Literature summary for 3.4.22.15 extracted from

Sosnowski, P.; Turk, D.
Caught in the act the crystal structure of cleaved cathepsin L bound to the active site of cathepsin L (2016), FEBS Lett., 590, 1253-1261 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Protein Variants

Protein Variants	Comment	Organism
C25S	site-directed mutagenesis, almost inactive mutant that still performs autocatalytic cleavage	Homo sapiens

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
lysosome	-	Homo sapiens	5764	-

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	P07711	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the proenzyme performs autocatalytic cleavage resulting in the mature enzyme	Homo sapiens

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme performs autocatalytic cleavage	Homo sapiens	?	-	?

Synonyms

Synonyms	Comment	Organism
cathepsin L1	-	Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
37	-	assay at	Homo sapiens

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.5	-	assay at	Homo sapiens

General Information

General Information	Comment	Organism
malfunction	the C25S mutation abolishes the enzyme activity	Homo sapiens
additional information	cathepsin L's structure reveals the fold of the papain-like enzyme composed of two domains named left (L-) and right (R-). The L-domain is alpha-helical, whereas the R-domain forms a beta-barrel fold. Between the two domains, locates a V-shaped active site cleft on which the L- and R-domain catalytic residues C25 and H163 are positioned	Homo sapiens
physiological function	cathepsin L is a ubiquitously expressed papain-like cysteine protease involved in the endosomal degradation of proteins and has numerous roles in physiological and pathological processes, such as arthritis, osteoporosis, and cancer	Homo sapiens