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

BRENDA support

Literature summary extracted from

  • Burster, T.; Macmillan, H.; Hou, T.; Schilling, J.; Truong, P.; Boehm, B.O.; Zou, F.; Lau, K.; Strohman, M.; Schaffert, S.; Busch, R.; Mellins, E.D.
    Masking of a cathepsin G cleavage site in vivo contributes to the proteolytic resistance of major histocompatibility complex class II molecules (2010), Immunology, 130, 436-46.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.4.21.20 aspartyl protease inhibitor pepstatin
-
 Homo sapiens
3.4.21.20 cysteine protease inhibitor E64
-
 Homo sapiens
3.4.21.20 leupeptin
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
3.4.21.20 Homo sapiens
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.4.21.20 neutrophil
-
 Homo sapiens
-
3.4.21.20 sputum
-
 Homo sapiens
-

Synonyms

EC Number Synonyms Comment Organism
3.4.21.20 CatG
-
 Homo sapiens
3.4.21.20 serine protease cathepsin G
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
3.4.21.20 physiological function acts as a major histocompatibility complex calls II-degrading protease, involved in major histocompatibility complex class II turnover Homo sapiens