactivate lysozyme molecules bound to human serum albumin, molecular dynamic calculations, overview | Gallus gallus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | the reaction follows a Michaelis-Menten mechanism | Gallus gallus | |
0.0008 | - |
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside | human serum albumin-bound enzyme, pH 5.2, 37°C | Gallus gallus | |
0.001 | - |
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside | free enzyme, pH 5.2, 37°C | Gallus gallus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Gallus gallus | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
egg white | - |
Gallus gallus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
4-methylumbelliferyl-beta-D-N,N',N''-triacetylchitotrioside + H2O | - |
Gallus gallus | ? | - |
? |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Gallus gallus |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5.2 | - |
assay at | Gallus gallus |
General Information | Comment | Organism |
---|---|---|
additional information | the reaction follows a Michaelis-Menten mechanism | Gallus gallus |