EC Number   |
Subunits |
Reference |
|---|
    4.1.1.90 | ? |
x * 94000, SDS-PAGE |
696184, 698705, 701022, 701214 |
| 4.1.1.90 | ? |
x * 99000, SDS-PAGE |
438309 |
| 4.1.1.90 | heterodimer |
- |
716060 |
| 4.1.1.90 | monomer |
- |
698697 |
| 4.1.1.90 | monomer |
1 * 77000, SDS-PAGE |
438307 |
| 4.1.1.90 | More |
binding site in the carboxyl half of the gamma-glutamyl carboxylase. Carboxylase may be cleaved by trypsin into an amino-terminal 30 kDa and a carboxyl-terminal 60 kDa fragment joined by disulfide bond(s), and the propeptide binds to the 60 kDa fragment |
698705 |
| 4.1.1.90 | More |
disulfide bond between cysteines 99 and 450, five transmembrane domains |
699860 |
| 4.1.1.90 | More |
five transmembrane domains. Transmembrane domain interactions and residue proline 378 are essential for proper structure, especially disulfide bond formation |
696271 |
| 4.1.1.90 | More |
limited tryptic digestion of the carboxylase yields two disulfide-linked fragments with molecular masses of 30 and 60 kDa, corresponding to the amino and carboxy-terminal part of the gamma-glutamyl carboxylase |
697924 |
