EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.79 | glycoprotein |
- |
708696 |
| 3.4.21.79 | glycoprotein |
the enzyme possibly contains N-linked carbohydrates |
755124 |
| 3.4.21.79 | proteolytic modification |
endogenous GrB is produced as a zymogen bearing an N-terminal Gly-Glu dipeptide that prevents the formation of a functional catalytic triad. Upon packaging into lytic granules inside the immune cell, GrB is processed by the dipeptidyl peptidase cathepsin C (CatC), which cleaves off GrB's Gly-Glu dipeptide and frees the newly N-terminal Ile16 residue to insert into the interior of the molecule and form a salt bridge with Asp194. The resulting conformational change enables the simultaneous generation of an oxyanion hole and maturation of the active-site S1 pocket. Endogenous GrB is activated prior to its release from the lytic granules of T cells and NK cells |
752377 |
| 3.4.21.79 | proteolytic modification |
first expressed as an inactive proenzyme |
708696 |
| 3.4.21.79 | proteolytic modification |
GrB is synthesized as a zymogen (proGrB) and activated in cytotoxic granules by cathepsin C and cathepsin H. Mice lacking both cathepsin C and cathepsin H show reduced convertase activity. Despite this, cytotoxic lymphocytes from transgenic mice retain cytotoxic activity and some residual GrB activity, indicating that other proteases must also possess convertase activity |
709114 |
| 3.4.21.79 | proteolytic modification |
GrB is synthesized as a zymogen (proGrB) and activated in cytotoxic granules by the lysosomal cysteine protease cathepsin C which removes the N-terminal dipeptide Gly-Glu. Cathepsin H is an additional convertase of proGrB |
709114 |
