Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.5 extracted from

  • Kasetty, G.; Papareddy, P.; Kalle, M.; Rydengard, V.; Moergelin, M.; Albiger, B.; Malmsten, M.; Schmidtchen, A.
    Structure-activity studies and therapeutic potential of host defense peptides of human thrombin (2011), Antimicrob. Agents Chemother., 55, 2880-2890.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

General Information

General Information Comment Organism
additional information peptides of the C-terminal region of human thrombin are released upon proteolysis and identified in human wounds displaying length- and sequence-dependent antimicrobial, e.g. against Gram-negative bacteria Escherichia coli and Pseudomonas aeruginosa, the Gram-positive bacterium Staphylococcus aureus, and the fungus Candida albicans, as well as immunomodulating effects. A peptide length of at least 20 amino acids is required for effective anti-inflammatory effects in macrophage models, as well as optimal antimicrobial activity Homo sapiens