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Literature summary extracted from

  • Monterroso, B.; Saiz, J.L.; Garcia, P.; Garcia, J.L.; Menendez, M.
    Insights into the structure-function relationships of pneumococcal cell wall lysozymes, LytC and Cpl-1 (2008), J. Biol. Chem., 283, 28618-28628.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
3.2.1.17 choline the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalent. Coupling between choline binding and folding indicates a high conformational plasticity that could correlate with the unusual alternation of short and long choline-binding repeats present in this enzyme. It can contribute to regulate enzymic activity Streptococcus pneumoniae

Organism

EC Number Organism UniProt Comment Textmining
3.2.1.17 Streptococcus pneumoniae
-
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.2.1.17 the cell wall binding module is intrinsically unstable, and the ultimate folding and stabilization of the active, monomeric form of the enzyme relies on choline binding. Complex formation proceeds in a rather slow way, and all sites behave as equivalent Streptococcus pneumoniae

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.17 45.4
-
 thermal denaturation of the catalytic module Streptococcus pneumoniae