EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.21 | glycoprotein |
putative |
717683 |
| 3.4.24.21 | phosphoprotein |
the protease has a putative signal peptide, 11 potential phosphorylation sites, and two disulfide bridges revealed by computational analysis |
733803 |
| 3.4.24.21 | proteolytic modification |
both LAST and LAST_MAM are synthesized as zymogens. LAST-MAM is active in its zymogen form |
699565 |
| 3.4.24.21 | proteolytic modification |
in active BMP-1 an additional ion seems to be coordinated by several residues. The new N-terminus that results from intracellular activation of BMP-1, Ala121, is acetylated (N-Ace A121) and, together with Glu224, Asp312 and three water molecules, it interacts with this ion, overview |
753172 |
| 3.4.24.21 | proteolytic modification |
the enzyme is synthesized as inactive zymogen, the N-terminal pro-segments are variable in length and rather unstructured, astacin-family zymogen structure, overview. They inhibit the catalytic zinc following an aspartate-switch mechanism mediated by an aspartate embedded in a conserved motif, FXGD. Removal of the prosegment reveals a deep and extended active-site cleft, which in general shows preference for aspartate residues in the specificity pocket, S1' |
733445 |
