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Literature summary 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

EC Number Organism UniProt Comment Textmining
3.4.25.1 Methanocaldococcus jannaschii
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.4.25.1
-
 Methanocaldococcus jannaschii

Renatured (Commentary)

EC Number Renatured (Comment) Organism
3.4.25.1 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)

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

Synonyms

EC Number Synonyms Comment Organism
3.4.25.1 20S proteasome
-
 Methanocaldococcus jannaschii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.25.1 95
-
 recombinant enzyme Methanocaldococcus jannaschii
3.4.25.1 119
-
 wild-type enzyme Methanocaldococcus jannaschii

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.4.25.1 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
3.4.25.1 100 130 100°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