| A | B |
|---|
| enzyme | a globular protein, sometimes with a cofactor, that catalyzes a biological reaction |
| substrate | the molecule that reacts in the active site in an enzyme catalyzed reaction |
| enzyme-substrate complex | occurs when the enzyme and the substrate are combined within the active site; is able to lower the energy required for catalyzing the reaction |
| Allosteric enzymes | an enzyme that regulates the rate of reaction when a regulator molecule attaches to a site other than the active site |
| substrate | the molecule that reacts in the active site in an enzyme catalyzed reaction |
| active site | a pocket in the part of the tertiary enzyme structure that binds to the substrate and catalyzes a reaction |
| Lock and Key model of enzyme activity | an early theory described the active site as rigid, nonflexible shape in which a substrate was a key that specifically fir the lock |
| Induced-fit model of enzyme action | dynamic model of enzyme action in which the flexibility of the active site allows it to adapt to the shape of the substrate and substrate can also be modified to fir the active site; replaced the lock and key theory |
| Competetive inhibitor | a molecule that has a STUCTURE SIMILAR TO THE SUBSTRATE, that inhibits enzyme action by competing for the active site |
| noncompetitive inhibitor | an inhibitor that DOES NOT resemble the substrate and attaches to the enzyme away from the active site away from the active site to prevent binding of the substrate |
| co-factors | a metal ion or an organic molecule that is necessary for a inactive enzyme to become an active enzyme |
| zymogen (proenzymes) | an inactive form of an enzyme that is activated by the removal of a peptide portion from one end of the protein |
| as enzyme concentration increases ________ | reaction rate increases |
| as substrate concentration increases_________ | reaction rate increases but then stops due to all of the enzyme being combined with the substrate |
| oxioreductase enzyme | catalyze oxidation-reduction reactions |
| transferases enzyme | catalyze the transfer of a functional group between 2 compounds |
| hydrolase enzyme | catalyze hydrolysis (add H2o) reactions that split a compound into 2 products |
| lyases enzyme | catalyze the addition or removal of a group without hydrolysis |
| isomerases enzyme | catalyze the rearrangement (isomerization) of atoms within a substrate |
| ligases enzyme | catalyze the joining of 2 substrate using ATP energy |
| ABSOLUTE is a type of substrate specificity that _______ | catalyzes one type of reaction for one substrate (example urea catalyzes hydrolysis of urea) |
| GROUP is a type of substrate specificity where ___________ | catalyzes one type of reaction for similar substrates |
| LINKAGE is a type of substrate specificity where ________ | catalyzes one type of reaction for a specific bond |
| These vitamins are fat soluble ______ and can cause toxicity if taken too much | A, D, E, K (these are polar) |
| Lower temperature _______ slows/stops activity of enzyme | low |
| high temperatures greater then _______ the shapes of most proteins are destroyed | above 50 C |
| optimum temperature of ______ is when enzymes are most active | 37 C (body temperature) |
| enzymes are most active at their optimum pH if the ph changes are _________ | small the enzyme can regain it tertiary or quaterneray structure and biological activity; if there is a large change the protein structure is destroyed |
| Water soluble vitamin | are polar and cannot be stored in the body |
| Lack of vitamin C can cause_______ | scurvy; forms collagen |
| Lack of B1 causes ________ | beriberi |
| lack of B3 causes ______ | pellagra |
| coenzyme | this is a cofactor that is organic |
| antioxidants | remove free radicals from the body (vitamin C, E and beta-carotene) |
| Feedback control | a type of inhibition where the END PRODUCT inhibits the first enzyme in a sequence of enzyme catalyzed reaction |
