EC Number   |
Protein Variants |
Reference |
|---|
   3.4.22.B49 | C25G |
inactive zymogen since the active site Cys is replaced by a Gly |
694804 |
| 3.4.22.B49 | C26G |
active site variant FheproCL1C26G cannot autocatalytically process. It is susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1 |
680776 |
| 3.4.22.B49 | L12P |
the autoactivation of the variant enzyme FheproCL1L12P is very slow but is increased 40fold in the presence of FheCL2 |
680776 |
| 3.4.22.B49 | L12P/C26G |
active site variant FheproCL1L12P/C26G cannot autocatalytically process. It is not susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1. 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 |
680776 |
| 3.4.22.B49 | L205A |
mutation of FheCL1 markedly alters the activity profile from wild type enzyme. This variant exhibits a broader substrate specificity by accepting Phe, Trp, and Tyr at P2, residues that are not accepted by wild type FheCL1. kcat/Km for benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide is 1.5fold higher than wild-type value, kcat/Km for benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide is 2.5fold lower than wild-type value, kcat/Km for benzyloxycarbonyl-Pro-L-Arg-4-methylcoumarinyl-7-amide is 2.2fold lower than wild-type value, kcat/Km for tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide is 6.6fold lower than wild-type value, kcat/Km for tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide is 5fold than wild-type value |
680930 |
| 3.4.22.B49 | L209A |
Ki value for benzyloxycarbonyl-Phe-Ala-diazomethyl ketone is 73fold lower than value for wild-type FheCL1 |
680930 |
| 3.4.22.B49 | L67Y |
no significant change in the P2 preference to wild type FheCL1. This substitution does not alter the activity of the enzyme toward Pro in the P2 position. kcat/Km for benzyloxycarbonyl-L-Phe-L-Arg-4-methylcoumarinyl-7-amide is 2.3fold lower than wild-type value, kcat/Km for benzyloxycarbonyl-L-Leu-L-Arg-4-methylcoumarinyl-7-amide is 1.8fold lower than wild-type value, kcat/Km for benzyloxycarbonyl-Pro-L-Arg-4-methylcoumarinyl-7-amide is 1.2fold lower than wild-type value, kcat/Km for tosyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide is similar to wild-type value, kcat/Km for tert-butoxycarbonyl-Gly-Pro-Arg-4-methylcoumarinyl-7-amide is 1.8fold higher than wild-type value. Ki value for benzyloxycarbonyl-Phe-Ala-diazomethyl ketone is 12fold lower than wild-type value |
680930 |
| 3.4.22.B49 | more |
construction and evaluation of a chimeric LAP-CL1 mutant made from Fasciola hepatica leucine ainopeptidase and cathepsin L1. The protein contains the most antigenic sequences of LAP (amino acids 192-281, UniProt ID Q17TZ3) and CL1 (amino acids 173-309) |
754321 |
| 3.4.22.B49 | more |
construction of a chimeric protein from leucine aminopeptidase (FhLAP) and cathepsin L1 (FhCL1) of Fasciola hepatica. The chimeric mutant protein with Quil A adjuvant is used for vaccination of Katahdin x East Friesian male sheep |
755635 |
| 3.4.22.B49 | more |
screening of cathepsin L1/cathepsin L2 mimotopes and use of an M13 phage random 12-mers peptide library to evaluate their immunogenicity in sheep |
700565 |
