EC Number   |
Posttranslational Modification |
Reference |
|---|
   3.4.22.B49 | glycoprotein |
the enzyme contains three potential glycosylation sites at residues 18 (N-A-S), 38 (N-S-S), and 99 (N-A-A) |
717398 |
| 3.4.22.B49 | proteolytic modification |
auto-activation of the inactive zymogen proCL1 in the slightly acidic gut. The autoactivation process is 40fold faster at pH 4.5 than at pH 7.0. Molecular weight of zymogen is 38 kDa, of mature form 25 kDA, respectively |
694804 |
| 3.4.22.B49 | proteolytic modification |
cleavage of the propeptide from proCTSL1 for enzyme maturation and activtaion |
754348 |
| 3.4.22.B49 | proteolytic modification |
FhCL1 is expressed as 37000 Da zymogen that autocatalytically processes at pH 4.5 to produce a 24500 Da mature enzyme |
680930 |
| 3.4.22.B49 | proteolytic modification |
procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11/His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11-/-His10 sequence by preactivated FheCL1, but the latter is not. Another Fasciola hepatica secreted protease FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1L12P/C26G by cleavage at the Pro12-Ser11-/-His10 sequence. The autoactivation of a variant enzyme with a single replacement, FheproCL1L12P, is very slow but is increased 40fold in the presence of FheCL2 |
680776 |
| 3.4.22.B49 | proteolytic modification |
procathepsin L1 autocatalytically processes and activates to its mature enzyme (FheCL1) over a wide pH range 4.0-7.3. Activation is more rapid at low pH. Maturation initiates with cleavages of a small proportion of molecules within the central region of the prosegment, possibly by intramolecular events. Activation to fully mature enzymes is achieved by a precise intermolecular cleavage at a Leu12-Ser11/His10 sequence within the nonconserved C-terminal region of the prosegment. Active site variant FheproCL1C26G and a double variant FheproCL1L12P/C26G cannot autocatalytically process. The former is susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1, but the latter is not. Another Fasciola hepatica secreted protease FheCL2, which, unlike FheCL1, can readily accept proline in the S2 subsite of its active site, can trans-process the double variant FheproCL1L12P/C26G by cleavage at the Pro12-Ser11/His10 sequence. The autoactivation of a variant enzyme with a single replacement, FheproCL1L12P, is very slow but is increased 40fold in the presence of FheCL2 |
680776 |
| 3.4.22.B49 | proteolytic modification |
slightly acidic pH of the parasite gut facilitates the auto-catalytic activation of FheCL1 from its inactive proFheCL1 zymogen. This process is about 40fold faster at pH 4.5 than at pH 7.0. The zymogen proFheCL1 (38000 Da) is auto-catalytically processed at pH 4.5 by intermolecular cleavage and removal of the prosegment to release a fully mature and active enzyme (25000 Da) |
694804 |
