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Literature summary extracted from

  • Zhan, D.; Han, W.; Feng, Y.
    Experimental and computational studies indicate the mutation of Glu12 to increase the thermostability of oligomeric protease from Pyrococcus horikoshii (2011), J. Mol. Model., 17, 1241-1249.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
3.4.22.B78 expression in Escherichia coli Pyrococcus horikoshii

Protein Variants

EC Number Protein Variants Comment Organism
3.4.11.B7 E12T protease activity of E12T is 3.8 fold higher than that of wild-type enzyme. The mutant is more stable than wild-type at 85°C Pyrococcus horikoshii
3.4.22.B78 E12T the mutant enzyme is more stable than the wild-type enzyme Pyrococcus horikoshii

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Organism

EC Number Organism UniProt Comment Textmining
3.4.11.B7 Pyrococcus horikoshii O59413
-
-
3.4.11.B7 Pyrococcus horikoshii DSM 12428 O59413
-
-
3.4.22.B78 Pyrococcus horikoshii O59413
-
-
3.4.22.B78 Pyrococcus horikoshii DSM 12428 O59413
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.11.B7 Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 is responsible for substrate binding Pyrococcus horikoshii Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
-
?
3.4.11.B7 Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 is responsible for substrate binding Pyrococcus horikoshii DSM 12428 Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
-
?
3.4.22.B78 Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 plays an important role in substrate binding Pyrococcus horikoshii Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
-
?
3.4.22.B78 Ala-Ala-Phe-Arg-7-amido-4-methylcoumarin + H2O Glu12 plays an important role in substrate binding Pyrococcus horikoshii DSM 12428 Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.B78 PhpI ambiguous Pyrococcus horikoshii

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.4.11.B7 85
-
assay at Pyrococcus horikoshii
3.4.22.B78 85
-
assay at Pyrococcus horikoshii

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.4.11.B7 85
-
mutant enzyme E12T is more stable than wild-type at 85°C Pyrococcus horikoshii

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.4.11.B7 7.5
-
assay at Pyrococcus horikoshii
3.4.22.B78 7.5
-
assay at Pyrococcus horikoshii