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Literature summary for 3.4.22.53 extracted from

  • Hosfield C.M.; Moldoveanu T.; Davies P.L.; Elce J.S.; Jia Z.
    Calpain mutants with increased Ca2+ sensitivity and implications for the role of the C2-like domain (2001), J. Biol. Chem., 276, 7404-7407.
    View publication on PubMed
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Crystallization (Commentary)

Crystallization (Comment) Organism
the refined crystal structure of the mutant enzymes K226S, K230E, K234S and E504S in absence of Ca2+ are indistinguishable from wilde-type calpain Rattus norvegicus
wild-type and mutant calpains Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
E504S Ca2+ concentration required for half-maximal activity is 0.129 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme Rattus norvegicus
E504S mutation decreases specific activity to 90% compared to wild-type enzyme Rattus norvegicus
K225S mutation decreases specific activity to 88% compared to wild-type enzyme Rattus norvegicus
K226S Ca2+ concentration required for half-maximal activity is 0.226 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme Rattus norvegicus
K230E Ca2+ concentration required for half-maximal activity is 0.256 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme Rattus norvegicus
K230E mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme Rattus norvegicus
K230S Ca2+ concentration required for half-maximal activity is 0.261 mM compared to 0.242 mM for the wild-type enzyme Rattus norvegicus
K230S mutation has no significant effect on specific activity Rattus norvegicus
K234E mutation decreases the specific activity of the enzyme to 16% compared with the wild-type enzyme Rattus norvegicus
K234S Ca2+ concentration required for half-maximal activity is 0.183 mM compared to 0.242 mM for the wild-type enzyme. Refined structure of the mutant enzyme in absence of Ca2+ is indistinguishable from wild-type enzyme Rattus norvegicus
K234S mutation decreases specific activity to 81% compared to wild-type enzyme Rattus norvegicus
K234W Ca2+ concentration required for half-maximal activity is 0.159 mM compared to 0.242 mM for the wild-type enzyme Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ half-maximal activity of wild-type enzyme at 0.242 mM Rattus norvegicus
Ca2+ half-maximal activity is 0.242 mM for wilde-type enzyme, 0.129 mM for the E504S mutant, 0.226 mM for the K226S mutant, 0.261 mM for the K230S mutant, 0.183 mM for the K234 mutant, 0.256 mM for the K230E mutant and 0.159 mM for the K234E mutant Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Rattus norvegicus Q07009
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Purification (Commentary)

Purification (Comment) Organism
recombinant wild-type and mutant enzymes Rattus norvegicus
wild-type and mutant calpains Rattus norvegicus