Where is elastase located?

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.

Where is elastase found in the neutrophil?

azurophil granules
The neutrophil form of elastase (EC 3.4. 21.37) is 218 amino acids long, with two asparagine-linked carbohydrate chains (see glycosylation). It is present in azurophil granules in the neutrophil cytoplasm.

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.

What amino acid does elastase cleave?

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 is pancreatic elastase made?

acinar cells
Pancreatic elastase is a form of elastase that is produced in the acinar cells of the pancreas, initially produced as an inactive zymogen and later activated in the duodenum by trypsin.

What is the substrate of elastase?

The best substrates for human pancreatic elastase 2 were glutaryl-Ala-Ala-Pro-Leu-p nitroanilide and succinyl-Ala-Ala-Pro-Met-p-nitroanilide. However, there was little difference among substrates with leucine, methionine, phenylalanine, tyrosine, norvaline, or norleucine in the P1 position.

Where is the catalytic triad located?

A catalytic triad is a set of three coordinated amino acids that can be found in the active site of some enzymes. Catalytic triads are most commonly found in hydrolase and transferase enzymes (e.g. proteases, amidases, esterases, acylases, lipases and β-lactamases).

What does trypsin bind to?

Function. Trypsin or serine protease 1 is a medium size globular protein that functions as a pancreatic serine protease. This enzyme hydrolyzes bonds by cleaving peptides on the C-terminal side of the amino acid residues lysine and arginine.

Which amino acids does elastase cleave?