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Literature summary for 3.2.1.17 extracted from

  • Calderon, C.; Abuin, E.; Lissi, E.; Montecinos, R.
    Effect of human serum albumin on the kinetics of 4-methylumbelliferyl-beta-D-N-N'-N'' triacetylchitotrioside hydrolysis catalyzed by hen egg white lysozyme (2011), Protein J., 30, 367-373.
    View publication on PubMed

Inhibitors

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 [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

Organism UniProt Comment Textmining
Gallus gallus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
egg white
-
Gallus gallus
-

Substrates and Products (Substrate)

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 [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.2
-
assay at Gallus gallus

General Information

General Information Comment Organism
additional information the reaction follows a Michaelis-Menten mechanism Gallus gallus