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Literature summary for 3.4.22.54 extracted from

  • Rey, M.A.; Davies, P.L.
    The protease core of the muscle-specific calpain, p94, undergoes Ca2+-dependent intramolecular autolysis (2002), FEBS Lett., 532, 401-406.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the C-terminally truncated form of the enzyme that comprises the protease cor, domains I and II, alone with its insertion sequence, IS1, and N-terminal leader sequence, NS is expressed in Escherichia coli BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information the C-terminally truncated form of the enzyme that comprises the protease core, domains I and II, alone with its insertion sequence, IS1, and N-terminal leader sequence, NS. This 47000 Da p94I-II minicalpain is stable during purification Homo sapiens

General Stability

General Stability Organism
isolation of the intact 94000 Da enzyme is difficult to achieve due to its rapid autolysis. The C-terminally truncated form of the enzyme that comprises the protease core, domains I and II, alone with its insertion sequence, IS1, and N-terminal leader sequence, NS. This 47000 Da p94I-II minicalpain is stable during purification. In the presence of Ca2+, p94I-II cleaves itself within the NS and IS1 sequences. Autolysis is an intramolecular event Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Homo sapiens
-