EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.26 | glycoprotein |
the recombinant elastase contains three potential N-glycosylation sites N43, N212, and N280 (Asn-Xaa-Ser/Thr consensus sequences), potential role of N-glycosylation in the activity and stability. Non- and glycosylated isoforms of rPAE display similar kinetic parameters for hydrolyzing casein in aqueous medium, and when catalyzing bipeptide synthesis in 50% v/v DMSO, they exhibit identical substrate specificity and activity, and produce similar yields. The N-linked oligosaccharides of Pichia pastoris-secreted glycoproteins are a high-mannose type (Man8GlcNAc2 or Man9GlcNAc2) with molecular weights close to 2 kDa |
733746 |
| 3.4.24.26 | proteolytic modification |
LasB is produced as a precursor protein that requires autocatalytic processing to ensure proper folding as it is exported across the outer membrane. Ca2+ is needed either for efficient transcription of lasB or during the process of folding and export, as calcium plays a role in the structural integrity of LasB |
-, 753798 |
| 3.4.24.26 | proteolytic modification |
the enzyme is synthesized in the cytoplasm as a pre-proenzyme consisting of a 2.4-kDa signal peptid, an 18.1-kDa pro-peptide and the 33.1-kDa mature protein. The signal peptide is cleaved from the pre-proenzyme during translocation across the inner membrane, leaving a 51.2-kDa proenzyme (consisting of the pro-peptide and the mature protein). In the periplasm, the proenzymeis folded, guided by the pro-peptide, and a disulfide bond between Cys270 and Cys297 is formed. The pro-peptide is then removed by autoproteolysis, but remains non-covalently attached to mature pseudolysin. A second disulfide bond between Cys30 and Cys58 of the enzyme is then formed. The pro-peptide and mature enzyme are secreted from the cell together, where they dissociate, and the liberated pro-peptide is degraded by the active enzyme |
733746 |
| 3.4.24.26 | proteolytic modification |
the pro-sequence, consisting of 174 amino acids, is cleaved by autoproteolytic processing in the periplasm to produce the active, mature elastase of 301 amino acids |
-, 717673 |
