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Encyclopedia > Trypsin
Trypsin

Crystal structure of Trypsin
Gene code:
Structure: Numerous
Recent publications:
protein type: Serine protease
Functions: digestion
Domains: serine protease domain
Diseases: cystic fibrosis, meconium ileus

Trypsin (EC 3.4.21.4) is a serine proteases found in the digestive system, where it breaks down proteins. It is used for numerous biotechnological processes. Image File history File links 1UTN.png‎ Summary X-ray crystallographic structure of Trypsin. ... X-ray crystallography is a technique in crystallography in which the pattern produced by the diffraction of X-rays through the closely spaced lattice of atoms in a crystal is recorded and then analyzed to reveal the nature of that lattice. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... In biochemistry, serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in proteins) that are characterised by the presence of a serine residue in the active center of the enzyme. ... Please wikify (format) this article as suggested in the Guide to layout and the Manual of Style. ... Contagious redirects here. ... Meconium from 12-hour-old newborn — the babys third bowel movement. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... In biochemistry, serine proteases or serine endopeptidases (newer name) are a class of peptidases (enzymes that cleave peptide bonds in proteins) that are characterised by the presence of a serine residue in the active center of the enzyme. ...

Contents


Chemistry and Function

Trypsin is secreted in to the intestine, where it acts to hydrolyse proteins in to smaller peptides or amino acids. This is necessary for the uptake of protein in the food. Trypsin catalyses the hydrolysis of peptide bonds. The enzymatic mechanism is like all other serine proteases: A catalytic triad serves to make the active site serine nucleophilic. This is achieved by modifying the electrostatic environment of the serine. The enzymatic reaction that trypsins catalyze is thermodynamically favorable but requires significant activation energy (it is "kinetically unfavorable"). Trypsins have an optimal operating pH of about 8 and optimal operating temperature of about 37°C[1]. The intestine is the portion of the alimentary canal extending from the stomach to the anus and, in humans and other mammals, consists of two segments, the small intestine and the large intestine. ... Hydrolysis is a chemical reaction or process in which a molecule is split into two parts by reacting with a molecule of water, which has the chemical formula H2O. One of the parts gets an OH- from the water molecule and the other part gets an H+ from the water. ... Peptides (from the Greek πεπτος, digestible), are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. ... Generic graph showing the effect of a catalyst in an hypothetical exothermic chemical reaction. ... Three amino acid residues found inside the active site of certain proteases. ... The active site of an enzyme is the binding site where catalysis occurs. ... Serine is one of the 20 natural amino acids. ... ‹ The template below has been proposed for deletion. ... The sparks generated by striking steel against a flint provide the activation energy to initiate combustion in this Bunsen burner. ... It has been suggested that this article or section be merged with Enzyme. ... pH is a measure of the acidity of a solution, in terms of activity of hydrogen ions (H+). For dilute solutions, however, it is convenient to substitute the activity of the hydrogen ions with the molarity (mol/L) of the hydrogen ions (however, this is not necessarily accurate at higher...


The aspartate residue (Asp 189) located in the catalytic pocket (S1) of trypsins is responsible for attracting and stabilizing positively-charged lysine and/or arginine, and is thus responsible for the specificity of the enzyme. This means that trypsin predominantly cleaves proteins at the carboxyl side (or "C-terminal side") of the amino acids lysine and arginine, except when either is followed by proline [1]. Trypsins are considered endopeptidases, i.e., the cleavage occurs within the polypeptide chain rather than at the terminal amino acids located at the ends of polypeptides. Aspartic acid, also known as aspartate, the name of its anion, is one of the 20 natural proteinogenic amino acids which are the building blocks of proteins. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... A carboxyl or carboxylic group is a functional group consisting of a carbon atom and an oxygen atom doubly bonded to each other. ... The C-terminal end refers to the extremity of a protein or polypeptide terminated by an amino acid with a free carboxyl group (COOH). ... An amino acid residue is what is left of an amino acid once a molecule of water has been lost (an H+ from the nitrogenous side and an OH- from the carboxylic side) in the formation of a peptide bond. ... Lysine is one of the 20 amino acids normally found in proteins. ... Arginine (Arg) is an α-amino acid. ... L-Proline is one of the twenty proteinogenic units which are used in living organisms as the building blocks of proteins. ... Peptidases (proteases [pronounced pro-tea-aces] and proteolytic enzymes are also commonly used) are enzymes which break peptide bonds of proteins. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ... Peptides (from the Greek πεπτος, digestible), are the family of short molecules formed from the linking, in a defined order, of various α-amino acids. ...


Trypsin is produced in the pancreas in the form of inactive zymogen, trypsinogen. It is then secreted into the small intestine, where the enzyme enterokinase activates it into trypsin by proteolytic cleavage. The resulting trypsins themselves activate more trypsinogens (autocatalysis), so only a small amount of enterokinase is necessary to start the reaction. This activation mechanism is common for most serine proteases, and serves to prevent autodigestion of the pancreas. The pancreas is an organ in the digestive system that serves two major functions: exocrine - producing pancreatic juice containing digestive enzymes. ... A zymogen or a proenzyme, is an inactive enzyme precursor. ... Trypsinogen (EC 3. ... Diagram showing the small intestine In biology the small intestine is the part of the gastrointestinal tract between the stomach and the large intestine (colon). ... Enterokinase is used to activate the zymogen, trypsinogen, to trypsin. ... A single chemical reaction is said to have undergone autocatalysis, or be autocatalytic, if the reaction product is itself the catalyst for that reaction. ...


The activity of trypsins is not affected by the inhibitor tosyl phenylalanyl chloromethyl ketone TPCK, which deactivates chymotrypsin. This is important because, in some applications, like mass spectrometry, the specificity of cleavage is important. An inhibitor is a type of effector (biology) that decreases or prevents a chemical reaction. ... Tosyl phenylalanyl chloromethyl ketone (TPCK) is a protease inhibitor. ... Chymotrypsin Chymotrypsin (bovine γ chymotrypsin: PDB 1AB9, EC 3. ... Basic schematic of mass spectrometry Mass spectrometry is an analytical technique used to measure the mass-to-charge ratio of ions. ...


Involvement in disease

One consequence of inheriting the autosomal recessive disease cystic fibrosis is a deficiency of trypsin and other digestive enzymes from the pancreas. This leads to the disorder termed meconium ileus. This disorder involves intestinal obstruction (ileus) due to overly thick meconium, the dark sticky stuff that is present in the intestine at birth and which is normally broken down by trypsins and other proteases, then defecated. The pancreas is an organ in the digestive system that serves two major functions: exocrine - producing pancreatic juice containing digestive enzymes. ... Meconium from 12-hour-old newborn — the babys third bowel movement. ... Ileus refers to limited or absent intestinal passage. ... Meconium from 12-hour-old newborn — the babys third bowel movement. ... The intestine is the portion of the alimentary canal extending from the stomach to the anus and, in humans and other mammals, consists of two segments, the small intestine and the large intestine. ...


Storage

Trypsins should be stored at very cold temperatures (between −20°C and −80°C) to prevent autolysis (self-cleavage). Autolysis may also be prevented by storage of trypsins at pH 3. When the pH is adjusted back to pH 8 activity returns.


Applications

Trypsin is available in high quantities in pancreases, and can be purified rather easily. Hence it has been used widely in various biotechnological processes.


In a tissue culture lab, trypsins are used to re-suspend cells adherent to the petri dish wall during the process of harvesting cells.


Trypsins can be used to breakdown casein in milk. If trypsin is added to a solution of milk powder, the breakdown of casein will cause the milk to become translucent. The rate of reaction can be measured by using the amount of time it takes for the milk to turn translucent. In optics, transparency is the property of being transparent, or allowing light to pass. ...


Trypsin can also be used to dissociate dissected cells. For example, prior to cell fixing and sorting.


Trypsin is commonly used in proteomics experiments to digest proteins into peptides. Trypsin is particularly suited for this, since it has a very well defined specificity. Proteomics is the large-scale study of proteins, particularly their structures and functions. ...


Trypsin can also be used to dissolve blood clots in its microbial form and treat inflammation in its pancreatic form.


References

  1. a  Promega PDF - 58kB

  Results from FactBites:
 
trypsin - Encyclopedia.com (1377 words)
Trypsin is one of the three principal digestive proteinases, the other two being pepsin and chymotrypsin.
Trypsin, produced in an inactive form by the pancreas, is remarkably similar in chemical composition and in structure to the other chief pancreatic proteinase, chymotrypsin.
In vitro degradation of a polyether urethane by trypsin
Trypsin (100 words)
The pH optimum for trypsin activity is pH 7-9, and it is permanently inactivated at pH > 11.
Trypsin retains activity in 0.1% SDS, 1 M guanidine[?] HCl, and 30% ethanol.
Together with pepsin and chymotrypsin, trypsin is one of the three principal digestive proteinases.
  More results at FactBites »

 
 

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