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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

Posttranslational Modification

Posttranslational Modification on EC 3.4.22.15 - cathepsin L

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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
phosphoprotein
investigation of the phosphorylation status of the secreted and lysosomal cathepsin L forms by treatment with alkaline phosphatase (ALP). The 32-kDa form of cathepsin L is phosphorylated, while the 34-kDa form is already dephosphorylated. The 32-kDa form might migrate to the anode faster than the dephosphorylated 34-kDa form because of the retention of the negative charge by the phosphate moiety. Acid phosphatase might remove the phosphorus group from the 32-kDa form as soon as it enters the lysosomes, thereby converting it to the 34-kDa form. The phosphorylated status of 32-kDa cathepsin L suggests that the secreted form has never enters lysosomes
proteolytic modification
side-chain modification