Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.22.63 extracted from

  • Wachmann, K.; Pop, C.; van Raam, B.J.; Drag, M.; Mace, P.D.; Snipas, S.J.; Zmasek, C.; Schwarzenbacher, R.; Salvesen, G.S.; Riedl, S.J.
    Activation and specificity of human caspase-10 (2010), Biochemistry, 49, 8307-8315.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.63

Activating Compound

Activating Compound Comment Organism Structure
additional information procaspase-10 is proteolytically activated to caspase-10, mechanism of activation and the role of the inter-subunit cleavage, overview. Caspase-10 follows the proximity-induced dimerization model for apical caspases. Chemically inducible dimerization fusions activate the wild-type but not the cleavage site mutant caspase-10 Homo sapiens
Sodium citrate activates the wild-type enzyme up to 500fold and the D297A mutant 100fold at up to 1.0 M, is inhibitory above probably due to precipitation Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
the caspase-10 gene is linked to the caspase-8 gene, EC 3.4.22.61, at the human chromosome locus 2q33-34. Expression of His-tagged truncated mutant, with and without the D279A mutation, in Escherichia coli strain BL21 (DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
D297A site-directed mutagenesis, the single mutation D297A completely abrogates autocleavage between the subunits, the purified mutant is a single chain of 35 kDa. The cleavage site mutant has restricted specificity and highly reduced activity on protein substrates, overview Homo sapiens
additional information construction of a truncated mutant lacking the first 202 residues, and of the truncation mutant with a substitution D297A in the catalytic site, cloning into a vector with chimeric protein with an N-terminal His-tag followed by the Fv-domain. Chemically inducible dimerization fusions activate the wild-type but not the cleavage site mutant caspase-10 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
procaspase-3 + H2O Homo sapiens
-
 caspase-3 + ?
-
 ?
procaspase-7 + H2O Homo sapiens
-
 caspase-7 + ?
-
 ?
RIPK1 + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q92851
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification procaspase-10 is activated to caspase-10, mechanism of activation and the role of the inter-subunit cleavage, overview. Caspase-10 follows the proximity-induced dimerization model for apical caspases Homo sapiens

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged truncated mutant, with and without the D279A mutation, from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Ac-IETD-4-trifluoromethylcoumarin-7-amide + H2O
-
 Homo sapiens Ac-IETD + 7-amino-4-trifluoromethylcoumarin
-
 ?
BID + H2O cleavage at sites LQTD/G and IEPD/S, for apical caspases Homo sapiens ?
-
 ?
procaspase-3 + H2O
-
 Homo sapiens caspase-3 + ?
-
 ?
procaspase-7 + H2O
-
 Homo sapiens caspase-7 + ?
-
 ?
RIPK1 + H2O
-
 Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
dimer caspase-10 follows the proximity-induced dimerization model for apical caspases. Chemically inducible dimerization fusions activate the wild-type but not the cleavage site mutant caspase-10 Homo sapiens
More homology modelling of caspase-10, structural modeling based on the structure of procaspase-8, PDB ID 2K7Z 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
7.4
-
 assay at Homo sapiens

General Information

General Information Comment Organism
evolution human caspase-10 and caspase-8, EC 3.4.22.61, are highly homologous in their protein sequence, 46% identical in the catalytic domain, and their genes are on the same region of human chromosome 2q33-34 suggesting that they have a common ancestor Homo sapiens
metabolism apoptosis is a form of programmed cell death that requires members of a family of aspartate-specific cysteine proteases, called caspases, to both initiate and execute the apoptotic phenotype Homo sapiens
additional information residue D297 is essential for autocleavage, while even though the sequence surrounding D319 is compatible for cleavage by caspase-10, its location close to the compact core makes it unavailable for cleavage Homo sapiens
physiological function prodeath role for both cleaved and uncleaved caspase-10 Homo sapiens