Literature summary for 3.4.21.107 extracted from

Sobiecka-Szkatula, A.; Polit, A.; Scire, A.; Gieldon, A.; Tanfani, F.; Szkarlat, Z.; Ciarkowski, J.; Zurawa-Janicka, D.; Skorko-Glonek, J.; Lipinska, B.
Temperature-induced conformational changes within the regulatory loops L1-L2-LA of the HtrA heat-shock protease from Escherichia coli (2009), Biochim. Biophys. Acta, 1794, 1573-1582.

Search for more literature for 3.4.21.107

Protein Variants

Protein Variants	Comment	Organism
S210A	proteolytically inactive, the mutant does not show significant changes of the secondary structure at the temperature range 20-45°C	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0C0V0	strain K-38 (pGP1-2)	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
beta-casein + H2O	-	Escherichia coli	?	-	?

Synonyms

Synonyms	Comment	Organism
DegP	-	Escherichia coli
HtrA	-	Escherichia coli

Temperature Stability [°C]

Temperature Stability Minimum [°C]	Temperature Stability Maximum [°C]	Comment	Organism
20	45	the proteolysis of casein at 20°C is negligible, then it increases in almost linear fashion up to 45°C. At the temperature range of 40-45°C, the activity is approximately 1.5fold higher than at 37°C	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)