What Thermolysin Cleaves?
Table of Contents
Thermolysin is a metallopeptidase and cleaves peptide bonds at the N-terminal of hydrophobic amino acids including alanine, isoleucine, leucine, methionine, phenylalanine, threonine, tryptophan, tyrosine, and valine [2. G.
What is the function of thermolysin?
Function. Thermolysin (TML) is a thermostable metalloproteinase enzyme from Bacillus thermoproteolyticus. It catalyzes the hydrolysis of peptide bonds containing hydrophobic residues.
What amino acids 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.
How do metalloproteases work?
Metalloproteases (metallo, metal) are members of a clan of proteases that contain a metal ion at their active site which acts as a catalyst in the hydrolysis peptide binds.
What does endopeptidase break down?
Endopeptidase or endoproteinase are proteolytic peptidases that break peptide bonds of nonterminal amino acids (i.e. within the molecule), in contrast to exopeptidases, which break peptide bonds from end-pieces of terminal amino acids.
Where does carboxypeptidase A cleave?
The carboxypeptidases cleave single amino acids off the free carboxyl ends of proteins. Carboxypeptidase A cleaves off aromatic or branched chain amino acids; carboxypeptidase B cleaves off basic amino acids. The end result of pancreatic proteolysis is some free amino acids and a mixture of oligopeptides.
Where is elastase found?
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.
What is the cleavage site for thermolysin?
Thermolysin preferentially cleaves at the N-terminus of the hydrophobic residues leucine, phenylalanine, valine, isoleucine, alanine and methionine. The optimal digestion temperature range is 65–85°C. Thermolysin activity is optimal at pH 5.0–8.5. Cut sites for Elastase, Pepsin and Thermolysin. Cut sites for Elastase, Pepsin and Thermolysin.
Why is thermolysin thermostable?
Active at High Digestion Temperatures Thermolysin is a thermostable metalloproteinase. The high digestion temperature stability of this enzyme may be useful as an alternative to denaturants to improve digestion of proteolytically resistant proteins.
Why is thermolysin used as an alternative to denaturant?
The high digestion temperature stability of this enzyme may be useful as an alternative to denaturants to improve digestion of proteolytically resistant proteins. Thermolysin preferentially cleaves at the N-terminus of the hydrophobic residues leucine, phenylalanine, valine, isoleucine, alanine and methionine.
What is the optimum temperature for thermolysin digestion?
Thermolysin preferentially cleaves at the N-terminus of the hydrophobic residues leucine, phenylalanine, valine, isoleucine, alanine and methionine. The optimal digestion temperature range is 65–85°C. Thermolysin activity is optimal at pH 5.0–8.5.