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Literature summary for 3.2.1.17 extracted from

  • Yaghoubi, H.; Khajeh, K.; Hosseinkhani, S.; Ranjbar, B.; Naderi-Manesh, H.
    Application of zero-length cross-linking to form lysozyme, horseradish peroxidase and lysozyme-peroxidase dimers: Activity and stability (2007), Int. J. Biol. Macromol., 41, 624-630.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Co2+ increases the formation of lysozyme dimers 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.
peptidoglycan + H2O Micrococcus lysodeikticus cells Gallus gallus ?
-
?

Subunits

Subunits Comment Organism
dimer formation of covalent bonds between lysozyme molecules by zero-length cross-linking. Approximately one-third of the total lysozyme becomes cross-linked. The enzymatic activity of cross-linked lysozyme dimer is the same as monomer. The activity of lysozyme dimer remains constant up to 10 min at 80°C. Lysozyme possess a compact structure in the dimer form Gallus gallus

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
80
-
the activity of lysozyme dimer remains constant up to 10 min Gallus gallus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5 5.5
-
Gallus gallus