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An esterase is a hydrolase enzyme that splits esters into an acid and an alcohol in a chemical reaction with water called hydrolysis.
A wide range of different esterases exist that differ in their substrate specificity, their protein structure, and their biological function.
EC classification/list of enzymes
-
- Acetylesterase (EC 3.1.1.6), splits off acetyl groups
- Cholinesterase
- Acetylcholinesterase, inactivates the neurotransmitter acetylcholine
- Pseudocholinesterase, broad substrate specificity, found in the blood plasma and in the liver
- Cholinesterase
- Pectinesterase (EC 3.1.1.11), clarifies fruit juices
- Acetylesterase (EC 3.1.1.6), splits off acetyl groups
- EC 3.1.3: Phosphoric monoester hydrolases
- Phosphatase (EC 3.1.3.x), hydrolyses phosphoric acid monoesters into a phosphate ion and an alcohol
- Alkaline phosphatase, removes phosphate groups from many types of molecules, including nucleotides, proteins, and alkaloids.
- Phosphodiesterase (PDE), inactivates the second messenger cAMP
- cGMP specific phosphodiesterase type 5, is inhibited by Sildenafil (Viagra)
- Fructose bisphosphatase (3.1.3.11), converts fructose-1,6-bisphosphate to fructose-6-phosphate in gluconeogenesis
- Phosphatase (EC 3.1.3.x), hydrolyses phosphoric acid monoesters into a phosphate ion and an alcohol
- EC 3.1.4: Phosphoric diester hydrolases
- EC 3.1.5: Triphosphoric monoester hydrolases
- EC 3.1.6: Sulfuric ester hydrolases (sulfatases)
- EC 3.1.7: Diphosphoric monoester hydrolases
- EC 3.1.8: Phosphoric triester hydrolases
- Exonucleases (deoxyribonucleases and ribonucleases)
- EC 3.1.11: Exodeoxyribonucleases producing 5'-phosphomonoesters
- EC 3.1.13: Exoribonucleases producing 5'-phosphomonoesters
- EC 3.1.14: Exoribonucleases producing 3'-phosphomonoesters
- EC 3.1.15: Exonucleases active with either ribo- or deoxy-
- Endonucleases (deoxyribonucleases and ribonucleases)
- Endodeoxyribonuclease
- Endoribonuclease
- either deoxy- or ribo-
See also
External links
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Wikipedia content modification information:
- This page was last modified on 4 November 2008, at 05:29.
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