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Literature summary for 3.4.22.59 extracted from

  • Mueller, I.; Lamers, M.B.; Ritchie, A.J.; Park, H.; Dominguez, C.; Munoz-Sanjuan, I.; Maillard, M.; Kiselyov, A.
    A new apo-caspase-6 crystal form reveals the active conformation of the apoenzyme (2011), J. Mol. Biol., 410, 307-315.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged apo-caspase-6 and caspase-6 in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
recombinant caspase-6 comprising residues 24–179 and 194–293 after self-cleavage of the zymogen, overall structure of the four caspase-6 p202/p102 tetramers in the asymmetric unit, and caspase-6 in complex with inhibitor Ac-VEID-CHO, hanging-drop vapor diffusion method, mixing of 0.001 ml protein solution containing 20 mM sodium acetate, pH 5.5, 50 mM NaCl, and 0.5 mM Tris(hydroxypropyl)phosphine with 0.001 ml of reservoir solution consisting of 3.3 M sodium nitrate, 0.1 M Tris, pH 7.4, 0.5% ethyl acetate, and 5 mM Tris(hydroxypropyl)phosphine, and microseeding, 1 week, 20°C, X-ray diffraction structure determination and analysis at 2.53 A resolution, molecular replacement, structure comparisons, overview Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
Ac-VEID-CHO a reversible caspase-6 inhibitor, enzyme-inhibitor complex structure, overview Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P55212
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged apo-caspase-6 and caspase-6 from Escherichia coli by nickel affinity chromatography and gel filtration Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Z-VEID-R110 + H2O caspase-6 recognition peptide covalently linked to two amine groups of the fluorescent dye rhodamine 110, fluorogenic assay Homo sapiens 2 Z-VEID + R110
-
?

Subunits

Subunits Comment Organism
More active canonical conformation of the apoenzyme apo-caspase-6, comparison to the apostructure of pH-inactivated caspase-6,crystal structure analysis, overview. Caspase-6 subunits p20 and p10 comprise residues 24–179 and 194–293, respectively Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
caspase-6 activity is optimal around neutral pH and is almost entirely lost at pH 5.0 and below Homo sapiens

General Information

General Information Comment Organism
physiological function caspase-6 is a key component in the pathway of neurodegenerative diseases such as Alzheimer's disease and Huntington's diseases Homo sapiens