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Published byGervais Henderson Modified over 8 years ago
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Biological catalysts that speed up chemical reactions. They are specialized globular proteins that provide substrates with a lower activation energy barrier. Catalysis occurs in the active site, which specifically binds to the substrates based on many chemical factors including shape, stereochemistry, electrical charge, and hydrophilic or hydrophobic considerations. Central to every biochemical process.
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They are all allosteric proteins. They remain unchanged by a reaction, and hence reusable. Enzymes can catalyze biochemical reactions at room temperature to the order of 10 to 100 million times. A small amount of enzyme can catalyze a large amount of substrate. Enzymes will catalyze those reactions that are thermodynamically feasible. They cannot change the position of equilibrium. Enzymes are affected by temperature, pH and pressure. They can be denatured by extreme conditions and chemicals. The reactions are reversible. Enzymes are specific to their substrates; one enzyme controls one reaction.
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Pro-drug therapy: Some medicines are delivered to the body in an inactive form. They only become active when they are acted on by enzymes in the body. Lisdexamfetamine is a drug that can be used to help children who are affected by ADHD. Lisdexamfetamine is a prodrug – it is inactive. In the body it is converted to dextroamphetamine by enzymes that remove a lysine (amino acid) group. The active drug acts on neurotransmitters including serotonin, dopamine and noradrenaline in the synapses of the brain
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The driving force in the development of enzyme technology is: The development of new and better products, processes, and services to meet needs The improvement of processes to produce existing products from new raw materials such as biomass. Cost reduction Improvement of biological properties and quality Utilization of new re-generable sources of raw materials Reduction of environmental impact
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