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Literature summary for 2.7.2.3 extracted from

  • Osvath, S.; Quynh, L.M.; Smeller, L.
    Thermodynamics and kinetics of the pressure unfolding of phosphoglycerate kinase (2009), Biochemistry, 48, 10146-10150.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
histidine-tagged PGK Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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Storage Stability

Storage Stability Organism
-80°C, 50 mM Tris buffer, 1 mM EDTA, 1 mM DTT, pH 7.8 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information pressure-jump unfolding kinetics of phosphoglycerate kinase at pressures between 50 and 150 MPa and time dependence of the conformational state of the protein followed by tryptophan fluorescence measurements from 30 s to 2 h: the activation volumes of the unfolding reaction are negative for the folded-intermediate, intermediate-unfolded, and unfolded-intermediate transitions Saccharomyces cerevisiae ?
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Synonyms

Synonyms Comment Organism
PGK
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Saccharomyces cerevisiae
phosphoglycerate kinase
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Saccharomyces cerevisiae