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Literature summary for 2.7.2.3 extracted from

  • Hess, D.; Hensel, R.
    The 3-phosphoglycerate kinase of the hyperthermophilic archaeum Pyrococcus woesei produced in Escherichia coli: loss of heat resistance due to internal translation initiation and its restoration by site-directed mutagenesis (1996), Gene, 172, 121-124.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli at optimal growth temperatures (37°C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation Pyrococcus woesei

Organism

Organism UniProt Comment Textmining
Pyrococcus woesei P61884
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Synonyms

Synonyms Comment Organism
PwPGK
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Pyrococcus woesei

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
85
-
the enzyme from the original organism is completely resistant to heat inactivation for 35 min. Expression in Escherichia coli at optimal growth temperatures (37°C) yields a product which shows a tight association with a 28000 Da protein and exhibits low thermal stability (about 80% loss of activity after 5 min) suggesting a misfolding of the protein. As proved by N-terminal amino acid sequence analysis, the 28000 Da protein represents a 226-amino acid C-terminal fragment of the 3-phosphoglycerate kinase. Mutagenesis experiments confirm the assumption that the fragment originates by an internal translation initiation Pyrococcus woesei