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Literature summary for 2.7.1.178 extracted from

  • Kim, S.; Lee, S.B.
    Soluble expression of archaeal proteins in Escherichia coli by using fusion-partners (2008), Protein Expr. Purif., 62, 116-119.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
produced as inclusion bodies in Escherichia coli when polyhistidine is used as a fusion tag. To reduce inclusion body formation in Escherichia coli, the enzyme is fused with three partners, thioredoxin, glutathione-S-transferase, and N-utilization substance A. With the use of fusion-partners, the solubility of the archaeal protein is remarkably enhanced, and the soluble fraction of the recombinant protein is increased in this order: thioredoxin > glutathione-S-transferase > N-utilization substance A. In the case of recombinant enzyme, the enzyme activity of the Trx-fused protein is 200-fold higher than that of the polyhistidine-fusion protein Saccharolobus solfataricus

Organism

Organism UniProt Comment Textmining
Saccharolobus solfataricus Q97U29
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-

Synonyms

Synonyms Comment Organism
2-keto-3-deoxy-D-gluconate kinase
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Saccharolobus solfataricus
KDGK
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Saccharolobus solfataricus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
assay at Saccharolobus solfataricus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2
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assay at Saccharolobus solfataricus