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Literature summary for 3.4.22.53 extracted from

  • Elce, J.S.; Hegadorn, C.; Gauthier, S.; Vince, J.W.; Davies, P.L.
    Recombinant calpain II: improved expression systems and production of a C105A active-site mutant for crystallography (1995), Protein Eng., 8, 843-848.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
the bacterial production of recombinant rat calpain II is improved greatly by the use of two compatible plasmids for the two subunits. The calpain small subunit C-terminal fragment is expressed from a new A15-based vector created by cloning T7 contol elements into pACYC177. This vector is compatible with the ColE1-based pET-24d(+) vector containing the calpain large subunit and the yield of calpain activity is increased at least 16fold by coexpression from theses two vectors. A high level of activity is also obtained from a bicistronic construct containing the subunit cDNAs under the control of one T7 promoter Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
C105S inactive mutant enzyme. The mutant enzyme provides a purified calpain, that is stable to autolysis and oxidation, which is likely to facilitate crystallization in both the presence and absence of calcium Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Rattus norvegicus

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
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Rattus norvegicus