In biochemistry, a zymogen (/ˈzaɪmədʒən, -moʊ-/[1][2]), also called a proenzyme (/ˌproʊˈɛnzaɪm/[3][4]), is an inactive precursor of an enzyme. A zymogen requires a biochemical change (such as a hydrolysis reaction revealing the active site, or changing the configuration to reveal the active site) for it to become an active enzyme. The biochemical change usually occurs in Golgi bodies, where a specific part of the precursor enzyme is cleaved in order to activate it. The inactivating piece which is cleaved off can be a peptide unit, or can be independently-folding domains comprising more than 100 residues. Although they limit the enzyme's ability, these N-terminal extensions of the enzyme or a "prosegment" often aid in the stabilization and folding of the enzyme they inhibit.[citation needed]
The pancreas secretes zymogens partly to prevent the enzymes from digesting proteins in the cells in which they are synthesised. Enzymes like pepsin are created in the form of pepsinogen, an inactive zymogen. Pepsinogen is activated when chief cells release it into the gastric acid, whose hydrochloric acid partially activates it.[5] Another partially inactivated pepsinogen completes the activation by removing the peptide, turning the pepsinogen into pepsin. Accidental activation of zymogens can happen when the secretion duct in the pancreas is blocked by a gallstone, resulting in acute pancreatitis.[citation needed]
Fungi also secrete digestive enzymes into the environment as zymogens. The external environment has a different pH than inside the fungal cell and this changes the zymogen's structure into an active enzyme.[citation needed]
Another way that enzymes can exist in inactive forms and later be converted to active forms is by activating only when a cofactor, called a coenzyme, is bound. In this system, the inactive form (the apoenzyme) becomes the active form (the holoenzyme) when the coenzyme binds.
In the duodenum, the pancreatic zymogens, trypsinogen, chymotrypsinogen, proelastase and procarboxypeptidase, are converted into active enzymes by enteropeptidase and trypsin. Chymotrypsinogen, a single polypeptide chain of 245 amino acids residues, is converted to alpha-chymotrypsin, which has three polypeptide chains linked by two of the five disulfide bond present in the primary structure of chymotrypsinogen.[6]
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Zymogen activation
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Zymogen Activation | What Is A Zymogen | Proteolytic Activation | Peptide Cleavage | Proenzymes |
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What is the role of zymogen? Why is it an Inactive precursor?
Transcription
Examples
Examples of zymogens:
- Trypsinogen
- Chymotrypsinogen
- Pepsinogen
- Most proteins in the coagulation system (examples, prothrombin, or plasminogen)
- Some of the proteins of the complement system
- Procaspases
- Pacifastin
- Proelastase
- Prolipase
- Procarboxypolypeptidases
See also
References
- ^ "zymogen". Merriam-Webster.com Dictionary. Retrieved 2016-01-24.
- ^ "zymogen". Lexico UK English Dictionary. Oxford University Press. Archived from the original on 2020-03-22.
- ^ "proenzyme". Merriam-Webster.com Dictionary. Retrieved 2016-01-24.
- ^ "proenzyme". Lexico UK English Dictionary. Oxford University Press. Archived from the original on 2020-03-22.
- ^ Dworken HJ (1982-01-01). "CHAPTER 4 - Functional Characteristics of the Stomach". Gastroenterology: Pathophysiology and Clinical Applications. Butterworth-Heinemann. pp. 85–104. doi:10.1016/b978-0-409-95021-2.50009-1. ISBN 978-0-409-95021-2. Retrieved 2020-12-15.
- ^ Mina U, Kumar P (January 2016). "Life Sciences, Fundamentals and Practice, Part I". ResearchGate. Retrieved 2020-12-15.
External links
- Zymogens - Washington.edu
- Molecular mechanisms for the conversion of zymogens to active proteolytic enzymes
This page was last edited on 18 April 2024, at 17:30