Enzyme Commission Number
EC 3.4.21.107
Product Overview
High-quality enzyme products.
Well-established quality management system.
Reaction
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val┼Val
Function
This serine endopeptidase is essential for the clearance of denatured or aggregated proteins from the inner-membrane and periplasmic space in Escherichia coli. Natural substrates of the enzyme include colicin A lysis protein, pilin subunits and MalS from E. coli. The enzyme has weak peptidase activity with casein and other non-native substrates. The peptidase acts as a chaperone at low temperatures but switches to a peptidase (heat shock protein) at higher temperatures. Molecular chaperones and peptidases control the folded state of proteins by recognizing hydrophobic stretches of polypeptide that become exposed by misfolding or unfolding. They then bind these hydrophobic substrates to prevent aggregation or assist in protein refolding. If attempts at refolding fail, then irreversibly damaged proteins are degraded by peptidases such as this enzyme. Belongs in peptidase family S1C.
Other name
DegP; DegP protease; HtrA; high temperature requirement protease A; HrtA heat shock protein; protease Do; Do protease
Production Methods
Fermentation
Package
on customer request
Applications
Research Use
Storage
Should be stored in a dry and cool place, avoiding high temperature.
Appearance / Form
powder or liquid
Odor
Normal microbial fermentation odour.
WARNINGS
Keep sealed after use every time to avoid microbial infections and inactivation of enzymes until its finish.
Description
Microbial enzymes have been used in a large number of fields, such as chemical, agricultural and biopharmaceutical industries. Our enzyme production services are based on bacteria, fungi, and yeast, from strain selection, optimization, and process development to scale-up production.
