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Τι (ποιος) είναι Enzyme - ορισμός
![recessive]] fashion because the enzymes from the unaffected genes are generally sufficient to prevent symptoms in carriers.](https://commons.wikimedia.org/wiki/Special:FilePath/Autosomal recessive inheritance for affected enzyme.png?width=200 "recessive]] fashion because the enzymes from the unaffected genes are generally sufficient to prevent symptoms in carriers.")
![The energies of the stages of a [[chemical reaction]]. Uncatalysed (dashed line), substrates need a lot of [[activation energy]] to reach a [[transition state]], which then decays into lower-energy products. When enzyme catalysed (solid line), the enzyme binds the substrates (ES), then stabilizes the transition state (ES<sup>‡</sup>) to reduce the activation energy required to produce products (EP) which are finally released.](https://commons.wikimedia.org/wiki/Special:FilePath/Enzyme catalysis energy levels 2.svg?width=200 "The energies of the stages of a [[chemical reaction]]. Uncatalysed (dashed line), substrates need a lot of [[activation energy]] to reach a [[transition state]], which then decays into lower-energy products. When enzyme catalysed (solid line), the enzyme binds the substrates (ES), then stabilizes the transition state (ES<sup>‡</sup>) to reduce the activation energy required to produce products (EP) which are finally released.")
Βικιπαίδεια
Enzymes () are proteins that act as biological catalysts by accelerating chemical reactions. The molecules upon which enzymes may act are called substrates, and the enzyme converts the substrates into different molecules known as products. Almost all metabolic processes in the cell need enzyme catalysis in order to occur at rates fast enough to sustain life.: 8.1 Metabolic pathways depend upon enzymes to catalyze individual steps. The study of enzymes is called enzymology and the field of pseudoenzyme analysis recognizes that during evolution, some enzymes have lost the ability to carry out biological catalysis, which is often reflected in their amino acid sequences and unusual 'pseudocatalytic' properties.
Enzymes are known to catalyze more than 5,000 biochemical reaction types. Other biocatalysts are catalytic RNA molecules, called ribozymes. Enzymes' specificity comes from their unique three-dimensional structures.
Like all catalysts, enzymes increase the reaction rate by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many therapeutic drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH, and many enzymes are (permanently) denatured when exposed to excessive heat, losing their structure and catalytic properties.
Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.
