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Enzyme modulators

Enzymes are protein catalysts that cause a chemical change in another substance, with the molecules being transformed by enzymes known as substrates.  Some enzymes act independently but others require the assistance of coenzymes in order to function correctly. 

There are six main families of enzymes, oxidoreductases, which catalyze oxidation and reduction reactions, transferases, which transfer a functional group (such as a methyl or phosphate group), hydrolases, which catalyze the hydrolysis of various bonds, lyases, which cleave various bonds by means other than hydrolysis, isomerases, which catalyze isomerization changes within a single molecule, and ligases, which join two molecules together with covalent bonds.  Enzymes are usually very selective as to which reactions they catalyze and the substrates that they act on. This selectivity is extremely important as enzymes serve a wide variety of key functions inside living organisms.  Enzymes are essential for metabolic function and signal transduction. 

Copeland et al (2007) Targeting enzyme inhibitors in drug discovery, Exp. Opinion Ther. Targets 11(7) 967 DOI: 10.1517/14728222.11.7.967

Cardinale et al (2010) Homodimeric Enzymes as Drug Targets.  Curr. Med. Chem. Volume 17(9) 826 https://doi.org/10.2174/092986710790712156

Alexander et al (2019) The Concise Guide to Pharmacology 2019/20: Enzymes. Br J Pharmacol. 176 S1 S297

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