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| Pertaining to the altered activity of an enzyme due to the binding of a molecule to a region other than the enzyme's active site. |
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| The energy-consuming process of incorporating nutrients into protoplasm through biosynthesis. |
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| The chemical breakdown of complex compounds into simpler units to be used in cell metabolism. |
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| A susbstance that alters the rate of reaction without being consumed or permanently changed by it. In cells, enzymes are catalysts. |
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| A complex inorganic molecule, several of which are derived from vitamins (eg. nicotinamide, riboflavin). Operates in conjunction with an enzyme. Serves as transient carrier of specific atoms or functional groups during metabolic reactions. |
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| An enzyme accessory. It can be organic, such as coenzyme, or inorganic, such as Fe, Mn, Zn or ions. |
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| An enzyme present in bacterial cells in constant amounts regardless of the presence of substrate. Enzymes of the central catabolic pathways are typical examples. |
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| A protein biocatalyst that facilitates metabolic reactions. |
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| An extracellular enzyme mainly for hydrolysis of nutrient macromolecules that are otherwise impervious to the cell membrane. It functions in saprobic decomposition of organic debris and can be a factor in invasiveness of pathogens. |
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| The extraction of energy through anaerobic degradation of substrates into simpler, reduced metabolites. In large industrial processes, fermentation can mean any use of microbial metabolism to manufacture organic chemicals of other products. |
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| The energy-yielding breakdown (fermentation) of glucose to pyruvic or lactic acid. Often called anaerobic glycolysis because no molecular oxygen is consumed in the degradation. |
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| An enzyme complete with its own apoenzyme and cofactors. |
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| A process in which water is used to break bonds in molecules. Usually occurs in conjunction with an enzyme. |
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| Molecules or compounds that are chemically unstable in the presence of environmental changes. |
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| Small organic molecules that are intermediates in the stepwise biosynthesis or breakdown of macromolecules. |
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| Enzyme regulation of matabolism by the end product of a multienzyme system that blocks the action of a "pacemaker" enzyme of or near the beginning of the pathway. |
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| The loss of electrons by one reactant (in chemical reactions) |
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| Denoting an oxidation-reduction reaction. |
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| The specific molecule upon which an enzyme acts. |
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| Protein enzymes catalyze by lowering the ________ of ________ of the reaction. |
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Definition
| The protein part of an enzyme, as opposed to the nonprotein or inorganic cofactors. |
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| An enzyme accessory. It can be organic, such as coenzymes, or inorganic, such as Fe, Mn or Zn ions. |
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| Note the differences between competitive and noncompetitive inhibition work. First, explain competitive inhibition. |
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Definition
| In competitive inhibition, both the normal substrate and a competitive inhibitor with a similar shape compete for the active site on the enzyme; if the normal substrate gets the active site position, a reaction proceeds; if the inhibitor does, a reaction is blocked because the inhibitor can't become a product. |
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| Glycolysis converts 1 glucose into ___ pyruvic acid molecules. |
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| Glycolysis nets _____ ATPs. |
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| Pyruvate participates in both respiration and __________ reactions. |
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| Substrate-level phosphorylation occurs in glycolysis and ________________. |
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| Carbon dioxide evolves in the intermediate reaction and _____________ cycle. |
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| _____________ are stripped off of glucose during glycolysis and the TCA cycle (oxidize/reduce) organic cofactors such as NAD. |
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Definition
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| In aerobic respiration _________ is the final electron acceptor. |
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| Chemiosmotic phosphorylation occurs where in eukaryotic cells? |
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Definition
| In the inner membrane space of the mitochondria |
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| How many ATPs occur as a result of chemiosmotic phosphorylation? |
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| Yeast fermentation produces a two-carbon molecule and a one-carbon molecule ... name them. |
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| Where does ATP in fermentation come from? |
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Definition
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| What does ATP synthase do? |
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| Where are triglycerides burned during catabolism? |
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| The formation of glucose (or glycogen) from noncarbohydrate sources such as protein or fat. Also called glyconegensis. |
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| What is the final electron acceptor in aerobic respiration? In fermentation? |
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| Contrast feedback inhibition with substrate inhibition. |
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| Formation of peptide bonds is an example of what? |
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| Hydrolysis of peptide bonds is an example of what? |
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| Drawing off organic and intermediates from the TCA cycle is termed what? |
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| Note the differences between competitive and noncompetitive inhibition work. (part two) Explain non-competitive inhibition. |
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Definition
| The substrate fits into the available active site of the enzyme; the regulatory molecule binds into a separate site on the enzyme. If the regulatory molecule doesn't actually bind into the site, the reaction will proceed; if it does, the reaction is blocked b/c binding of regulatory molecules in reg. sites changes the conformation of the active site so the substrate cannot enter. (whichever one gets there first fits). |
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