My Study Guide2

My Study Guide2 - Chapter 5 Enzyme – a biomolecule...

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Chapter 5 Enzyme – a biomolecule, usually a protein, that acts as a biological catalyst to speed the rate of a biochemical reaction Activation energy – amount of energy required to convert molecules in a reacting system from the ground state to transition state. Prosthetic group – small organic molecule or metal ion associated with a protein usually by covalent or ionic bonds. Apoenzyme – an enzyme in its polypeptide form without any necessary prosthetic groups of cofactors Km Turnover number Active site – specific region on an enzyme where the substrate molecule binds. Induced-fit model – used to describe conformational changes in an enzyme caused by the binding of a substrate molecule. Transition State Analog – recognizes substrates and orients it to promote catalysis. Irreversible inhibitor – compounds that form covalent bonds or very strong noncovalent bonds with an enzyme, thus permanently damaging the enzyme. Lineweaver-burk graph Substrate saturation Lock and key model – used to describe the binding interactiong between an enzyme and its substrate molecule. Holoenzyme – an enzyme in its complete form, including polypeptides and cofactor Oxidoreductase – a class of enzymes that catalyzes oxidation and reduction reactions; also called dehydrogenases Initial velocity Michaelis-menten graph Vmax – number that compares the velocity versus the concentration of the substrate. Acid-base catalysis – functional groups can act as acids (COOH) or bases (COO-, NH2-) Metal Ion catalysis – assist catalysis – orients substrate in active site, polarizes bonds or stabilizes an intermediate. Covalent Catalysis – nucleophilic group reacts and forms a bond with substrate. Lead to highly reactive intermediate. And will eventually lead to broken bonds and release product. Noncompetitive inhibitor – will bind to another part of the enzyme (not the active site) Uncompetitive inhibitor – will bind to part other than active site, but only if ES complex Competitive – inhibitor that competes for substrate for binding (about same size) Reversible inhibition – substrate can bind to enzyme and become unbound. Study Guide Stuff Types of Enzymes (6) Oxidoreductases transfer electrons as hydride ion Transferases transfer functional groups from one molecule to another Hydrolases cleavage of bond by hydrolysis Lyases form double bonds by removing groups or addition of groups Isomerases transfer groups within a molecule to yield isomeric forms Ligases form c-c, c-s, c-o, c-n bonds by condensation
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Chapter 6 Vocab Vitamin – organic molecules that are essential for proper growth/dev. Coenzyme – organic or organometallic cofactor that is either bound tight or loosely to enzyme Prosthetic group – the coenzymes that are attached to the enzyme. Micronutrient – a substance such as a metal ion, that is required in minute amounts by an
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This note was uploaded on 04/06/2008 for the course BBMB 301 taught by Professor Girton during the Fall '07 term at Iowa State.

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My Study Guide2 - Chapter 5 Enzyme – a biomolecule...

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