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Flashcards covering the basics of enzymes, their function, nomenclature, and industrial applications based on lecture notes.
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Enzyme
Proteins that act as biological catalysts by accelerating chemical reactions.
Substrates
The molecules upon which enzymes act.
Allostery
The ability of a protein to change shape, resulting in a change in binding affinity at a different binding site.
Allosteric enzymes
Enzymes with the active site, as well as an additional site (allosteric site).
Activation energy
The energy barrier separating the reactants and the products in a chemical reaction.
Recommended enzyme name
Short name, most used, has the suffix ‘-ase’ attached to the substrate of the reaction or the description of the reaction performed.
Systematic enzyme name
More complete, complex enzyme name used when an enzyme must be identified without ambiguity.
Oxidoreductases
Catalyze reactions in which one molecule is oxidized while the other is reduced (transfer of electrons and hydrogens).
Transferases
Transfer carbon, nitrogen, or phosphate groups.
Hydrolases
Enzymes that catalyze a hydrolytic cleavage reaction (use water to break a chemical bond).
Lyases
Catalyze the cleavage of C-C, C-S, and C-N bonds (catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure).
Isomerases
Catalyze the rearrangement of bonds within a single molecule, transfer of groups within molecules to yield isomeric forms.
Ligases
Join two molecules in an energy-dependent process; catalyze formation of bonds between carbon and O, S, and N coupled to hydrolysis of high energy phosphates.
Synthetase
Requires ATP (ligase class).
Synthase
No ATP required (lyase class).
Phosphatase
Remove phosphates (hydrolase class).
Phosphorylase
Transfer (add) inorganic phosphates (transferase class).
Active sites
Contain a special pocket with high specificity, containing amino acid side chains that participate in substrate binding and catalysis.