Literature summary for 3.4.22.38 extracted from

Li, Z.; Kienetz, M.; Cherney, M.M.; James, M.N.; Broemme, D.
The crystal and molecular structures of a cathepsin K:chondroitin sulfate complex (2008), J. Mol. Biol., 383, 78-91.

Search for more literature for 3.4.22.38

Activating Compound

Activating Compound	Comment	Organism	Structure
chondroitin 4-sulfate	18.5 kDa and 37 kDa fractions, the unique triple-helical collagen-degrading activity of cathepsin K depends on the formation of complexes with bone-or cartilage-resident glycosaminoglycans, such as chondroitin 4-sulfate, structure of the complex involving Asp6, Arg8, Lys9, Lys10, Ile171, Glu172, and Asn190 for interaction, the binding sites with chondroitin 4-sulfate are located in the R-domain of cathepsin K and are distant from its active site, detailed overview	Homo sapiens

Cloned(Commentary)

Cloned (Comment)	Organism
expression as the proenzyme in Pichia pastoris	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
purified and activated, recombinant cathepsin K in complex with chondroitin sulfate in presence or absence of inhibitor E64, which prevents autocatalytic cleavage of cathepsin K, 25 mg/ml enzyme-inhibitor complex of ratio 1:1 in 50 mM sodium acetate buffer, pH 5.5, hanging drop vapor diffusion method, mixing with an equal volume of reservoir solution containing 30% v/v 2-methyl-2,4-pentanediol, 0.1 M sodium acetate buffer, pH 4.5, and 20 mM calcium chloride, macroseeding, X-ray diffraction structure determination and analysis at 1.8 A resolution	Homo sapiens

Crystallization (Comment)

Organism

purified and activated, recombinant cathepsin K in complex with chondroitin sulfate in presence or absence of inhibitor E64, which prevents autocatalytic cleavage of cathepsin K, 25 mg/ml enzyme-inhibitor complex of ratio 1:1 in 50 mM sodium acetate buffer, pH 5.5, hanging drop vapor diffusion method, mixing with an equal volume of reservoir solution containing 30% v/v 2-methyl-2,4-pentanediol, 0.1 M sodium acetate buffer, pH 4.5, and 20 mM calcium chloride, macroseeding, X-ray diffraction structure determination and analysis at 1.8 A resolution

Homo sapiens

Inhibitors

Inhibitors	Comment	Organism	Structure
E64	i.e. L-3-carboxy-trans-2,3-epoxypropionyl-leucylamido-(4-guanidino)butane, inhibitor-enzyme complex structure 9in presence of different chondroitin 4-sulfate fractions, overview	Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
additional information	Homo sapiens	cathepsin K is the major collagenolytic enzyme produced by bone-resorbing osteoclasts	?	-	?

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
proteolytic modification	the recombinant proenzyme is activated by cleavage through pepsin	Homo sapiens

Source Tissue

Source Tissue	Comment	Organism	Textmining
osteoclast	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	cathepsin K is the major collagenolytic enzyme produced by bone-resorbing osteoclasts	Homo sapiens	?	-	?