EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.16 | glycoprotein |
- |
707007 |
| 3.4.22.16 | glycoprotein |
the deduced amino acid sequence has three potential N-glycosylation sites at the Asn96, Asn223 and Asn267 residues |
698021 |
| 3.4.22.16 | glycoprotein |
the enzyme harbors two glycosylation sites, Asn79P on the mini-chain of the prodomain and Asn115 on the mature domain. No glycan is built for Asn79P in cathepsin H due to poor electron density, although it is glycosylated |
755176 |
| 3.4.22.16 | proteolytic modification |
- |
638836 |
| 3.4.22.16 | proteolytic modification |
mutant lacking the mini chain, autocatalytic processing at pH 5.0, 37°C, processing is accelerated in presence of 0.025 mg/ml of dextran, prolonged activation results in both cases in decrease of enzyme acivtiy |
650194 |
| 3.4.22.16 | proteolytic modification |
posttranslational processing |
638815 |
| 3.4.22.16 | proteolytic modification |
processing in three steps from proenzyme to endopeptidase intermediate to aminopeptidase, mini-chain formed from part of propeptide that is cleaved off |
638836 |
| 3.4.22.16 | proteolytic modification |
propeptide-binding region of enzyme is structurally rearranged during maturation processing and mini-chain formation, which impairs the effective recognition of mature enzyme by its propeptide |
667865 |
| 3.4.22.16 | proteolytic modification |
the enzyme is synthesized as an inactive proenzyme, the N-terminal prodomain (Ala1P-Pro93P) is cleaved off for maturation, a C-terminal mature domain (Tyr1-Val220) with a disulfide bridge between Cys212 and the mini-chain Cys80P remains. Procathepsin H is not autoactivated but can be transactivated by cathepsin L. The prodomain of procathepsin H has an N-terminal helical subdomain (Ala1P-Ser75P) and an extended portion (Glu76P-Pro93P) that links the helical subdomain to Tyr1 of the mature domain |
755176 |
| 3.4.22.16 | proteolytic modification |
time-course of synthesis and posttranslational processing: proforms of MW 41000 are converted to single-chain cathepsin of MW 28000 within 1 h of translation |
638819 |
