EC Number   |
Protein Variants |
Reference |
|---|
   3.4.21.109 | A118D |
mutation causes an intra-molecular structural imbalance that impairs matriptase-2 activation |
708655 |
| 3.4.21.109 | A757S |
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme |
731663 |
| 3.4.21.109 | A757S/L785S |
site-directed mutagenesis, the mutant shows altered sensitivity to inhibition by prototype low-molecular weight ligands compared to the wild-type enzyme |
731663 |
| 3.4.21.109 | D217A |
site-directed mutagenesis, the mutant shows altered inhibition kinetics with different inhibitors, overview |
683778 |
| 3.4.21.109 | D482Y |
inhibited activation of matriptase |
652419 |
| 3.4.21.109 | D519Y |
inhibited activation of matriptase |
652419 |
| 3.4.21.109 | D521N |
point mutations D521N and E522K located in the conserved D/NXSDE motif in the LDLa2 domain of matriptase-2 are associated with iron-refractory iron deficiency anemia in patients and affect residues predicted to bind Ca2+. In vitro, the D521N and E522K mutants show reduced cell surface localization, increased Golgi retention, impaired autoactivation of matriptase-2, impaired cleavage of hemojuvelin, and impaired ability to repress Hamp1 reporter expression but are able to bind hemojuvelin |
706998 |
| 3.4.21.109 | D555Y |
inhibited activation of matriptase |
652419 |
| 3.4.21.109 | D598Y |
inhibited activation of matriptase |
652419 |
| 3.4.21.109 | D603-V855 |
using CHO-K1 cells, a secreted variant of rat r-matriptase consisting of the of the catalytic domain (and its N-terminal spacer region) (Asp603ΒVal855) L-matriptase is produced. HL-matriptase and L-matriptase are inhibited by purified maHAI-1 with a similar extent when t-butyloxycarbonyl-Gln-Ala-Arg-MCA and acetyl-Lys-Thr-Lys-Gln-Leu-Arg-MCA are were used as substrates |
698665 |
