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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

Crystallization

Crystallization on EC 3.4.22.15 - cathepsin L

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chimera C25S/S24A/W26Y/M161L/D162N/G164A/V165M/E159S/D160S/E153S/P154S plus 173ESTESDNN180 to ISNNQ to 1.5 A resolution. Structure is almost identical to cathepsin L
crystal structure of the major histocompatibility complex class II-associated p41 li fragment bound to cathepsin L
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docking studies using inhibitor S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate reveal the simultaneous occupation of the S2, S3, and S1' subsites by hydrophobic and aromatic functionalities of the thiocarbazate. A key hydrogen bond is observed between the Gly66 backbone NH and the amino acid derived carbonyl of the diacyl hydrazine
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enzyme complexed with E-64
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hanging drop vapor diffusion method, 1.9 A X-ray structure of the complex of cathepsin L with the inhibitor 13
hanging drop vapour diffusion method with 17% (w/v) polyethylene glycol 8000 and 0.2 M ammonium sulfate
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in complex with inhibitor biphenylacetyl-(Nepsilon-biphenylacetyl)-L-Lys-D-Arg-L-Tyr-N-phenylethyl, hanging drop vapor diffusion method, using 19%(w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate, or in complex with inhibitor biphenylacetyl-(Nepsilon-biphenylacetyl)L-Lys-D-Arg-L-Phe-N-phenylethyl hanging drop vapor diffusion method, using 25% (w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate, or in complex with biphenylacetyl-M-Cys-D-Arg-L-Phe-N-phenylethyl, hanging drop vapor diffusion method, using 30% (w/v) polyethylene glycol 8000 and 200 mM ammonium sulfate
in complex with inhibitor Phe-Tyr-(OBut)-COCHO, hanging drop vapor diffusion method, using 15% (w/v) PEG 8K and 200 mM ammonium sulfate, pH 4.8. In complex with inhibitor Phe-Tyr-(tert-Bu)-diazomethylketone, hanging drop vapor diffusion method, using 30% (w/v) PEG 8K and 200 mM ammonium sulfate, pH 5.2
modelling 3D-structure of cathepsin L (PDB entry 1ICF), analysing residues binding the inhibitor p41-fragment, comparing binding sites of different Cathepsins
molecular docking study with inhibitor S-[2-[(2-ethylphenyl)amino]-2-oxoethyl] 2-[(2S)-2-[(tert-butoxycarbonyl)amino]-3-(1H-indol-3-yl)propanoyl]hydrazinecarbothioate using the structure of papain/CLIK-148, PDB entry 1cvz
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molecular modeling of complex with fragment p41 of major histocompatibility complex class II-associated invariant chain
purified inactivated cathepsin L mutant C25S, method optimization, rod-shaped crystals grow within 2 weeks in 0.1 M bis-Tris-HCl, pH 5.5, and 2 M ammonium sulfate, cube-shaped crystals grow within 2 weeks in 0.11 M HEPES-NaOH, pH 7.5, and 2.14 M ammonium sulfate, X-ray diffraction structure determination and analysis at 1.42 A resolution. The cathepsin L molecule is cleaved autocatalytically, with the cleaved region trapped in the active site cleft of the neighboring molecule demonstrated remaining low levels of catalytic activity
the inactive C25A cathepsin L mutant is cocrystallized with a histone H3 peptide covering residues 19-33 of the human histone H3 tail (QLATKAARKSAPATG), sitting drop vapor diffusion method, using 10% (v/v) isopropanol, 0.1 M sodium acetate trihydrate, pH 4.0, 22% polyethylene glycol 6000. The final crystallization condition for the apo-mC25A crystals is 0.2 M ammonium sulfate, 0.1 M sodium acetate trihydrate, pH 4.6, 30% (w/v) polyethylene glycol 2000 monomethylether
modelling 3D-structure of cathepsin L (PDB entry 1ICF), analysing residues binding the inhibitor p41-fragment, comparing binding sites of different Cathepsins
molecular modeling of complex with fragment p41 of major histocompatibility complex class II-associated invariant chain
homology modeling of the mature domain using human cathepsin L as a template. Enzyme contains a non-canonical aspartic acid at the base of the predicted active site S2 pocket, which limits substrate access
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in complex with propeptide, sitting drop vapor diffusion method, using 40% (w/v) polyethylene glycol 8000, 0.1 M ammonium bromide, and 0.1 M sodium citrate, at pH 4.0 and 25°C