EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.21 | glycoprotein |
- |
695182, 755547 |
| 3.4.21.21 | glycoprotein |
modified on two sites by diantennary, disialylated non-fucosylated (A2S2) glycans |
692535 |
| 3.4.21.21 | glycoprotein |
N-glycosylation at Asn322, rapid deglycosylation by PNGase F |
684040 |
| 3.4.21.21 | glycoprotein |
N-glycosylation at Asp145 and Asp322, and O-glycosylation |
683855 |
| 3.4.21.21 | more |
FVII undergoes many posttranslational modifications such as gamma-carboxylation, N- and O-glycosylation, beta-hydroxylation |
692535 |
| 3.4.21.21 | proteolytic modification |
factor VII is activated by thrombin |
683297, 683298 |
| 3.4.21.21 | proteolytic modification |
FVII is secreted as a single-chain polypeptide and a peptide bond cleavage (after arginine 152) results in the enzymatically active form FVIIa. The two polypeptide chains are referred to as light (152 residues) and heavy (254 residues). The light chain contains an N-terminal gamma-carboxyglutamic acid (Gla) domain, in which all ten Glu residues are posttranslationally-carboxylated |
710606 |
| 3.4.21.21 | proteolytic modification |
proteolytic cleavage of the peptide bond between Arg152 and Ile153 converts the procoagulant protein factor VII to an activated two-chain form. The formation of a salt bridge between Ile153 and Asp343 drives the conversion to the active form |
654508 |
| 3.4.21.21 | proteolytic modification |
the activated two-chain enzyme factor VIIa is formed from the single chain zymogen factor VII |
95326 |
| 3.4.21.21 | proteolytic modification |
the product of the reaction with factor X, the activated factor X is also the most efficient activator of zymogen factor VII |
654496 |
