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Literature summary for 2.7.11.1 extracted from

  • Akizuki, K.; Toyama, T.; Yamashita, M.; Sugiyama, Y.; Ishida, A.; Kameshita, I.; Sueyoshi, N.
    Facile preparation of highly active casein kinase 1 using Escherichia coli constitutively expressing lambda phosphatase (2018), Anal. Biochem., 549, 99-106 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
recombinant CK1 undergoes autoinactivation via autophosphorylation in Escherichia coli cells and thus is undesirably prepared as a phosphorylated and inactivated kinase. To circumvent this problem, a protein expression system is established using Escherichia coli strain BL21(DE3)plambdaPP in which lambda protein phosphatase (lambdaPPase) is constitutively expressed. Using this system, recombinant CK1 isoforms (alpha, delta and epsilon) are readily prepared as unphosphorylated forms. CK1s prepared using BL21(DE3)plambdaPP show markedly higher activity than those prepared by the conventional BL21(DE3). The kinase activity of CK1delta from BL21(DE3)plambdaPP is higher than that prepared by a conventional method consisting of troublesome steps such as in vitro lambdaPPase treatment. The simple method using BL21(DE3)plambdaPP is valuable for preparing highly active CK1s Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q8BK63
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Mus musculus Q9DC28
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Mus musculus Q9JMK2
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-

Purification (Commentary)

Purification (Comment) Organism
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Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
brain
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Mus musculus
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Synonyms

Synonyms Comment Organism
casein kinase 1
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Mus musculus
CK1alpha
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Mus musculus
CK1delta
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Mus musculus
CK1epsilon
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Mus musculus