Information about Zymogenic
A zymogen (or proenzyme) is an inactive enzyme precursor. 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 a lysosome where a specific part of the precursor enzyme is cleaved in order to activate it. The amino acid chain that is released upon activation is called the activation peptide.
Hydrolysis is a chemical reaction or process in which a chemical compound is broken down by reaction with water.[1][2] This is the type of reaction that is used to break down polymers.
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Etymology
Very often the suffix "-ogen" can be added to the name of the enzyme to indicate that it is in the precursor form. Some enzymes have a pro- prefix to denote their inactive status e.g. Proalbumin, which is converted into albumin.Examples
Examples of zymogens:- Trypsinogen
- Chymotrypsinogen
- Pepsinogen
- Most proteins in the coagulation system
- Some of the proteins of the complement system
- Caspases
- Proelastase
- Prolipase
See also
Enzymes are proteins that catalyze (i.e. accelerate) chemical reactions.[1] In enzymatic reactions, the molecules at the beginning of the process are called substrates, and the enzyme converts them into different molecules, the products.
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A protein precursor, also called a pro-protein or pro-peptide, is an inactive protein (or peptide) that can be turned into an active form by posttranslational modification. The name of the precursor for a protein is often prefixed by pro.
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- :Not to be confused with electrolysis
Hydrolysis is a chemical reaction or process in which a chemical compound is broken down by reaction with water.[1][2] This is the type of reaction that is used to break down polymers.
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Lysosomes are organelles that contain digestive enzymes (acid hydrolases). They digest excess or worn out organelles, food particles, and engulfed viruses or bacteria. The membrane surrounding a lysosome prevents the digestive enzymes inside from destroying the cell.
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amino acid is a molecule that contains both amine and carboxyl functional groups. In biochemistry, this term refers to alpha-amino acids with the general formula H2NCHRCOOH, where R is an organic substituent.
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Trypsinogen (EC 3.4.23.18/20/21/23/24/26) is the precursor form of the pancreatic enzyme trypsin or a zymogen. It is found in pancreatic juice, along with amylase, lipase, and chymotrypsinogen.
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Chymotrypsinogen is a precursor of the digestive enzyme chymotrypsin (zymogen).
This molecule is inactive and must be cleaved by trypsin, and then by other chymotrypsin molecules before it can reach its full activity. Its activity is the conversion of proteins to amino acids.
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This molecule is inactive and must be cleaved by trypsin, and then by other chymotrypsin molecules before it can reach its full activity. Its activity is the conversion of proteins to amino acids.
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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.
According to American Heritage Dictionary, pepsin derives from the Greek word pepsis, meaning digestion (
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According to American Heritage Dictionary, pepsin derives from the Greek word pepsis, meaning digestion (
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Coagulation is a complex process by which blood forms solid clots. It is an important part of hemostasis (the cessation of blood loss from a damaged vessel) whereby a damaged blood vessel wall is covered by a platelet- and fibrin-containing clot to stop bleeding and begin repair of
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Caspases are enzymes known as proteases, which play essential roles in apoptosis (cell death) and inflammation. As proteases, they are enzymes that cleave (cut) other proteins.
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