EC Number   |
Posttranslational Modification |
Reference |
|---|
   1.10.3.1 | glycoprotein |
- |
658894, 727645 |
| 1.10.3.1 | glycoprotein |
13% carbohydrate |
673001 |
| 1.10.3.1 | glycoprotein |
recombinant secreted enzyme, glycosylated at its only potential N-glycosylation site, with a glycan consisting of two N-acetylglucosamines and five mannoses, low amounts of shorter glycan forms can be detected at this site |
673560 |
| 1.10.3.1 | glycoprotein |
the full-length AoCO4 shows O-glycosylation at Thr14 (mannose residue) and N-glycosylation at Asn30 (N-acetylglucosamine residue), Asn104 (N-acetylglucosamineN-acetylglucosaminemannose), Asn222 (N-acetylglucosamine) and Asn348 (N-acetylglucosamine). The glycans in AoCO4 might be involved in stabilising the secreted protein |
725559 |
| 1.10.3.1 | proteolytic modification |
PPO from membrane shows no diphenolase activity unless it is roteolytically activated by trypsin, kinetics of the activation process of latent PPO by trypsin at pH 7.0 and 25°C |
674774 |
| 1.10.3.1 | proteolytic modification |
proteolytic activation by trypsin and chymotrypsin, proteolytic inactivation by papain |
675076 |
| 1.10.3.1 | proteolytic modification |
the mature protein is processed from the C-terminus by a cleavage of a peptide fragment of about 20 kDa |
673560 |
| 1.10.3.1 | proteolytic modification |
the N-terminal analysis of the protein reveals N-terminal processing taking place in the Kex2/furin-type protease cleavage site and removing the first 51 amino acids from the putative N-terminus |
701876 |
| 1.10.3.1 | ribonucleoprotein |
- |
658894 |
