Literature summary for 3.4.22.B78 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.

Search for more literature for 3.4.22.B78

Cloned(Commentary)

Cloned (Comment)	Organism
expression in Escherichia coli	Pyrococcus horikoshii

Protein Variants

Protein Variants	Comment	Organism
E12T	the mutant enzyme is more stable than the wild-type enzyme	Pyrococcus horikoshii

Organism

Organism	UniProt	Comment	Textmining
Pyrococcus horikoshii	O59413	-	-
Pyrococcus horikoshii DSM 12428	O59413	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?
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

Synonyms	Comment	Organism
PhpI	ambiguous	Pyrococcus horikoshii

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
85	-	assay at	Pyrococcus horikoshii

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Pyrococcus horikoshii

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Release 2023.1 (January 2023)