Literature summary for 4.2.1.140 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.

Search for more literature for 4.2.1.140

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

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	-	-	-

Synonyms

Synonyms	Comment	Organism
D-gluconate dehydratase	-	Saccharolobus solfataricus
GNAD	-	Saccharolobus solfataricus

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Release 2023.1 (January 2023)