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3.4.22.15: cathepsin L

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

Word Map on EC 3.4.22.15

Reaction

similar to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity towards protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity =

Synonyms

AgCatL, Aldrichina grahami cysteine proteinase, cat L, Cat L-A, Cath L, cath-L, cathepsin L, cathepsin L isoform CRA-b, cathepsin L-A, cathepsin L-A1, cathepsin L-A2, cathepsin L-A3, cathepsin L-B, cathepsin L-like, cathepsin L-like cysteine protease, cathepsin L-like enzyme, cathepsin L-like protease, cathepsin L-like protein, cathepsin L-like proteinase, cathepsin L-like rCPB2.8, cathepsin L1, cathepsin L1H, cathepsin L3, cathepsin-L, cathepsin-L T2V, CathL, CatL, CATL A IV, CATL-1, CATL-2, CatL1G, CatL1H, CatL5, CL1, CL3, CL41.5, CPL, cpl-1, CsCPL, CsCPL-m, CtL, CTSL, CTSL1, CTSL2, Cwp84, FhCL1, FhCL3, Har-CatL, human cathepsin L, major excreted protein, MEP, PDP, progesterone-dependent protein, rhodesain, SMCL1, SoCatL, sperm-histone protease, TsolCL

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.22 Cysteine endopeptidases
                3.4.22.15 cathepsin L

Engineering

Engineering on EC 3.4.22.15 - cathepsin L

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L69W
-
isoform CatL5 mutant, compared to the wild type enzyme the mutant has a higher efficiency of cleavage (kcat) against tosyl-Gly-L-Pro-L-Arg-7-amido-4-methylcoumarin
A205L
-
mutant shows an effective cathepsin K-like preference for Leu and Pro
C25A
inactive
C25S/S24A/W26Y
mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity
C25S/S24A/W26Y/M161L/D162N/G164A/V165M
mutant constructed to confer silica condensing activity to cathepsin L. Mutant displays significant condensing activity, but less than mutant C25S/S24A/W26Y
G139R
L67Y/A205L
-
mutation induces a switch of the enzymatic specificity toward small selective inhibitors and peptidyl substrates
T223V
T223V/C138S
the mutations prevent catalytic activity
T223V/C138S/K99A/K104A
the mutations disrupt the putative heparin binding site
T223V/DELTAE286-E289
the mutation shows reduced enzyme activity
T223V/DELTAE286-N293
the mutation shows reduced enzyme activity
T223V/M274L/D275N/G277A/V278M
the mutation shows reduced enzyme activity
C143A
site-directed mutagenesis
additional information