Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

3.4.22.B49: cathepsin L1

This is an abbreviated version!
For detailed information about cathepsin L1, go to the full flat file.

Word Map on EC 3.4.22.B49

Reaction

clear preference for Arg at P1 position (Lys, Glu, Thr, and Met are less efficient). FheCL1 shows distinct preference for hydrophobic amino acids in the P2, Leu is favored. Cathepsin L1 can accommodate Pro in the P2 position, but less efficiently than cathepsin L2. FheCL1 produces clear degradation fragments from collagen =

Synonyms

cat-L1H, cathepsin L1, cathepsin L1 cysteine protease, cathepsin L1 protease, cathepsin L1 proteinase, cathepsin L1g, cathepsin L1H, CatL1, CgCTSL1, CGI_10027418, CL1, CPFhW, CTSL1, cysteine proteinase 3, Da-CTSL1, FgCatL1H, FhCL1, FheCL1, FhpCL1

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.B49 cathepsin L1

Engineering

Engineering on EC 3.4.22.B49 - cathepsin L1

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C25G
-
inactive zymogen since the active site Cys is replaced by a Gly
C26G
-
active site variant FheproCL1C26G cannot autocatalytically process. It is susceptible to trans-processing at a Leu12-Ser11/His10 sequence by preactivated FheCL1
L12P
-
the autoactivation of the variant enzyme FheproCL1L12P is very slow but is increased 40fold in the presence of FheCL2
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
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
L209A
Ki value for benzyloxycarbonyl-Phe-Ala-diazomethyl ketone is 73fold lower than value for wild-type FheCL1
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
additional information