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Literature summary for 3.4.25.1 extracted from

  • Frankenberg, R.J.; Hsu, T.S.; Yakota, H.; Kim, R.; Clark, D.S.
    Chemical denaturation and elevated folding temperatures are required for wild-type activity and stability of recombinant Methanococcus jannaschii 20S proteasome (2001), Protein Sci., 10, 1887-1896.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Methanocaldococcus jannaschii

Renatured (Commentary)

Renatured (Comment) Organism
denaturation of the proteasome by 4 M urea followed by high-temperature dialysis. The wild-type temperature optimum is restored, but only if proteasome subunits are denatured and refolded prior to assembly Methanocaldococcus jannaschii

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide + H2O
-
Methanocaldococcus jannaschii ?
-
?

Synonyms

Synonyms Comment Organism
20S proteasome
-
Methanocaldococcus jannaschii

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
95
-
recombinant enzyme Methanocaldococcus jannaschii
119
-
wild-type enzyme Methanocaldococcus jannaschii

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
80 100 80°C: about 60% of maximal activity, 100°C: about 45% of maximal activity, recombinant enzyme, hydrolysis of benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide Methanocaldococcus jannaschii
100 130 100°C: about 40% of maximal activity, 130°C: about 20% of maximal activity, wild-type enzyme, hydrolysis of benzyloxycarbonyl-Ala-Ala-Leu-4-nitroanilide Methanocaldococcus jannaschii