What is elastase activated by?
Table of Contents
What is elastase activated by?
Biosynthesis. Pancreatic elastase is formed by activation of proelastase from mammalian pancreas by trypsin. After processing to proelastase, it is stored in the zymogen granules and then activated to elastase in the duodenum by the tryptic cleavage of a peptide bond in the inactive form of the precursor molecule.
What does the elastase enzyme break down?
Elastase is an enzyme made by special tissue in the pancreas, an organ in your upper abdomen. Elastase helps break down fats, proteins, and carbohydrates after you eat. It’s a key part of your digestive process. In a healthy pancreas, elastase will be passed in the stool.
What peptide bonds does elastase cleave?
Elastase also has the important immunological role of breaking down Shigella virulence factors. This is accomplished through the cleavage of peptide bonds in the target proteins. The specific peptide bonds cleaved are those on the carboxyl side of small, hydrophobic amino acids such as glycine, alanine, and valine.
How does elastase cleave?
A serine protease that preferentially cleaves at the C-terminus of alanine, valine, serine, glycine, leucine or isoleucine. Elastase has a unique ability to digest elastin. This enzyme can be used alone or in combination with other proteases for protein analysis by mass spectrometry and other applications.
What type of enzyme is elastase?
serine protease
Elastase-1 Elastase (EC 3.4. 21.36) is a serine protease produced by the pancreas that catalyzes cleavage of carboxyl groups present on small hydrophobic amino acids, such as glycine, alanine, and valine.
What is the role of elastase?
Elastase (EC 3.4. 21.36) is a serine protease produced by the pancreas that catalyzes cleavage of carboxyl groups present on small hydrophobic amino acids, such as glycine, alanine, and valine. Its primary role is the breakdown of elastin, a protein that imparts elasticity to connective tissue.
Where does elastase cleave?
What is the product of elastase?