Literature summary for 3.4.11.B7 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 3.4.11.B7

Protein Variants

Protein Variants	Comment	Organism
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

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 is responsible for substrate binding	Pyrococcus horikoshii	Ala-Ala-Phe-Arg + 7-amino-4-methylcoumarin	-	?
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	-	?

Temperature Optimum [°C]

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

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
85	-	mutant enzyme E12T is more stable than wild-type at 85°C	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)