Lyase: Difference between revisions
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Latest revision as of 12:59, 18 March 2025
Lyase is a class of enzymes that catalyze the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction can also often be performed. For example, an enzyme that catalyzed this reaction would be a lyase:
ATP → cAMP + PPi
Lyases differ from other enzymes in that they require only one substrate for the reaction in one direction, but two for the reverse reaction.
Classification[edit]
Lyases are classified as EC 4 in the EC number classification of enzymes. Lyases can be further classified into seven subclasses:
- EC 4.1 includes enzymes that cleave carbon-carbon bonds, such as decarboxylases, aldolases, and dehydratases.
- EC 4.2 includes enzymes that cleave carbon-oxygen bonds, such as dehydratases.
- EC 4.3 includes enzymes that cleave carbon-nitrogen bonds.
- EC 4.4 includes enzymes that cleave carbon-sulfur bonds.
- EC 4.5 includes enzymes that cleave carbon-halide bonds.
- EC 4.6 includes enzymes that cleave phosphorus-oxygen bonds.
- EC 4.99 includes other lyases.
Examples[edit]
Some of the enzymes classified as lyases include:
- Adenylyl cyclase
- ATP citrate lyase
- ATP: corrinoid adenosyltransferase
- Carbamoyl phosphate synthetase
- Cystathionine beta synthase
- Fructose-1,6-bisphosphatase
- Fumarase
- Histidine ammonia-lyase
- Isocitrate lyase
- Methylmalonyl-CoA mutase
- Pectin lyase
- Phosphoenolpyruvate carboxykinase
- Pyruvate decarboxylase
- Succinate dehydrogenase
See also[edit]
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