EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.24.27 | more |
no glycoprotein |
31136 |
| 3.4.24.27 | proteolytic modification |
autodegradation at position 154-155 |
717113 |
| 3.4.24.27 | proteolytic modification |
autolytic processing. Secreted proteases are produced as prepro-proteins. The pre-peptide is cleaved-off during Sec-controlled secretion, and the active protease emerges outside the cell after folding of the proprotein and autolytic removal of the pro-peptide. The protein is translocated through the membrane at the expense of ATP and the pre-peptide is cleaved off by a type I signal peptidase. The pro-part plays two roles in this process: it facilitates folding by acting as an intra-molecular chaperone and it inhibits protease activity of the folded pro-enzyme |
718367 |
| 3.4.24.27 | proteolytic modification |
synthesis as a pre-proprotein |
670784 |
| 3.4.24.27 | proteolytic modification |
the pre-pro-enzyme contains a signal peptide and a prosequence, the prosequence acts as an intramolecular chaperone for autocatalytic cleavage of the linking peptide bond |
-, 683276 |
| 3.4.24.27 | proteolytic modification |
thermolysin encoded by LIC13322 has a signal peptide for secretion, a fungalin/thermolysin propeptide (FTP) domain, a propeptide (PepSY) domain, and a catalytic domain M4 that includes peptidase_M4 and peptidase_M4_C |
-, 753062 |
| 3.4.24.27 | proteolytic modification |
thermolysin is synthesized as inactive pre-proenzyme and receives autocatalytic cleavage of the peptide bond linking the pro- and mature sequences, overview |
684019 |
| 3.4.24.27 | proteolytic modification |
thermolysin performs Co2+-stimulable autolysis |
683616 |
