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Definition
| Biological catalysts that speed up the rates of reactions without being consumed |
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Definition
| Can increase rates of reactions 10^9 to 10^20 times compared to uncatalyzed reactions |
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| Based on the substrate or type of reaction that is catalyzed. Usually end in "-ase". |
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| An enzyme that hydrolyzed the carboxyl terminal residue of a polypeptide |
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Definition
| An enzyme that hydrolyzes the ester bond of the neurotransmitter acetylcholine |
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| A family of enzymes that transfer hydrogen from the substrate to a coenzyme. Enzymes that remove hydrogen. |
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Definition
| Reactants of an enzyme catalyzed reaction |
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| The site on an enzyme where substrate binds and where reaction takes place |
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Definition
| A non-protein component required by some enzymes for activity. |
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Definition
| Metal ions, coenzymes (organic or metallic organic cofactors such as heme) |
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| A cofactor that is tightly bound to the protein (ex: heme) |
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Definition
| Any process that initiates or increases the activity of an enzyme |
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Definition
| Any process that decreases the activity of an enzyme |
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Definition
| Measure of rate of an enzyme catalyzed reaction |
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Definition
| Rate of reaction = proportional to substrate concentration |
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Definition
| As temp increases, rate increases until it reaches an optimum temp. After the temp continues to increase, rate of reaction drops off because the enzyme becomes denatured. |
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Definition
| Enzymes typically function within a narrow pH. Changing pH results in changes of the ionic state of residues and hydrogen bonding, resulting in denaturation. |
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Definition
| By Emil Fischer, proposes a rigid activation site, only the substrate with correct shape fits the active site. |
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Definition
| Daniel Koshland Jr. Active site is more flexible, and binding of correct substrate induces the active site to assume shape for catalysis. |
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Term
| Enzyme activity regulation |
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Definition
| Increasing or decreasing activity to prevent wasteful expenditure of energy to produce products when they are not needed |
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Term
| Types of enzyme activity regulation |
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Definition
1. Allosteric regulation (allosterism)
2. Feedback inhibition (feedback control)
3. Proenzymes
4. Protein modification |
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Term
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Definition
| Enzymes whose activity is altered by the binding of small molecules called effectors or regulators |
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Term
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Definition
| Bind to sites on the molecule distinctly different from the active site to alter enzyme activities |
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Definition
| Binding of the regulator to the enzyme increases its activity. Active site can then bind to a substrate more easily. |
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Definition
| Binding of the regulator to the enzyme decreases the activity |
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Term
| Classes of reversible inhibitors |
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Definition
1. Competitive inhibitors
2. Noncompetitive inhibitors |
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Term
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Definition
| First antimicrobial drugs. Inhibit an enzyme in the pathway used by bacteria to synthesize folic acid. Without it, bacteria die. |
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| Noncompetetive inhibitors |
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Definition
| Bind to a site distinctly different from active site. Does not compete with the substrate for binding. Instead, they alter the shape of the active site so binding cannot occur. |
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Term
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Definition
1. Obtain energy
2. Generate building blocks for protein synthesis
3. Synthesize proteins
4. Produce or modify biological molecules |
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Definition
| Set of pathways that breakdown molecules |
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Definition
1. Degradation (break things down)
2. Oxidation
3. Reactions that release energy |
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Definition
| Set of metabolic reactions to build molecules |
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Definition
1. Synthesis of molecules
2. Reduction reactions
3. Reactions that require energy input |
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Definition
| Contains aqueous, gel-like solution. Contains enzymes of oxidative metabolism. |
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Term
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Definition
| Very porous, ions flow through |
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Definition
| Energy factory, generate most of the cell's ATP |
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Term
| Inner membrane of mitochondria |
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Definition
| Impermeable to most ions & molecules. Highly folded to increase surface area. |
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Term
| Two parts of the common metabolic pathway |
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Definition
1. Citric acid cycle
2. Electron transport chain |
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Term
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Definition
| Adenosine triphosphate. Energy currency of cell. Has two high energy phosphoanhydride bonds and one phosphoester bond. |
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Term
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Definition
| Adenosine diphosphate. Two phosphate groups, contains one phosphoanhydride bond. One phosphoester bond. |
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Term
| Agents for transfer of electrons in biological oxidation-reduction reactions (help carry them out) |
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Definition
1. Nicotinamide adenine dinucleotide: NAD+
2. Flavin adenine dinucleotide: FAD |
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Term
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Definition
| Nicotinamide adenine dinucleotide. Nicotinamide + ribose + ADP. Oxidized form of NADH. Reaction of NAD+ to NADH is reversible. |
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Term
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Definition
| Riboflavin (Vitamin B2) + ADP. Oxidized form of FADH2). |
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| Agent for transfer of Acetyl groups |
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Definition
Coenzyme A (CoA).
Made of phosphorylated ADP + pantothenic acid + mercaptoethylamine. |
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Term
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Definition
| A major metabolic pathway involved in the oxidation of carbohydrates, lipids and proteins. It is part of the third and final stage in the overall pathway of catabolism. |
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Term
| Highlights of the citric acid cycle |
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Definition
1. Conversion of citrate to isocitrate
2. Oxidative decarboxylation
3. Substrate level phosphorylation
4. Other oxidative reactions |
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Term
| Conversion of citrate to isocitrate |
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Definition
| Converts tertiary alcohol to a secondary alcohol which can be oxidized |
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Term
| Oxidative decarboxylation |
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Definition
| Isocitrate + NAD+ = alpha ketoglutoride + CO2 + NADH + H |
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Term
| Substrate level phosphorylation |
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Definition
| Succinyl-CoA + GDP + Pi = Succinate + GTP + CoA |
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Term
| Other oxidative reactions |
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Definition
Succinate + FAD = Fumarate + FADH2
Malate + NAD = Oxalacetate + NADH + H |
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Term
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Definition
Activators: Acetal CoA
Inhibitors: NADH |
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Term
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Definition
Activated by Ca2+ & ADP
Inhibited by NADH, ATP
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Term
| Alpha-ketoglutarate dehydrogenase |
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Definition
Activators: Ca2+
Inhibitors: NADH, ATP, succinyl-CoA |
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