EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.21.35 | glycoprotein |
- |
683016, 717572 |
| 3.4.21.35 | glycoprotein |
the enzyme has two glycosylated sites within the active protease domain |
753294 |
| 3.4.21.35 | proteolytic modification |
activation by trypsin |
647504, 647505 |
| 3.4.21.35 | proteolytic modification |
preprokallikrein consists of 262 amino acid residues |
647500 |
| 3.4.21.35 | proteolytic modification |
thermolysin activates prokallikrein cleaving off the N-terminal Ile1-Val2 |
647487 |
| 3.4.21.35 | proteolytic modification |
urinary and renal kallikrein exist in both active and proenzyme form |
647505 |
| 3.4.21.35 | proteolytic modification |
zymogen: prokallikrein |
647502, 647504 |
| 3.4.21.35 | proteolytic modification |
zymogen: prokallikrein can by activated by two types of enzymes, serine proteases which cleave at the C-terminus of basic amino acids and by a metalloproteinase that cleaves at the N-terminus of hydrophobic amino acids |
647487 |
| 3.4.21.35 | side-chain modification |
- |
647485 |
| 3.4.21.35 | side-chain modification |
both kallikrein and prokallikrein display multiple molecular forms with differences in both molecular sizes and charges. The structural differences are found to be due to glycosylation, with the high-molecular-weight species glycosylated at three Asn-linked sites and the low-molecular-weight species at two of the three Asn-linked sites. The multiply charged kallikrein isoforms are derived from different numbers of sialic acids attached at the detected Asn-linked carbohydrates |
647501 |
