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Encyclopedia > Pepsin
Pepsin

Pepsin in complex with pepstatin Image File history File links Information_icon. ... Image File history File links 1PSO.png‎ Pepsin in complex with pepstatin. ...

Other names: Pepsinogen
Genetic data
Gene code: 8885 (HGNCid)
Protein Structure/Function
Protein type: protease
Functions: digestion
Other
Molecular interactions: pepstatin
Database Links
EC number: 3.4.23.1

Pepsin is a digestive protease (EC 3.4.23.1) released by the chief cells in the stomach that functions to degrade food proteins into peptides. For a non-technical introduction to the topic, please see Introduction to genetics. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Proteases (proteinases, peptidases, or proteolytic enzymes) are enzymes that break peptide bonds between amino acids of proteins. ... This article or section does not adequately cite its references or sources. ... In science, a molecule is a group of atoms in a definite arrangement held together by chemical bonds. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... For the Physics term GUT, please refer to Grand unification theory The gastrointestinal or digestive tract, also referred to as the GI tract or the alimentary canal or the gut, is the system of organs within multicellular animals which takes in food, digests it to extract energy and nutrients, and... Proteases (proteinases, peptidases, or proteolytic enzymes) are enzymes that break peptide bonds between amino acids of proteins. ... The Enzyme Commission number (EC number) is a numerical classification scheme for enzymes, based on the chemical reactions they catalyze. ... A gastric chief cell (or peptic cell, or gastric zymogenic cell) is a cell in the stomach that releases pepsinogen and rennin. ... With the exception of the animal varients box, this article deals with the human stomach. ... A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... Peptides are the family of molecules formed from the linking, in a defined order, of various amino acids. ...


According to American Heritage Dictionary, pepsin derives from the Greek word pepsis, meaning digestion (peptein: to digest). The American Heritage Dictionary of the English Language The American Heritage Dictionary of the English Language (AHD) is an American dictionary of the English language published by Boston publisher Houghton-Mifflin, the first edition of which appeared in 1969. ... This article or section does not adequately cite its references or sources. ...


Pepsin was discovered by Theodor Schwann[1] in 1836. It was the first animal enzyme to be discovered. Theodore Schwann Theodor Schwann (December 7, 1810 in Neuss, Prussia - January 11, 1882, in Cologne) was a German physiologist, histologist and cytologist. ... Year 1836 (MDCCCXXXVI) was a leap year starting on Friday (link will display the full calendar) of the Gregorian Calendar (or a leap year starting on Wednesday of the 12-day slower Julian calendar). ... Ribbon diagram of the enzyme TIM, surrounded by the space-filling model of the protein. ...

Contents

Precursor

Pepsin are expressed as a pro-form zymogen, pepsinogen, whose primary structure has an additional 44 amino acids. Protein expression is a subcomponent of gene expression. ... A zymogen or a proenzyme, is an inactive enzyme precursor. ... A protein primary structure is a chain of amino acids. ... Phenylalanine is one of the standard amino acids. ...


In the stomach, chief cells release pepsinogen. This zymogen is activated by hydrochloric acid (HCl), which is released from parietal cells in the stomach lining. The hormone gastrin and the vagus nerve trigger the release of both pepsinogen and HCl from the stomach lining when food is ingested. HCl creates an acidic environment which allows pepsinogen to unfold and cleave itself in an autocatalytic fashion, thereby generating pepsin (the active form). Pepsin cleaves the 44 amino acids from pepsinogen to create more pepsin. Pepsin will digest up to 20% of ingested carbon bonds by cleaving preferentially after the N-terminal of aromatic amino acids such as phenylalanine and tyrosine. It will not cleave at bonds containing valine, alanine or glycine. Peptides may be further digested by other proteases (in the duodenum) and eventually absorbed by the body. In general, a Chief cell (or a zymogenic cell) is a cell which releases a precursor enzyme. ... Pepsin is a protease, a digestive enzyme that degrades food proteins in the stomach; the other important digestive enzymes are trypsin and chymotrypsin. ... The chemical compound hydrochloric acid is the aqueous (water-based) solution of hydrogen chloride gas (HCl). ... Parietal cells (also called oxyntic cells) are cells located in the stomach epithelium. ... In humans, gastrin is a hormone that stimulates secretion of gastric acid by the stomach. ... The vagus nerve (also called pneumogastric nerve or cranial nerve X) is the tenth of twelve paired cranial nerves, and is the only nerve that starts in the brainstem (within the medulla oblongata) and extends, through the jugular foramen, down below the head, to the abdomen. ... Pepsin is a protease, a digestive enzyme that degrades food proteins in the stomach; the other important digestive enzymes are trypsin and chymotrypsin. ... A single chemical reaction is said to have undergone autocatalysis, or be autocatalytic, if the reaction product is itself the catalyst for that reaction. ... Phe redirects here. ... Tyrosine (from the Greek tyros, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in cheese[1][2]), 4-hydroxyphenylalanine, or 2-amino-3(4-hydroxyphenyl)-propanoic acid, is one of the 20 amino acids that are used by cells to synthesize proteins. ... Valine is one of the 20 natural amino acids, and is coded for in DNA. Nutritionally, valine is also an essential amino acid. ... Alanine (Ala, A) also 2-aminopropanoic acid is a non-essential α-amino acid. ... For the plant, see Glycine (plant). ... In anatomy of the digestive system, the duodenum is a hollow jointed tube connecting the stomach to the jejunum. ...


Pepsin is stored as pepsinogen so it will only be released when needed, and does not digest the body's own proteins in the stomach's lining.


Pepsin functions best in acidic environments, particularly those in a pH of 1.


See also

Other important digestive proteases are the pancreatic enzymes trypsin and chymotrypsin. Pepsin degrade if the pH is more than 5.0 Trypsin (EC 3. ... Chymotrypsin (bovine γ chymotrypsin: PDB 1AB9, EC 3. ...


External links

  • Pepsin A description from BRENDA database
  • MeSH Pepsin+A
  • MeSH Pepsinogens
  • MeSH Pepsinogen+A
  • MeSH Pepsinogen+C

Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. ... Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. ... Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. ... Medical Subject Headings (MeSH) is a huge controlled vocabulary (or metadata system) for the purpose of indexing journal articles and books in the life sciences. ...

References

  1. ^ Florkin M (1957). "Discovery of pepsin by Theodor Schwann.". Rev Med Liege 12 (5): 139-44. PMID 13432398. 

  Results from FactBites:
 
Pepsin - LoveToKnow 1911 (416 words)
PEPSIN, an enzyme or ferment obtained by drying the mucous lining of the fresh and healthy stomach of a pig, sheep or calf.
Pepsin is used to help gastric digestion in old people and in those in whom there is a deficient secretion of the gastric juice.
Pepsin digests the albumens but is useless in the digestion of fats or carbohydrates.
pepsin - Encyclopedia.com (1137 words)
Pepsin is one of three principal protein-degrading, or proteolytic, enzymes in the digestive system, the other two being chymotrypsin and trypsin.
Pepsin is synthesized in an inactive form by the stomach lining; hydrochloric acid, also produced by the gastric mucosa, is necessary to convert the inactive enzyme and to maintain the optimum acidity (p H 1-3) for pepsin function.
Pepsin and other proteolytic enzymes are used in the laboratory analysis of various proteins; pepsin is also used in the preparation of cheese and other protein-containing foods.
  More results at FactBites »

 
 

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